|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
39-1290 |
1.79e-180 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 573.13 E-value: 1.79e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 39 KKKPEKMNMVSPlavFRYSDRQDKLLMVLGTTMAVLHGASLPLMMIVFGDMTDTFIASENTTyPANFSLLNSTSVNFSME 118
Cdd:PTZ00265 39 KIKTQKIPFFLP---FKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVN-DIIFSLVLIGIFQFILS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 119 FFSYLILgeleeemtryayyysgigagvlfaayiqvsfwTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVD 198
Cdd:PTZ00265 115 FISSFCM--------------------------------DVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 199 DISKINEGIGEKIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEV 278
Cdd:PTZ00265 163 YLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 279 LAAVRTVVAFGGQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSE--------DYTIG 350
Cdd:PTZ00265 243 LVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDlsnqqpnnDFHGG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 351 KVFTVFFSILVGAFSVGQAAPSMEAFANARGAAYAIFNIIDNEPQIDSSsNAGYKLDHVKgNLEFQNVFFSYPARPDIKI 430
Cdd:PTZ00265 323 SVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENN-DDGKKLKDIK-KIQFKNVRFHYDTRKDVEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITI-DGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENI 509
Cdd:PTZ00265 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 RYG--------------RED----------------------------VTMEEIERATKEANA---------------YD 532
Cdd:PTZ00265 481 KYSlyslkdlealsnyyNEDgndsqenknkrnscrakcagdlndmsntTDSNELIEMRKNYQTikdsevvdvskkvliHD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 533 FIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIR--KGRTILVIAHRL 610
Cdd:PTZ00265 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 611 STVRNADLIAAFEN-----------------------------------------------GVITEQGTHDELMEQK-GV 642
Cdd:PTZ00265 641 STIRYANTIFVLSNrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagSYIIEQGTHDALMKNKnGI 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 643 YYKLVNMQ-----ASETEDQLQEEGNASSVSEEA--------LNGSVLTGQKRQSTRKSIKRVriqndelDVKADQLDKN 709
Cdd:PTZ00265 721 YYTMINNQkvsskKSSNNDNDKDSDMKSSAYKDSergydpdeMNGNSKHENESASNKKSCKMS-------DENASENNAG 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 710 mPPSSFFKIMKLNKTEWPY---------------FVVGTLCAIINGALQPIFSVMISDVIGMFVEkgkAAIRETNST-YA 773
Cdd:PTZ00265 794 -GKLPFLRNLFKRKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFALLYAKYVSTLFD---FANLEANSNkYS 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 774 LLFLGFGLISFVTFFLQGFTFGKAGEIL--TMRLRsmAFRAILRQEISWFDEPKNSTGELITRLANDASQVKgaTGsrla 851
Cdd:PTZ00265 870 LYILVIAIAMFISETLKNYYNNVIGEKVekTMKRR--LFENILYQEISFFDQDKHAPGLLSAHINRDVHLLK--TG---- 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 852 lVAQNIANLGTGIVLSLIYgwqlTLLLLAIVPIIA--ITGM--IQMKMLAGHAK----KD--KKELETLGKV-------- 913
Cdd:PTZ00265 942 -LVNNIVIFTHFIVLFLVS----MVMSFYFCPIVAavLTGTyfIFMRVFAIRARltanKDveKKEINQPGTVfaynsdde 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 914 --------ASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGH 985
Cdd:PTZ00265 1017 ifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGT 1096
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 986 MRFKDVLLVFSAIVFGAMALGQSTSFTPDYAKAKMSAAHLFLLFERVPLIDSYSEEGEKPK---MFGGNITFKDVAFKYP 1062
Cdd:PTZ00265 1097 ILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKnknDIKGKIEIMDVNFRYI 1176
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1063 TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYD------------------------------------- 1105
Cdd:PTZ00265 1177 SRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvn 1256
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1106 -----------------PLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGdnSREVSHEEIVSAAKA 1168
Cdd:PTZ00265 1257 efsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKF 1334
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1169 ANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEAL----DKAreGRTC 1244
Cdd:PTZ00265 1335 AAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTI 1412
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1245 IVIAHRLSTIQNADKIAVIQN----GKVIE-QGTHQQLL-AEKGFYYSLVNV 1290
Cdd:PTZ00265 1413 ITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLsVQDGVYKKYVKL 1464
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
53-653 |
2.11e-180 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 544.76 E-value: 2.11e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 53 VFRYSdRQDKLLMVLGTTMAVLHGASLPLMMIVFGDMTDTFIASENTTYpanfsllnstsvnfsmeffsylilgeleeeM 132
Cdd:COG1132 12 LLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA------------------------------L 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 133 TRYAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIA 212
Cdd:COG1132 61 LLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 213 MFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQR 292
Cdd:COG1132 141 QLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 293 KETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVFTVFFSILVGAFSVGQAAPS 372
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 373 MEAFANARGAAYAIFNIIDNEPQIDSSSNAGyKLDHVKGNLEFQNVFFSYParPDIKILKGLNLKVNCGQTVALVGGSGC 452
Cdd:COG1132 301 LNQLQRALASAERIFELLDEPPEIPDPPGAV-PLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 453 GKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYD 532
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 533 FIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLST 612
Cdd:COG1132 458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLST 537
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2024474312 613 VRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQASE 653
Cdd:COG1132 538 IRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
711-1293 |
1.62e-178 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 539.75 E-value: 1.62e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 711 PPSSFFKIMKLNKTEWPYFVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAAireTNSTYALLFLGFGLISFVTFFLQ 790
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLS---ALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 791 GFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIY 870
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 871 GWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIK 950
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 951 KAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHMRFKDVLLVFSAIVFGAMALGQSTSFTPDYAKAKMSAAHLFLLFE 1030
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1031 RVPLIDSySEEGEKPKMFGGNITFKDVAFKYPtrPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGE 1110
Cdd:COG1132 320 EPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1111 VLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNsrEVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKG 1190
Cdd:COG1132 397 ILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1191 AQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIE 1270
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
570 580
....*....|....*....|...
gi 2024474312 1271 QGTHQQLLAEKGFYYSLVNVQSG 1293
Cdd:COG1132 555 QGTHEELLARGGLYARLYRLQFG 577
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1052-1291 |
1.11e-157 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 472.02 E-value: 1.11e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFDCTIAENIAYGDNSREVshEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQP 1211
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVNVQ 1291
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
414-650 |
7.38e-153 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 459.31 E-value: 7.38e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 414 EFQNVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGV 493
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 494 VNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKIL 573
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 574 LLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQ 650
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
65-386 |
1.29e-142 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 435.55 E-value: 1.29e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 65 MVLGTTMAVLHGASLPLMMIVFGDMTDTFIASENTTYPANFSLLNSTSVNFSmeffsylilgELEEEMTRYAYYYSGIGA 144
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSAGPFE----------KLEEEMTLYAYYYLIIGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 145 GVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTG 224
Cdd:cd18558 71 IVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 225 FIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLED 304
Cdd:cd18558 151 FIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 305 AKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVFTVFFSILVGAFSVGQAAPSMEAFANARGAAY 384
Cdd:cd18558 231 AKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAY 310
|
..
gi 2024474312 385 AI 386
Cdd:cd18558 311 HI 312
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
141-651 |
4.16e-142 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 448.90 E-value: 4.16e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 141 GIGAGVLFAAYIQV--SFWTLAAGRQI-KRIRQEFFHAVMRQEIGWFDVNDVCELNTRIvDDISKINEGIGEKIAMFFQA 217
Cdd:COG2274 201 GLLLALLFEGLLRLlrSYLLLRLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLD 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 218 VATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETER 297
Cdd:COG2274 280 LLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRR 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 298 YQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVftVFFSILVGAF--SVGQAAPSMEA 375
Cdd:COG2274 360 WENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQL--IAFNILSGRFlaPVAQLIGLLQR 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 376 FANARGAAYAIFNIIDNEPQIDSSSNAGyKLDHVKGNLEFQNVFFSYPARpDIKILKGLNLKVNCGQTVALVGGSGCGKS 455
Cdd:COG2274 438 FQDAKIALERLDDILDLPPEREEGRSKL-SLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 456 TTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIM 535
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 536 KLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRN 615
Cdd:COG2274 596 ALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL 675
|
490 500 510
....*....|....*....|....*....|....*.
gi 2024474312 616 ADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQA 651
Cdd:COG2274 676 ADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
707-1291 |
1.26e-139 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 442.35 E-value: 1.26e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 707 DKNMPPSSFFKIMKLNKTEWPYFVVGTLCAIINGALQPIFS-VMISDVIGmfvekgkAAIRETNSTYALLFLGFGLISFV 785
Cdd:COG2274 139 EKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTqVVIDRVLP-------NQDLSTLWVLAIGLLLALLFEGL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 786 TFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLaNDASQVKGATGSRLALVAQNIANLGTGIV 865
Cdd:COG2274 212 LRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 866 LSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAghaKKDKKELETLGKVAS---EAIENIRTVVALTQERKFEYMYGQNLQ 942
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLR---RLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 943 VSYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHMRFkDVLLVFSAIVFGAMA-LGQSTSFTPDYAKAKMS 1021
Cdd:COG2274 366 KYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1022 AAHLFLLFERVPLIDSYSEEGEKPKmFGGNITFKDVAFKYPTRpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLE 1101
Cdd:COG2274 445 LERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1102 RFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDnsREVSHEEIVSAAKAANIHSFIESLPKK 1181
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEAARLAGLHDFIEALPMG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1182 YNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIA 1261
Cdd:COG2274 601 YDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII 680
|
570 580 590
....*....|....*....|....*....|
gi 2024474312 1262 VIQNGKVIEQGTHQQLLAEKGFYYSLVNVQ 1291
Cdd:COG2274 681 VLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
719-1035 |
3.88e-137 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 421.09 E-value: 3.88e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 719 MKLNKTEWPYFVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAAIRETNSTYALLFLGFGLISFVTFFLQGFTFGKAG 798
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 799 EILTMRLRSMAFRAILRQEISWFDEPKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLL 878
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 879 LAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFT 958
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 959 FAFTQAIMYFTYAGCFRFGAYLVKNGHMRFKDVLLVFSAIVFGAMALGQSTSFTPDYAKAKMSAAHLFLLFERVPLI 1035
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
158-647 |
1.53e-136 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 434.15 E-value: 1.53e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 158 TLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTGFIVGFTKGWKLTL 237
Cdd:TIGR00958 226 NYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTM 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 238 VILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDAKRMGIQKAISAN 317
Cdd:TIGR00958 306 VTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 318 ISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVFtvffSILVGAFSVGQAAPSMEAFAN----ARGAAYAIFNIIDNE 393
Cdd:TIGR00958 386 GYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSgmmqAVGASEKVFEYLDRK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 394 PQIdsSSNAGYKLDHVKGNLEFQNVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTIT 473
Cdd:TIGR00958 462 PNI--PLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 474 IDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMS 553
Cdd:TIGR00958 540 LDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 554 GGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAalDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTH 633
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
490
....*....|....
gi 2024474312 634 DELMEQKGVYYKLV 647
Cdd:TIGR00958 698 KQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
130-650 |
2.07e-127 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 405.24 E-value: 2.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 130 EEMTRYAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGE 209
Cdd:TIGR02204 55 GLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 210 KIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFG 289
Cdd:TIGR02204 135 SLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 290 GQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKV--FtVFFSILVGAfSVG 367
Cdd:TIGR02204 215 HEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgqF-VFYAVMVAG-SIG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 368 QAAPSMEAFANARGAAYAIFNIIDNEPQIDSSSNAGYKLDHVKGNLEFQNVFFSYPARPDIKILKGLNLKVNCGQTVALV 447
Cdd:TIGR02204 293 TLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 448 GGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKE 527
Cdd:TIGR02204 373 GPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 528 ANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIA 607
Cdd:TIGR02204 453 AHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIA 532
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2024474312 608 HRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQ 650
Cdd:TIGR02204 533 HRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
65-386 |
7.33e-123 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 382.59 E-value: 7.33e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 65 MVLGTTMAVLHGASLPLMMIVFGDMTDTFIasenttypaNFSLLNSTSvnfsmeffsylilGELEEEMTRYAYYYSGIGA 144
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFT---------DFGSGESSP-------------DEFLDDVNKYALYFVYLGI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 145 GVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTG 224
Cdd:cd18577 59 GSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 225 FIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLED 304
Cdd:cd18577 139 FIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 305 AKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVFTVFFSILVGAFSVGQAAPSMEAFANARGAAY 384
Cdd:cd18577 219 ARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAA 298
|
..
gi 2024474312 385 AI 386
Cdd:cd18577 299 KI 300
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
716-1288 |
7.72e-121 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 392.16 E-value: 7.72e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 716 FKIMKLNKTEWPYFVVGTL---CAIINGALQPIFSVMISDVIGmfveKGKAAIRETNSTYALLFLGFGliSFVTFFLQGF 792
Cdd:TIGR00958 150 FRLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYTGRVIDTLG----GDKGPPALASAIFFMCLLSIA--SSVSAGLRGG 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 793 TFGKAGEILTMRLRSMAFRAILRQEISWFDEpkNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGW 872
Cdd:TIGR00958 224 SFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 873 QLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQE----RKFEYMYGQNLQVSYRNS 948
Cdd:TIGR00958 302 RLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEegeaSRFKEALEETLQLNKRKA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 949 IKKAhifgfTFAFTQAIM-YFTYAGCFRFGAYLVKNGHMRfKDVLLVFsaiVFGAMALGQS----TSFTPDYAKAKMSAA 1023
Cdd:TIGR00958 382 LAYA-----GYLWTTSVLgMLIQVLVLYYGGQLVLTGKVS-SGNLVSF---LLYQEQLGEAvrvlSYVYSGMMQAVGASE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1024 HLFLLFERVPLIdsySEEGE-KPKMFGGNITFKDVAFKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLER 1102
Cdd:TIGR00958 453 KVFEYLDRKPNI---PLTGTlAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1103 FYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNSREvsHEEIVSAAKAANIHSFIESLPKKY 1182
Cdd:TIGR00958 530 LYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP--DEEIMAAAKAANAHDFIMEFPNGY 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1183 NTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEalDKAREGRTCIVIAHRLSTIQNADKIAV 1262
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILV 685
|
570 580
....*....|....*....|....*.
gi 2024474312 1263 IQNGKVIEQGTHQQLLAEKGFYYSLV 1288
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
213-657 |
4.71e-117 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 378.39 E-value: 4.71e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 213 MFFQAVATFF----TGFIVGFTKGWKLTLVILAlspvlgfssALWAKIISTF--TNKEL-------TAYAKAGAVAEEVL 279
Cdd:COG5265 155 LLFNILPTLLeialVAGILLVKYDWWFALITLV---------TVVLYIAFTVvvTEWRTkfrremnEADSEANTRAVDSL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 280 AAVRTVVAFGGQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVftvffsI 359
Cdd:COG5265 226 LNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDF------V 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 360 LVGAFSVGQAAPsmeafANARGAAY-----------AIFNIIDNEPQIDSSSNAGyKLDHVKGNLEFQNVFFSY-PARPd 427
Cdd:COG5265 300 LVNAYLIQLYIP-----LNFLGFVYreirqaladmeRMFDLLDQPPEVADAPDAP-PLVVGGGEVRFENVSFGYdPERP- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 ikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAE 507
Cdd:COG5265 373 --ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAY 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 508 NIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 587
Cdd:COG5265 451 NIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 588 SVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQASETEDQ 657
Cdd:COG5265 531 RAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAE 600
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
149-653 |
1.06e-116 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 376.36 E-value: 1.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 149 AAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTGFIVG 228
Cdd:TIGR02203 70 CSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 229 FTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERY----QKNLED 304
Cdd:TIGR02203 150 LYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFdavsNRNRRL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 305 AKRMGIQKAISANISMgvsfflIYGSYALAFWYGTILVLSED--YTIGKvFTVFFSilvgafSVGQAAPSMEAFANARG- 381
Cdd:TIGR02203 230 AMKMTSAGSISSPITQ------LIASLALAVVLFIALFQAQAgsLTAGD-FTAFIT------AMIALIRPLKSLTNVNAp 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 382 ------AAYAIFNIIDNEPQIDSSSNAgykLDHVKGNLEFQNVFFSYPARpDIKILKGLNLKVNCGQTVALVGGSGCGKS 455
Cdd:TIGR02203 297 mqrglaAAESLFTLLDSPPEKDTGTRA---IERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 456 TTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGR-EDVTMEEIERATKEANAYDFI 534
Cdd:TIGR02203 373 TLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFV 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 535 MKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVR 614
Cdd:TIGR02203 453 DKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE 532
|
490 500 510
....*....|....*....|....*....|....*....
gi 2024474312 615 NADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQASE 653
Cdd:TIGR02203 533 KADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
762-1291 |
4.99e-116 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 374.42 E-value: 4.99e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 762 KAAIRETNSTYALLF---LGFGLISFVTFFLqgftFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLAND 838
Cdd:TIGR02204 51 KDSSGLLNRYFAFLLvvaLVLALGTAARFYL----VTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 839 ASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAI 918
Cdd:TIGR02204 125 TTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 919 ENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHMRFKDV-LLVFSA 997
Cdd:TIGR02204 205 GAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgQFVFYA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 998 iVFGAMALGQSTSFTPDYAKAKMSAAHLFLLFERVPLIDSYSEEGEKPKMFGGNITFKDVAFKYPTRPEVKVLQGLNIEV 1077
Cdd:TIGR02204 285 -VMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1078 EKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGdnSREV 1157
Cdd:TIGR02204 364 RPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG--RPDA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1158 SHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDK 1237
Cdd:TIGR02204 442 TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALET 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1238 AREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVNVQ 1291
Cdd:TIGR02204 522 LMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
714-1291 |
5.43e-114 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 369.05 E-value: 5.43e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 714 SFFKIMKLNKTEWPYFVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKaaiRETNSTYALLFLGFGLISFVTFFLQGFT 793
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRD---RSVLWWVPLVVIGLAVLRGICSFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 794 FGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKG-ATGSRLALVAQNIANLGTGIVLsLIYGW 872
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASaATDAFIVLVRETLTVIGLFIVL-LYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 873 QLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQE----RKFEYMYGQNLqvsyRNS 948
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQayetRRFDAVSNRNR----RLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 949 IKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHMRFKDVLLVFSAIVFGAMALGQSTSFTPDYAKAKMSAAHLFLL 1028
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1029 FERVPLIDSYSEEGEKPKmfgGNITFKDVAFKYPTRpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLS 1108
Cdd:TIGR02203 311 LDSPPEKDTGTRAIERAR---GDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1109 GEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDnSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGD 1188
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1189 KGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKV 1268
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|...
gi 2024474312 1269 IEQGTHQQLLAEKGFYYSLVNVQ 1291
Cdd:TIGR02203 546 VERGTHNELLARNGLYAQLHNMQ 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
161-653 |
7.25e-114 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 368.96 E-value: 7.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 161 AGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDD------------ISKINEG---IGEKIAMFFQAvatfftgf 225
Cdd:PRK11176 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREGasiIGLFIMMFYYS-------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 226 ivgftkgWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDA 305
Cdd:PRK11176 165 -------WQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 306 KRMGIQKAISANISMGVSFFLiyGSYALAF--WYGTILVLSEDYTIGKvFTVFFSILVGAFSVGQAAPSMEA-FANARGA 382
Cdd:PRK11176 238 RQQGMKMVSASSISDPIIQLI--ASLALAFvlYAASFPSVMDTLTAGT-ITVVFSSMIALMRPLKSLTNVNAqFQRGMAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 383 AYAIFNIIDNEPQIDSSSnagYKLDHVKGNLEFQNVFFSYPARpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQ 462
Cdd:PRK11176 315 CQTLFAILDLEQEKDEGK---RVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 463 RFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDV-TMEEIERATKEANAYDFIMKLPKKF 541
Cdd:PRK11176 391 RFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 542 ETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAA 621
Cdd:PRK11176 471 DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILV 550
|
490 500 510
....*....|....*....|....*....|..
gi 2024474312 622 FENGVITEQGTHDELMEQKGVYYKLVNMQASE 653
Cdd:PRK11176 551 VEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
413-646 |
3.17e-112 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 351.15 E-value: 3.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKI 572
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 573 LLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKL 646
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
729-1025 |
5.42e-111 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 351.19 E-value: 5.42e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAAIRETNS-----------------TYALLFLGFGLISFVTFFLQG 791
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSglnssagpfekleeemtLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 792 FTFGKAGEILTMRLRSMAFRAILRQEISWFdePKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYG 871
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 872 WQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKK 951
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 952 AHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHMR-FKDVLLVFSAIVFGAMALGQSTSFTPdYAKAKMSAAHL 1025
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1052-1287 |
1.24e-110 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 346.91 E-value: 1.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEvKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFDCTIAENIAYGDnsREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQP 1211
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSL 1287
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
413-650 |
4.28e-107 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 337.28 E-value: 4.28e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKI 572
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 573 LLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQ 650
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1049-1292 |
1.84e-106 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 349.50 E-value: 1.84e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1049 GGNITFKDVAFKY-PTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLR 1127
Cdd:COG5265 355 GGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 AQIGIVSQEPILFDCTIAENIAYGDNsrEVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARAL 1207
Cdd:COG5265 432 AAIGIVPQDTVLFNDTIAYNIAYGRP--DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1208 IRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSL 1287
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
....*
gi 2024474312 1288 VNVQS 1292
Cdd:COG5265 590 WARQQ 594
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1052-1291 |
4.70e-105 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 331.89 E-value: 4.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFDCTIAENIAYGDNSreVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQP 1211
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVNVQ 1291
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
411-641 |
2.62e-102 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 324.18 E-value: 2.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 411 GNLEFQNVFFSYpaRPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI 490
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNP 570
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 571 KILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKG 641
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
726-1293 |
3.69e-101 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 334.29 E-value: 3.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 726 WPY-------FVVGTLCAIINGALQpifSVMISDVIGMFVEKGKAAIRETNSTYALLFLGF----GLISFVTFFLQGFTF 794
Cdd:PRK11176 17 WPTiapfkagLIVAGVALILNAASD---TFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLmilrGITSFISSYCISWVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 795 GKageiLTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQL 874
Cdd:PRK11176 94 GK----VVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 875 TLLLLAIVPIIAITgmiqMKMLAGHAKKDKKELE-TLGKVASEAIENIR--TVVAL-----TQERKFEY----MYGQNLQ 942
Cdd:PRK11176 168 SLILIVIAPIVSIA----IRVVSKRFRNISKNMQnTMGQVTTSAEQMLKghKEVLIfggqeVETKRFDKvsnrMRQQGMK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 943 VSYRNSIKKAHIfgftfaftQAIMYFTYAgcfrFGAYLVKnghmrFKDVLLVFSA----IVFGAM-----ALGQSTSFTP 1013
Cdd:PRK11176 244 MVSASSISDPII--------QLIASLALA----FVLYAAS-----FPSVMDTLTAgtitVVFSSMialmrPLKSLTNVNA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1014 DYAKAKMSAAHLFLLFERVPLIDSYSEEGEKPKmfgGNITFKDVAFKYPTRpEVKVLQGLNIEVEKGQTLALVGSSGCGK 1093
Cdd:PRK11176 307 QFQRGMAACQTLFAILDLEQEKDEGKRVIERAK---GDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1094 STVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNSReVSHEEIVSAAKAANIHS 1173
Cdd:PRK11176 383 STIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQ-YSREQIEEAARMAYAMD 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1174 FIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLST 1253
Cdd:PRK11176 462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLST 541
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2024474312 1254 IQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVNVQSG 1293
Cdd:PRK11176 542 IEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
314-656 |
3.79e-101 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 334.62 E-value: 3.79e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 314 ISANISMgVSFFLIygsyalafwyGTILVLSEDYTIGKV--FTVFFSILVG------AF--SVGQAAPSMEAFanargaa 383
Cdd:PRK13657 248 AASTITM-LAILVL----------GAALVQKGQLRVGEVvaFVGFATLLIGrldqvvAFinQVFMAAPKLEEF------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 384 yaiFNIIDNEPQIDSSSNAGyKLDHVKGNLEFQNVFFSYPARPdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQR 463
Cdd:PRK13657 310 ---FEVEDAVPDVRDPPGAI-DLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQR 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 464 FYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFET 543
Cdd:PRK13657 384 VFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDT 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 544 VVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFE 623
Cdd:PRK13657 464 VVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFD 543
|
330 340 350
....*....|....*....|....*....|...
gi 2024474312 624 NGVITEQGTHDELMEQKGVYYKLVNMQASETED 656
Cdd:PRK13657 544 NGRVVESGSFDELVARGGRFAALLRAQGMLQED 576
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1050-1282 |
3.73e-99 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 315.70 E-value: 3.73e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1050 GNITFKDVAFKYptRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQ 1129
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 IGIVSQEPILFDCTIAENIAYGDNsrEVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIR 1209
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRP--NATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1210 QPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKG 1282
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
160-641 |
2.22e-97 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 323.25 E-value: 2.22e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 160 AAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDIskinegigEKIAMFF--------QAVATFFTGFIVGFTK 231
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV--------EALDGYFarylpqlfLAALVPLLILVAVFPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 232 GWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDAKRmgiq 311
Cdd:COG4988 157 DWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRK---- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 312 kaisanISMGV-------SF---FLIYGSYALAFWYGTILVLSEDYTIGKVFTV------FFSIL--VGAFsvgqaapsM 373
Cdd:COG4988 233 ------RTMKVlrvaflsSAvleFFASLSIALVAVYIGFRLLGGSLTLFAALFVlllapeFFLPLrdLGSF--------Y 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 374 EAFANARGAAYAIFNIIDNEPQIDSSSNAGYKLDHvKGNLEFQNVFFSYPARPdiKILKGLNLKVNCGQTVALVGGSGCG 453
Cdd:COG4988 299 HARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 454 KSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDF 533
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEF 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 534 IMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTV 613
Cdd:COG4988 456 VAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL 535
|
490 500
....*....|....*....|....*...
gi 2024474312 614 RNADLIAAFENGVITEQGTHDELMEQKG 641
Cdd:COG4988 536 AQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
718-1282 |
5.19e-93 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 310.92 E-value: 5.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 718 IMKLNKTEWPYFVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAaiRETNSTYALLFLGFGLISFVTFFLQGFTFGKA 797
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAP--LSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 798 GEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLAndaSQVKGATG------SRLALVAqnIANLGTGIVLSLIYg 871
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLR--GKSTGELATLLT---EGVEALDGyfarylPQLFLAA--LVPLLILVAVFPLD- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 872 WQLTLLLLAIVPIIAItGMIQMKMLAghAKKDKKELETLGKVASEAIENIR---TVVALTQERKfeymygqnlqvsYRNS 948
Cdd:COG4988 158 WLSGLILLVTAPLIPL-FMILVGKGA--AKASRRQWRALARLSGHFLDRLRgltTLKLFGRAKA------------EAER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 949 IKKAhifgfTFAFTQAIM--------------YFTYAG--------CFRFGaylvkNGHMRFKDVLLVF--SAIVFGAM- 1003
Cdd:COG4988 223 IAEA-----SEDFRKRTMkvlrvaflssavleFFASLSialvavyiGFRLL-----GGSLTLFAALFVLllAPEFFLPLr 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1004 ALGQstsftpDY---AKAKMSAAHLFLLFERvPLIDSYSEEGEKPKMFGGNITFKDVAFKYPTRPEVkvLQGLNIEVEKG 1080
Cdd:COG4988 293 DLGS------FYharANGIAAAEKIFALLDA-PEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1081 QTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDnsREVSHE 1160
Cdd:COG4988 364 ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1161 EIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKARE 1240
Cdd:COG4988 442 ELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK 521
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2024474312 1241 GRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKG 1282
Cdd:COG4988 522 GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
801-1287 |
3.22e-90 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 303.61 E-value: 3.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 801 LTMRLRSMAFRAILRQEISWFdePKNSTGELITRLANDASQVKGATgsrLALVAQNIANLGTGIVLSLIYGWQLTLLLLA 880
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 881 IVPIIAITGMIqMKMLAGHA--KKDKKELETLGKVASEAIENIRTVVALT----QERKFEYMygQNLQVSYRNSIKKAHI 954
Cdd:COG4987 161 LALGLLLAGLL-LPLLAARLgrRAGRRLAAARAALRARLTDLLQGAAELAaygaLDRALARL--DAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 955 F-GFTFAFTQAIMYFTYAGCFRFGAYLVKNGHMrfKDVLLVfsAIVFGAMALGQSTSFTPD----YAKAKMSAAHLFLLF 1029
Cdd:COG4987 238 LsALAQALLQLAAGLAVVAVLWLAAPLVAAGAL--SGPLLA--LLVLAALALFEALAPLPAaaqhLGRVRAAARRLNELL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1030 ERVPLIDSYSEEGEKPKmfGGNITFKDVAFKYPTRPEvKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSG 1109
Cdd:COG4987 314 DAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1110 EVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNsrEVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDK 1189
Cdd:COG4987 391 SITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEG 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1190 GAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVI 1269
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
490
....*....|....*...
gi 2024474312 1270 EQGTHQQLLAEKGFYYSL 1287
Cdd:COG4987 549 EQGTHEELLAQNGRYRQL 566
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
217-646 |
3.70e-90 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 303.23 E-value: 3.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 217 AVATFFTGFIVgftkgWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAyAKAGAVAE--EVLAAVRTVVAFGGQRKE 294
Cdd:COG4987 144 LAAVAFLAFFS-----PALALVLALGLLLAGLLLPLLAARLGRRAGRRLAA-ARAALRARltDLLQGAAELAAYGALDRA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 295 TERY---QKNLEDA-KRMGIQKAISANISMGVSFFLIygsyALAFWYGTILVLSedytiGKVFTVFFSILV-GAFSVGQA 369
Cdd:COG4987 218 LARLdaaEARLAAAqRRLARLSALAQALLQLAAGLAV----VAVLWLAAPLVAA-----GALSGPLLALLVlAALALFEA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 370 -APSMEAFAN---ARGAAYAIFNIIDNEPQIDSSSNAGYKLDHVkgNLEFQNVFFSYPARPDIkILKGLNLKVNCGQTVA 445
Cdd:COG4987 289 lAPLPAAAQHlgrVRAAARRLNELLDAPPAVTEPAEPAPAPGGP--SLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 446 LVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERAT 525
Cdd:COG4987 366 IVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 526 KEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILV 605
Cdd:COG4987 446 ERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLL 525
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2024474312 606 IAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKL 646
Cdd:COG4987 526 ITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
413-650 |
4.18e-88 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 285.53 E-value: 4.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYpaRPDIK-ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREII 491
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPK 571
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 572 ILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQ 650
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1052-1291 |
1.46e-86 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 281.30 E-value: 1.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKY-PTRPEVkvLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQI 1130
Cdd:cd03252 1 ITFEHVRFRYkPDGPVI--LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEPILFDCTIAENIAYGDNSreVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQ 1210
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1211 PRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVNV 1290
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 2024474312 1291 Q 1291
Cdd:cd03252 237 Q 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1045-1268 |
3.32e-86 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 279.74 E-value: 3.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1045 PKMFGGNITFKDVAFKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQ 1124
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1125 WLRAQIGIVSQEPILFDCTIAENIAYGDNSreVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIA 1204
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1205 RALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKV 1268
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
407-627 |
8.37e-86 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 278.59 E-value: 8.37e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 407 DHVKGNLEFQNVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRY 486
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 487 LREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARAL 566
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 567 VRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVI 627
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
222-650 |
1.34e-84 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 291.65 E-value: 1.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 222 FTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKN 301
Cdd:TIGR01846 267 VVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 302 LEDAKRMGIQKAISANI-SMGVSffLIYG-SYALAFWYGTILVLSEDYTIGKVftVFFSILVGAFS--VGQAAPSMEAFA 377
Cdd:TIGR01846 347 LAAYVAASFRVTNLGNIaGQAIE--LIQKlTFAILLWFGAHLVIGGALSPGQL--VAFNMLAGRVTqpVLRLAQLWQDFQ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 378 NARGAAYAIFNIIdNEPqIDSSSNAGYKLDHVKGNLEFQNVFFSYpaRPDI-KILKGLNLKVNCGQTVALVGGSGCGKST 456
Cdd:TIGR01846 423 QTGIALERLGDIL-NSP-TEPRSAGLAALPELRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKST 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 457 TVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMK 536
Cdd:TIGR01846 499 LTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 537 LPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNA 616
Cdd:TIGR01846 579 LPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRAC 658
|
410 420 430
....*....|....*....|....*....|....
gi 2024474312 617 DLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQ 650
Cdd:TIGR01846 659 DRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
851-1291 |
3.02e-84 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 287.24 E-value: 3.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 851 ALVAqnianLGTGIVLSLIYGWQLTLLLLAIVPI-IAITGMIQMKMLAGHAKKDKKElETLGKVASEAIENIRTV----- 924
Cdd:PRK13657 140 TLVA-----LVVLLPLALFMNWRLSLVLVVLGIVyTLITTLVMRKTKDGQAAVEEHY-HDLFAHVSDAIGNVSVVqsynr 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 925 -VALTQERKFeymygqnlqvsYRNSIKKAHI-----FGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHMRFKDVLlvfSAI 998
Cdd:PRK13657 214 iEAETQALRD-----------IADNLLAAQMpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVV---AFV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 999 VFGAMALG---QSTSFTpdyAKAKMSAAHLFLLFErvpLIDSYSEEGEKPKM-----FGGNITFKDVAFKYP-TRPEVKv 1069
Cdd:PRK13657 280 GFATLLIGrldQVVAFI---NQVFMAAPKLEEFFE---VEDAVPDVRDPPGAidlgrVKGAVEFDDVSFSYDnSRQGVE- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 lqGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIA 1149
Cdd:PRK13657 353 --DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1150 YGdnsRE-VSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESE 1228
Cdd:PRK13657 431 VG---RPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1229 KIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVNVQ 1291
Cdd:PRK13657 508 AKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
727-1288 |
8.76e-82 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 283.76 E-value: 8.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 727 PYFVVGTLCAIINGALQPIFS-VMISDVIgmfvekgkaaIRETNSTYALLFLGFGLISFVTFFLQGF--TFGKAGEI-LT 802
Cdd:TIGR03796 157 LYLLLAGLLLVLPGLVIPAFSqIFVDEIL----------VQGRQDWLRPLLLGMGLTALLQGVLTWLqlYYLRRLEIkLA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 803 MRLRSMAFRAILRQEISWFDEpkNSTGELITRL-ANDasQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAI 881
Cdd:TIGR03796 227 VGMSARFLWHILRLPVRFFAQ--RHAGDIASRVqLND--QVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 882 VPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQE----RKFEYMYG------QNLQVSyrnsikk 951
Cdd:TIGR03796 303 AAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLEsdffSRWAGYQAkllnaqQELGVL------- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 952 AHIFGftfAFTQAIMYFTYAGCFRFGAYLVKNGHMR------FKDVLLVFSAIVFGAMALGQS-TSFTPDYAKAK--MSA 1022
Cdd:TIGR03796 376 TQILG---VLPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTlQELEGDLNRLDdvLRN 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1023 AhLFLLFERVPLIDSYSEEGEKpkmFGGNITFKDVAFKYpTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLER 1102
Cdd:TIGR03796 453 P-VDPLLEEPEGSAATSEPPRR---LSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAG 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1103 FYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNSreVSHEEIVSAAKAANIHSFIESLPKKY 1182
Cdd:TIGR03796 528 LYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGY 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1183 NTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALdkAREGRTCIVIAHRLSTIQNADKIAV 1262
Cdd:TIGR03796 606 DAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIV 683
|
570 580
....*....|....*....|....*.
gi 2024474312 1263 IQNGKVIEQGTHQQLLAEKGFYYSLV 1288
Cdd:TIGR03796 684 LERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
729-1025 |
1.68e-81 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 269.34 E-value: 1.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVIGMFV-----EKGKAAIRETNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTM 803
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 804 RLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVP 883
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 884 IIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQ 963
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 964 AIMYFTYAGCFRFGAYLVKNGHMRFKDVLLVFSAIVFGAMALGQSTSFTPDYAKAKMSAAHL 1025
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1052-1267 |
1.81e-81 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 264.25 E-value: 1.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEvKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFDCTIAENIaygdnsrevsheeivsaakaanihsfieslpkkyntrvgdkgaqLSGGQKQRIAIARALIRQP 1211
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGK 1267
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
413-625 |
1.77e-80 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 261.16 E-value: 1.77e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFATTIAENIrygredvtmeeieratkeanaydfimklpkkfetvvgergaqMSGGQKQRIAIARALVRNPKI 572
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 573 LLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENG 625
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
769-1293 |
4.14e-80 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 278.55 E-value: 4.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 769 NSTYALLFLGFGLISFVTF-----FLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVK 843
Cdd:TIGR01846 173 RGLSTLSVLALAMLAVAIFepalgGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFE--SRRVGDTVARVRELEQIRN 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 844 GATGSRLALVAQNIANLgTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAghaKKDKKELETLGKVAS---EAIEN 920
Cdd:TIGR01846 251 FLTGSALTVVLDLLFVV-VFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILR---KRVEDKFERSAAATSflvESVTG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 921 IRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHMRFKDvLLVFSaivf 1000
Cdd:TIGR01846 327 IETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ-LVAFN---- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1001 gaMALGQSTSFTPDYAKAKMSAAHLFLLFERV-PLIDSYSEEGEK-----PKMFGGnITFKDVAFKY-PTRPEVkvLQGL 1073
Cdd:TIGR01846 402 --MLAGRVTQPVLRLAQLWQDFQQTGIALERLgDILNSPTEPRSAglaalPELRGA-ITFENIRFRYaPDSPEV--LSNL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1074 NIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDN 1153
Cdd:TIGR01846 477 NLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNP 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1154 SreVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQE 1233
Cdd:TIGR01846 557 G--APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMR 634
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1234 ALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVNVQSG 1293
Cdd:TIGR01846 635 NMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
59-396 |
1.66e-78 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 261.62 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 59 RQDKLLMVLGTTMAVLHGASLPLMMIVFGDMTDTFIASENttypanfsllnstsvnfsmeffsylilGELEEEMTRYAYY 138
Cdd:cd18578 5 KPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDD---------------------------DELRSEANFWALM 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 139 YSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFD--VNDVCELNTRIVDDISKINEGIGEKIAMFFQ 216
Cdd:cd18578 58 FLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 217 AVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETE 296
Cdd:cd18578 138 AIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 297 RYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVFTVFFSILVGAFSVGQAAPSMEAF 376
Cdd:cd18578 218 KYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDI 297
|
330 340
....*....|....*....|
gi 2024474312 377 ANARGAAYAIFNIIDNEPQI 396
Cdd:cd18578 298 AKAKAAAARIFRLLDRKPEI 317
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
338-660 |
2.09e-75 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 262.13 E-value: 2.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 338 GTILVLSEDYTIGKV--FTVFFSILVGAFSvgqaapSMEAFAN----ARGAAYAIFNIIDNEPQIDSSSNAGyKLDHVKG 411
Cdd:TIGR01192 261 GTVLVIKGELSVGEViaFIGFANLLIGRLD------QMSGFITqifeARAKLEDFFDLEDSVFQREEPADAP-ELPNVKG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 412 NLEFQNVFFSYPARPdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREII 491
Cdd:TIGR01192 334 AVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSI 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPK 571
Cdd:TIGR01192 412 ATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAP 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 572 ILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQA 651
Cdd:TIGR01192 492 ILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSG 571
|
....*....
gi 2024474312 652 SETEDQLQE 660
Cdd:TIGR01192 572 LLTNQPATK 580
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
827-1291 |
9.65e-74 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 260.27 E-value: 9.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 827 STGELITRlANDASQVkgatgsRLALVAQNIANLGTGI------VLSLIYGWQLTL----LLLAIVPIIAITGMIQMKml 896
Cdd:TIGR03797 231 STGDLASR-AMGISQI------RRILSGSTLTTLLSGIfallnlGLMFYYSWKLALvavaLALVAIAVTLVLGLLQVR-- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 897 aghakKDKKELETLGKVASEAIENIRTV----VALTQERKFeYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAG 972
Cdd:TIGR03797 302 -----KERRLLELSGKISGLTVQLINGIsklrVAGAENRAF-ARWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 973 CFRFGAYLVKNGHMRFKDVLLVFSAIV-FGAMALGQSTSFTpdyakakmSAAHLFLLFERV-PLIDS---YSEEGEKPKM 1047
Cdd:TIGR03797 376 LFAAAISLLGGAGLSLGSFLAFNTAFGsFSGAVTQLSNTLI--------SILAVIPLWERAkPILEAlpeVDEAKTDPGK 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1048 FGGNITFKDVAFKYptRPE-VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWL 1126
Cdd:TIGR03797 448 LSGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1127 RAQIGIVSQEPILFDCTIAENIAyGDNSreVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARA 1206
Cdd:TIGR03797 526 RRQLGVVLQNGRLMSGSIFENIA-GGAP--LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1207 LIRQPRILLLDEATSALDTESEKIVQEALDKAREGRtcIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYS 1286
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQ 680
|
....*
gi 2024474312 1287 LVNVQ 1291
Cdd:TIGR03797 681 LARRQ 685
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
65-364 |
1.28e-73 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 246.40 E-value: 1.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 65 MVLGTTMAVLHGASLPLMMIVFGDMTDTFIasenttypanfsllnstsVNFSMEFFsylilgeleeEMTRYAYYYSGIGA 144
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLL------------------PDGDPETQ----------ALNVYSLALLLLGL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 145 GVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTG 224
Cdd:pfam00664 53 AQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 225 FIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLED 304
Cdd:pfam00664 133 IIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEE 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 305 AKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGK--VFTVFFSILVGAF 364
Cdd:pfam00664 213 ALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
699-1291 |
5.12e-73 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 268.05 E-value: 5.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 699 LDVKaDQLDKNMPPSSFFKIMKLNKTE-WPYFV--------------VGTLCAIINGALQPIFsvmISdVIGMFVEKGKA 763
Cdd:PTZ00265 18 LSIK-DEVEKELNKKGTFELYKKIKTQkIPFFLpfkclpashrkllgVSFVCATISGGTLPFF---VS-VFGVIMKNMNL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 764 AIRETNSTYALLFLGfgLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVK 843
Cdd:PTZ00265 93 GENVNDIIFSLVLIG--IFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHD--NNPGSKLTSDLDFYLEQVN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 844 GATGSR-LALVAQNIANLGTGIvLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIR 922
Cdd:PTZ00265 169 AGIGTKfITIFTYASAFLGLYI-WSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 923 TVVALTQE----RKF---EYMYGQ-NLQVSYRNSIKKAHIFGFTFAftqaimyfTYAGCFRFGAYLV--------KNGHM 986
Cdd:PTZ00265 248 TVVSYCGEktilKKFnlsEKLYSKyILKANFMESLHIGMINGFILA--------SYAFGFWYGTRIIisdlsnqqPNNDF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 987 RFKDVLLVFSAIVFGAMALGQSTSFTPDYAKAKMSAAHLFLLFERVPLIDSySEEGEKPKMFGgNITFKDVAFKYPTRPE 1066
Cdd:PTZ00265 320 HGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1067 VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLL-DGRNTKTLNIQWLRAQIGIVSQEPILFDCTIA 1145
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1146 ENIAY------------------------GDNSRE-------------------------------VSHEEIVSAAKAAN 1170
Cdd:PTZ00265 478 NNIKYslyslkdlealsnyynedgndsqeNKNKRNscrakcagdlndmsnttdsneliemrknyqtIKDSEVVDVSKKVL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1171 IHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIA 1248
Cdd:PTZ00265 558 IHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIA 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1249 HRLSTIQNADKIAVIQNGK-----------------------------------------------VIEQGTHQQLLAEK 1281
Cdd:PTZ00265 638 HRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNK 717
|
730
....*....|.
gi 2024474312 1282 -GFYYSLVNVQ 1291
Cdd:PTZ00265 718 nGIYYTMINNQ 728
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
172-647 |
5.28e-72 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 255.64 E-value: 5.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 172 FFHAVMRQEIGWFDVNDVCELNTRiVDDISKINEGIGEKIA-MFFQAVATFFTgFIVGFTKGWKLTLVILALSPVLGFSS 250
Cdd:TIGR03796 233 FLWHILRLPVRFFAQRHAGDIASR-VQLNDQVAEFLSGQLAtTALDAVMLVFY-ALLMLLYDPVLTLIGIAFAAINVLAL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 251 ALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQ----RKETERYQKNLEDAKRMGIQKAISANISMGVSFFl 326
Cdd:TIGR03796 311 QLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLEsdffSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSL- 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 327 iygSYALAFWYGTILVLSEDYTIGKVftVFFSILVGAFS--------VGQAAPSMEAFANaR---GAAYAIFNIIDNEPQ 395
Cdd:TIGR03796 390 ---NSALILVVGGLRVMEGQLTIGML--VAFQSLMSSFLepvnnlvgFGGTLQELEGDLN-RlddVLRNPVDPLLEEPEG 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 396 IDSSSNAGYKLdhvKGNLEFQNVFFSYpARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITID 475
Cdd:TIGR03796 464 SAATSEPPRRL---SGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFD 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 476 GQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGG 555
Cdd:TIGR03796 540 GIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 556 QKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDkiRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDE 635
Cdd:TIGR03796 620 QRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEE 697
|
490
....*....|..
gi 2024474312 636 LMEQKGVYYKLV 647
Cdd:TIGR03796 698 LWAVGGAYARLI 709
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
416-1287 |
3.51e-71 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 262.57 E-value: 3.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 416 QNVFFSYpARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGqdlkslNVRYlreiigvVN 495
Cdd:TIGR00957 640 HNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------SVAY-------VP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 QEPVLFATTIAENIRYGREdvTMEEIERATKEANAY--DFIMkLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKIL 573
Cdd:TIGR00957 706 QQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 574 LLDEATSALDTEsesVVQAALDKI------RKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLV 647
Cdd:TIGR00957 783 LFDDPLSAVDAH---VGKHIFEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 648 NMQASETEDQLQEEGNASSVS---EEAL---NGSVLTgqkrQSTRKSIKR--VRIQNDELDV-----KADQLDKNMPPSS 714
Cdd:TIGR00957 860 RTYAPDEQQGHLEDSWTALVSgegKEAKlieNGMLVT----DVVGKQLQRqlSASSSDSGDQsrhhgSSAELQKAEAKEE 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 715 FFKIMKLNKTE---------WPYFVVGTLC---AIINGALQPIFSVMISDV-IGMFVEKGKAAIRETNSTYAL-LFLGFG 780
Cdd:TIGR00957 936 TWKLMEADKAQtgqvelsvyWDYMKAIGLFitfLSIFLFVCNHVSALASNYwLSLWTDDPMVNGTQNNTSLRLsVYGALG 1015
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 781 LISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIAN- 859
Cdd:TIGR00957 1016 ILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNv 1093
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 860 LGTGIVLSLIygwqlTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKeLETLGKVA-----SEAIENIRTVVALTQERKFE 934
Cdd:TIGR00957 1094 IGALIVILLA-----TPIAAVIIPPLGLLYFFVQRFYVASSRQLKR-LESVSRSPvyshfNETLLGVSVIRAFEEQERFI 1167
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 935 YMygQNLQVsyrNSIKKAhifgftfaftqaimYFTYAGCFRF---GAYLVKNGHMRFKDVLLVFSAIVFGAMALGQSTSF 1011
Cdd:TIGR00957 1168 HQ--SDLKV---DENQKA--------------YYPSIVANRWlavRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSY 1228
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1012 TPDYAKA-----KMSA--AHLFLLFERVpliDSYSE-EGEKPKMF-----------GGNITFKDVAFKYptRPEVK-VLQ 1071
Cdd:TIGR00957 1229 SLQVTFYlnwlvRMSSemETNIVAVERL---KEYSEtEKEAPWQIqetappsgwppRGRVEFRNYCLRY--REDLDlVLR 1303
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1072 GLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIayg 1151
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL--- 1380
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1152 DNSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIV 1231
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1232 QEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSL 1287
Cdd:TIGR00957 1461 QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
781-1284 |
5.70e-69 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 243.08 E-value: 5.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 781 LISFVTFFLQGF----TFGkAGEILTMRLRSMAFRAILRQEISWFdePKNSTGELITRLANDASQVKGATGSR-LALVAQ 855
Cdd:PRK10789 44 LIAVVVYLLRYVwrvlLFG-ASYQLAVELREDFYRQLSRQHPEFY--LRHRTGDLMARATNDVDRVVFAAGEGvLTLVDS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 856 NIANLGTGIVLSLIYGWQLTLLLLAIVPIIAItgMIQMKMLAGHA--KKDKKELETLGKVASEAIENIRTVVALTQERKF 933
Cdd:PRK10789 121 LVMGCAVLIVMSTQISWQLTLLALLPMPVMAI--MIKRYGDQLHErfKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 934 EYMYGQNLQVSYRNSIKKAHI---FGFTFAFTQAIMYFTYAGCfrfGAYLVKNGhmrfkdvllvfsaivfgAMALGQSTS 1010
Cdd:PRK10789 199 SALFAADAEDTGKKNMRVARIdarFDPTIYIAIGMANLLAIGG---GSWMVVNG-----------------SLTLGQLTS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1011 FT--------PDYAKAKM-------SAAH--LFLLFERVPLIDsyseEGEKPKMFG-GNITFKDVAFKYPTRpEVKVLQG 1072
Cdd:PRK10789 259 FVmylglmiwPMLALAWMfnivergSAAYsrIRAMLAEAPVVK----DGSEPVPEGrGELDVNIRQFTYPQT-DHPALEN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1073 LNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGd 1152
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALG- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1153 nSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQ 1232
Cdd:PRK10789 413 -RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQIL 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1233 EALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFY 1284
Cdd:PRK10789 492 HNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
748-1291 |
1.21e-68 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 242.70 E-value: 1.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 748 VMISDVIGMFVEKGKAAIRETnSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFD-EPkn 826
Cdd:PRK10790 44 LLISYFIDNMVAKGNLPLGLV-AGLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDtQP-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 827 sTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKE 906
Cdd:PRK10790 121 -VGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 907 LETLGKVASEAIENIRTVVALTQERKFeymyGQNLQVSYRnsikkAHifgftfaftqaimYFTYAGCFRFGAYLVKnghm 986
Cdd:PRK10790 200 LADINDGFNEVINGMSVIQQFRQQARF----GERMGEASR-----SH-------------YMARMQTLRLDGFLLR---- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 987 rfkDVLLVFSAIVF-GAMAL-GQSTSFTPDYAKAKMSAAHLFLLFErvPLIDSYSEE---------GEK-------PK-- 1046
Cdd:PRK10790 254 ---PLLSLFSALILcGLLMLfGFSASGTIEVGVLYAFISYLGRLNE--PLIELTTQQsmlqqavvaGERvfelmdgPRqq 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1047 -------MFGGNITFKDVAFKYptRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTK 1119
Cdd:PRK10790 329 ygnddrpLQSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1120 TLNIQWLRAQIGIVSQEPILFDCTIAENIAYGdnsREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQ 1199
Cdd:PRK10790 407 SLSHSVLRQGVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1200 RIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA 563
|
570
....*....|..
gi 2024474312 1280 EKGFYYSLVNVQ 1291
Cdd:PRK10790 564 AQGRYWQMYQLQ 575
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1050-1273 |
1.43e-67 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 226.99 E-value: 1.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1050 GNITFKDVAFKYptRPEVK-VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRA 1128
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALI 1208
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1209 RQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGT 1273
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1050-1272 |
2.05e-67 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 226.32 E-value: 2.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1050 GNITFKDVAFKYPTRpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQ 1129
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 IGIVSQEPILFDCTIAENIAYGDnsREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIR 1209
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1210 QPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQG 1272
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
337-1294 |
6.50e-66 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 246.04 E-value: 6.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 337 YGTILVLSEDYTIGKVFTVFFSILVGAFSVGQAAPSMEAFANARGAAYAIFNIIDNEPQIDSSSNAgykLDHVKGNLEFQ 416
Cdd:PLN03232 542 FGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPP---LQPGAPAISIK 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 417 NVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIdgqdlkslnvryLREIIGVVNQ 496
Cdd:PLN03232 619 NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQ 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 497 EPVLFATTIAENIRYGrEDVTMEEIERATK-EANAYDFIMkLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLL 575
Cdd:PLN03232 687 VSWIFNATVRENILFG-SDFESERYWRAIDvTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIF 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 576 DEATSALDTE-SESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNmQASET 654
Cdd:PLN03232 765 DDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME-NAGKM 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 655 EDQLQEEGNASSVSEEALNGSVLTGQKRQSTRKSIKRVRiqndelDVKADQLDKNMPPSSFFKIMKLNKTEWPYFVVGTL 734
Cdd:PLN03232 844 DATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKRGR------SVLVKQEERETGIISWNVLMRYNKAVGGLWVVMIL 917
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 735 CAIIngALQPIFSVMISDVIGMFVEKGKAAIRETN---STYALLflGFGLISfVTFfLQGFTFGKAGEILTMRLRSMAFR 811
Cdd:PLN03232 918 LVCY--LTTEVLRVSSSTWLSIWTDQSTPKSYSPGfyiVVYALL--GFGQVA-VTF-TNSFWLISSSLHAAKRLHDAMLN 991
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 812 AILRQEISWFDepKNSTGELITRLANDASQVKgatgsrlalvaQNIANLGTGIVLSLiygWQL--TLLLLAIVPIIAITG 889
Cdd:PLN03232 992 SILRAPMLFFH--TNPTGRVINRFSKDIGDID-----------RNVANLMNMFMNQL---WQLlsTFALIGTVSTISLWA 1055
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 890 MIQMKMLAGHA----KKDKKELETLGKVASEAI-----ENIRTVVALTQERKFEYMYGQNLQvSYRNSIKkahifgFTFA 960
Cdd:PLN03232 1056 IMPLLILFYAAylyyQSTSREVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMAKINGK-SMDNNIR------FTLA 1128
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 961 FTQ-----AIMYFTYAG-------CFRFGAYLVKNGHMRFKDVL-LVFSAIVfgamalgQSTSFTPDYAKAKMSAAHLFL 1027
Cdd:PLN03232 1129 NTSsnrwlTIRLETLGGvmiwltaTFAVLRNGNAENQAGFASTMgLLLSYTL-------NITTLLSGVLRQASKAENSLN 1201
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1028 LFERVP-LIDSYSE-----EGEKPKM---FGGNITFKDVAFKYptRPEVK-VLQGLNIEVEKGQTLALVGSSGCGKSTVV 1097
Cdd:PLN03232 1202 SVERVGnYIDLPSEataiiENNRPVSgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSML 1279
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1098 QLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVSAAKAANIHSFIES 1177
Cdd:PLN03232 1280 NALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDR 1356
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1178 LPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNA 1257
Cdd:PLN03232 1357 NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC 1436
|
970 980 990
....*....|....*....|....*....|....*..
gi 2024474312 1258 DKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVNVQSGP 1294
Cdd:PLN03232 1437 DKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGP 1473
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
142-665 |
1.67e-65 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 233.07 E-value: 1.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 142 IGAGVLFAA--YIQVSFWTL----AAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFF 215
Cdd:PRK10789 39 IGTMVLIAVvvYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 216 QAVATFFTGFIVGFTK-GWKLTLVILALSPVLgfssalwAKIISTFTNKELTAYAKAGAV-------AEEVLAAVRTVVA 287
Cdd:PRK10789 119 DSLVMGCAVLIVMSTQiSWQLTLLALLPMPVM-------AIMIKRYGDQLHERFKLAQAAfsslndrTQESLTSIRMIKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 288 FGGQRKETERYQKNLEDAKRMGIQKA-ISAN------ISMGVSFFLIYGSyalafwyGTILVLSEDYTIGKVfTVFFSIL 360
Cdd:PRK10789 192 FGLEDRQSALFAADAEDTGKKNMRVArIDARfdptiyIAIGMANLLAIGG-------GSWMVVNGSLTLGQL-TSFVMYL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 361 vgafsvGQAAPSMEAFA---N--ARG-AAYA-IFNIIDNEPQIDSSSNAgykLDHVKGNLEFQNVFFSYPARpDIKILKG 433
Cdd:PRK10789 264 ------GLMIWPMLALAwmfNivERGsAAYSrIRAMLAEAPVVKDGSEP---VPEGRGELDVNIRQFTYPQT-DHPALEN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 434 LNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGR 513
Cdd:PRK10789 334 VNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 514 EDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAA 593
Cdd:PRK10789 414 PDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 594 LDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVY---YKLVNMQASETEDQLQEEGNAS 665
Cdd:PRK10789 494 LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYrdmYRYQQLEAALDDAPEIREEAVD 568
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
977-1280 |
4.68e-65 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 231.56 E-value: 4.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 977 GAYLVKNGHMrfkdvllvfSAivfGAM----------------ALGQSTSFTpdyaKAKMSAAHLFLLFERVPlidsysE 1040
Cdd:COG4618 260 GAYLVIQGEI---------TP---GAMiaasilmgralapieqAIGGWKQFV----SARQAYRRLNELLAAVP------A 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1041 EGE-----KPKmfgGNITFKDVAFKYPTRPEVkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDG 1115
Cdd:COG4618 318 EPErmplpRPK---GRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1116 RNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAygdnsR--EVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQL 1193
Cdd:COG4618 394 ADLSQWDREELGRHIGYLPQDVELFDGTIAENIA-----RfgDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1194 SGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVIQNGKVIEQG 1272
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548
|
....*...
gi 2024474312 1273 THQQLLAE 1280
Cdd:COG4618 549 PRDEVLAR 556
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
729-1003 |
4.88e-65 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 221.75 E-value: 4.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAAIRETNStYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSM 808
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNV-YSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 809 AFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAIT 888
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 889 GMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYF 968
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 2024474312 969 TYAGCFRFGAYLVKNGHMRFKD--VLLVFSAIVFGAM 1003
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
348-650 |
6.24e-65 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 234.47 E-value: 6.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 348 TIGKVFTVFFSILV---------------GAF-----SVGQAAPSMEAFANARGAAYAIF-------NIIDNEPQIDSSS 400
Cdd:TIGR03797 363 VFNAVLPVLTSAALfaaaisllggaglslGSFlafntAFGSFSGAVTQLSNTLISILAVIplwerakPILEALPEVDEAK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 401 NAGYKLdhvKGNLEFQNVFFSYpaRPD-IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDL 479
Cdd:TIGR03797 443 TDPGKL---SGAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 480 KSLNVRYLREIIGVVNQEPVLFATTIAENIrYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQR 559
Cdd:TIGR03797 518 AGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQR 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 560 IAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRtiLVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQ 639
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAR 674
|
330
....*....|.
gi 2024474312 640 KGVYYKLVNMQ 650
Cdd:TIGR03797 675 EGLFAQLARRQ 685
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
411-631 |
6.41e-65 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 219.38 E-value: 6.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 411 GNLEFQNVFFSYPARPdIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI 490
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNP 570
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 571 KILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQG 631
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
411-632 |
2.35e-64 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 217.75 E-value: 2.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 411 GNLEFQNVFFSYpaRPDIK-ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLRE 489
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQEPVLFATTIAENI----RYgredvTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARA 565
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 566 LVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGT 632
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
226-619 |
3.72e-64 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 227.94 E-value: 3.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 226 IVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDA 305
Cdd:TIGR02857 137 AAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEY 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 306 KR--MGIQK-------------AIS-ANISMGVSFFLIYGSYAL--AFWygtILVLSEDytigkvftvFFSIL--VGAfs 365
Cdd:TIGR02857 217 RErtMRVLRiaflssavlelfaTLSvALVAVYIGFRLLAGDLDLatGLF---VLLLAPE---------FYLPLrqLGA-- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 366 vgqaapSMEAFANARGAAYAIFNIIDNEPQIDSSSnaGYKLDHVKGNLEFQNVFFSYPARPdiKILKGLNLKVNCGQTVA 445
Cdd:TIGR02857 283 ------QYHARADGVAAAEALFAVLDAAPRPLAGK--APVTAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 446 LVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERAT 525
Cdd:TIGR02857 353 LVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREAL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 526 KEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILV 605
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
|
410
....*....|....
gi 2024474312 606 IAHRLSTVRNADLI 619
Cdd:TIGR02857 513 VTHRLALAALADRI 526
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
828-1290 |
2.59e-63 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 230.01 E-value: 2.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 828 TGELITRLAnDASQVKGATGSRLALVaqnIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKEL 907
Cdd:TIGR01193 252 TGEIVSRFT-DASSIIDALASTILSL---FLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAM 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 908 ETLGKVASEAIEN---IRTVVALTQE----RKFEYMYGQNLQVSYRNSIKKAhIFGFTFAFTQAIMYFTyagCFRFGAYL 980
Cdd:TIGR01193 328 QANAVLNSSIIEDlngIETIKSLTSEaerySKIDSEFGDYLNKSFKYQKADQ-GQQAIKAVTKLILNVV---ILWTGAYL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 981 VKNGHMRFKDvLLVFSAIV-FGAMALGQSTSFTPDYAKAKMSAAHLfllfERVPLIDSysEEGEKPKM-----FGGNITF 1054
Cdd:TIGR01193 404 VMRGKLTLGQ-LITFNALLsYFLTPLENIINLQPKLQAARVANNRL----NEVYLVDS--EFINKKKRtelnnLNGDIVI 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1055 KDVAFKYPTRPEVkvLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVS 1134
Cdd:TIGR01193 477 NDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLP 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1135 QEPILFDCTIAENIAYGdNSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRIL 1214
Cdd:TIGR01193 555 QEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1215 LLDEATSALDTESEKIVQEALDKAREgRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVNV 1290
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
727-1263 |
3.12e-62 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 222.16 E-value: 3.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 727 PYFVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAaiRETNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLR 806
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAGEP--LAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 807 SMAFRAILRQEISWFDepKNSTGELITRLANDASQVKG-ATGSRLALVAQNIANLGTGIVLSLIyGWQLTLLLLAIVPII 885
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQ--GRPSGELATLALEGVEALDGyFARYLPQLVLAVIVPLAILAAVFPQ-DWISGLILLLTAPLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 886 AITgMIqmkmLAGHAKKDK--KELETLGKVASEAIENIR---TVVALTQERKfeymygqnlqvsYRNSIKK--------- 951
Cdd:TIGR02857 158 PIF-MI----LIGWAAQAAarKQWAALSRLSGHFLDRLRglpTLKLFGRAKA------------QAAAIRRsseeyrert 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 952 ------AHIFGFTFAFTQAI---MYFTYAGcFRfgayLVkNGHMRFKDVLLVFsaivfgAMA------LGQSTSFTPDYA 1016
Cdd:TIGR02857 221 mrvlriAFLSSAVLELFATLsvaLVAVYIG-FR----LL-AGDLDLATGLFVL------LLApefylpLRQLGAQYHARA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1017 KAKMSAAHLFLLFERVPLIdsYSEEGEKPKMFGGNITFKDVAFKYPTRPEVkvLQGLNIEVEKGQTLALVGSSGCGKSTV 1096
Cdd:TIGR02857 289 DGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1097 VQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDnsREVSHEEIVSAAKAANIHSFIE 1176
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1177 SLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN 1256
Cdd:TIGR02857 443 ALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAAL 522
|
....*..
gi 2024474312 1257 ADKIAVI 1263
Cdd:TIGR02857 523 ADRIVVL 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
237-639 |
6.92e-62 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 222.32 E-value: 6.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 237 LVILALSPVLGFSSALWAKIISTFT--NKELT---------AYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDA 305
Cdd:COG4618 148 AVLFLFHPLLGLLALVGALVLVALAllNERLTrkplkeaneAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 306 KRMGIQKAISANISMGVS----FFLIYGSYALafwyGTILVLSEDYTIGKVFTVffSILVG-AFS-VGQAAPSMEAFANA 379
Cdd:COG4618 228 LALQARASDRAGGFSALSkflrLLLQSAVLGL----GAYLVIQGEITPGAMIAA--SILMGrALApIEQAIGGWKQFVSA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 380 RGAAYAIFNIIDNEPQIDSSSnagyKLDHVKGNLEFQNVFFSYP--ARPdikILKGLNLKVNCGQTVALVGGSGCGKSTT 457
Cdd:COG4618 302 RQAYRRLNELLAAVPAEPERM----PLPRPKGRLSVENLTVVPPgsKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 458 VQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENI-RYGreDVTMEEIERATKEANAYDFIMK 536
Cdd:COG4618 375 ARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILR 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 537 LPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTVRN 615
Cdd:COG4618 453 LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAA 532
|
410 420
....*....|....*....|....
gi 2024474312 616 ADLIAAFENGVITEQGTHDELMEQ 639
Cdd:COG4618 533 VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
998-1287 |
3.42e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 220.47 E-value: 3.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 998 IVFGAMA--------------LGQSTSftpdyakakmSAAHLFLLFERVPLIDSYSEEGEKPKmfGGNITFKDVAFKYPT 1063
Cdd:PRK11160 283 FVFAALAafealmpvagafqhLGQVIA----------SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1064 RPEvKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCT 1143
Cdd:PRK11160 351 QPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSAT 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIAYGDNsrEVSHEEIVSAAKAANIHSFIESlPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:PRK11160 430 LRDNLLLAAP--NASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1224 DTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSL 1287
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
382-646 |
9.00e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 216.23 E-value: 9.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 382 AAYAIFNIIDNEPQIDSSSNAGYKLDHvkGNLEFQNVFFSYPARPDiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLI 461
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 462 QRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANaydfIMKL---P 538
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG----LEKLledD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 539 KKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADL 618
Cdd:PRK11160 463 KGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDR 542
|
250 260
....*....|....*....|....*...
gi 2024474312 619 IAAFENGVITEQGTHDELMEQKGVYYKL 646
Cdd:PRK11160 543 ICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
147-672 |
5.69e-59 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 214.58 E-value: 5.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 147 LFAA---YIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFT 223
Cdd:PRK10790 76 LLAAglhYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 224 GFIVGFTKGWKLTLVILALSPVLGFSSALWAKIiSTFTNKELTAY-AKAGAVAEEVLAAVRTVVAFGGQrketERYQKNL 302
Cdd:PRK10790 156 MLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRY-STPIVRRVRAYlADINDGFNEVINGMSVIQQFRQQ----ARFGERM 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 303 EDAKRMGIQKAISAnisMGVSFFLIygSYALAFWYGTILVlsedytiGKVFTVFFSiLVGAFSVGqaapSMEAFANARG- 381
Cdd:PRK10790 231 GEASRSHYMARMQT---LRLDGFLL--RPLLSLFSALILC-------GLLMLFGFS-ASGTIEVG----VLYAFISYLGr 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 382 --------------------AAYAIFNIIDNEPQidsssnaGYKLDH---VKGNLEFQNVFFSYpaRPDIKILKGLNLKV 438
Cdd:PRK10790 294 lneplielttqqsmlqqavvAGERVFELMDGPRQ-------QYGNDDrplQSGRIDIDNVSFAY--RDDNLVLQNINLSV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 439 NCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGReDVTM 518
Cdd:PRK10790 365 PSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 519 EEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIR 598
Cdd:PRK10790 444 EQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 599 KGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQasetedQLQEEGNASSVSEEAL 672
Cdd:PRK10790 524 EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ------LAGEELAASVREEESL 591
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
151-648 |
7.03e-58 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 213.83 E-value: 7.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 151 YIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDdISKINEGIGEKI-AMFFQAVATFFTGFIVGF 229
Cdd:TIGR01193 214 YIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTIlSLFLDMWILVIVGLFLVR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 230 tKGWKLTLVILALSPVlgFSSALWA--KIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGqrkETERYQK------- 300
Cdd:TIGR01193 293 -QNMLLFLLSLLSIPV--YAVIIILfkRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsefgd 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 301 ----NLEDAKRMGIQKAISANISMGVSFFLIygsyalafWYGTILVLSEDYTIGKVFTvfFSILVGAF-----SVGQAAP 371
Cdd:TIGR01193 367 ylnkSFKYQKADQGQQAIKAVTKLILNVVIL--------WTGAYLVMRGKLTLGQLIT--FNALLSYFltpleNIINLQP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 372 SMEA--FANAR-GAAYAIFNIIDNEPQIDSSSNagykldhVKGNLEFQNVFFSYPARPdiKILKGLNLKVNCGQTVALVG 448
Cdd:TIGR01193 437 KLQAarVANNRlNEVYLVDSEFINKKKRTELNN-------LNGDIVINDVSYSYGYGS--NILSDISLTIKMNSKTTIVG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 449 GSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYG-REDVTMEEIERATKE 527
Cdd:TIGR01193 508 MSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEI 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 528 ANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIrKGRTILVIA 607
Cdd:TIGR01193 588 AEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVA 666
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024474312 608 HRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVN 648
Cdd:TIGR01193 667 HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
416-1294 |
1.21e-57 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 219.61 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 416 QNVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIdgqdlkslnvryLREIIGVVN 495
Cdd:PLN03130 618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 QEPVLFATTIAENIRYGREdVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLL 575
Cdd:PLN03130 686 QVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 576 DEATSALDTEsesVVQAALDK-IR---KGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNmQA 651
Cdd:PLN03130 765 DDPLSALDAH---VGRQVFDKcIKdelRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME-NA 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 652 SETEDQLQEEGNAS---SVSEEALNGSVLTGQKRQST---RKSIKRVRIQNDELDVKAdqldknmppSSFFKIMKLNKTE 725
Cdd:PLN03130 841 GKMEEYVEENGEEEddqTSSKPVANGNANNLKKDSSSkkkSKEGKSVLIKQEERETGV---------VSWKVLERYKNAL 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 726 WPYFVVGTL--CAIingaLQPIFSVMISDVIGMFVEKGKAAIRET---NSTYALLFLGFGLISFVTFFLQGFTFGKAGEi 800
Cdd:PLN03130 912 GGAWVVMILflCYV----LTEVFRVSSSTWLSEWTDQGTPKTHGPlfyNLIYALLSFGQVLVTLLNSYWLIMSSLYAAK- 986
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 801 ltmRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKgatgsrlalvaQNIANLGTGIVLSLiygWQL--TLLL 878
Cdd:PLN03130 987 ---RLHDAMLGSILRAPMSFFH--TNPLGRIINRFAKDLGDID-----------RNVAVFVNMFLGQI---FQLlsTFVL 1047
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 879 LAIVPIIAITGMIQMKMLAGHA-------KKDKKELETLGKVA-----SEAIENIRTVVALTQERKFEYMYGQNLQVSYR 946
Cdd:PLN03130 1048 IGIVSTISLWAIMPLLVLFYGAylyyqstAREVKRLDSITRSPvyaqfGEALNGLSTIRAYKAYDRMAEINGRSMDNNIR 1127
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 947 NS---IKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNgHMRFKDVL-LVFSaivfgaMALGQSTSFTPDYAKAKMsA 1022
Cdd:PLN03130 1128 FTlvnMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAEN-QAAFASTMgLLLS------YALNITSLLTAVLRLASL-A 1199
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1023 AHLFLLFERV-PLIDSYSE-----EGEKPKM---FGGNITFKDVAFKYptRPEVK-VLQGLNIEVEKGQTLALVGSSGCG 1092
Cdd:PLN03130 1200 ENSLNAVERVgTYIDLPSEaplviENNRPPPgwpSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAG 1277
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1093 KSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVSAAKAANIH 1172
Cdd:PLN03130 1278 KSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLK 1354
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1173 SFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKarEGRTC--IVIAHR 1250
Cdd:PLN03130 1355 DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHR 1432
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 2024474312 1251 LSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLVnVQS-GP 1294
Cdd:PLN03130 1433 LNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM-VQStGA 1476
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
217-610 |
6.80e-56 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 203.75 E-value: 6.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 217 AVATFFTGFIVGFTKGWKLTL-VILALSPVLGFSSALWAKiistfTNKELTAYAKAGAVAEEVLAAVR---TVVAFGGQ- 291
Cdd:TIGR02868 139 VVGAAAVAAIAVLSVPAALILaAGLLLAGFVAPLVSLRAA-----RAAEQALARLRGELAAQLTDALDgaaELVASGALp 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 292 --RKETERYQKNLEDA-KRMGIQKAISANISMgvsffLIYGSYALafwyGTILVLSEDYTIGKVFTVFFSILV----GAF 364
Cdd:TIGR02868 214 aaLAQVEEADRELTRAeRRAAAATALGAALTL-----LAAGLAVL----GALWAGGPAVADGRLAPVTLAVLVllplAAF 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 365 SVGQAAP-SMEAFANARGAAYAIFNIIDNEPQIDSSS---NAGYKLDHVkgNLEFQNVFFSYParPDIKILKGLNLKVNC 440
Cdd:TIGR02868 285 EAFAALPaAAQQLTRVRAAAERIVEVLDAAGPVAEGSapaAGAVGLGKP--TLELRDLSAGYP--GAPPVLDGVSLDLPP 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 441 GQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEE 520
Cdd:TIGR02868 361 GERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 521 IERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKG 600
Cdd:TIGR02868 441 LWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG 520
|
410
....*....|
gi 2024474312 601 RTILVIAHRL 610
Cdd:TIGR02868 521 RTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1065-1287 |
7.89e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 205.08 E-value: 7.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQG-LNIEVEKGQTLALVGSSGCGKSTVVQLLERFYdPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCT 1143
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIAYGDNsrEVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:PRK11174 439 LRDNVLLGNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1224 DTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSL 1287
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
215-639 |
3.52e-55 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 202.19 E-value: 3.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 215 FQAVATFFTG--FIVGFTKGWK--LTLVILALSPVLGFSSALWAKII-------STFTNKEL----TAYAKAGAVAEEVL 279
Cdd:TIGR01842 108 LDQLRQFLTGpgLFAFFDAPWMpiYLLVCFLLHPWIGILALGGAVVLvglallnNRATKKPLkeatEASIRANNLADSAL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 280 AAVRTVVAFGGQRKETERYQKnlEDAKRMGIQKAIS--ANISMGVS--FFLIYGSYALAFwyGTILVLSEDYTIGKVftV 355
Cdd:TIGR01842 188 RNAEVIEAMGMMGNLTKRWGR--FHSKYLSAQSAASdrAGMLSNLSkyFRIVLQSLVLGL--GAYLAIDGEITPGMM--I 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 356 FFSILVG-AFS-VGQAAPSMEAFANARGAAYAIFNIIDNEPqidsSSNAGYKLDHVKGNLEFQNVFFSyPARPDIKILKG 433
Cdd:TIGR01842 262 AGSILVGrALApIDGAIGGWKQFSGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIV-PPGGKKPTLRG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 434 LNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGR 513
Cdd:TIGR01842 337 ISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFG 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 514 EDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAA 593
Cdd:TIGR01842 417 ENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA 496
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2024474312 594 LDKIRK-GRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQ 639
Cdd:TIGR01842 497 IKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
375-657 |
6.23e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.38 E-value: 6.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 375 AFANARGAAYAIFNIIDNEpqIDSSSNAGYKLDHVKGN-LEFQN-VFFSyparPDIKILKG-LNLKVNCGQTVALVGGSG 451
Cdd:PRK11174 313 AKAQAVGAAESLVTFLETP--LAHPQQGEKELASNDPVtIEAEDlEILS----PDGKTLAGpLNFTLPAGQRIALVGPSG 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 452 CGKSTTVQLIQRFYdPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAY 531
Cdd:PRK11174 387 AGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 532 DFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLS 611
Cdd:PRK11174 466 EFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE 545
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2024474312 612 TVRNADLIAAFENGVITEQGTHDELMEQKGVYYklvNMQASETEDQ 657
Cdd:PRK11174 546 DLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA---TLLAHRQEEI 588
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1052-1281 |
1.87e-52 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 184.07 E-value: 1.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPI--LFDCTIAENIAYGDNSREVSHEEIVSAAKAA----NIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIAR 1205
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGTHQQLLAEK 1281
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
977-1280 |
4.50e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 189.87 E-value: 4.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 977 GAYLVKNGHMrfKDVLLVFSAIVFGAmALG---QSTSFTPDYAKAKMSAAHLFLLFERVPLIDSYSEEGEkPKmfgGNIT 1053
Cdd:TIGR01842 246 GAYLAIDGEI--TPGMMIAGSILVGR-ALApidGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLPE-PE---GHLS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1054 FKDVAFKYPTrPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIV 1133
Cdd:TIGR01842 319 VENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1134 SQEPILFDCTIAENIA-YGDNsreVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPR 1212
Cdd:TIGR01842 398 PQDVELFPGTVAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPK 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1213 ILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1052-1279 |
6.44e-51 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 188.57 E-value: 6.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRP--EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN---IQWL 1126
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1127 RAQIGIVSQEPIL-FDC--TIAENIAYG-DNSREVSHEEIvsAAKAANI-------HSFIESLPkkyntrvgdkgAQLSG 1195
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAER--RERVAELlervglpPDLADRYP-----------HELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1196 GQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*..
gi 2024474312 1273 THQQLLA 1279
Cdd:COG1123 488 PTEEVFA 494
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1052-1268 |
2.28e-50 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 175.87 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEVkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFDCTIAENIaygdnsrevsheeivsaakaanihsfieslpkkyntrvgdkgaqLSGGQKQRIAIARALIRQP 1211
Cdd:cd03246 80 YLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVIQNGKV 1268
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1052-1268 |
5.00e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 176.16 E-value: 5.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFDCTIAENIAYGDNSRE--VSHEEIVSAAKAANihsfiesLPKKY-NTRVgdkgAQLSGGQKQRIAIARALI 1208
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRErkFDRERALELLERLG-------LPPDIlDKPV----ERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1209 RQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKV 1268
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1052-1277 |
6.15e-50 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 176.60 E-value: 6.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLSGEVLLDGRNTKTLNIQ-- 1124
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1125 WLRAQIGIVSQEPILFDCTIAENIAYGDNSREVS----HEEIVSAA--KAAnihsfiesLPKKYNTRVgdKGAQLSGGQK 1198
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKlkeeLDERVEEAlrKAA--------LWDEVKDRL--HALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1199 QRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQL 1277
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
994-1251 |
2.12e-49 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 184.49 E-value: 2.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 994 VFSAIVFGAMALGQSTSFTPDYA----KAKMSAAHLFLLFERVPLIDSYSEEGEKPKMFGG-NITFKDVAFKYPTRPEVk 1068
Cdd:TIGR02868 272 TLAVLVLLPLAAFEAFAALPAAAqqltRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 vLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENI 1148
Cdd:TIGR02868 351 -LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 AYGdnSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESE 1228
Cdd:TIGR02868 430 RLA--RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
250 260
....*....|....*....|...
gi 2024474312 1229 KIVQEALDKAREGRTCIVIAHRL 1251
Cdd:TIGR02868 508 DELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1052-1272 |
5.01e-49 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 172.11 E-value: 5.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEvKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwLRAQIG 1131
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFDCTIAENIaygdnsrevsheeivsaakaanihsfieslpkkyntrvgdkGAQLSGGQKQRIAIARALIRQP 1211
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQG 1272
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
413-639 |
5.41e-49 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 183.18 E-value: 5.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARP--DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI 490
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 ---IGVVNQEPV--LFAT-TIAENIRYG---REDVTMEEIERATKEANA-----YDFIMKLPkkfetvvgergAQMSGGQ 556
Cdd:COG1123 341 rrrVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAERRERVAELLErvglpPDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 557 KQRIAIARALVRNPKILLLDEATSALDTesesVVQAA----LDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITE 629
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV----SVQAQilnlLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250
....*....|
gi 2024474312 630 QGTHDELMEQ 639
Cdd:COG1123 486 DGPTEEVFAN 495
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1054-1267 |
6.30e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 173.04 E-value: 6.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1054 FKDVAFKYPTRPEvKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIV 1133
Cdd:cd03225 2 LKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1134 SQEP--ILFDCTIAENIAYGDNSREVSHEEIVSAAKAA----NIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIARAL 1207
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1208 IRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVIQNGK 1267
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
413-627 |
6.36e-48 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 168.55 E-value: 6.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYP--ARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI 490
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEPVLFATTIAENIrygredvtmeeieratkeanaydfimklpkkfetvvgergaqMSGGQKQRIAIARALVRNP 570
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 571 KILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTVRNADLIAAFENGVI 627
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
413-640 |
7.82e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 170.59 E-value: 7.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPV--LFATTIAENIRYGRE--DVTMEEIERATKEA----NAYDFIMKLPkkfetvvgergAQMSGGQKQRIAIAR 564
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPEnlGLPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELMEQK 640
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1052-1272 |
9.06e-48 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 170.38 E-value: 9.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRP-EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWL---R 1127
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 AQIGIVSQEPI-----LFdcTIAENIAygdnsrevsheEIVSAAKAANIHSFIESLPKKYNTRVGDKGA-------QLSG 1195
Cdd:cd03257 82 KEIQMVFQDPMsslnpRM--TIGEQIA-----------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1196 GQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1052-1273 |
1.83e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 173.34 E-value: 1.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRP-EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQ---LLERfydPLSGEVLLDGRNTKTLNIQWLR 1127
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 A---QIGIVSQEPILFD-CTIAENIAY-----GdnsreVSHEEIvsAAKAANIhsfIEslpkkyntRVG--DKG----AQ 1192
Cdd:COG1135 79 AarrKIGMIFQHFNLLSsRTVAENVALpleiaG-----VPKAEI--RKRVAEL---LE--------LVGlsDKAdaypSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1193 LSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNGKVI 1269
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
....
gi 2024474312 1270 EQGT 1273
Cdd:COG1135 221 EQGP 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
431-580 |
3.63e-47 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 165.51 E-value: 3.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLF-ATTIAENI 509
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 510 RYGREdvtMEEIERATKEANAYDFI--MKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATS 580
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
413-636 |
4.69e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 168.13 E-value: 4.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYD-----PKEGTITIDGQDLKSLNVR-- 485
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 486 YLREIIGVVNQEPVLFATTIAENIRYG-------REDVTMEEIERATKEANaydfimkLPKKfetvVGER--GAQMSGGQ 556
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAA-------LWDE----VKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 557 KQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDE 635
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 2024474312 636 L 636
Cdd:cd03260 227 I 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
414-625 |
1.97e-46 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 165.72 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 414 EFQNVFFSYPARpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGV 493
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 494 VNQEP--VLFATTIAENIRYGRE--DVTMEEIERATKEANAydfIMKLPKKFETVVgergAQMSGGQKQRIAIARALVRN 569
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 570 PKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTVRN-ADLIAAFENG 625
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
413-631 |
3.34e-46 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 164.02 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNvRYLREIIG 492
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFATTIAENIrygredvtmeeieratkeanaydfimklpkkfetvvgerGAQMSGGQKQRIAIARALVRNPKI 572
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 573 LLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQG 631
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1050-1273 |
6.63e-46 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 164.12 E-value: 6.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1050 GNITFKDVAFKYptRPEV-KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRA 1128
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVSAakaanihsfieslpkkynTRVGDKGAQLSGGQKQRIAIARALI 1208
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1209 RQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGT 1273
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1052-1271 |
7.96e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.83 E-value: 7.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPT-RPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQL---LERfydPLSGEVLLDGRNTKTLN---IQ 1124
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1125 WLRAQ-IGIVSQEPILFDC-TIAENIA----YGDNSREVSHEEIVSAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQK 1198
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1199 QRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQ 1271
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1052-1271 |
8.55e-46 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 164.57 E-value: 8.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTR-PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWLRAQI 1130
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEPILFD-CTIAENIAYGDNSREVSHEEIVSAAKAAnihsfIEslpkkyntRVGDKGA------QLSGGQKQRIAI 1203
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-----LE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1204 ARALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQN--GKVIEQ 1271
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
103-386 |
1.06e-45 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 166.58 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 103 ANFSLLNSTSVNFSMEFFS-----YLILGELEEEMTRYAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVM 177
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIgrlidTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 178 RQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKII 257
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 258 STFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWY 337
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2024474312 338 GTILVLSEDYTIGKVFT-VFFSILVgAFSVGQAAPSMEAFANARGAAYAI 386
Cdd:cd18557 241 GGYLVLSGQLTVGELTSfILYTIMV-ASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1052-1279 |
5.58e-45 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 162.75 E-value: 5.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRP-EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQ---LLERfydPLSGEVLLDGRNTKTLN---IQ 1124
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1125 WLRAQIGIVSQEPILFDC-TIAENIAYgdnSREVSHEEivsaakAANIHSFIESLPKkyntRVG--DKG----AQLSGGQ 1197
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVAL---PLEIAGVP------KAEIEERVLELLE----LVGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1198 KQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTH 1274
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*
gi 2024474312 1275 QQLLA 1279
Cdd:cd03258 226 EEVFA 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
411-632 |
6.87e-45 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 161.43 E-value: 6.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 411 GNLEFQNVFFSYpaRPDI-KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLRE 489
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQEPVLFATTIAENI-RYGREDvtMEEIERATKeanaydfimklpkkfetvVGERGAQMSGGQKQRIAIARALVR 568
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGT 632
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1052-1279 |
7.44e-45 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 162.66 E-value: 7.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPE-VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQI 1130
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEPIL-------FDCTIAE--NIAYGDNSREvsheEIVSAAKAANihsfiesLPKKYNTRvgdKGAQLSGGQKQRI 1201
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEplRIHGLPDREE----RIAELLEQVG-------LPPSFLDR---YPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1202 AIARALIRQPRILLLDEATSALDTesekIVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTH 1274
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTV 223
|
....*
gi 2024474312 1275 QQLLA 1279
Cdd:COG1124 224 ADLLA 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1052-1278 |
7.77e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 162.91 E-value: 7.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPIL-FDCTIAENIAYG-----DNSREVSHE--EIVSAA-KAANIHSFIEslpKKYNTrvgdkgaqLSGGQKQRIA 1202
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlGLFGRPSAEdrEAVEEAlERTGLEHLAD---RPVDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1203 IARALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1052-1279 |
1.19e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 170.08 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDP---LSGEVLLDGRNTKTLNIQWLRA 1128
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPI--LFDCTIAENIAYGDNSREVSHEEIVSAAKAANIHSFIESLPKKYNtrvgdkgAQLSGGQKQRIAIARA 1206
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1207 LIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
413-631 |
1.97e-44 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 160.75 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPD-IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI- 490
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 --IGVVNQEPvlFAT-----TIAENIRYGREDVTMEEIERATKEANAYDFI-MKLPKKFETvvgERGAQMSGGQKQRIAI 562
Cdd:cd03257 82 keIQMVFQDP--MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPEEVLN---RYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 563 ARALVRNPKILLLDEATSALDTesesVVQAA----LDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQG 631
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDV----SVQAQildlLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
413-636 |
2.46e-44 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 160.82 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARP-DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI- 490
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 --IGVVNQEPVLFAT-TIAENIRYGRE--DVTMEEIERATKE----------ANAYdfimklPkkfetvvgergAQMSGG 555
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVLEllelvgledkADAY------P-----------AQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 556 QKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGT 632
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....
gi 2024474312 633 HDEL 636
Cdd:cd03258 225 VEEV 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1052-1272 |
5.46e-44 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 158.84 E-value: 5.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlRAQIG 1131
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFD-CTIAENIAYGDNSREVSHEEIVSAAKAA----NIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIARA 1206
Cdd:cd03259 76 MVFQDYALFPhLTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYP-----------HELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1207 LIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQG 1272
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1052-1280 |
7.41e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.46 E-value: 7.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWlRAQIG 1131
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILF-DCTIAENIAYGDNSREVSHEEIvsaakAANIHSFIE--SLPKKYNTRVGdkgaQLSGGQKQRIAIARALI 1208
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRFFARLYGLPRKEA-----RERIDELLElfGLTDAADRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1209 RQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1052-1281 |
7.95e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 160.67 E-value: 7.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTL-NIQWLRAQI 1130
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEPilfD-----CTIAENIAYGDNSREVSHEEIVS----AAKAANIHSFIESLPkkyntrvgdkgAQLSGGQKQRI 1201
Cdd:TIGR04520 80 GMVFQNP---DnqfvgATVEDDVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1202 AIARALIRQPRILLLDEATSALDTESEKIVQEALDKAR--EGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 2024474312 1280 EK 1281
Cdd:TIGR04520 226 QV 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
413-608 |
5.34e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.13 E-value: 5.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFATTIAENI----RYGREDVTMEEIERATKEANaydfimkLPkkfETVVGERGAQMSGGQKQRIAIARALVR 568
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LP---PDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKIR--KGRTILVIAH 608
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1070-1221 |
8.44e-43 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 153.19 E-value: 8.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILF-DCTIAENI 1148
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1149 AYGDNSREVSHEEivSAAKAANIHSFIeSLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATS 1221
Cdd:pfam00005 81 RLGLLLKGLSKRE--KDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
413-632 |
8.47e-43 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 159.86 E-value: 8.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARP-DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI- 490
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 --IGVVNQEPVLFAT-TIAENIRYGRE--DVTMEEIERATKE----------ANAYdfimklPkkfetvvgergAQMSGG 555
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKRVAEllelvglsdkADAY------P-----------SQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 556 QKQRIAIARALVRNPKILLLDEATSALDTES-ESVVqAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQG 631
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETtRSIL-DLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223
|
.
gi 2024474312 632 T 632
Cdd:COG1135 224 P 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1066-1279 |
1.78e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 155.54 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTV---VQLLERfydPLSGEVLLDGRN--TKTLNIQWLRAQIGIVSQEPILF 1140
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1141 -DCTIAENIAYGD-NSREVSHEEIVSAAKAAnihsfiesLpkkynTRVG--DKG----AQLSGGQKQRIAIARALIRQPR 1212
Cdd:COG1126 90 pHLTVLENVTLAPiKVKKMSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1213 ILLLDEATSALDTEsekIVQEALD--K--AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:COG1126 157 VMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
413-637 |
1.89e-42 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 155.54 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFA-TTIAENIrygrEDV-TMEEIERATKEANAYDfIMKL----PKKFetvvGER-GAQMSGGQKQRIAIARA 565
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI----ALVpKLLKWPKEKIRERADE-LLALvgldPAEF----ADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 566 LVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRL-STVRNADLIAAFENGVITEQGTHDELM 637
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1052-1279 |
2.01e-42 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 155.35 E-value: 2.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN---IQWLRA 1128
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPILFDC-TIAENIAY-----GDNSREVSHEEIVSAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQKQRIA 1202
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFplrehTRLSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1203 IARALIRQPRILLLDEATSALD-TESEKIVQEALD-KAREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1047-1273 |
2.19e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 159.11 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1047 MFGGNITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWL 1126
Cdd:COG3842 1 MAMPALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-----VTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1127 RAQ---IGIVSQEPILF-DCTIAENIAYGDNSREVSHEEIvsAAKAAnihsfiESLpkkynTRVGDKG------AQLSGG 1196
Cdd:COG3842 73 PPEkrnVGMVFQDYALFpHLTVAENVAFGLRMRGVPKAEI--RARVA------ELL-----ELVGLEGladrypHQLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS---TIqnADKIAVIQNGKVIEQ 1271
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQV 217
|
..
gi 2024474312 1272 GT 1273
Cdd:COG3842 218 GT 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1053-1267 |
3.18e-42 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 151.63 E-value: 3.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1053 TFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGI 1132
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1133 VSQepilfdctiaeniaygdnsrevsheeivsaakaanihsfieslpkkyntrvgdkgaqLSGGQKQRIAIARALIRQPR 1212
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1213 ILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQNA-DKIAVIQNGK 1267
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
413-639 |
3.74e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 162.77 E-value: 3.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK---EGTITIDGQDLKSLNVRYLRE 489
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQEP--VLFATTIAENIRYGRE--DVTMEEIERATKEANAYDFImklpkkfETVVGERGAQMSGGQKQRIAIARA 565
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVLELLEAVGL-------ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 566 LVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELMEQ 639
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
732-1032 |
9.52e-42 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 155.41 E-value: 9.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 732 GTLCAIINGALQpifsVMISDVIGMFVEKGKAAIRETN-STYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAF 810
Cdd:cd18557 1 GLLFLLISSAAQ----LLLPYLIGRLIDTIIKGGDLDVlNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 811 RAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGM 890
Cdd:cd18557 77 SSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 891 IQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTY 970
Cdd:cd18557 155 IYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 971 AGCFRFGAYLVKNGHMRFKDVL--LVFSAIVfgAMALGQSTSFTPDYAKAkMSAAhlfllfERV 1032
Cdd:cd18557 235 LLVLWYGGYLVLSGQLTVGELTsfILYTIMV--ASSVGGLSSLLADIMKA-LGAS------ERV 289
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1052-1267 |
1.60e-41 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 150.42 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQW--LRAQ 1129
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 IGIVSQEPILF-DCTIAENIAYGdnsrevsheeivsaakaanihsfieslpkkyntrvgdkgaqLSGGQKQRIAIARALI 1208
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG-----------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1209 RQPRILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIAHRLSTIQN-ADKIAVIQNGK 1267
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
413-638 |
1.66e-41 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 153.03 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARP-DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREII 491
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEP---------VlfATTIAENIRYGREDVTMEEIERATKEANaydfimkLPKKFetvVGERGAQMSGGQKQRIAI 562
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVG-------LPPSF---LDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 563 ARALVRNPKILLLDEATSALDTesesVVQAA----LDKIRK--GRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDE 635
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDV----SVQAEilnlLKDLREerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVAD 225
|
...
gi 2024474312 636 LME 638
Cdd:COG1124 226 LLA 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1052-1279 |
1.70e-41 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 152.83 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN---IQWLRA 1128
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPILFDC-TIAENIAYGDnsREVSH------EEIVSAA-KAANIHSFIESLPkkyntrvgdkgAQLSGGQKQR 1200
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPL--REHTDlseaeiRELVLEKlELVGLPGAADKMP-----------SELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1201 IAIARALIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQL 1277
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 2024474312 1278 LA 1279
Cdd:COG1127 230 LA 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1052-1267 |
1.87e-41 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 151.47 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEV--KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLL--ErfYDPLSGEVLLDGRntktlniqwlr 1127
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 aqIGIVSQEPILFDCTIAENIAYGdnsREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARAL 1207
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFG---KPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1208 IRQPRILLLDEATSALDTE-SEKIVQEALDKA-REGRTCIVIAHRLSTIQNADKIAVIQNGK 1267
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHvGRHIFENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
413-638 |
2.54e-41 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 152.44 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-- 490
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 -IGVVNQEPVLF-ATTIAENIRYG-RE--DVTMEEIERATKE-------ANAYDfimKLPkkfetvvgergAQMSGGQKQ 558
Cdd:COG1127 83 rIGMLFQGGALFdSLTVFENVAFPlREhtDLSEAEIRELVLEklelvglPGAAD---KMP-----------SELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 559 RIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDE 635
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
...
gi 2024474312 636 LME 638
Cdd:COG1127 229 LLA 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1052-1279 |
3.18e-41 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 152.07 E-value: 3.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILF-DCTIAENIAYGDNSREVSHEEIvsAAKAANIHSFIESLPKKYNTRVGDkgaQLSGGQKQRIAIARALIRQ 1210
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKI--RERADELLALVGLDPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1211 PRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRL-STIQNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
413-625 |
3.93e-41 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 149.64 E-value: 3.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN--VRYLREI 490
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEPVLFAT-TIAENIRYGredvtmeeieratkeanaydfimklpkkfetvvgergaqMSGGQKQRIAIARALVRN 569
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 570 PKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENG 625
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1052-1270 |
4.15e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 152.55 E-value: 4.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRP-EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWLRAQI 1130
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEPILFD-CTIAENIAYGDNSREVSHEEIVSAAKAA----NIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIAR 1205
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAH------RLstiqnADKIAVIQN--GKVIE 1270
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
413-662 |
4.17e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 152.58 E-value: 4.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSL-NVRYLREII 491
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEP--VLFATTIAENIRYGRED--VTMEEIERATKEA----NAYDFIMKLPkkfetvvgergAQMSGGQKQRIAIA 563
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREP-----------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 564 RALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKG 641
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVE 228
|
250 260
....*....|....*....|....*.
gi 2024474312 642 vyyKLVNM-----QASETEDQLQEEG 662
Cdd:TIGR04520 229 ---LLKEIgldvpFITELAKALKKRG 251
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1052-1282 |
5.49e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 151.55 E-value: 5.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIqWLRAQIG 1131
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFD-CTIAENIAYGDNSREVSHEEIvsAAKAAN-IHSFIesLPKKYNTRVGDkgaqLSGGQKQRIAIARALIR 1209
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYFAELYGLFDEEL--KKRIEElIELLG--LEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1210 QPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIA-HRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAEKG 1282
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
418-1284 |
8.03e-41 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 165.08 E-value: 8.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 418 VFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlkslnvrylreiIGVVNQE 497
Cdd:TIGR01271 429 LFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 498 PVLFATTIAENIRYGredVTMEEIeRATKEANAYDF---IMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILL 574
Cdd:TIGR01271 496 SWIMPGTIKDNIIFG---LSYDEY-RYTSVIKACQLeedIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 575 LDEATSALDTESES-VVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELM---------------- 637
Cdd:TIGR01271 572 LDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQakrpdfsslllgleaf 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 638 -------------------------------EQKGVYYK--------------LVN-----------------MQASETE 655
Cdd:TIGR01271 652 dnfsaerrnsiltetlrrvsidgdstvfsgpETIKQSFKqpppefaekrkqsiILNpiasarkfsfvqmgpqkAQATTIE 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 656 DQLQEEGN-------ASSVSEEAL-------NGSVLTGQKRQS-----------------TRKSIKRVRI---QND---E 698
Cdd:TIGR01271 732 DAVREPSErkfslvpEDEQGEESLprgnqyhHGLQHQAQRRQSvlqlmthsnrgenrreqLQTSFRKKSSitqQNElasE 811
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 699 LDVKADQLDKNMP------------PSSFFKIMKL--NKTEWPYFV-----------VGTLCAII-----NGALQPIFsv 748
Cdd:TIGR01271 812 LDIYSRRLSKDSVyeiseeineedlKECFADERENvfETTTWNTYLryittnrnlvfVLIFCLVIflaevAASLLGLW-- 889
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 749 MISDV-IGMFVEKG-----------KAAIRETNSTYALLFLGFGLI-SFVTF-FLQGFTFGKAGEILTMRLRSMAFRAIL 814
Cdd:TIGR01271 890 LITDNpSAPNYVDQqhanasspdvqKPVIITPTSAYYIFYIYVGTAdSVLALgFFRGLPLVHTLLTVSKRLHEQMLHSVL 969
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 815 RQEISWFDEPKnsTGELITRLANDASQVKgatgSRLALVAQNIANLgTGIVLSLIYGWQLT--LLLLAIVPIIAITGMIQ 892
Cdd:TIGR01271 970 QAPMAVLNTMK--AGRILNRFTKDMAIID----DMLPLTLFDFIQL-TLIVLGAIFVVSVLqpYIFIAAIPVAVIFIMLR 1042
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 893 MKMLAGHAKKDKKELETLGKVASEAIENIR---TVVALTQERKFEYMYGQNLQVSYRN-----SIKKAHIFGFTFAFtqa 964
Cdd:TIGR01271 1043 AYFLRTSQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANwflylSTLRWFQMRIDIIF--- 1119
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 965 IMYFTYAGCFRFGAYLVKNGHMrfkDVLLVFSAIVFGAMALGQSTSFTPDyakAKMSAAHLFLLFERVPLIDSYSEEGEK 1044
Cdd:TIGR01271 1120 VFFFIAVTFIAIGTNQDGEGEV---GIILTLAMNILSTLQWAVNSSIDVD---GLMRSVSRVFKFIDLPQEEPRPSGGGG 1193
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1045 PKMF-----------------GGNITFKDVAFKYpTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPl 1107
Cdd:TIGR01271 1194 KYQLstvlvienphaqkcwpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST- 1271
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1108 SGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVG 1187
Cdd:TIGR01271 1272 EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLV 1348
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1188 DKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGK 1267
Cdd:TIGR01271 1349 DGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSS 1428
|
1050
....*....|....*..
gi 2024474312 1268 VIEQGTHQQLLAEKGFY 1284
Cdd:TIGR01271 1429 VKQYDSIQKLLNETSLF 1445
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
141-646 |
1.30e-40 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 164.35 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 141 GIGAGVL-FAAYIQVSFWTLAAGRqikRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVA 219
Cdd:TIGR00957 1015 GILQGFAvFGYSMAVSIGGIQASR---VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLF 1091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 220 TFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKiiSTFTNKELTAYAKAGAVAE--EVLAAVRTVVAFggQRKETER 297
Cdd:TIGR00957 1092 NVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVA--SSRQLKRLESVSRSPVYSHfnETLLGVSVIRAF--EEQERFI 1167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 298 YQKNLE-DAKRMGIQKAISAN--ISMGVSF-----------FLIYGSYALAfwyGTILVLSEDYTIGkvFTVFFSILVGA 363
Cdd:TIGR00957 1168 HQSDLKvDENQKAYYPSIVANrwLAVRLECvgncivlfaalFAVISRHSLS---AGLVGLSVSYSLQ--VTFYLNWLVRM 1242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 364 FSvgqaapSMEA--FANARGAAYAifNIIDNEPQIDSSSNAGYKLDHVkGNLEFQNVFFSYpaRPDIK-ILKGLNLKVNC 440
Cdd:TIGR00957 1243 SS------EMETniVAVERLKEYS--ETEKEAPWQIQETAPPSGWPPR-GRVEFRNYCLRY--REDLDlVLRHINVTIHG 1311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 441 GQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENI----RYGREDV 516
Cdd:TIGR00957 1312 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEV 1391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 517 TMeeierATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDK 596
Cdd:TIGR00957 1392 WW-----ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT 1466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2024474312 597 IRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKL 646
Cdd:TIGR00957 1467 QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
413-639 |
2.05e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYlREIIG 492
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFAT-TIAENIRY------GREDVTMEEIERATKEANAYDFIMKLPKKFetvvgergaqmSGGQKQRIAIARA 565
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfarlygLPRKEARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 566 LVRNPKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELMEQ 639
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
413-637 |
2.55e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 149.81 E-value: 2.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVL-FATTIAENIRYGR------------EDvtMEEIERATKEANAYDFIMKLpkkfetvVGErgaqMSGGQKQR 559
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrpsaED--REAVEEALERTGLEHLADRP-------VDE----LSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 560 IAIARALVRNPKILLLDEATSALDtesesvV---QAALDKIRK-----GRTILVIAHRLS-TVRNADLIAAFENGVITEQ 630
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLD------LahqLEVLELLRRlarerGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQ 219
|
....*..
gi 2024474312 631 GTHDELM 637
Cdd:COG1120 220 GPPEEVL 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
413-608 |
2.68e-40 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 148.77 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYP-ARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylreiI 491
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFA-TTIAENIRYGREDVTM------EEIERATKEANAYDFIMKLPKkfetvvgergaQMSGGQKQRIAIAR 564
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVpkaearERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAH 608
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTH 190
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
413-627 |
3.40e-40 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 148.41 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPD-IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN----VRYL 487
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 488 REIIGVVNQEPVLFAT-TIAENIRYGredVTMEEIERATKEANAYDFI--MKLPKKFETVVgergAQMSGGQKQRIAIAR 564
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRNADLIAAFENGVI 627
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
413-608 |
6.53e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.08 E-value: 6.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARP-DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylreiI 491
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFA-TTIAENIRYGREDVTMEEIERAtKEANAY-------DFIMKLPKkfetvvgergaQMSGGQKQRIAIA 563
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERR-ERARELlelvglaGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024474312 564 RALVRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAH 608
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH 197
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1283 |
6.64e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 149.37 E-value: 6.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPilfD-----CTIAENIAYGDNSREVSHEE----IVSAAKAANIHSFIESLPKKyntrvgdkgaqLSGGQKQRIA 1202
Cdd:PRK13632 87 IIFQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1203 IARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGR--TCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
...
gi 2024474312 1281 KGF 1283
Cdd:PRK13632 233 KEI 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1052-1277 |
8.80e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 148.65 E-value: 8.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYD--P---LSGEVLLDGRN--TKTLNIQ 1124
Cdd:COG1117 12 IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDiyDPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1125 WLRAQIGIVSQEPILFDCTIAENIAYG-----DNSREVsHEEIVSAA--KAAnihsfiesLPKKYNTRVGDKGAQLSGGQ 1197
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSE-LDEIVEESlrKAA--------LWDEVKDRLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1198 KQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREgRTCIVI-------AHRLStiqnaDKIAVIQNGKVIE 1270
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVE 233
|
....*..
gi 2024474312 1271 QGTHQQL 1277
Cdd:COG1117 234 FGPTEQI 240
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1052-1268 |
1.18e-39 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 146.87 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPE-VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN----IQWL 1126
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1127 RAQIGIVSQE----PILfdcTIAENIAYGDNSREVSHEEIvsaakAANIHSFIES--LPKKYNTRVgdkgAQLSGGQKQR 1200
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKER-----RERAEELLERvgLGDRLNHYP----SELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1201 IAIARALIRQPRILLLDEATSALDTESEKIVQEAL-DKAREGRTCIVIA-HRLSTIQNADKIAVIQNGKV 1268
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
413-639 |
1.33e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.45 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDL--KSLNVRYLREI 490
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEPVLFA-TTIAENIRYG--------REDVT---MEEIER---ATKeANAYdfimklPkkfetvvgergAQMSGG 555
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvkkmsKAEAEeraMELLERvglADK-ADAY------P-----------AQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 556 QKQRIAIARALVRNPKILLLDEATSALDTESESVVqaaLDKIRK----GRTILVIAHRLSTVRN-ADLIAAFENGVITEQ 630
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEV---LDVMRDlakeGMTMVVVTHEMGFAREvADRVVFMDGGRIVEE 217
|
....*....
gi 2024474312 631 GTHDELMEQ 639
Cdd:COG1126 218 GPPEEFFEN 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
413-630 |
1.50e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.73 E-value: 1.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPA-RPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLI---QRfydPKEGTITIDGQDLKSLN----V 484
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 485 RYLREIIGVVNQEPVLFAT-TIAENI----RYGREDVTmEEIERATKEANA---YDFIMKLPkkfetvvgergAQMSGGQ 556
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENValplLLAGVSRK-ERRERARELLERvglGDRLDHRP-----------SQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 557 KQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRNADLIAAFENGVITEQ 630
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1052-1278 |
2.67e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 149.91 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQL---LERfydPLSGEVLLDGRNTKTlniqWLRA 1128
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFT----NLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 Q---IGIVSQEPILF-DCTIAENIAYGDNSREVSHEEIvsAAKAAN----IHsfIESLPKKYNtrvgdkgAQLSGGQKQR 1200
Cdd:COG1118 73 RerrVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEI--RARVEEllelVQ--LEGLADRYP-------SQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1201 IAIARALIRQPRILLLDEATSALDT----ESEKIVQEALDkaREGRTCIVIAH------RLstiqnADKIAVIQNGKVIE 1270
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQ 214
|
....*...
gi 2024474312 1271 QGTHQQLL 1278
Cdd:COG1118 215 VGTPDEVY 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
413-639 |
3.82e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 149.86 E-value: 3.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVrYLREIiG 492
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKRNV-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFA-TTIAENIRYG--REDVTMEEIERATKEANAydfIMKLPKkfetvVGERG-AQMSGGQKQRIAIARALVR 568
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAELLE---LVGLEG-----LADRYpHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLS---TVrnADLIAAFENGVITEQGTHDELMEQ 639
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
413-631 |
4.41e-39 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 144.97 E-value: 4.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylREIIG 492
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFAT-TIAENIRYGREDVTMEEIERATKEANAYDFIMklpkkFETVVGERGAQMSGGQKQRIAIARALVRNPK 571
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVPKAEIRARVRELLELVG-----LEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 572 ILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLS-TVRNADLIAAFENGVITEQG 631
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
129-382 |
5.34e-39 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 147.40 E-value: 5.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 129 EEEMTRYAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIG 208
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 209 EKIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAF 288
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 289 GGQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGkVFTVF--FSILVgAFSV 366
Cdd:cd18780 198 AKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTG-LLTSFllYTLTV-AMSF 275
|
250
....*....|....*.
gi 2024474312 367 GQAAPSMEAFANARGA 382
Cdd:cd18780 276 AFLSSLYGDFMQAVGA 291
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1052-1270 |
8.37e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.42 E-value: 8.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEVkvLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN---IQWLRA 1128
Cdd:COG2884 2 IRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQE-PILFDCTIAENIAYGDNSREVSHEEIVSAAKAAnihsfIE--SLPKKYNTRVgdkgAQLSGGQKQRIAIAR 1205
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALPLRVTGKSRKEIRRRVREV-----LDlvGLSDKAKALP----HELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1206 ALIRQPRILLLDEATSALDTE-SEKIVqEALDKAREGRTCIVIA-HRLSTIQNADK-IAVIQNGKVIE 1270
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
413-636 |
8.91e-39 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 144.95 E-value: 8.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-- 490
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 -IGVVNQEPVLF-ATTIAENIRYG-REDVTM--EEIERATKeanaydfiMKLpkkfeTVVGERG------AQMSGGQKQR 559
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlREHTRLseEEIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 560 IAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1055-1272 |
2.21e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 141.80 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1055 KDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVS 1134
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1135 QepilfdctiaeniaygdnsrevsheeivsAAKAANIHSFIEslpKKYNTrvgdkgaqLSGGQKQRIAIARALIRQPRIL 1214
Cdd:cd03214 80 Q-----------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1215 LLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQG 1272
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
414-625 |
5.40e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 139.69 E-value: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 414 EFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGV 493
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 494 VnqepvlfattiaenirygredvtmeeieratkeanaydfimklpkkfetvvgergAQMSGGQKQRIAIARALVRNPKIL 573
Cdd:cd00267 78 V-------------------------------------------------------PQLSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 574 LLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTVRNA-DLIAAFENG 625
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
413-627 |
7.04e-38 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 139.84 E-value: 7.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSlNVRYLREIIG 492
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFAT-TIAENIRYgredvtmeeieratkeanaydfimklpkkfetvvgergaqmSGGQKQRIAIARALVRNPK 571
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 572 ILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTVRN-ADLIAAFENGVI 627
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1052-1279 |
7.82e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 143.62 E-value: 7.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYP--TRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRntkTLNIQ--W-L 1126
Cdd:PRK13635 6 IRVEHISFRYPdaATY---ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEEtvWdV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1127 RAQIGIVSQEPilfD-----CTIAENIAYGDNSREVSHEEIV----SAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQ 1197
Cdd:PRK13635 80 RRQVGMVFQNP---DnqfvgATVQDDVAFGLENIGVPREEMVervdQALRQVGMEDFLNREP-----------HRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1198 KQRIAIARALIRQPRILLLDEATSALDTESEkivQEALD-----KAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQG 1272
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
....*..
gi 2024474312 1273 THQQLLA 1279
Cdd:PRK13635 223 TPEEIFK 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
429-1289 |
9.09e-38 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 155.32 E-value: 9.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 429 KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTItidgqdlkslnvrYLREIIGVVNQEPVLFATTIAEN 508
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 509 IRYGREdvtmeeiERATKEANAYDF------IMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSAL 582
Cdd:PTZ00243 741 ILFFDE-------EDAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 583 DTE-SESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMeQKGVYYKlvnMQASETEDQlqeE 661
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYAT---LAAELKENK---D 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 662 GNASSVSEEALNGSVLTGQKRQSTRKSIKRVRIQNDELDVKADqldknmPPSSFFKIMKLNKT---EWPYFVV-----GT 733
Cdd:PTZ00243 887 SKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALD------AAAGRLMTREEKASgsvPWSTYVAylrfcGG 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 734 LCAIinGALQPIFSVM----ISDVI--GMFVEKGkaaIRETNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRS 807
Cdd:PTZ00243 961 LHAA--GFVLATFAVTelvtVSSGVwlSMWSTRS---FKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHR 1035
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 808 MAFRAILRQEISWFDepKNSTGELITRLANDAsqvkGATGSRLALVAQNIANLGTGIVLS-LIYGWQLTLLLLAIVPIia 886
Cdd:PTZ00243 1036 DLLRSVSRGTMSFFD--TTPLGRILNRFSRDI----DILDNTLPMSYLYLLQCLFSICSSiLVTSASQPFVLVALVPC-- 1107
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 887 itGMIQMKMLAGHAKKDKkELETLGKVA--------SEAIENIRTVVA------LTQE--RKFEYMYG-QNLQ-VSYRns 948
Cdd:PTZ00243 1108 --GYLYYRLMQFYNSANR-EIRRIKSVAkspvftllEEALQGSATITAygkahlVMQEalRRLDVVYScSYLEnVANR-- 1182
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 949 ikkahIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHmrfkDVLLVFSAIVFGAMALGQSTSFTPDYA--KAKMSAAHLF 1026
Cdd:PTZ00243 1183 -----WLGVRVEFLSNIVVTVIALIGVIGTMLRATSQ----EIGLVSLSLTMAMQTTATLNWLVRQVAtvEADMNSVERL 1253
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1027 LLF------ERVPLIDSY-----SEEGEKPKMFG-------------------GNITFKDVAFKY----PTrpevkVLQG 1072
Cdd:PTZ00243 1254 LYYtdevphEDMPELDEEvdaleRRTGMAADVTGtvviepasptsaaphpvqaGSLVFEGVQMRYreglPL-----VLRG 1328
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1073 LNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIAENIaygD 1152
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---D 1405
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1153 NSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALI-RQPRILLLDEATSALDTESEKIV 1231
Cdd:PTZ00243 1406 PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQI 1485
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1232 QEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQL-LAEKGFYYSLVN 1289
Cdd:PTZ00243 1486 QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVE 1544
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1052-1273 |
1.04e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 145.33 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPT-RPEVKVLQGLNIEVEKGQTLALVGSSGCGKST---VVQLLERfydPLSGEVLLDGRNTKTLNIQWLR 1127
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 A---QIGIVSQE-PILFDCTIAENIAYGdnsrevshEEIVSAAKAAnIHSFIESLPKkyntRVG--DKG----AQLSGGQ 1197
Cdd:PRK11153 79 KarrQIGMIFQHfNLLSSRTVFDNVALP--------LELAGTPKAE-IKARVTELLE----LVGlsDKAdrypAQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1198 KQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKA-RE-GRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGT 1273
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1052-1280 |
4.41e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.22 E-value: 4.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWLRAQIG 1131
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQE-------PIlfdcTIAENIAYG--------DNSREVSHEEIVSAAKAANIHSFIeslpkkyNTRVGdkgaQLSGG 1196
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMGrygrrglfRRPSRADREAVDEALERVGLEDLA-------DRPIG----ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTI-QNADKIAVIqNGKVIEQGTH 1274
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*.
gi 2024474312 1275 QQLLAE 1280
Cdd:COG1121 223 EEVLTP 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1069-1278 |
5.18e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 139.78 E-value: 5.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlRAQIGIVSQEPILF-DCTIAEN 1147
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1148 IAYGDNSREVSHEEIvsAAKAANIHSF--IESLPKKYNTRvgdkgaqLSGGQKQRIAIARALIRQPRILLLDEATSALDT 1225
Cdd:cd03299 92 IAYGLKKRKVDKKEI--ERKVLEIAEMlgIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1226 ESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:cd03299 163 RTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1061-1280 |
5.34e-37 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 142.50 E-value: 5.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1061 YPTRP-EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPL---SGEVLLDGRNTKTLN---IQWLR-AQIGI 1132
Cdd:COG0444 11 FPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeLRKIRgREIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1133 VSQEPI-----LFdcTIAENIA-----YGDNSREVSHEEIVSAAKAANIH---SFIESLPKkyntrvgdkgaQLSGGQKQ 1199
Cdd:COG0444 91 IFQDPMtslnpVM--TVGDQIAeplriHGGLSKAEARERAIELLERVGLPdpeRRLDRYPH-----------ELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1200 RIAIARALIRQPRILLLDEATSALDTesekIVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQG 1272
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEG 233
|
....*...
gi 2024474312 1273 THQQLLAE 1280
Cdd:COG0444 234 PVEELFEN 241
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1048-1288 |
7.16e-37 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 140.04 E-value: 7.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1048 FGGNITFKDVAFKYPT--RPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQW 1125
Cdd:cd03288 16 LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1126 LRAQIGIVSQEPILFDCTIAENIaygDNSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIAR 1205
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEK-GFY 1284
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
....
gi 2024474312 1285 YSLV 1288
Cdd:cd03288 250 ASLV 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1052-1277 |
1.90e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 141.75 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWLRAQ-- 1129
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-----VTDLPPKdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 -IGIVSQEPILFD-CTIAENIAYGDNSREVSHEEI----VSAAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAI 1203
Cdd:COG3839 76 nIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIdrrvREAAELLGLEDLLDRKPK-----------QLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1204 ARALIRQPRILLLDEATSALD------TESE-KIVQEALdkareGRTCIVIAHRLS---TIqnADKIAVIQNGKVIEQGT 1273
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
....
gi 2024474312 1274 HQQL 1277
Cdd:COG3839 218 PEEL 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1052-1277 |
2.21e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 138.27 E-value: 2.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpeVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN---IQWLRA 1128
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPILFD-CTIAENI---AYGDNS------REVSHEEIVSAAKAanihsfIES--LPKKYNTRVGdkgaQLSGG 1196
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERALEA------LERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGT 1273
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGP 230
|
....
gi 2024474312 1274 HQQL 1277
Cdd:COG3638 231 PAEL 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
414-632 |
2.66e-36 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 141.09 E-value: 2.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 414 EFQNVFFSYP-ARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-- 490
Cdd:PRK11153 3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 -IGVVNQEPVLFAT-TIAENIRYGRE--DVTMEEIERATKE----------ANAYdfimklPkkfetvvgergAQMSGGQ 556
Cdd:PRK11153 83 qIGMIFQHFNLLSSrTVFDNVALPLElaGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 557 KQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGT 632
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
427-627 |
2.69e-36 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 136.89 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDL--KSLNVRYLREIIGVVNQEPVLFA-T 503
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPhL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENIRYGRedVTMEEIERATKEANAYDFIMKlpkkfetvVG------ERGAQMSGGQKQRIAIARALVRNPKILLLDE 577
Cdd:cd03262 92 TVLENITLAP--IKVKGMSKAEAEERALELLEK--------VGladkadAYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 578 ATSALDTEsesVVQAALDKIR----KGRTILVIAHRLSTVRN-ADLIAAFENGVI 627
Cdd:cd03262 162 PTSALDPE---LVGEVLDVMKdlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
142-383 |
3.53e-36 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 139.22 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 142 IGAGVLFAA--YIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVA 219
Cdd:cd07346 46 LLLALLRALlsYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 220 TFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQ 299
Cdd:cd07346 126 TLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 300 KNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGkVFTVFFSILVGAFS-VGQAAPSMEAFAN 378
Cdd:cd07346 206 EANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG-ELVAFLAYLGMLFGpIQRLANLYNQLQQ 284
|
....*
gi 2024474312 379 ARGAA 383
Cdd:cd07346 285 ALASL 289
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
414-640 |
4.76e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.20 E-value: 4.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 414 EFQNVFFSYParPDIK-ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK13632 9 KVENVSFSYP--NSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEP--VLFATTIAENIRYGRED--VTMEE----IERATKEANAYDFIMKLPKKfetvvgergaqMSGGQKQRIAIAR 564
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENkkVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKIRKGR--TILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQK 640
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
135-648 |
5.63e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 149.36 E-value: 5.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 135 YAYYYSGIGAGVLfAAYIQVSFWTLAAG-RQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAM 213
Cdd:PLN03232 952 YIVVYALLGFGQV-AVTFTNSFWLISSSlHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 214 F----FQAVATFFTGFIVGFTKGWK-LTLVILALSPVLGF-SSALWAKIISTFTNKELtaYAKAGavaeEVLAAVRTVVA 287
Cdd:PLN03232 1031 FmnqlWQLLSTFALIGTVSTISLWAiMPLLILFYAAYLYYqSTSREVRRLDSVTRSPI--YAQFG----EALNGLSSIRA 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 288 FGGQRKETERYQKNLEDAKRMGIQK-------AISANISMGVSFFLI-------YGSYALAFWYGTILVLSEDYTIgKVF 353
Cdd:PLN03232 1105 YKAYDRMAKINGKSMDNNIRFTLANtssnrwlTIRLETLGGVMIWLTatfavlrNGNAENQAGFASTMGLLLSYTL-NIT 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 354 TVFFSILVGAFSVGQAAPSMEAFANARGAAYAIFNIIDNEPQIdsssnAGYKLdhvKGNLEFQNVFFSYpaRPDIK-ILK 432
Cdd:PLN03232 1184 TLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPV-----SGWPS---RGSIKFEDVHLRY--RPGLPpVLH 1253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 433 GLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYG 512
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPF 1333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 513 RE--DVTMEEierATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVV 590
Cdd:PLN03232 1334 SEhnDADLWE---ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 591 QAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKG-VYYKLVN 648
Cdd:PLN03232 1411 QRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVH 1469
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
413-641 |
6.21e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 136.91 E-value: 6.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIiG 492
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFAT-TIAENIRYGRE--DVTMEEIERATKEAnAYDFIMKLPKKfetvvgERGAQMSGGQKQRIAIARALVRN 569
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEEL-IELLGLEEFLD------RRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 570 PKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQKG 641
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
729-986 |
7.58e-36 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 138.07 E-value: 7.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKaaiRETNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSM 808
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD---LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 809 AFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAIT 888
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 889 GMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYF 968
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250
....*....|....*...
gi 2024474312 969 TYAGCFRFGAYLVKNGHM 986
Cdd:cd07346 236 GTALVLLYGGYLVLQGSL 253
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1052-1268 |
8.87e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 134.06 E-value: 8.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwLRAQIG 1131
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILF-DCTIAENIaygdnsrevsheeivsaakaanihsfieslpkkyntrvgdkgaQLSGGQKQRIAIARALIRQ 1210
Cdd:cd03230 77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1211 PRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKV 1268
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
730-986 |
1.06e-35 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 137.77 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 730 VVGTLCAIingALQPIFSVMISDVIGMFVEKGKAAIRETNsTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMA 809
Cdd:cd18780 6 LVSSGTNL---ALPYFFGQVIDAVTNHSGSGGEEALRALN-QAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 810 FRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITG 889
Cdd:cd18780 82 FSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 890 MIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFT 969
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLA 239
|
250
....*....|....*..
gi 2024474312 970 YAGCFRFGAYLVKNGHM 986
Cdd:cd18780 240 IVLVLWYGGRLVIDGEL 256
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
413-639 |
1.07e-35 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 138.65 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARP-DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK---EGTITIDGQDLKSLNVRYLR 488
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 489 EI----IGVVNQEPvlFA---------TTIAENIRYgREDVTMEEIERATKEA-------NAYDFIMKLPKkfetvvger 548
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRI-HGGLSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 549 gaQMSGGQKQRIAIARALVRNPKILLLDEATSALDTesesVVQAA----LDKIRK--GRTILVIAHRLSTVRN-ADLIAA 621
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQilnlLKDLQRelGLAILFITHDLGVVAEiADRVAV 223
|
250
....*....|....*...
gi 2024474312 622 FENGVITEQGTHDELMEQ 639
Cdd:COG0444 224 MYAGRIVEEGPVEELFEN 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
413-625 |
1.19e-35 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 134.52 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDI--KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlkslnvrylrei 490
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEPVLFATTIAENIRYGREdvtMEEiERatkeanaYDFIMK----------LPKKFETVVGERGAQMSGGQKQRI 560
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP---FDE-ER-------YEKVIKacalepdleiLPDGDLTEIGEKGINLSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 561 AIARALVRNPKILLLDEATSALDTES-----ESVVQAALdkiRKGRTILVIAHRLSTVRNADLIAAFENG 625
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
130-383 |
1.23e-35 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 137.67 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 130 EEMTRYAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGE 209
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 210 KIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFG 289
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 290 GQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKV--FTVFFSILVGAF-SV 366
Cdd:cd18572 193 TEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLvtFMLYQQQLGEAFqSL 272
|
250
....*....|....*..
gi 2024474312 367 GQAAPSMeafANARGAA 383
Cdd:cd18572 273 GDVFSSL---MQAVGAA 286
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
413-639 |
1.67e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 1.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylreiIG 492
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVL---FATTIAENI------------RYGREDVtmEEIERATKEANAYDFIMKLpkkfetvVGErgaqMSGGQK 557
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgrygrrglfrRPSRADR--EAVDEALERVGLEDLADRP-------IGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 558 QRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTVR-NADLIAAFENGVITEqGTHDE 635
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEE 224
|
....
gi 2024474312 636 LMEQ 639
Cdd:COG1121 225 VLTP 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1074-1280 |
1.83e-35 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 136.23 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1074 NIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRA----QIGIVSQEPILF-DCTIAENI 1148
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 AYGDNSREVSHEEIVSAA----KAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIARALIRQPRILLLDEATSALD 1224
Cdd:cd03294 124 AFGLEVQGVPRAEREERAaealELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1225 TESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
413-629 |
1.03e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.48 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN---VRYLRE 489
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQE-PVLFATTIAENIRY-----GREDvtmEEIERATKEA----NAYDFIMKLPkkfetvvgergAQMSGGQKQR 559
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREVldlvGLSDKAKALP-----------HELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 560 IAIARALVRNPKILLLDEATSALDTE-SESVVQaALDKI-RKGRTILVIAHrlstvrNADLIAAF-------ENGVITE 629
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPEtSWEIME-LLEEInRRGTTVLIATH------DLELVDRMpkrvlelEDGRLVR 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
413-656 |
1.05e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 133.62 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYD--PK---EGTITIDGQDL--KSLNVR 485
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 486 YLREIIGVVNQEPVLFATTIAENIRYG------REDVTMEEI-ERATKEANAYDfimklpkkfEtvVGER----GAQMSG 554
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWD---------E--VKDRlkksALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 555 GQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLS-TVRNADLIAAFENGVITEQGTH 633
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFGPT 237
|
250 260
....*....|....*....|...
gi 2024474312 634 DELMEqkgvyyklvNMQASETED 656
Cdd:COG1117 238 EQIFT---------NPKDKRTED 251
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1052-1281 |
1.32e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 133.08 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDG---RNTKTLNIQWLRA 1128
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdiNKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPILFD-CTIAENI---AYGDNS------REVSHEEIVSAAKAanihsfIES--LPKKYNTRVGdkgaQLSGG 1196
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVlsgRLGRRStwrslfGLFPKEEKQRALAA------LERvgLLDKAYQRAD----QLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEAL-DKARE-GRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGT 1273
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGP 228
|
....*...
gi 2024474312 1274 HQQLLAEK 1281
Cdd:cd03256 229 PAELTDEV 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1052-1268 |
1.39e-34 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 131.88 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR--NTKTLNIQWLRAQ 1129
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLklTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 IGIVSQEPILF-DCTIAENIAYGdnSREVSHeeiVSAAKAanihsfiESLPKKYNTRVG--DKG----AQLSGGQKQRIA 1202
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENITLA--PIKVKG---MSKAEA-------EERALELLEKVGlaDKAdaypAQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1203 IARALIRQPRILLLDEATSALDTEsekIVQEALDK----AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKV 1268
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
138-641 |
2.65e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 143.73 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 138 YYSGIGAGVLFAayiQV------SFW----TLAAGrqiKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGI 207
Cdd:PLN03130 954 FYNLIYALLSFG---QVlvtllnSYWlimsSLYAA---KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNV 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 208 GEKIAMF----FQAVATFFTGFIVGFTKGWK-LTLVILALSPVLGF-SSALWAKIISTFTNKELtaYAKAGavaeEVLAA 281
Cdd:PLN03130 1028 AVFVNMFlgqiFQLLSTFVLIGIVSTISLWAiMPLLVLFYGAYLYYqSTAREVKRLDSITRSPV--YAQFG----EALNG 1101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 282 VRTVVAFGGQRKETERYQKNLEDAKRMGIQKaISANISMGVSFFLIYGsyaLAFWY-GTILVL----SEDY-----TIGK 351
Cdd:PLN03130 1102 LSTIRAYKAYDRMAEINGRSMDNNIRFTLVN-MSSNRWLAIRLETLGG---LMIWLtASFAVMqngrAENQaafasTMGL 1177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 352 VFTVFFSILVGAFSVGQAAPSMEAFANA--RGAAY------AIFNIIDNEPQIDSSSNagykldhvkGNLEFQNVFFSYp 423
Cdd:PLN03130 1178 LLSYALNITSLLTAVLRLASLAENSLNAveRVGTYidlpseAPLVIENNRPPPGWPSS---------GSIKFEDVVLRY- 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 424 aRPDIK-ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFA 502
Cdd:PLN03130 1248 -RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFS 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 503 TTIAENIRYGRE--DVTM-EEIERAtkeaNAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEAT 579
Cdd:PLN03130 1327 GTVRFNLDPFNEhnDADLwESLERA----HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 580 SALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKG 641
Cdd:PLN03130 1403 AAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1051-1279 |
2.72e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.80 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1051 NITFKDVAFKYPTRPevkvLQgLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIqwlrAQ- 1129
Cdd:COG3840 1 MLRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AEr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 -IGIVSQEPILFD-CTIAENIAYGDNSR----EVSHEEIVSAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAI 1203
Cdd:COG3840 72 pVSMLFQENNLFPhLTVAQNIGLGLRPGlkltAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1204 ARALIRQPRILLLDEATSALD----TESEKIVQEALDkaREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
.
gi 2024474312 1279 A 1279
Cdd:COG3840 219 D 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1063-1279 |
3.17e-34 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 139.43 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1063 TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFyDPLSGEVLLDGRNTKTLN---IQWLRAQIGIVSQEPil 1139
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1140 FDC-----TIAENIAYG--DNSREVSHEEIVSAAKAAnihsfiesLpkkynTRVG-DKGA------QLSGGQKQRIAIAR 1205
Cdd:COG4172 372 FGSlsprmTVGQIIAEGlrVHGPGLSAAERRARVAEA--------L-----EEVGlDPAArhryphEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1206 ALIRQPRILLLDEATSALDteseKIVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:COG4172 439 ALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
.
gi 2024474312 1279 A 1279
Cdd:COG4172 515 D 515
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
413-640 |
3.41e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 131.92 E-value: 3.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPArpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-- 490
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 -IGVVNQEPVLFA-TTIAENIRYGRED-----------VTMEEIERATKEANAYDfimkLPKKFETvvgeRGAQMSGGQK 557
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRLGrrstwrslfglFPKEEKQRALAALERVG----LLDKAYQ----RADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 558 QRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAHRLSTVR-NADLIAAFENGVITEQGTHD 634
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
....*.
gi 2024474312 635 ELMEQK 640
Cdd:cd03256 231 ELTDEV 236
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
767-986 |
5.10e-34 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 133.02 E-value: 5.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 767 ETNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGAT 846
Cdd:cd18573 38 LSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD--KNKTGELVSRLSSDTSVVGKSL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 847 GSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMI---QMKMLAghaKKDKKELETLGKVASEAIENIRT 923
Cdd:cd18573 116 TQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFygrYVRKLS---KQVQDALADATKVAEERLSNIRT 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 924 VVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18573 193 VRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGEL 255
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
396-647 |
5.46e-34 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 131.95 E-value: 5.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 396 IDSSSNAGykLDHVKGNLEFQNVFFSYPA--RPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTIT 473
Cdd:cd03288 5 ISGSSNSG--LVGLGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 474 IDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENIRYGREdVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMS 553
Cdd:cd03288 80 IDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 554 GGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTH 633
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTP 238
|
250
....*....|....*
gi 2024474312 634 DELMEQK-GVYYKLV 647
Cdd:cd03288 239 ENLLAQEdGVFASLV 253
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
413-628 |
7.92e-34 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 129.84 E-value: 7.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVR---YLRE 489
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQEPVLFAT-TIAENIRYgredvTMEEIERATKEANAydfimKLPKKFEtVVGERG------AQMSGGQKQRIAI 562
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAF-----ALEVTGVPPREIRK-----RVPAALE-LVGLSHkhralpAELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 563 ARALVRNPKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHrlstvrNADLIAAFENGVIT 628
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATH------AKELVDTTRHRVIA 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1054-1272 |
8.37e-34 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 129.58 E-value: 8.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1054 FKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWLRAQIGIV 1133
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1134 SQEPIL---FDCTIAENIAYGDNSReVSHEEIVSAAKAANIHSFIEslpkkyntRVGDKG------AQLSGGQKQRIAIA 1204
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGH-KGLFRRLSKADKAKVDEALE--------RVGLSEladrqiGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1205 RALIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVIqNGKVIEQG 1272
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
414-627 |
1.13e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 129.19 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 414 EFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlkslNVRYLREIIGV 493
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 494 VNQEPVL---FATTIAENI------------RYGREDvtMEEIERATKEANAYDFIMKlpkkfetvvgeRGAQMSGGQKQ 558
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmglyghkglfrRLSKAD--KAKVDEALERVGLSELADR-----------QIGELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 559 RIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAHRLSTV-RNADLIAAFENGVI 627
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
413-639 |
1.15e-33 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 130.05 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLksLNVRYLREIIG 492
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFA-TTIAENIRYG--REDVTMEEIERATKEAnaydfiMKLpKKFETVVGERGAQMSGGQKQRIAIARALVRN 569
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrLKKLPKAEIKERVAEA------LDL-VQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 570 PKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLS---TVrnADLIAAFENGVITEQGTHDELMEQ 639
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
413-639 |
1.21e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYP--ARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI 490
Cdd:PRK13635 6 IRVEHISFRYPdaATY---ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEP--VLFATTIAENIRYGREDVTM---EEIER---ATKEANAYDFIMKLPkkfetvvgergAQMSGGQKQRIAI 562
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLENIGVpreEMVERvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 563 ARALVRNPKILLLDEATSALDTESEsvvQAALDKIR-----KGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELM 637
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGR---REVLETVRqlkeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
..
gi 2024474312 638 EQ 639
Cdd:PRK13635 229 KS 230
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
729-986 |
1.29e-33 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 131.51 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALqPIF-SVMISDVIGMfveKGKAAIRETNSTYALLFLGFGLISFvtffLQGFTFGKAGEILTMRLRS 807
Cdd:cd18572 2 FVFLVVAALSELAI-PHYtGAVIDAVVAD---GSREAFYRAVLLLLLLSVLSGLFSG----LRGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 808 MAFRAILRQEISWFDEpkNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAI 887
Cdd:cd18572 74 DLFRSLLRQDIAFFDA--TKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 888 T----GMIQMKMLaghakkdKKELETLGK---VASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFA 960
Cdd:cd18572 152 ItkvyGRYYRKLS-------KEIQDALAEanqVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVA 224
|
250 260
....*....|....*....|....*.
gi 2024474312 961 FTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18572 225 VNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
413-638 |
1.50e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.18 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPArpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-- 490
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 -IGVVNQEPVLFA-TTIAENI----------------RYGREDVT--MEEIERatkeanaydfimklpkkfetvVG---- 546
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVlagrlgrtstwrsllgLFPPEDREraLEALER---------------------VGladk 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 547 --ERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAHRLSTVRN-ADLIAA 621
Cdd:COG3638 140 ayQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRyADRIIG 219
|
250 260
....*....|....*....|..
gi 2024474312 622 FENGVI-----TEQGTHDELME 638
Cdd:COG3638 220 LRDGRVvfdgpPAELTDAVLRE 241
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1063-1280 |
1.62e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 132.55 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1063 TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN---IQWLRAQIGIVSQEPil 1139
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1140 FDC-----TIAENIAYG-DNSREVSHEEivsaaKAANIHSFIEslpkkyntRVGDKGA-------QLSGGQKQRIAIARA 1206
Cdd:COG4608 105 YASlnprmTVGDIIAEPlRIHGLASKAE-----RRERVAELLE--------LVGLRPEhadryphEFSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1207 LIRQPRILLLDEATSALDteseKIVQ-------EALdKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:COG4608 172 LALNPKLIVCDEPVSALD----VSIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELY 246
|
..
gi 2024474312 1279 AE 1280
Cdd:COG4608 247 AR 248
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1052-1268 |
1.74e-33 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 128.68 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN---IQWLRA 1128
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQE-PILFDCTIAENIAYGDNSREVSHEEIVSAAKAA----NIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAI 1203
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1204 ARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADK--IAVIQNGKV 1268
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1069-1277 |
1.96e-33 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 129.28 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTktLNIQWLRAQIGIVSQEPILF-DCTIAEN 1147
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1148 IAYGDNSREVSHEEIVSAAKAANIHSFIESLPKKYNtrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTES 1227
Cdd:cd03300 93 IAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKP-------SQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1228 EKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQL 1277
Cdd:cd03300 166 RKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
433-639 |
1.98e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 132.16 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 433 GLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI---IGVVNQEPvlFA------- 502
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--YAslnprmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 503 --TTIAENIRYgREDVTMEEIERATKEA------NAyDFIMKLPKKFetvvgergaqmSGGQKQRIAIARALVRNPKILL 574
Cdd:COG4608 114 vgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 575 LDEATSALDtesesV-VQAA----LDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQ 639
Cdd:COG4608 181 CDEPVSALD-----VsIQAQvlnlLEDLQDelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1052-1279 |
4.41e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 129.85 E-value: 4.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVSAAKAA----NIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIAR 1205
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
435-639 |
6.98e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 128.92 E-value: 6.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 435 NLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI----IGVVNQEPVLFA-TTIAENI 509
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 RYGREDVTMEEIERATKEANAY------DFIMKLPKkfetvvgergaQMSGGQKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALelvgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 584 TESESVVQAALDKIRK--GRTILVIAHRLS-TVRNADLIAAFENGVITEQGTHDELMEQ 639
Cdd:cd03294 193 PLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
427-638 |
9.77e-33 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 126.78 E-value: 9.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRY-LREIIGVVNQEPVLFAT-T 504
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 505 IAENIRYGREDVTMEEIERATKEAnaYDFIMKLPKKFETvvgeRGAQMSGGQKQRIAIARALVRNPKILLLDEATSALdt 584
Cdd:cd03224 92 VEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQ----LAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL-- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 585 eSESVVQ---AALDKIRK-GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELME 638
Cdd:cd03224 164 -APKIVEeifEAIRELRDeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
414-631 |
1.11e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 125.24 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 414 EFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGV 493
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 494 VNQepvlfattiaenirygredvtmeeierATKEANAYDFIMKLpkkFETvvgergaqMSGGQKQRIAIARALVRNPKIL 573
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 574 LLDEATSALDTESEsvvQAALDKIRK-----GRTILVIAHRLS-TVRNADLIAAFENGVITEQG 631
Cdd:cd03214 120 LLDEPTSHLDIAHQ---IELLELLRRlarerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1065-1272 |
1.23e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.99 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNI-QWLRAQIGIVSQEPILF-DC 1142
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1143 TIAENIAYGDNSRE---VSHEEIVSAAKAAnihsfIESL-----PkkyNTRVGDkgaqLSGGQKQRIAIARALIRQPRIL 1214
Cdd:COG1129 95 SVAENIFLGREPRRgglIDWRAMRRRAREL-----LARLgldidP---DTPVGD----LSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1215 LLDEATSAL-DTESE---KIVQEaLdkAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:COG1129 163 ILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTG 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1073-1272 |
1.63e-32 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 125.87 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1073 LNIEVE-KGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR----NTKTLNIQWLRAQIGIVSQEPILF-DCTIAE 1146
Cdd:cd03297 15 LKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1147 NIAYG-----DNSREVSHEEIVSAAKaanihsfIESLPKKYNtrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATS 1221
Cdd:cd03297 95 NLAFGlkrkrNREDRISVDELLDLLG-------LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1222 ALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:cd03297 161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1055-1269 |
2.23e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 125.45 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1055 KDVAFKYptRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKtlniQWLRAQ-IGIV 1133
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK----AKERRKsIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1134 SQEP--ILFDCTIAENIAYGDNSREVSHEEIVSAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIARALIRQP 1211
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVI 1269
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1052-1262 |
4.13e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 124.51 E-value: 4.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWlRAQIG 1131
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILF-DCTIAENIA-----YGdnsREVSHEEIVSAAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIAR 1205
Cdd:COG4133 79 YLGHADGLKpELTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIA-HRLSTIQNADKIAV 1262
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1067-1273 |
9.82e-32 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 124.47 E-value: 9.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1067 VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwLRAQIGIVS--QEPILF-DCT 1143
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIA--------YGDNSREVSHEEIVSAAKAANIHSFIEsLPKKYNTRVGDkgaqLSGGQKQRIAIARALIRQPRILL 1215
Cdd:cd03219 92 VLENVMvaaqartgSGLLLARARREEREARERAEELLERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1216 LDEATSAL-DTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGT 1273
Cdd:cd03219 167 LDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
123-383 |
1.25e-31 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 126.06 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 123 LILGEL----EEEMTRYAYYYSGIGAGVLFAA-----YIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELN 193
Cdd:cd18576 17 LLAGQLidaaLGGGDTASLNQIALLLLGLFLLqavfsFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 194 TRIVDDISKINEGIGEKIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGA 273
Cdd:cd18576 97 SRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 274 VAEEVLAAVRTVVAFGGQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVF 353
Cdd:cd18576 177 IVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLV 256
|
250 260 270
....*....|....*....|....*....|.
gi 2024474312 354 T-VFFSILVGAfSVGQAAPSMEAFANARGAA 383
Cdd:cd18576 257 AfLLYTLFIAG-SIGSLADLYGQLQKALGAS 286
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
431-638 |
1.28e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 124.37 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylREIIGVVNQEPVLFA-TTIAENI 509
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 RYG--REDVTMEEIERATKEANAYDFIMK-LPKKFETvvgergaqMSGGQKQRIAIARALVRNPKILLLDEATSALDTES 586
Cdd:cd03299 93 AYGlkKRKVDKKEIERKVLEIAEMLGIDHlLNRKPET--------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 587 ESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELME 638
Cdd:cd03299 165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
413-638 |
1.31e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.43 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLK--SLNVRYLREI 490
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEPVLFATTIA-ENIRYGREDVtmeeieRATKEANAYDFIMKLPKKfetvVG--ERG----AQMSGGQKQRIAIA 563
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGPLRV------RGASKEEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 564 RALVRNPKILLLDEATSALDTE-SESVVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELME 638
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
413-583 |
1.44e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.50 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYlREIiG 492
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLF-ATTIAENIRYG--REDVTMEEIERATKEANAydfIMKLpkkfETVVGERGAQMSGGQKQRIAIARALVRN 569
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAAE---LLGL----EDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170
....*....|....
gi 2024474312 570 PKILLLDEATSALD 583
Cdd:COG3839 152 PKVFLLDEPLSNLD 165
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
412-637 |
1.59e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 123.71 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 412 NLEFQNVFFSYPARPdikilKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVrYLREIi 491
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFA-TTIAENI--------RYGREDVtmEEIERATKEANAYDFIMKLPkkfetvvgergAQMSGGQKQRIAI 562
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIglglrpglKLTAEQR--AQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 563 ARALVRNPKILLLDEATSALDtesesvvqAAL--------DKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQG 631
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALD--------PALrqemldlvDELCRerGLTVLMVTHDPEDAARiADRVLLVADGRIAADG 212
|
....*.
gi 2024474312 632 THDELM 637
Cdd:COG3840 213 PTAALL 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1069-1271 |
2.29e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.37 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlRAQIGIVSQEPILF-DCTIAEN 1147
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1148 IAYGDNSREVSHEEIVS----AAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:PRK09452 107 VAFGLRMQKTPAAEITPrvmeALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1224 DTESEKIVQEALdKA--RE-GRTCIVIAH-RLSTIQNADKIAVIQNGKvIEQ 1271
Cdd:PRK09452 176 DYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGR-IEQ 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1060-1277 |
2.48e-31 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 123.00 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1060 KYPTRPeVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTlNIQWLRAQIGIVSQEPIL 1139
Cdd:cd03263 9 TYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1140 FD-CTIAENIAYGDNSREVSHEEIvsaakAANIHSFIE--SLPKKYNTRVGDkgaqLSGGQKQRIAIARALIRQPRILLL 1216
Cdd:cd03263 87 FDeLTVREHLRFYARLKGLPKSEI-----KEEVELLLRvlGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1217 DEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQL 1277
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
675-1284 |
2.88e-31 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 133.92 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 675 SVLTGQKRQSTRKSIKRVRI--QNDELDVKADQLDKNmppSSFFKImkLNKTEWPYFVVGTLCAIINGALQPIFSVMISD 752
Cdd:TIGR00957 268 SAVYGKKDPSKPKGSSQLDAneEVEALIVKSPHKPRK---PSLFKV--LYKTFGPYFLMSFCFKAIHDLMMFIGPQILSL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 753 VIGmFVEKGKAAIRETNSTYALLFLGFGLISFV--TFFLQGFTFGkageiltMRLRSMAFRAILRQEISWFDEPKNST-- 828
Cdd:TIGR00957 343 LIR-FVNDPMAPDWQGYFYTGLLFVCACLQTLIlhQYFHICFVSG-------MRIKTAVMGAVYRKALVITNSARKSStv 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 829 GELITRLANDASQVKGatgsrLALVAQNIANLGTGIVLSLIYGWQ-LTLLLLA----IVPIIAITGMIQMKMLAGHAKKD 903
Cdd:TIGR00957 415 GEIVNLMSVDAQRFMD-----LATYINMIWSAPLQVILALYFLWLnLGPSVLAgvavMVLMVPLNAVMAMKTKTYQVAHM 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 904 KKELETLgKVASEAIENIRTVVALTQERKF----EYMYGQNLQVsyrnsIKKAHIFGFTFAFTQAIMYFTYAGC-FRFGA 978
Cdd:TIGR00957 490 KSKDNRI-KLMNEILNGIKVLKLYAWELAFldkvEGIRQEELKV-----LKKSAYLHAVGTFTWVCTPFLVALItFAVYV 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 979 YLVKNGHMRFKDV---LLVFSAIVFGAMALGQSTSftpDYAKAKMSAAHL--FLLFERvplIDSYSEEGEKPKMFGGN-I 1052
Cdd:TIGR00957 564 TVDENNILDAEKAfvsLALFNILRFPLNILPMVIS---SIVQASVSLKRLriFLSHEE---LEPDSIERRTIKPGEGNsI 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1053 TFKDVAFKYpTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGrntktlniqwlraQIGI 1132
Cdd:TIGR00957 638 TVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAY 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1133 VSQEPILFDCTIAENIAYGDNSREVSHEEIVsaaKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPR 1212
Cdd:TIGR00957 704 VPQQAWIQNDSLRENILFGKALNEKYYQQVL---EACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1213 ILLLDEATSALDTESEKIVQEAL---DKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFY 1284
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1066-1280 |
3.24e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 122.54 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRN-TKTLNIQWLRAQIGIVSQEPILF-DCT 1143
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHERARAGIGYVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIAYGDNSREvsheeivSAAKAANIHSFIESLPKKYnTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:cd03224 92 VEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1224 dteSEKIVQE---ALDK-AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:cd03224 164 ---APKIVEEifeAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1288 |
4.24e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.08 E-value: 4.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYptRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVS----AAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIAR 1205
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERrveeALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQG-----THQQLL 1278
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250
....*....|
gi 2024474312 1279 AEKGFYYSLV 1288
Cdd:PRK13647 232 EQAGLRLPLV 241
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1066-1280 |
8.02e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 123.62 E-value: 8.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRN--TKTLNIQWLRAQIGIVSQEP--ILFD 1141
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1142 CTIAENIAYGDNSREVSHEEIVSAAKAAnihsfIESLPKKYNTrVGDKGA-QLSGGQKQRIAIARALIRQPRILLLDEAT 1220
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1221 SALDTeseKIVQEALDKARE-----GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK13637 173 AGLDP---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKE 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
413-639 |
1.12e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.87 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKS-LNVRYLReiI 491
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERR--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFA-TTIAENIRYG-----------REDVtMEEIER--ATKEANAYdfimklPkkfetvvgergAQMSGGQK 557
Cdd:COG1118 78 GFVFQHYALFPhMTVAENIAFGlrvrppskaeiRARV-EELLELvqLEGLADRY------P-----------SQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 558 QRIAIARALVRNPKILLLDEATSALDT----ESESVVQAALDKIrkGRTILVIAH-RLSTVRNADLIAAFENGVITEQGT 632
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
....*..
gi 2024474312 633 HDELMEQ 639
Cdd:COG1118 218 PDEVYDR 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1055-1281 |
1.28e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.49 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1055 KDVAFKYPTRPEVkvLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWL--RAQIGI 1132
Cdd:PRK13639 5 RDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1133 VSQEP--ILFDCTIAENIAYGDNSREVSHEEI----VSAAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIARA 1206
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVekrvKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1207 LIRQPRILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQ-NADKIAVIQNGKVIEQGTHQQLLAEK 1281
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1052-1277 |
1.53e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 121.81 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLSGEVLLDGRNT---KTLNI 1123
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1124 QwLRAQIGIVSQEPILFDCTIAENIAYG-----DNSREVSHEEIVSAAKAANIHSFIESlpkkyntRVGDKGAQLSGGQK 1198
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1199 QRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRL---STIqnADKIAVIQNGKVIEQGTHQ 1275
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTK 232
|
..
gi 2024474312 1276 QL 1277
Cdd:PRK14239 233 QM 234
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
130-350 |
2.09e-30 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 122.62 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 130 EEMTRYAYYYSGIGAGVL----FAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINE 205
Cdd:cd18573 34 EIFGLSLKTFALALLGVFvvgaAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 206 GIGEKIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTV 285
Cdd:cd18573 114 SLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTV 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 286 VAFGGQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIG 350
Cdd:cd18573 194 RAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVG 258
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
413-639 |
2.13e-30 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 127.49 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPAR--------PDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFyDPKEGTITIDGQDLKSLN- 483
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 484 --VRYLREIIGVVNQEPvlFAT-----TIAENIRYG----REDVTMEEIERATKEA-----------NAYdfimklPKKF 541
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRY------PHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 542 etvvgergaqmSGGQKQRIAIARALVRNPKILLLDEATSALDteseSVVQAA-LDKIRK-----GRTILVIAHRLSTVRN 615
Cdd:COG4172 427 -----------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDLLRDlqrehGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....*
gi 2024474312 616 -ADLIAAFENGVITEQGTHDELMEQ 639
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
413-636 |
2.24e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.12 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEP--VLFATTIAENIRYGRED--VTMEEIERATKEA----NAYDFIMKLPkkfetvvgergAQMSGGQKQRIAIAR 564
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKIRKGR--TILVIAHRLSTVRNADLIAAFENGVITEQGTHDEL 636
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
429-656 |
2.42e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 121.04 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 429 KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYD--PK---EGTITIDGQDLKSLNVRY--LREIIGVVNQEPVLF 501
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 502 ATTIAENIRYG-------REDVTMEEIERATKEANAYDFIMKlpKKFETVVGergaqMSGGQKQRIAIARALVRNPKILL 574
Cdd:PRK14239 99 PMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 575 LDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTV-RNADLIAAFENGVITEQG-THDELMeqkgvyyklvNMQAS 652
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNdTKQMFM----------NPKHK 241
|
....
gi 2024474312 653 ETED 656
Cdd:PRK14239 242 ETED 245
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
413-638 |
2.46e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 124.29 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKslNVRYLREIIG 492
Cdd:PRK09452 15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFA-TTIAENIRYG--REDVTMEEIERATKEAnaydfiMKLpKKFETVVGERGAQMSGGQKQRIAIARALVRN 569
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRM-VQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 570 PKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAH----RLSTvrnADLIAAFENGVITEQGTHDELME 638
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYE 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1057-1279 |
2.58e-30 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 127.49 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1057 VAFKYPTRpEVKVLQGLNIEVEKGQTLALVGSSGCGKS----TVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRA---- 1128
Cdd:COG4172 14 VAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPI-----LFdcTIAENIAygdnsrEV--SHEEIVSAAKAANIhsfIESLpkkynTRVGDKGA---------Q 1192
Cdd:COG4172 93 RIAMIFQEPMtslnpLH--TIGKQIA------EVlrLHRGLSGAAARARA---LELL-----ERVGIPDPerrldayphQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1193 LSGGQKQRIAIARALIRQPRILLLDEATSALDTesekIVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADKIAVIQN 1265
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQ 232
|
250
....*....|....
gi 2024474312 1266 GKVIEQGTHQQLLA 1279
Cdd:COG4172 233 GEIVEQGPTAELFA 246
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1070-1277 |
3.64e-30 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 120.14 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlRAQIGIVSQEPILF-DCTIAENI 1148
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 AYGDNSREVShEEIVSAAKAANIHSFI-----ESLPKKYNtrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:cd03296 96 AFGLRVKPRS-ERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1224 DTESEKIVQEALDKARE--GRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQL 1277
Cdd:cd03296 168 DAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
413-638 |
4.82e-30 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 119.70 E-value: 4.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNV-RYLREII 491
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFAT-TIAENIRYGREDVTMEEIERATKEAnAYDFimkLPkkfetVVGER----GAQMSGGQKQRIAIARAL 566
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLER-VYEL---FP-----RLKERrrqrAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 567 VRNPKILLLDEATSALdteSESVVQ---AALDKIRK-GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELME 638
Cdd:COG0410 152 MSRPKLLLLDEPSLGL---APLIVEeifEIIRRLNReGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1070-1226 |
5.61e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 118.74 E-value: 5.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDP---LSGEVLLDGRNTKTLNIQwlRAQIGIVSQEPILFD-CTIA 1145
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1146 ENIAYG---DNSREVSHEEIVSAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSA 1222
Cdd:COG4136 95 ENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
....
gi 2024474312 1223 LDTE 1226
Cdd:COG4136 164 LDAA 167
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1052-1278 |
5.62e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.43 E-value: 5.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR--NTKTLNIQWLRAQ 1129
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 IGIVSQEPILF-DCTIAENIAYGDNSrevsheeiVSAAKAANIHSFIESLPKKYN--TRVGDKGAQLSGGQKQRIAIARA 1206
Cdd:PRK09493 79 AGMVFQQFYLFpHLTALENVMFGPLR--------VRGASKEEAEKQARELLAKVGlaERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1207 LIRQPRILLLDEATSALDTEsekIVQEAL----DKAREGRTCIVIAHRlstIQNADKIA----VIQNGKVIEQGTHQQLL 1278
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPE---LRHEVLkvmqDLAEEGMTMVIVTHE---IGFAEKVAsrliFIDKGRIAEDGDPQVLI 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1052-1271 |
8.11e-30 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 118.13 E-value: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlRAQIG 1131
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILF-DCTIAENIAYGDNSREVSHEEIV----SAAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIARA 1206
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRKVPKDEIDervrEVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1207 LIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAH-RLSTIQNADKIAVIQNGKvIEQ 1271
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQ-IQQ 211
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
732-1004 |
1.06e-29 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 120.28 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 732 GTLCAIINGALQPIFSVMISDVIG-MFVEKGKAAIRetnsTYALLFLG-FGLISFVTFFlQGFTFGKAGEILTMRLRSMA 809
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDaALGGGDTASLN----QIALLLLGlFLLQAVFSFF-RIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 810 FRAILRQEISWFDEpkNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITG 889
Cdd:cd18576 76 YRHLQRLPLSFFHE--RRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 890 MIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERkFEYM-YGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYF 968
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLLFG 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 2024474312 969 TYAGCFRFGAYLVKNGHMRFKDV--LLVFSAIVFGAMA 1004
Cdd:cd18576 233 AIVAVLWYGGRLVLAGELTAGDLvaFLLYTLFIAGSIG 270
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1065-1269 |
1.20e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 115.99 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN-IQWLRAQIGIVSQepilfdct 1143
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 iaeniaygdnsrevsheeivsaakaanihsfieslpkkyntrvgdkgaqLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2024474312 1224 -DTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVI 1269
Cdd:cd03216 114 tPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
413-636 |
1.24e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.84 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEP--VLFATTIAENIRYGRED--VTMEEIERATKEA----NAYDFIMKLPkkfetvvgergAQMSGGQKQRIAIAR 564
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDEL 636
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
417-608 |
1.30e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 117.36 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 417 NVFFSYpaRPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSlnvRYLREIIGVVNQ 496
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 497 EP--VLFATTIAENIRYGREDV--TMEEIERATKEANAYDFIMKLPkkfetvvgergAQMSGGQKQRIAIARALVRNPKI 572
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELdaGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024474312 573 LLLDEATSALDTES-ESVVQAALDKIRKGRTILVIAH 608
Cdd:cd03226 148 LIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITH 184
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1050-1284 |
1.70e-29 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 119.19 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1050 GNITFKDVAFKYpTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDpLSGEVLLDGRNTKTLNIQWLRAQ 1129
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 IGIVSQEPILFDCTIAENIaygDNSREVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIR 1209
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNL---DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1210 QPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFY 1284
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1052-1289 |
2.18e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 119.13 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEvKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGE---VLLDGRNTKTLNIQWLRA 1128
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVSAAKAA----NIHSFIESLPkkyntrvgdkgAQLSGGQKQRIA 1202
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVladvGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1203 IARALIRQPRILLLDEATSALDTESE----KIVQEALDKarEGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGT----- 1273
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKeqilKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpveif 231
|
250 260
....*....|....*....|.
gi 2024474312 1274 -HQQLLAEKG----FYYSLVN 1289
Cdd:PRK13640 232 sKVEMLKEIGldipFVYKLKN 252
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1049-1272 |
2.93e-29 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 116.11 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1049 GGNITFKDVAF---KYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLL--ERFYDPLSGEVLLDGRNTKtlnI 1123
Cdd:cd03213 1 GVTLSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1124 QWLRAQIGIVSQEPILFDC-TIAENIAYgdnsrevsheeivsaakAANIHSfieslpkkyntrvgdkgaqLSGGQKQRIA 1202
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTlTVRETLMF-----------------AAKLRG-------------------LSGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1203 IARALIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLST--IQNADKIAVIQNGKVIEQG 1272
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
413-636 |
3.77e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.20 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPArpdIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-I 491
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFAT-TIAENIRYGREDVTM-----EEIERATKEANAYdfiMKLPKKFETVVGErgaqMSGGQKQRIAIARA 565
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRGglidwRAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 566 LVRNPKILLLDEATSALdTESEsvVQAALDKIR----KGRTILVIAHRLSTVRN-ADLIAAFENGVITEQG-----THDE 635
Cdd:COG1129 155 LSRDARVLILDEPTASL-TERE--VERLFRIIRrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDE 231
|
.
gi 2024474312 636 L 636
Cdd:COG1129 232 L 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1055-1279 |
5.85e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.89 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1055 KDVAFKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVS 1134
Cdd:PRK13642 8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1135 QEP--ILFDCTIAENIAYGDNSREVSHEEIV----SAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIARALI 1208
Cdd:PRK13642 88 QNPdnQFVGATVEDDVAFGMENQGIPREEMIkrvdEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1209 RQPRILLLDEATSALD----TESEKIVQEALDKARegRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1049-1266 |
8.28e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 123.38 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1049 GGNITFKDVAFkypTRPEVKVL-QGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDgRNTKTLniqwlr 1127
Cdd:COG4178 360 DGALALEDLTL---RTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP-AGARVL------ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 aqigIVSQEPILFDCTIAENIAYGDNSREVSHEEIVSAAKAANIHSFIESLpkkynTRVGDKGAQLSGGQKQRIAIARAL 1207
Cdd:COG4178 430 ----FLPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1208 IRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNG 1266
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
413-631 |
8.98e-29 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 115.04 E-value: 8.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVrYLREIiG 492
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP-KDRDI-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFA-TTIAENIRYG--REDVTMEEIERATKEANAydfIMKLpkkfETVVGERGAQMSGGQKQRIAIARALVRN 569
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQI----EHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 570 PKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAH-RLSTVRNADLIAAFENGVITEQG 631
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
430-636 |
9.50e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 116.39 E-value: 9.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTI-----TIDGQdlKSLN-----VRYLREIIGVVNQEPV 499
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 500 LFA-TTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKfETVVGERgaqMSGGQKQRIAIARALVRNPKILLLDEA 578
Cdd:PRK11264 96 LFPhRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK-ETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 579 TSALDTEsesVVQAALDKIR----KGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:PRK11264 172 TSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
413-640 |
1.01e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.10 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYL--REI 490
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEP--VLFATTIAENIRYGREDV--TMEEIERATKEA----NAYDFIMKLPKkfetvvgergaQMSGGQKQRIAI 562
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 563 ARALVRNPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELMEQK 640
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1052-1280 |
1.18e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.11 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEVK---VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQW-LR 1127
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 AQIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVS----AAKAANIHSFieslpKKYNTRVgdkgaqLSGGQKQRI 1201
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEY-----RRHAPHL------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1202 AIARALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 2024474312 1280 E 1280
Cdd:PRK13633 234 E 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1281 |
1.60e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.04 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKY-PTRP-EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR----NTKTLNIQW 1125
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1126 LRAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVSAAKAAnihsfIE--SLPKKYNTRvgdKGAQLSGGQKQRI 1201
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLAR---SPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1202 AIARALIRQPRILLLDEATSALDTESEKIVQE---ALDKaREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQL 1277
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
....
gi 2024474312 1278 LAEK 1281
Cdd:PRK13634 234 FADP 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1052-1278 |
2.03e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 115.90 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDpLSGEVLLDGR--------NTKTLNI 1123
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1124 QWLRAQIGIVSQEPILFDCTIAENIAYGDN----SREVSHEEIV-SAAKAANIHSFIESlpkkyntRVGDKGAQLSGGQK 1198
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVeSALKDADLWDEIKH-------KIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1199 QRIAIARALIRQPRILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIAHRLSTIQN-ADKIAVIQN-----GKVIE 1270
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVE 236
|
....*...
gi 2024474312 1271 QGTHQQLL 1278
Cdd:PRK14258 237 FGLTKKIF 244
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
413-636 |
2.47e-28 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 114.14 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDIkILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSlNVRYLREIIG 492
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFAT-TIAENIR-YGRedVTMEEIERATKEANAYDFIMKLPKKFETVVGergaQMSGGQKQRIAIARALVRNP 570
Cdd:cd03263 79 YCPQFDALFDElTVREHLRfYAR--LKGLPKSEIKEEVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 571 KILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1277 |
2.47e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.62 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTrPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVSaaKAANIHSFIESLpkkynTRVGDKGAQLSGGQKQRIAIARALIR 1209
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEMHR--RVSEALKQVDML-----ERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1210 QPRILLLDEATSALDTESEKIVQEALDKAREGR--TCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQL 1277
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
429-631 |
4.30e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 113.16 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 429 KILKGLNLKVNC---GQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDL----KSLNVRYLREIIGVVNQEPVLF 501
Cdd:cd03297 8 KRLPDFTLKIDFdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 502 A-TTIAENIRYG-REDVTMEEIERATKEANAYDFimklpkkfETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEAT 579
Cdd:cd03297 88 PhLNVRENLAFGlKRKRNREDRISVDELLDLLGL--------DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 580 SALDTESESVVQAALDKIRK--GRTILVIAHRLSTV-RNADLIAAFENGVITEQG 631
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1281 |
4.59e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.33 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEVkvLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR--NTKTLNIQWLRAQ 1129
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 IGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVSAAKAANIHSFIESLPKKyntrvgdKGAQLSGGQKQRIAIARAL 1207
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1208 IRQPRILLLDEATSALD----TESEKIVQEALDKAreGRTCIVIAHRLSTIQ-NADKIAVIQNGKVIEQGTHQQLLAEK 1281
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1052-1281 |
7.29e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.93 E-value: 7.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKY-PTRP-EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR----NTKTLNIQW 1125
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1126 LRAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVSAAKaanihsfieslpkKYNTRVG------DKGA-QLSGG 1196
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKAL-------------KWLKKVGlsedliSKSPfELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALDTESEK-IVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGTH 1274
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASP 229
|
....*..
gi 2024474312 1275 QQLLAEK 1281
Cdd:PRK13641 230 KEIFSDK 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1084-1279 |
7.41e-28 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 116.74 E-value: 7.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1084 ALVGSSGCGKSTVVQL---LERfydPLSGEVLLDGRntkTL----NIQWL---RAQIGIVSQEPILFD-CTIAENIAYG- 1151
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGE---VLqdsaRGIFLpphRRRIGYVFQEARLFPhLSVRGNLLYGr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1152 ----DNSREVSHEEIVSAAKaanihsfIESLPKKYNtrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTES 1227
Cdd:COG4148 103 krapRAERRISFDEVVELLG-------IGHLLDRRP-------ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1228 -EKIVQ--EALdkAREGRTCIV-IAH------RLstiqnADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:COG4148 169 kAEILPylERL--RDELDIPILyVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLS 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1065-1269 |
7.47e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.36 E-value: 7.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGrntKTLNI----QWLRAQIGIVSQEPILF 1140
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIrsprDAIALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1141 DC-TIAENIAYGdnsREVSHEEIVSAAKAANIhsfIESLPKKY------NTRVGDkgaqLSGGQKQRIAIARALIRQPRI 1213
Cdd:COG3845 93 PNlTVAENIVLG---LEPTKGGRLDRKAARAR---IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1214 LLLDEATSALdTESEkiVQE---ALDK-AREGRTCIVIAHRLSTI-QNADKIAVIQNGKVI 1269
Cdd:COG3845 163 LILDEPTAVL-TPQE--ADElfeILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKVV 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1052-1278 |
7.69e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 113.64 E-value: 7.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSG-EVLLDGRNTKTLNIQWLRAQI 1130
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVS---QEPILFDCTIAENIAYGDNS-----REVSHEEIvsaAKAANIhsfIESLpkkyntRVGDKG----AQLSGGQK 1198
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFDsiglyREPTDEQR---ERAREL---LELL------GLAHLAdrpfGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1199 QRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIV-IAHRLSTIQNA-DKIAVIQNGKVIEQGTHQ 1275
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGPKE 228
|
...
gi 2024474312 1276 QLL 1278
Cdd:COG1119 229 EVL 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1067-1273 |
1.07e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 113.60 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1067 VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNiQWLRAQIGIVS--QEPILF-DCT 1143
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFpELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIAYG-------------DNSREVSHEEIVSAAKAANIHSFIEsLPKKYNTRVGDkgaqLSGGQKQRIAIARALIRQ 1210
Cdd:COG0411 96 VLENVLVAaharlgrgllaalLRLPRARREEREARERAEELLERVG-LADRADEPAGN----LSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1211 PRILLLDEATSAL-DTESEKIVqEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGT 1273
Cdd:COG0411 171 PKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
729-1023 |
1.17e-27 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 114.45 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQ---P-IFSVMISDVIGmfvekgkAAIRETNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMR 804
Cdd:cd18542 1 YLLAILALLLATALNlliPlLIRRIIDSVIG-------GGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 805 LRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPI 884
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 885 IAITGMIQMKML-AGHAKKDKKELEtLGKVASEAIENIRTVVALTQER----KFEymyGQNLQVsYRNSIKKAHIFGFTF 959
Cdd:cd18542 152 IALFSYVFFKKVrPAFEEIREQEGE-LNTVLQENLTGVRVVKAFAREDyeieKFD---KENEEY-RDLNIKLAKLLAKYW 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 960 AFTQAIMYFTYAGCFRFGAYLVKNGHMRFkDVLLVFSA----IVFGAMALGQSTSftpDYAKAKMSAA 1023
Cdd:cd18542 227 PLMDFLSGLQIVLVLWVGGYLVINGEITL-GELVAFISylwmLIWPVRQLGRLIN---DMSRASASAE 290
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
430-630 |
1.26e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 113.75 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN---VRYLREIIGVVNQE---PVLFAT 503
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENIRYGREDVT-MEEIERATKEANAYDfIMKLPkkfETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSAL 582
Cdd:TIGR02769 106 TVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 583 DTESESVVQAALDKIRK--GRTILVIAHRLSTV-RNADLIAAFENGVITEQ 630
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQafGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
413-647 |
1.40e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.68 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYpaRPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEP--VLFATTIAENIRYGRED--VTMEEIERATKEA----NAYDFIMKLPKkfetvvgergaQMSGGQKQRIAIAR 564
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQG-----THDELM 637
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250
....*....|
gi 2024474312 638 EQKGVYYKLV 647
Cdd:PRK13647 232 EQAGLRLPLV 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1067-1279 |
1.44e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 115.06 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1067 VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN---IQWLRAQIGIVSQEPilfdct 1143
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 iaeniaYGD-NSRE----------VSHEEIVSAAKAANIHSFIEslpkkyntRVGDKGAQ-------LSGGQKQRIAIAR 1205
Cdd:PRK11308 102 ------YGSlNPRKkvgqileeplLINTSLSAAERREKALAMMA--------KVGLRPEHydryphmFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEAL-DKAREGRTCIV-IAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1066-1272 |
2.16e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 111.22 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlraQIGIVSQEPILF-DCTI 1144
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1145 AENIAYGDNSREVSHEEIvsaakAANIHSFIES--LPKKYNTRVgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSA 1222
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEA-----RRRIDEWLERleLSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1223 LDTESEKIVQEAL-DKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:cd03269 159 LDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1052-1272 |
2.19e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 111.05 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkvlQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlRAQIG 1131
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILF-DCTIAENIAYGDNSR----EVSHEEIVSAAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIARA 1206
Cdd:cd03298 74 MLFQENNLFaHLTVEQNVGLGLSPGlkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1207 LIRQPRILLLDEATSALD-TESEKIVQEALDKARE-GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDpALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
413-637 |
2.40e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 112.10 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEG-TITIDGQDLKSLNVRYLREII 491
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVN---------QEPVL-------FATTiaeniryGR-EDVTMEEIERATKEANAYDFIMKLPKKFETvvgergaqMSG 554
Cdd:COG1119 81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLyREPTDEQRERARELLELLGLAHLADRPFGT--------LSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 555 GQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLStvrnaDLIAAF------ENGV 626
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVE-----EIPPGIthvlllKDGR 220
|
250
....*....|.
gi 2024474312 627 ITEQGTHDELM 637
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1052-1280 |
2.60e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.77 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN-IQWLRAQI 1130
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVSAAKAAnihsFIESLPKKYNTRvgdKGAQLSGGQKQRIAIARALI 1208
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1209 RQPRILLLDEATSALDTESEKIVQEALDKA-REGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
413-619 |
2.71e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 110.65 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYlREIIG 492
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFAT-TIAENIR-----YGReDVTMEEIERATKEanaydfiMKLPKkFETVvgeRGAQMSGGQKQRIAIARAL 566
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAG-LADL---PVRQLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 567 VRNPKILLLDEATSALDTESESVVQAAL-DKIRKGRTILVIAHRLSTVRNADLI 619
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
413-631 |
3.04e-27 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 110.66 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikilKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylREIIG 492
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFA-TTIAENIRYGR------EDVTMEEIERATKEANAYDFIMKLPKkfetvvgergaQMSGGQKQRIAIARA 565
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLspglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 566 LVRNPKILLLDEATSALDTESESVVQAALDKIRKGR--TILVIAHRLSTVRN-ADLIAAFENGVITEQG 631
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1052-1283 |
3.08e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.92 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYP--TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR----NTKTLNIQW 1125
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1126 LRAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVSAAKAA-NIHSFIESLPKKyntrvgdKGAQLSGGQKQRIA 1202
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1203 IARALIRQPRILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQD 235
|
...
gi 2024474312 1281 KGF 1283
Cdd:PRK13649 236 VDF 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
413-639 |
3.97e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 111.28 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNV---FFSYPArpdikiLKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylRE 489
Cdd:cd03296 3 IEVRNVskrFGDFVA------LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQEPVLFA-TTIAENIRYGREdvtMEEIERATKEANAYDFIMKLPK--KFETVVGERGAQMSGGQKQRIAIARAL 566
Cdd:cd03296 75 NVGFVFQHYALFRhMTVFDNVAFGLR---VKPRSERPPEAEIRAKVHELLKlvQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 567 VRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAHRLS-TVRNADLIAAFENGVITEQGTHDELMEQ 639
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1069-1280 |
4.11e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.77 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSG-----EVLLDGrnTKTLN-----IQWLRAQIGIVSQEPI 1138
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDT--ARSLSqqkglIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 LFDC-TIAENIAYGDN-SREVSHEEIVSAAKaanihsfiESLPKkyntrVGDKGAQ------LSGGQKQRIAIARALIRQ 1210
Cdd:PRK11264 96 LFPHrTVLENIIEGPViVKGEPKEEATARAR--------ELLAK-----VGLAGKEtsyprrLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1211 PRILLLDEATSALDTEsekIVQEALDK----AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK11264 163 PEVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
429-639 |
5.37e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.45 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 429 KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDL--KSLNVRYLREIIGVVNQEP--VLFATT 504
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 505 IAENIRYGREDVTM--EEIERATKEAnaydfiMKLPK-KFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSA 581
Cdd:PRK13637 101 IEKDIAFGPINLGLseEEIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 582 LDTESESVVQAALDKIRK--GRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELMEQ 639
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
428-637 |
6.23e-27 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 110.60 E-value: 6.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVrylREI----IGVVNQEPVLFAT 503
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP---HEIarlgIGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 -TIAENIR-----YGREDVTMEEIERATKEANAYDF----IMKLPKKFETVVGErgaqMSGGQKQRIAIARALVRNPKIL 573
Cdd:cd03219 90 lTVLENVMvaaqaRTGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 574 LLDEATSAL-DTESESVVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELM 637
Cdd:cd03219 166 LLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
413-628 |
7.18e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 107.90 E-value: 7.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPArpdIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlkslnvrylreiig 492
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 vvnqePVLFATTiaenirygredvtmeeieratKEANAydfimklpKKFETVvgergAQMSGGQKQRIAIARALVRNPKI 572
Cdd:cd03216 63 -----EVSFASP---------------------RDARR--------AGIAMV-----YQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 573 LLLDEATSAL-DTESESVVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVIT 628
Cdd:cd03216 104 LILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1073-1277 |
9.17e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.78 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1073 LNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKtlNIQWLRAQIGIVSQEPILF-DCTIAENIAYG 1151
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1152 DNSREVSHEEIvsAAKAANIHSFIESlpKKYNTRvgdKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTE-SEKI 1230
Cdd:PRK11607 116 LKQDKLPKAEI--ASRVNEMLGLVHM--QEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRDRM 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024474312 1231 VQEALD-KAREGRTCIVIAH-RLSTIQNADKIAVIQNGKVIEQGTHQQL 1277
Cdd:PRK11607 189 QLEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1069-1277 |
1.07e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 113.28 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlRAQIGIVSQEPILF-DCTIAEN 1147
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1148 IAYGDNSREVSHEEIVSAAKAA----NIHSFIEslpkkyntRVGDkgaQLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEAlelvDLAGFED--------RYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1224 DTESEKIVQEaldKARE-----GRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQL 1277
Cdd:PRK11432 168 DANLRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1065-1266 |
1.07e-26 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 109.34 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQ----IGIVSQEPILF 1140
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1141 DCTIAENIAYGDNSREVSHEEIVsaaKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEAT 1220
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVT---DACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024474312 1221 SALDTE-SEKIVQEALDK--AREGRTCIVIAHRLSTIQNADKIAVIQNG 1266
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
729-1019 |
1.26e-26 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 111.37 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGAL---QPIFsvmISDVIGMFVEKGkaaireTNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRL 805
Cdd:cd18551 1 LILALLLSLLGTAAslaQPLL---VKNLIDALSAGG------SSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 806 RSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRL-ALVAQNIANLGTGIVLSLIyGWQLTLLLLAIVPI 884
Cdd:cd18551 72 RRRLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLpQLVTGVLTVVGAVVLMFLL-DWVLTLVTLAVVPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 885 IAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQA 964
Cdd:cd18551 149 AFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 965 IMYFTYAGCFRFGAYLVKNGHMRFKD----VLLVFSAIvfgaMALGQSTSFTPDYAKAK 1019
Cdd:cd18551 229 AVQLALLVVLGVGGARVASGALTVGTlvafLLYLFQLI----TPLSQLSSFFTQLQKAL 283
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1073-1285 |
1.60e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 112.51 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1073 LNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR----NTKTLNIQWLRAQIGIVSQEPILF-DCTIAEN 1147
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1148 IAYG-----DNSREVSHEEIVsaaKAANIHSFIESLPKKyntrvgdkgaqLSGGQKQRIAIARALIRQPRILLLDEATSA 1222
Cdd:TIGR02142 96 LRYGmkrarPSERRISFERVI---ELLGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1223 LDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAEKGFYY 1285
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1052-1272 |
1.69e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 108.43 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpevKVLQGLNIEVEKGQTlALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTlNIQWLRAQIG 1131
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFD-CTIAENIAY-----GDNSREVsHEEIVSAAKAANIhsfieslpkkyNTRVGDKGAQLSGGQKQRIAIAR 1205
Cdd:cd03264 76 YLPQEFGVYPnFTVREFLDYiawlkGIPSKEV-KARVDEVLELVNL-----------GDRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
413-623 |
1.85e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 110.13 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK-----EGTITIDGQDL--KSLNVR 485
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 486 YLREIIGVVNQEPVLFATTIAENIRYG------REDVTMEEI-ERATKEANAYDFIM-KLPKKfetvvgerGAQMSGGQK 557
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKhKIHKS--------ALDLSGGQQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 558 QRIAIARALVRNPKILLLDEATSALDTES----ESVVQAAldKIRKGRTILVIAHRLSTV-RNADLIAAFE 623
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSL--RLRSELTMVIVSHNLHQVsRLSDFTAFFK 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
430-639 |
2.42e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 115.17 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTT----VQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI----IGVVNQEPV-- 499
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgnrIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 500 ---LFatTI----AENIR----YGREDVTMEEIE--------RATKEANAYDFimklpkkfetvvgergaQMSGGQKQRI 560
Cdd:COG4172 105 lnpLH--TIgkqiAEVLRlhrgLSGAAARARALEllervgipDPERRLDAYPH-----------------QLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 561 AIARALVRNPKILLLDEATSALDTesesVVQAA----LDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTH 633
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDV----TVQAQildlLKDLQRelGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPT 241
|
....*.
gi 2024474312 634 DELMEQ 639
Cdd:COG4172 242 AELFAA 247
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
444-695 |
2.89e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 111.74 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 444 VALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYL----REIIGVVNQEPVLFA-TTIAENIRYGREDVTM 518
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPhLSVRGNLRYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 519 EEieRATKEANAYDFImklpkKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIR 598
Cdd:TIGR02142 106 SE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 599 K--GRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELMEQKGVYYKLVNMQASETEDQLQEEGNASSVSEEALNGS 675
Cdd:TIGR02142 179 AefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLIEGVVAEHDQHYGLTALRLGGG 258
|
250 260
....*....|....*....|
gi 2024474312 676 VLTGQKRQSTRKSIKRVRIQ 695
Cdd:TIGR02142 259 HLWVPENLGPTGARLRLRVP 278
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1052-1272 |
3.14e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 107.69 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWlrAQIG 1131
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFD-CTIAENIAYGDNSREVSHEEIVSAAKAANIHsfieslpkkynTRVGDKGAQLSGGQKQRIAIARALIRQ 1210
Cdd:cd03268 76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1211 PRILLLDEATSALDTESEKIVQEAL-DKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1074-1279 |
3.19e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.52 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1074 NIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRN-TKTLNIQwlRAqIGIVSQEPILFD-CTIAENIAYG 1151
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPPSR--RP-VSMLFQENNLFShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1152 DNS----REVSHEEIVSAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSALD--- 1224
Cdd:PRK10771 96 LNPglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpal 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1225 -TESEKIVQEALDkaREGRTCIVIAHRLstiQNADKIA----VIQNGKVIEQGTHQQLLA 1279
Cdd:PRK10771 165 rQEMLTLVSQVCQ--ERQLTLLMVSHSL---EDAARIAprslVVADGRIAWDGPTDELLS 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
726-1288 |
3.23e-26 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 117.32 E-value: 3.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 726 WPYFVVGTLCAI--INGALQPIfsvMISDVIGMFVEKGKaairETNSTYALLFLGFGLISFV-TFFLQGFTFGKAGEILT 802
Cdd:TIGR01271 80 WRFVFYGILLYFgeATKAVQPL---LLGRIIASYDPFNA----PEREIAYYLALGLCLLFIVrTLLLHPAIFGLHHLGMQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 803 MR--LRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGsrLALVAQnIANLGTGIVLSLIygWQLT----- 875
Cdd:TIGR01271 153 MRiaLFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLA--LAHFVW-IAPLQVILLMGLI--WELLevngf 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 876 -----LLLLAIVPiiAITGMIQMKMLAGHAKKDKKELetlgKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIK 950
Cdd:TIGR01271 226 cglgfLILLALFQ--ACLGQKMMPYRDKRAGKISERL----AITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 951 KAHIfgftfaftqaiMYFtYAGCFRFGAYLVKNG----HMRFKDVLL--VFSAIVF-------------GAM-----ALG 1006
Cdd:TIGR01271 300 IAYL-----------RYF-YSSAFFFSGFFVVFLsvvpYALIKGIILrrIFTTISYcivlrmtvtrqfpGAIqtwydSLG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1007 QSTSFTPDYAKAKMSAAHLFLLFERVPLID--SYSEEG-----EKPK-------MFGGNITFKDVAFKYPTRPevkVLQG 1072
Cdd:TIGR01271 368 AITKIQDFLCKEEYKTLEYNLTTTEVEMVNvtASWDEGigelfEKIKqnnkarkQPNGDDGLFFSNFSLYVTP---VLKN 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1073 LNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRntktlniqwlraqIGIVSQEPILFDCTIAENIAYGd 1152
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFG- 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1153 nsreVSHEEI--VSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEK- 1229
Cdd:TIGR01271 511 ----LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKe 586
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1230 IVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLV 1288
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1051-1274 |
4.92e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1051 NITFKDVAFKYPTrpeVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDG------RNTKTLNIQ 1124
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1125 WLRAQIGIVSQE----PILfdcTIAENIAYG-----DNSREVSHEEIVSAAKAANIHSFIESLPkkyntrvgdkgAQLSG 1195
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1196 GQKQRIAIARALIRQPRILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGT 1273
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
.
gi 2024474312 1274 H 1274
Cdd:COG4161 225 A 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
413-631 |
5.16e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 107.28 E-value: 5.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpdiKILKGLNLKVNCGQTvALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSlNVRYLREIIG 492
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFAT-TIAENIRY---------GREDvtmEEIERATKEANAYDFIMKLPKKFetvvgergaqmSGGQKQRIAI 562
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkgipsKEVK---ARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 563 ARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQG 631
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
413-660 |
5.57e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 5.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKE---GTITIDGQDLKSLNVRYLRE 489
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQEP--VLFATTIAENIRYGRED--VTMEE----IERATKEANAYDFIMKLPkkfetvvgergAQMSGGQKQRIA 561
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEmikiVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 562 IARALVRNPKILLLDEATSALDTESESVVqaaLDKIR-----KGRTILVIAHRLSTVRNADLIAAFENGVITEQGT---- 632
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQI---LKLIRklkkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpvei 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2024474312 633 --HDELMEQKGV----YYKLVNM---------QASETEDQLQE 660
Cdd:PRK13640 231 fsKVEMLKEIGLdipfVYKLKNKlkekgisvpQEINTEEKLVQ 273
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1066-1270 |
5.77e-26 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 107.90 E-value: 5.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQL---LERfydPLSGEVLLDGRNTKTLN----IQWLRAQIGIVSQE-- 1136
Cdd:COG4181 24 ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1137 --PILfdcTIAEN------IAYGDNSREVSHEEIvsaakaanihsfieslpkkynTRVGDKG------AQLSGGQKQRIA 1202
Cdd:COG4181 101 llPTL---TALENvmlpleLAGRRDARARARALL---------------------ERVGLGHrldhypAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1203 IARALIRQPRILLLDEATSALDTE-SEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVIQNGKVIE 1270
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAAtGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1066-1272 |
8.59e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.69 E-value: 8.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEP-IL 1139
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1140 FDCTIAENIAYG------DNSREVSHEEIVSAAKAANihsfiesLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRI 1213
Cdd:PRK14247 95 PNLSIFENVALGlklnrlVKSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1214 LLLDEATSALDTESEKIVQEALDKAREGRTCIVIAH------RLStiqnaDKIAVIQNGKVIEQG 1272
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1066-1279 |
1.11e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 106.99 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWLRAQ------IGIVSQEPIL 1139
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-----ITGLPPHriarlgIGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1140 F-DCTIAENI---AYGDNSREVSHEEIvsaakaANIHSFIESLPKKYNTRvgdkGAQLSGGQKQRIAIARALIRQPRILL 1215
Cdd:COG0410 90 FpSLTVEENLllgAYARRDRAEVRADL------ERVYELFPRLKERRRQR----AGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1216 LDEATSALdteSEKIVQEALDK----AREGRTCIVI---AHRLSTIqnADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:COG0410 160 LDEPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1051-1272 |
1.17e-25 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 106.59 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1051 NITFKDVAFKYP-TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLE---RFYDPLSGEVLLDGRntkTLNIQWL 1126
Cdd:cd03234 3 VLPWWDVGLKAKnWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQ---PRKPDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1127 RAQIGIVSQEPILFDC-TIAENIAYGDNSRevSHEEIVSAAKAANIHsfIESLPKKYNTRVGDKG-AQLSGGQKQRIAIA 1204
Cdd:cd03234 80 QKCVAYVRQDDILLPGlTVRETLTYTAILR--LPRKSSDAIRKKRVE--DVLLRDLALTRIGGNLvKGISGGERRRVSIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1205 RALIRQPRILLLDEATSALDTESE-KIVQEALDKAREGRTCIVIAH--RLSTIQNADKIAVIQNGKVIEQG 1272
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1068-1275 |
1.22e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1068 KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDG------RNTKTLNIQWLRAQIGIVSQE----P 1137
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 ILfdcTIAEN-IAYGDNSREVSHEEIVSAAKAanihsFIESLpkkyntRVGDKGA----QLSGGQKQRIAIARALIRQPR 1212
Cdd:PRK11124 96 HL---TVQQNlIEAPCRVLGLSKDQALARAEK-----LLERL------RLKPYADrfplHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1213 ILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQ 1275
Cdd:PRK11124 162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1055-1264 |
1.71e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.34 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1055 KDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVS 1134
Cdd:PRK10247 11 QNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1135 QEPILFDCTIAENIAYGDNSREVSHEEivsAAKAANIHSFieSLPkkyNTRVGDKGAQLSGGQKQRIAIARALIRQPRIL 1214
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPWQIRNQQPDP---AIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1215 LLDEATSALDTESEKIVQEALDK-AREGRTCIV-IAHRLSTIQNADKIAVIQ 1264
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1069-1272 |
1.82e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.85 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLSGEVLLDGRNTKTLNIQWL--RAQIGIVSQEPILF- 1140
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1141 DCTIAENIAYG------DNSREVSHEEIVSAAKAAnihsfieSLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRIL 1214
Cdd:PRK14267 99 HLTIYDNVAIGvklnglVKSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1215 LLDEATSALDTESEKIVQEALDKAREGRTCIVIAHrlSTIQNA---DKIAVIQNGKVIEQG 1272
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1065-1269 |
2.06e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 111.94 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYdP---LSGEVLLDGRNTKTLNIQWL-RAQIGIVSQEPILF 1140
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1141 -DCTIAENIAYGdnsREVSHEEIVSAAKaanIHSFIESLPKKY------NTRVGDkgaqLSGGQKQRIAIARALIRQPRI 1213
Cdd:PRK13549 95 kELSVLENIFLG---NEITPGGIMDYDA---MYLRAQKLLAQLkldinpATPVGN----LGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1214 LLLDEATSALdTESE-----KIVQealDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVI 1269
Cdd:PRK13549 165 LILDEPTASL-TESEtavllDIIR---DLKAHGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1070-1280 |
2.37e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.79 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPL-----SGEVLLDGRNTKTLNIQ--WLRAQIGIVSQEPILFDC 1142
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1143 TIAENIAYGD--NSREVSHEEIV--SAAKAAnihsfiesLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDE 1218
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVerSLRQAA--------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1219 ATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
413-585 |
2.80e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.59 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYP-ARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN----VRYL 487
Cdd:COG4181 9 IELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 488 REIIGVVNQEPVLFAT-TIAENI-----RYGREDVTmeeiERATKEanaydfimklpkkFETV-VGERG----AQMSGGQ 556
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVmlpleLAGRRDAR----ARARAL-------------LERVgLGHRLdhypAQLSGGE 151
|
170 180
....*....|....*....|....*....
gi 2024474312 557 KQRIAIARALVRNPKILLLDEATSALDTE 585
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAA 180
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1069-1281 |
3.56e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 106.43 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRA---QIGIVSQepilfDCTIA 1145
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ-----DSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1146 EN--IAYGDNSRE-VSH-EEIVSAAKAANIHSFIESLpkKYNTRVGDK-GAQLSGGQKQRIAIARALIRQPRILLLDEAT 1220
Cdd:TIGR02769 101 VNprMTVRQIIGEpLRHlTSLDESEQKARIAELLDMV--GLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1221 SALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAEK 1281
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
430-640 |
4.10e-25 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 105.30 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNV-RYLREIIGVVNQEPVLFAT-TIAE 507
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPhERARAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 508 NIRYGREdvtmeeiERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALdteSE 587
Cdd:TIGR03410 95 NLLTGLA-------ALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI---QP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 588 SVVQ---AALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQK 640
Cdd:TIGR03410 165 SIIKdigRVIRRLRAegGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
424-632 |
4.29e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.31 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 424 ARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVR----YLREI-------IG 492
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkaFRRDIqmvfqdsIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVN---------QEPVLFATTIAENIRYGREDVTMEEIERATKEANaydfimKLPkkfetvvgergAQMSGGQKQRIAIA 563
Cdd:PRK10419 101 AVNprktvreiiREPLRHLLSLDKAERLARASEMLRAVDLDDSVLD------KRP-----------PQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 564 RALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTV-RNADLIAAFENGVITEQGT 632
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNGQIVETQP 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
413-608 |
5.30e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.55 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYlreiiG 492
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQ-EPVLFATTIAENIRYGREdvtMEEIERATKEANAYDFIMKlpkkfetvVGERGA------QMSGGQKQRIAIARA 565
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024474312 566 LVRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAH 608
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITH 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
429-637 |
7.00e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.44 E-value: 7.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 429 KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSL-------------NVRYLREIIGVVN 495
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 QEPVLFA-TTIAENIRygREDVTMEEIERATKEANAYDFIMKLPKKfETVVGERGAQMSGGQKQRIAIARALVRNPKILL 574
Cdd:PRK10619 99 QHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 575 LDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTVRNADLIAAF-ENGVITEQGTHDELM 637
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1052-1249 |
8.86e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.33 E-value: 8.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYP-TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWLRAQI 1130
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEPILFD-CTIAENIAYGDNSREVSHEEIVSAAkAANIHsfieslpkkyntRVGDKGA------QLSGGQKQRIAI 1203
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARA-EELLA------------LVGLADFarrriwQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2024474312 1204 ARALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAH 1249
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
413-662 |
8.87e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 8.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDIK---ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSL-NVRYLR 488
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 489 EIIGVVNQEP--VLFATTIAENIRYGRED--VTMEEI----ERATKEANAYDFimklpKKFETVVgergaqMSGGQKQRI 560
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIrervDESLKKVGMYEY-----RRHAPHL------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 561 AIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELME 638
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
250 260
....*....|....*....|....*.
gi 2024474312 639 QKGVYYK--LVNMQASETEDQLQEEG 662
Cdd:PRK13633 234 EVEMMKKigLDVPQVTELAYELKKEG 259
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
413-640 |
9.82e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.63 E-value: 9.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSY-PARP-DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDL----KSLNVRY 486
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 487 LREIIGVVNQ--EPVLFATTIAENIRYGREDVTMEeIERAtkEANAYDFIMKLpkKFETVVGERGA-QMSGGQKQRIAIA 563
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 564 RALVRNPKILLLDEATSALDTESESVVQAALDKIR--KGRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELMEQK 640
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1058-1272 |
1.05e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 103.60 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1058 AFKYPTRPeVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTlNIQWLRAQIGIVSQEP 1137
Cdd:cd03266 10 RFRDVKKT-VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 ILFD-CTIAENIAY-GDnsrevsheeiVSAAKAANIHSFIESLPKKY------NTRVGDkgaqLSGGQKQRIAIARALIR 1209
Cdd:cd03266 88 GLYDrLTARENLEYfAG----------LYGLKGDELTARLEELADRLgmeellDRRVGG----FSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1210 QPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIA-HRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
413-631 |
1.17e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 102.63 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDI---KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLI--QRFYDPKEGTITIDGQDLKSLNVRYl 487
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 488 reIIGVVNQEPVLFAT-TIAENIrygredvtmeeieratkeanayDFIMKLpkkfetvvgeRGaqMSGGQKQRIAIARAL 566
Cdd:cd03213 83 --IIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 567 VRNPKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLST--VRNADLIAAFENGVITEQG 631
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1283 |
1.21e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.94 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKY----PTrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTL------ 1121
Cdd:PRK13651 3 IKVKNIVKIFnkklPT--ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1122 ------------------NIQWLRAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVSAAKaanihSFIE--SLP 1179
Cdd:PRK13651 81 ekvleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAA-----KYIElvGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1180 KKYNTRvgdKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKA-REGRTCIVIAHRL-STIQNA 1257
Cdd:PRK13651 156 ESYLQR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWT 232
|
250 260
....*....|....*....|....*.
gi 2024474312 1258 DKIAVIQNGKVIEQGTHQQLLAEKGF 1283
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDILSDNKF 258
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
413-638 |
1.22e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.83 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDIKiLKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEP--VLFATTIAENIRYGRE------DVTMEEIERATKEANAYDFIMKLPKkfetvvgergaQMSGGQKQRIAIAR 564
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLEnhavpyDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKIR--KGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELME 638
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
431-632 |
1.22e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.86 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYD-----PKEGTITIDGQDLKSLNVR--YLREIIGVVNQEPVLFAT 503
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENIRYGRE----DVTMEE-IERATKEANAYDFIM-KLPkkfetvvgERGAQMSGGQKQRIAIARALVRNPKILLLDE 577
Cdd:PRK14243 106 SIYDNIAYGARingyKGDMDElVERSLRQAALWDEVKdKLK--------QSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 578 ATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGT 632
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1069-1288 |
1.43e-24 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 105.32 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRntktlniqwlraqIGIVSQEPILFDCTIAENI 1148
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 AYGdnsreVSHEEI--VSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTE 1226
Cdd:cd03291 119 IFG-----VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1227 SEK-IVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGFYYSLV 1288
Cdd:cd03291 194 TEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
729-986 |
2.02e-24 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 104.81 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVI-GMFVEKGKAAIRetnsTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRS 807
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLdDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 808 MAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIA- 886
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 887 ITGMIQMKMLaghaKKDKKELETLGKVAS---EAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQ 963
Cdd:cd18552 155 PIRRIGKRLR----KISRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
|
250 260
....*....|....*....|...
gi 2024474312 964 AIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGEL 253
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1059-1279 |
2.02e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 104.15 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1059 FKYPT----RPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWlRAQ-IGIV 1133
Cdd:COG4167 14 FKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKhIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1134 SQEPilfdctiaeNIAYgdNSREvsheeivsaakaaNIHSFIEsLPKKYNT----------------RVG-------DKG 1190
Cdd:COG4167 93 FQDP---------NTSL--NPRL-------------NIGQILE-EPLRLNTdltaeereerifatlrLVGllpehanFYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1191 AQLSGGQKQRIAIARALIRQPRILLLDEATSALD-TESEKIVQEALD-KAREGRTCIVIAHRLSTIQN-ADKIAVIQNGK 1267
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDmSVRSQIINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGE 227
|
250
....*....|..
gi 2024474312 1268 VIEQGTHQQLLA 1279
Cdd:COG4167 228 VVEYGKTAEVFA 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1069-1278 |
2.23e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPIL-FDCTIAEN 1147
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1148 IAYG--DNSREVSH-EEIVSAA-KAANIHSFIESLpkkYntrvgdkgAQLSGGQKQRIAIARALIR------QPRILLLD 1217
Cdd:PRK13548 97 VAMGraPHGLSRAEdDALVAAAlAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLAQlwepdgPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1218 EATSALD-TESEKIVQEALDKARE-GRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:PRK13548 166 EPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
428-635 |
2.32e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 103.97 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylrEII--GVVN--QEPVLFAT 503
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH---RIArlGIARtfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 -TIAENIRYGREDVTMEEIERA--------TKEANAYDFIMKLPKKF--ETVVGERGAQMSGGQKQRIAIARALVRNPKI 572
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAAllrlprarREEREARERAEELLERVglADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 573 LLLDEATSAL-DTESESVVQaALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENG-VITEqGTHDE 635
Cdd:COG0411 174 LLLDEPAAGLnPEETEELAE-LIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGrVIAE-GTPAE 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
413-627 |
2.38e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.81 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPA-RPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN----VRYL 487
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 488 REIIGVVNQEPVLFA-TTIAENIRYgreDVTMEEIERATKEANAYDFIMKLpkKFETVVGERGAQMSGGQKQRIAIARAL 566
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 567 VRNPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAHRLSTVRNADLIAAFENGVI 627
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1059-1269 |
3.18e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1059 FKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNiQWLRAQ-IGIVSQEP 1137
Cdd:COG1101 11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAKyIGRVFQDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 ILFDC---TIAENIAYGDN---SREVSheeivSAAKAANIHSFIES-------LPKKYNTRVGdkgaQLSGGQKQRIAIA 1204
Cdd:COG1101 90 MMGTApsmTIEENLALAYRrgkRRGLR-----RGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1205 RALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVI 1269
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1059-1284 |
4.12e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.93 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1059 FKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQ-------------LLERFY--DPLSGEVLLDGRNTKTL-N 1122
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigDKKNNHELITNPYSKKIkN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1123 IQWLRAQIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEivsAAKAANIH--------SFIESLPkkyntrvgdkgAQ 1192
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYlnkmglddSYLERSP-----------FG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1193 LSGGQKQRIAIARALIRQPRILLLDEATSALDTESEK-IVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIE 1270
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILK 256
|
250
....*....|....
gi 2024474312 1271 QGTHQQLLAEKGFY 1284
Cdd:PRK13631 257 TGTPYEIFTDQHII 270
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
427-636 |
4.29e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.07 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQ----LIQRFYDPK-EGTITIDGQDLKSLNVRYLREIIGVVNQEPVLF 501
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 502 AT-TIAENIRYG----REDVTMEEIERATKEAnaydfiMKLPKKFETV---VGERGAQMSGGQKQRIAIARALVRNPKIL 573
Cdd:PRK14247 95 PNlSIFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 574 LLDEATSALDTESESVVQAALDKIRKGRTILVIAH-RLSTVRNADLIAAFENGVITEQGTHDEL 636
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
445-637 |
4.89e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 105.18 E-value: 4.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 445 ALVGGSGCGKSTTVQLI---QRfydPKEGTITIDGQDL----KSLNV-RYLREIiGVVNQEPVLFAT-TIAENIRYGREd 515
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLqdsaRGIFLpPHRRRI-GYVFQEARLFPHlSVRGNLLYGRK- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 516 vtmeeieRATKEANAYDFimklpkkfETVVG--------ERG-AQMSGGQKQRIAIARALVRNPKILLLDEATSALDTES 586
Cdd:COG4148 104 -------RAPRAERRISF--------DEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 587 ESVVQAALDKIRK--GRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELM 637
Cdd:COG4148 169 KAEILPYLERLRDelDIPILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
413-617 |
5.54e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.71 E-value: 5.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFATTIAENIRYGRedvtmeEIERATKEANAY-DFIMK--LPkkfETVVGERGAQMSGGQKQRIAIARALVRN 569
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024474312 570 PKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAHRLSTVRNAD 617
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHAD 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1069-1279 |
5.59e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.87 E-value: 5.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKS-TVVQLLERFYDP----LSGEVLLDGRNTKTLNIQWLRA----QIGIVSQEPIL 1139
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1140 -------FDCTIAENIA-YGDNSREVSHEEIVSAAKAANIHSfieslPKKyntRVGDKGAQLSGGQKQRIAIARALIRQP 1211
Cdd:PRK15134 104 slnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQ-----AAK---RLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1212 RILLLDEATSALD-TESEKIVQEALDKARE-GRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK15134 176 ELLIADEPTTALDvSVQAQILQLLRELQQElNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1052-1281 |
6.28e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.32 E-value: 6.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYP--TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDG----RNTKTLNIQW 1125
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1126 LRAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVSAAkaaniHSFIESLPKKYNTrVGDKGAQLSGGQKQRIAI 1203
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDLGFSRDV-MSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1204 ARALIRQPRILLLDEATSALDTESEKIVQEALDKAR--EGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 2024474312 1281 K 1281
Cdd:PRK13646 237 K 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1069-1278 |
6.71e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.43 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERF---YDP---LSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILF-D 1141
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1142 CTIAENIAYGDNSREVSHEEIVSAAKAANIHSFieSLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATS 1221
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1222 ALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1060-1279 |
7.29e-24 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 101.47 E-value: 7.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1060 KYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIqWLRAQIGI--VSQEP 1137
Cdd:cd03218 9 RYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 ILF-DCTIAENIAYGDNSREVSHEEIVSAAKAAnIHSF-IESLPKKyntrvgdKGAQLSGGQKQRIAIARALIRQPRILL 1215
Cdd:cd03218 85 SIFrKLTVEENILAVLEIRGLSKKEREEKLEEL-LEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1216 LDEATSALDTESEKIVQEALDKAREGRTCIVIA-HRLS-TIQNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
417-625 |
8.25e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 101.25 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 417 NVFFSYParPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTI----TIDGQDLKSLNVRYLREIIG 492
Cdd:cd03290 5 NGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFATTIAENIRYGrEDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKI 572
Cdd:cd03290 83 YAAQKPWLLNATVEENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 573 LLLDEATSALDTE-SESVVQAALDKIRKG--RTILVIAHRLSTVRNADLIAAFENG 625
Cdd:cd03290 162 VFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
413-637 |
8.37e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.76 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN-VRYLREII 491
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEP--VLFATTIAENIRYGREDVTMEEIE------RATKEANAYDFIMKLPKkfetvvgergaQMSGGQKQRIAIA 563
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEirkrvdRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 564 RALVRNPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELM 637
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1074-1278 |
8.78e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.50 E-value: 8.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1074 NIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWL----RAQIGIVSQE-PILFDCTIAENI 1148
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 AYGDN----SREVSHEEIVSAAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIARALIRQPRILLLDEATSALD 1224
Cdd:PRK10070 128 AFGMElagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1225 TESEKIVQEALDK--AREGRTCIVIAHRL-STIQNADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
413-608 |
9.11e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.25 E-value: 9.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPA-RPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylReii 491
Cdd:COG4525 4 LTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFA-TTIAENIRYGredVTMEEIERATKEANAYDFIMKlpkkfetvVGERGA------QMSGGQKQRIAIAR 564
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARAEELLAL--------VGLADFarrriwQLSGGMRQRVGIAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAH 608
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH 193
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1049-1268 |
1.37e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 101.68 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1049 GGNITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEvLLDGRNTktlnIQWLRA 1128
Cdd:PRK11247 10 GTPLLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAP----LAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPILFDC-TIAENIAYG--DNSREVSHEEIVSAAKAanihsfieslpkkynTRVGDKGAQLSGGQKQRIAIAR 1205
Cdd:PRK11247 82 DTRLMFQDARLLPWkKVIDNVGLGlkGQWRDAALQALAAVGLA---------------DRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQNGKV 1268
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
434-639 |
1.46e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 103.65 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 434 LNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYlREIIgVVNQEPVLFA-TTIAENIRYG 512
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RDIC-MVFQSYALFPhMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 513 --REDVTMEEIERATKEANAydfIMKLpKKFEtvvgERGA-QMSGGQKQRIAIARALVRNPKILLLDEATSALDTeseSV 589
Cdd:PRK11432 103 lkMLGVPKEERKQRVKEALE---LVDL-AGFE----DRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDA---NL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 590 VQAALDKIRK-----GRTILVIAHRLS---TVrnADLIAAFENGVITEQGTHDELMEQ 639
Cdd:PRK11432 172 RRSMREKIRElqqqfNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1052-1283 |
1.55e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKY-PTRP-EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEV----LLDGRNTKTLNIQW 1125
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1126 LRAQIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEivsAAKAANIHSFIESLPKKYNTRvgdKGAQLSGGQKQRIAI 1203
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEK---AEKIAAEKLEMVGLADEFWEK---SPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1204 ARALIRQPRILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAEK 1281
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEV 235
|
..
gi 2024474312 1282 GF 1283
Cdd:PRK13643 236 DF 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
419-636 |
1.65e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 103.25 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 419 FFSYPARpdIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI---IGVVN 495
Cdd:PRK15079 27 FWQPPKT--LKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 QEPV-------LFATTIAENIRYGREDVTMEEIERATKEanaydFIMK---LPKkfetVVGERGAQMSGGQKQRIAIARA 565
Cdd:PRK15079 105 QDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKA-----MMLKvglLPN----LINRYPHEFSGGQCQRIGIARA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 566 LVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:PRK15079 176 LILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
431-637 |
1.69e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.73 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI----IGVVNQEPVLFA-TTI 505
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 506 AENIRYGREDVTMEEIERATKEANAYDFImklpkKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTE 585
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQV-----GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 586 SESVVQAALDKI--RKGRTILVIAHRL-STVRNADLIAAFENGVITEQGTHDELM 637
Cdd:PRK10070 199 IRTEMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1051-1273 |
1.82e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 103.77 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1051 NITFKDVAFKYPTRpeVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQL---LERFydpLSGEVLLDGRNTKTLniqwlr 1127
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 aqigivsqEPILFDC-------------TIAENIAYGDNSREVSHEEI----VSAAKAANIHSFIESLPkkyntrvgdkg 1190
Cdd:PRK11650 72 --------EPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIeervAEAARILELEPLLDRKP----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1191 AQLSGGQKQRIAIARALIRQPRILLLDEATSALDTeseKI-VQEALD----KAREGRTCIVIAH-RLSTIQNADKIAVIq 1264
Cdd:PRK11650 133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA---KLrVQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVM- 208
|
250
....*....|
gi 2024474312 1265 NGKVIEQ-GT 1273
Cdd:PRK11650 209 NGGVAEQiGT 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
427-636 |
2.22e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRF---YDPK---EGTITIDGQDLKSLNVRYLREIIGVVNQEPVL 500
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 501 FA-TTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEAT 579
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 580 SALDTESESVVQAALDKIRKGRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDEL 636
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
413-638 |
2.39e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.76 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDIKilkGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLkSLNVRYLREIiG 492
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPI-N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFA-TTIAENIRYG--REDVTMEEIERATKEANAYDFIMKLPKKfetvvgeRGAQMSGGQKQRIAIARALVRN 569
Cdd:PRK11607 95 MMFQSYALFPhMTVEQNIAFGlkQDKLPKAEIASRVNEMLGLVHMQEFAKR-------KPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 570 PKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAH-RLSTVRNADLIAAFENGVITEQGTHDELME 638
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDIleRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1066-1266 |
3.16e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 99.82 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTkTLNI------QWL---RAQIGIVSQ- 1135
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGG-WVDLaqasprEILalrRRTIGYVSQf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1136 --------------EPILfdctiaeniaygdnSREVSHEEivSAAKAA------NIHSFIESLPKkyntrvgdkgAQLSG 1195
Cdd:COG4778 102 lrviprvsaldvvaEPLL--------------ERGVDREE--ARARARellarlNLPERLWDLPP----------ATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1196 GQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIV-IAHRLSTIQN-ADKIAVIQNG 1266
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
413-640 |
3.34e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.97 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDI--KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDL----KSLNVRY 486
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 487 LREIIGVVNQ--EPVLFATTIAENIRYGRED--VTMEEIERATKEAnaydfiMKLPKKFETVVGERGAQMSGGQKQRIAI 562
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 563 ARALVRNPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGT------HD 634
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKpkdifqDV 236
|
....*.
gi 2024474312 635 ELMEQK 640
Cdd:PRK13649 237 DFLEEK 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
428-608 |
4.09e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 99.43 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQ----DLKSLNVR---YLRE-IIGVVNQepv 499
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRrTIGYVSQ--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 500 lFATTIAeniRYGREDVTMEE-IERATKEANAYDFIMKLPKKFEtvVGER-----GAQMSGGQKQRIAIARALVRNPKIL 573
Cdd:COG4778 101 -FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERlwdlpPATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024474312 574 LLDEATSALDTES-ESVVQAALDKIRKGRTILVIAH 608
Cdd:COG4778 175 LLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFH 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1070-1266 |
4.73e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 99.08 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWLRAQIGIVSQEPILFD-CTIAENI 1148
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ-----ITEPGPDRMVVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 AYGDNS-----REVSHEEIVSaakaanihsfiESLPKKYNTRVGDKG-AQLSGGQKQRIAIARALIRQPRILLLDEATSA 1222
Cdd:TIGR01184 76 ALAVDRvlpdlSKSERRAIVE-----------EHIALVGLTEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2024474312 1223 LDTESEKIVQEALDKARE--GRTCIVIAHRL-STIQNADKIAVIQNG 1266
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
142-358 |
5.27e-23 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 100.97 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 142 IGAGVL--FAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVA 219
Cdd:cd18542 46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 220 TFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKII-STFTNKElTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERY 298
Cdd:cd18542 126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVrPAFEEIR-EQEGELNTVLQENLTGVRVVKAFAREDYEIEKF 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 299 QKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGkVFTVFFS 358
Cdd:cd18542 205 DKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLG-ELVAFIS 263
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
412-631 |
6.02e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 98.88 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 412 NLEFQNVFFSYP-ARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLI---QRFYDPKEGTITIDGQDLKslnvRYL 487
Cdd:cd03234 3 VLPWWDVGLKAKnWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRK----PDQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 488 -REIIGVVNQEPVLFAT-TIAENIRY-----------GREDVTMEEIERATKEANaydfimklpkkfETVVGERGAQMSG 554
Cdd:cd03234 79 fQKCVAYVRQDDILLPGlTVRETLTYtailrlprkssDAIRKKRVEDVLLRDLAL------------TRIGGNLVKGISG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 555 GQKQRIAIARALVRNPKILLLDEATSALDTESE-SVVQAALDKIRKGRTILVIAH--RLSTVRNADLIAAFENGVITEQG 631
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1052-1280 |
6.43e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYptRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEP--ILFDCTIAENIAYGD-----NSREVSHeEIVSAAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIA 1204
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPinlglDEETVAH-RVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1205 RALIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
413-640 |
7.09e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYL-REII 491
Cdd:PRK11231 3 LRTENLTVGYGTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLaRRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFATTIAENIRYGRE-----------------DVTMEEIEratkeanaydfimklpkkFETVVGERGAQMSG 554
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRSpwlslwgrlsaednarvNQAMEQTR------------------INHLADRRLTDLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 555 GQKQRIAIARALVRNPKILLLDEATSALDTESesvvQAALDKI-----RKGRTILVIAHRLSTV-RNADLIAAFENGVIT 628
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH----QVELMRLmrelnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVM 217
|
250
....*....|..
gi 2024474312 629 EQGTHDELMEQK 640
Cdd:PRK11231 218 AQGTPEEVMTPG 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
431-636 |
7.93e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 98.21 E-value: 7.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSlNVRYLREIIGVVNQEPvlfattIAENIR 510
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 511 YGREDVTM-------------EEIERATKEANAYDFIMKLPKKFetvvgergaqmSGGQKQRIAIARALVRNPKILLLDE 577
Cdd:cd03265 89 TGWENLYIharlygvpgaerrERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 578 ATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
419-636 |
8.24e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 101.19 E-value: 8.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 419 FFSYPARpdIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN---VRYLREIIGVVN 495
Cdd:PRK11308 21 LFKPERL--VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 QEPvlfattiaenirYG----REDV--TMEE-------IERATKEANAYDFIMKLPKKFETVvgERGAQM-SGGQKQRIA 561
Cdd:PRK11308 99 QNP------------YGslnpRKKVgqILEEpllintsLSAAERREKALAMMAKVGLRPEHY--DRYPHMfSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 562 IARALVRNPKILLLDEATSALDTEsesvVQAA-----LDKIRK-GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHD 634
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVS----VQAQvlnlmMDLQQElGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKE 240
|
..
gi 2024474312 635 EL 636
Cdd:PRK11308 241 QI 242
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
411-648 |
8.87e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.02 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 411 GNLEFQNVFFSYpaRPDIK-ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLRE 489
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQEPVLFATTIAENIRYGREdVTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALV-R 568
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDEL-MEQKGVYYKLV 647
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
.
gi 2024474312 648 N 648
Cdd:PTZ00243 1544 E 1544
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1066-1277 |
9.24e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 98.21 E-value: 9.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDG----RNTKTLniqwlRAQIGIVSQEPILFD 1141
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREV-----RRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1142 -CTIAENIA-----YGdNSREVSHEEIVSAAKAANIHSFIESLPKKYntrvgdkgaqlSGGQKQRIAIARALIRQPRILL 1215
Cdd:cd03265 87 eLTGWENLYiharlYG-VPGAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1216 LDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGTHQQL 1277
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
413-585 |
9.86e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.55 E-value: 9.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK---EGTITIDGQDLKSLNVrYLRE 489
Cdd:COG4136 2 LSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA-EQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IiGVVNQEPVLFA-TTIAENIRYG-REDVTMEE----IERATKEANAYDFIMKLPkkfetvvgergAQMSGGQKQRIAIA 563
Cdd:COG4136 78 I-GILFQDDLLFPhLSVGENLAFAlPPTIGRAQrrarVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALL 145
|
170 180
....*....|....*....|..
gi 2024474312 564 RALVRNPKILLLDEATSALDTE 585
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAA 167
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1069-1279 |
1.39e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 103.63 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYdPLSGEVLLDGRNTKTLNIQWL---RAQIGIVSQEP---ILFDC 1142
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1143 TIAENIAYGdnsREVSHEEIVSAAKAANIHSFIESLPKKYNTRvGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSA 1222
Cdd:PRK15134 380 NVLQIIEEG---LRVHQPTLSAAQREQQVIAVMEEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1223 LDteseKIVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK15134 456 LD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
423-631 |
1.46e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 97.44 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 423 PARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLkSLNVRYLREIIGVVNQEPVLFA 502
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 503 -TTIAENIRY-GRedvtMEEIERATKEANAYDFIMKLpkKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATS 580
Cdd:cd03266 92 rLTARENLEYfAG----LYGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 581 ALDTESesvVQAALDKIRK----GRTILVIAHRLSTV-RNADLIAAFENGVITEQG 631
Cdd:cd03266 166 GLDVMA---TRALREFIRQlralGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
412-634 |
1.51e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 412 NLEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDG------QDLKSLNVR 485
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 486 YLREIIGVVNQE----PVLfatTIAENIRYGREDVTMEEIERATKEAnaydfiMKLPKKFE-TVVGER-GAQMSGGQKQR 559
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKA------MKLLARLRlTDKADRfPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 560 IAIARALVRNPKILLLDEATSALDTE-SESVVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHD 634
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1061-1258 |
1.62e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.53 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1061 YPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlraqigiVSQEPILF 1140
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1141 DCTIAENIAYGDNSREVSHEEIVSAAKAANIHSFieslpkkynTRVGDKG------AQLSGGQKQRIAIARALIRQPRIL 1214
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDAL---------ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2024474312 1215 LLDEATSALDTESEKIVQEAL-DKAREGRTCIVIAHRLSTIQNAD 1258
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
103-383 |
1.68e-22 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 99.10 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 103 ANFSLLNSTSVNFSM-EFFSYLI----LGELEEEMTRYAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVM 177
Cdd:cd18575 1 ALIALLIAAAATLALgQGLRLLIdqgfAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 178 RQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKII 257
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 258 STFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWY 337
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2024474312 338 GTILVLSEDYTIGKVFT-VFFSILVgAFSVGQAAPSMEAFANARGAA 383
Cdd:cd18575 241 GAHDVLAGRMSAGELSQfVFYAVLA-AGSVGALSEVWGDLQRAAGAA 286
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1061-1249 |
2.03e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1061 YPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlnIQWLRAQIGIVSQ-EPIL 1139
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQnEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1140 FDCTIAENIAYGDNSREVSHEEIVSAAKaanihsfiESLPKkyntrVGDKGA------QLSGGQKQRIAIARALIRQPRI 1213
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAH--------QMLKK-----VGLEGAekryiwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024474312 1214 LLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAH 1249
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
415-640 |
2.15e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 415 FQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGqdlkslNVRylreiIGVV 494
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 495 NQEPVLFAT-TIAENIRYGREDV--TMEEIERATKEANAYDFIMKLPKKFETVVGERGA--------------------- 550
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELraLEAELEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 551 -----QMSGGQKQRIAIARALVRNPKILLLDEATSALDTES----ESVVQAaldkiRKGrTILVIAH-R--LSTVrnADL 618
Cdd:COG0488 147 drpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKN-----YPG-TVLVVSHdRyfLDRV--ATR 218
|
250 260
....*....|....*....|...
gi 2024474312 619 IAAFENGVITE-QGTHDELMEQK 640
Cdd:COG0488 219 ILELDRGKLTLyPGNYSAYLEQR 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
413-640 |
2.31e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSY-PARP-DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLK----SLNVRY 486
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 487 LREIIGVVNQ--EPVLFATTIAENIRYGREDVTMEEIERATKeanAYDFIMKLPKKfETVVGERGAQMSGGQKQRIAIAR 564
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK---ALKWLKKVGLS-EDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 565 ALVRNPKILLLDEATSALDTES-ESVVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQK 640
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
413-634 |
2.39e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQ--DLKSLN----VRY 486
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPsdkaIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 487 LREIIGVVNQEPVLFA-TTIAENIRYGREDVTMEEIERATKEAnaydfiMKLPKKFE-TVVGER-GAQMSGGQKQRIAIA 563
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLIEAPCRVLGLSKDQALARA------EKLLERLRlKPYADRfPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 564 RALVRNPKILLLDEATSALDTE-SESVVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHD 634
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
413-643 |
2.50e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.92 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVL-FATTIAENIRYGREDVTmeeiERATKEANAYDFIMKlpkkfET-VVGERG---AQMSGGQKQRIAIARALV 567
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRAPHG----LSRAEDDALVAAALA-----QVdLAHLAGrdyPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 568 R------NPKILLLDEATSALD-TESESVVQAALDKIRK-GRTILVIAHRLS-TVRNADLIAAFENGVITEQGT-----H 633
Cdd:PRK13548 151 QlwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTpaevlT 230
|
250
....*....|
gi 2024474312 634 DELMEQkgVY 643
Cdd:PRK13548 231 PETLRR--VY 238
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1069-1273 |
2.63e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 97.21 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWL-RAQIGIVSQEPILF-DCTIAE 1146
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFpRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1147 NIAYGDNSREVSHEEIVsaakaANIHSFIESLPKKYNTRVGDkgaqLSGGQKQRIAIARALIRQPRILLLDEATSALDTE 1226
Cdd:TIGR03410 95 NLLTGLAALPRRSRKIP-----DEIYELFPVLKEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1227 SEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGT 1273
Cdd:TIGR03410 166 IIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1068-1281 |
2.84e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1068 KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPIL-FDCTIAE 1146
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1147 NIAYGdNSREVSH--------EEIVSAAKAAnihSFIESLPKKyntRVGDkgaqLSGGQKQRIAIARALIRQPRILLLDE 1218
Cdd:PRK11231 96 LVAYG-RSPWLSLwgrlsaedNARVNQAMEQ---TRINHLADR---RLTD----LSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1219 ATSALD----TESEKIVQEAldkAREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQLLAEK 1281
Cdd:PRK11231 165 PTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
429-636 |
2.87e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 429 KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLReiIGVVNQEPVLFA-TTIAE 507
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 508 NIRYG------REDVTMEEIERAtkeanaydfIMKLpkkFETV----VGER-GAQMSGGQKQRIAIARALVRNPKILLLD 576
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAK---------VTQL---LEMVqlahLADRyPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 577 EATSALDTESESVVQAALDKIR---KGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDEL 636
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHeelKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
427-639 |
3.68e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.06 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLI--QRFYDPKEGTITIDGQDLKSLNV--R----------YLREIIG 492
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPdeRaragiflafqYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEpvlFATTIAENIRYGREDVT--MEEIERATKEanaydfiMKLPKKFetvvGERG--AQMSGGQKQRIAIARALVR 568
Cdd:COG0396 92 VSVSN---FLRTALNARRGEELSARefLKLLKEKMKE-------LGLDEDF----LDRYvnEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAH--RLSTVRNADLIAAFENGVITEQGTHdELMEQ 639
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-ELALE 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1066-1271 |
4.37e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.39 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQW---LRAQ-IGIVSQEPILFD 1141
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1142 CTIA-ENIAY-----GDNSREvSHEEIVSAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIARALIRQPRILL 1215
Cdd:PRK10584 102 TLNAlENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1216 LDEATSALDTES-EKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVIQNGKVIEQ 1271
Cdd:PRK10584 170 ADEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1067-1269 |
5.27e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 101.44 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1067 VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFY--DPLSGEVLLDGRNTKTLNIQWL-RAQIGIVSQEPILF-DC 1142
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1143 TIAENIAYGDnsrEVSHEEIVSAAKAA--NIHSFIE--SLPKKYNTR-VGDKGaqlsGGQKQRIAIARALIRQPRILLLD 1217
Cdd:TIGR02633 94 SVAENIFLGN---EITLPGGRMAYNAMylRAKNLLRelQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1218 EATSAL-DTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVI 1269
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1066-1283 |
6.09e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.29 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLL---ERfYDPLSGEVLLDGRNTKTLNIQwLRAQIGI-VS-QEPI-- 1138
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 ------LFDCTIAENIAYGDNSREVSHEEIVSAAKAANihsfiesLPKKYNTR---VGdkgaqLSGGQKQRIAIARALIR 1209
Cdd:COG0396 90 pgvsvsNFLRTALNARRGEELSAREFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1210 QPRILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAH--RLSTIQNADKIAVIQNGKVIEQGTHQ--QLLAEKGF 1283
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElaLELEEEGY 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
413-642 |
6.14e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 96.07 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNV-RYLREII 491
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFAT-TIAENIRYGREDVTMEEIERATK-EANAYDF-IMKLPKKFetvvgerGAQMSGGQKQRIAIARALVR 568
Cdd:cd03218 78 GYLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKlEELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAHR----LSTVRNADLIAAfenGVITEQGTHDELMEQKGV 642
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKdRGIGVLITDHNvretLSITDRAYIIYE---GKVLAEGTPEEIAANELV 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
435-637 |
6.29e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.19 E-value: 6.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 435 NLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRylREIIGVVNQEPVLFA-TTIAENIRYG- 512
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 513 REDVTMEEIERATKEANAY-----DFIMKLPkkfetvvgergAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 587
Cdd:PRK10771 97 NPGLKLNAAQREKLHAIARqmgieDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 588 SVVQAALDKIRKGR--TILVIAHRLS-TVRNAD---LIAafeNGVITEQGTHDELM 637
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
413-642 |
6.61e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.23 E-value: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQ--DLKSLNVRYLREI 490
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEP--VLFATTIAENIRYGREDVTM--EEIERATKEANAYDFIMKLPKKfetvvgeRGAQMSGGQKQRIAIARAL 566
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 567 VRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVR-NADLIAAFENGVITEQGTHDELMEQKGV 642
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1068-1277 |
6.95e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.00 E-value: 6.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1068 KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwlRAQIGIVSQEPILF-DCTIAE 1146
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1147 NIAYGDN---SREVSHEEIVSAaKAANIHSFI--ESLPKKYNtrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATS 1221
Cdd:PRK10851 94 NIAFGLTvlpRRERPNAAAIKA-KVTQLLEMVqlAHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1222 ALDTESEKIVQEALDKARE--GRTCIVIAH-RLSTIQNADKIAVIQNGKvIEQ-GTHQQL 1277
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGN-IEQaGTPDQV 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
413-662 |
7.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.50 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSY-PARP-DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDG----QDLKSLNVRY 486
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 487 LREIIGVVNQEP--VLFATTIAENIRYGRED--VTMEEIERATKEANAydfIMKLPKKFETvvgERGAQMSGGQKQRIAI 562
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEKLE---MVGLADEFWE---KSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 563 ARALVRNPKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQK 640
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEV 235
|
250 260
....*....|....*....|....
gi 2024474312 641 GVY--YKLVNMQASETEDQLQEEG 662
Cdd:PRK13643 236 DFLkaHELGVPKATHFADQLQKTG 259
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1066-1273 |
7.62e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.49 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRntkTLNiQWLRAQIGIVSQEPILF-DCTI 1144
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLD-PEDRRRIGYLPEERGLYpKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1145 AENIAY-----GdnsrevsheeiVSAAKA-ANIHSFIE--SLPKKYNTRVGDkgaqLSGGQKQRIAIARALIRQPRILLL 1216
Cdd:COG4152 89 GEQLVYlarlkG-----------LSKAEAkRRADEWLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1217 DEATSALDTES-EKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGT 1273
Cdd:COG4152 154 DEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1063-1273 |
8.37e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 96.68 E-value: 8.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1063 TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN---IQWLRAQIGIVSQEPI- 1138
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSIs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 LFDC--TIAENIA--------YGDNSREVSHEEIVSAAKAANihSFIESLPkkyntrvgdkgAQLSGGQKQRIAIARALI 1208
Cdd:PRK10419 101 AVNPrkTVREIIReplrhllsLDKAERLARASEMLRAVDLDD--SVLDKRP-----------PQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1209 RQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGT 1273
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVETQP 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1051-1272 |
1.00e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.56 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1051 NITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGrntKTLN-IQWLRAQ 1129
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNdVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 IGIVSQEPILF-DCTIAENIAYGDNSREVSHEEIVS----AAKAANIHSFIESLPKkyntrvgdkgaQLSGGQKQRIAIA 1204
Cdd:PRK11000 77 VGMVFQSYALYpHLSVAENMSFGLKLAGAKKEEINQrvnqVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1205 RALIRQPRILLLDEATSALDTE---SEKIVQEALDKaREGRTCIVIAH-RLSTIQNADKIAVIQNGKVIEQG 1272
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAAlrvQMRIEISRLHK-RLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1056-1279 |
1.18e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1056 DVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR--NTKTLNIQWLRAQIGIV 1133
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1134 SQEP--ILFDCTIAENIAYGDNSREVSHEEIvsAAKAANIHSFIESlpkkynTRVGDKGAQ-LSGGQKQRIAIARALIRQ 1210
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSLRNLGVPEAEI--TRRVDEALTLVDA------QHFRHQPIQcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1211 PRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
148-365 |
1.18e-21 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 96.72 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 148 FAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTGFIV 227
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 228 GFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDAKR 307
Cdd:cd18552 134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 308 MGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGkVFTVFFSILVGAFS 365
Cdd:cd18552 214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPG-EFISFITALLLLYQ 270
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1066-1283 |
1.55e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 93.75 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERF--YDPLSGEVLLDGRNTKTLNIQwLRAQIGI--VSQEPILFd 1141
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1142 ctiaENIAYGDNSREVsheeivsaakaanihsfieslpkkyntrvgDKGaqLSGGQKQRIAIARALIRQPRILLLDEATS 1221
Cdd:cd03217 90 ----PGVKNADFLRYV------------------------------NEG--FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1222 ALDTESEKIVQEALDKAR-EGRTCIVIAH--RLSTIQNADKIAVIQNGKVIEQGTHQ--QLLAEKGF 1283
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1061-1268 |
1.62e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.16 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1061 YPTRPEVkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVlldgrntktlniqWLRAQIGIVSQEPILF 1140
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1141 DCTIAENIAYGDNSREvshEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEAT 1220
Cdd:PTZ00243 734 NATVRGNILFFDEEDA---ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024474312 1221 SALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKV 1268
Cdd:PTZ00243 811 SALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
783-1277 |
1.70e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.98 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 783 SFVTFFlqGFTFGKAGEI--------LTMRLRSMAFRAILRQEISWFDEPKNS--TGELITRLANDASQvkgatgsrLAL 852
Cdd:PLN03232 344 AFLIFF--GVTFGVLCESqyfqnvgrVGFRLRSTLVAAIFHKSLRLTHEARKNfaSGKVTNMITTDANA--------LQQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 853 VAQNIANLGTG---IVLSLIYGWQL--------TLLLLAIVPIIAITgMIQMKMLA--GHAKKDKKEletlgKVASEAIE 919
Cdd:PLN03232 414 IAEQLHGLWSApfrIIVSMVLLYQQlgvaslfgSLILFLLIPLQTLI-VRKMRKLTkeGLQWTDKRV-----GIINEILA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 920 NIRTVVALTQERKFEYMYgQNLQVSYRNSIKKAHIFgftFAFTQAIMYFT--YAGCFRFGAYLVKNGHM---RFKDVLLV 994
Cdd:PLN03232 488 SMDTVKCYAWEKSFESRI-QGIRNEELSWFRKAQLL---SAFNSFILNSIpvVVTLVSFGVFVLLGGDLtpaRAFTSLSL 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 995 FSAIVFGAMALGQSTSFTPDYAKAKMSAAHLFLLFERVPLIDSYSEEGEKPkmfggnITFKDVAFKYPTRPEVKVLQGLN 1074
Cdd:PLN03232 564 FAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPA------ISIKNGYFSWDSKTSKPTLSDIN 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1075 IEVEKGQTLALVGSSGCGKSTVVQllerfydPLSGEvlLDGRNTKTLNIqwlRAQIGIVSQEPILFDCTIAENIAYGDns 1154
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLIS-------AMLGE--LSHAETSSVVI---RGSVAYVPQVSWIFNATVRENILFGS-- 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1155 rEVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTE-SEKIVQE 1233
Cdd:PLN03232 704 -DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDS 782
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2024474312 1234 ALDKAREGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQL 1277
Cdd:PLN03232 783 CMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1052-1281 |
1.70e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.59 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTlNIQWLRAQIG 1131
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQepilFD-----CTIAENIA-----YGDNSREVshEEIVSaakaanihSFIE--SLPKKYNTRVgdkgAQLSGGQKQ 1199
Cdd:PRK13536 118 VVPQ----FDnldleFTVRENLLvfgryFGMSTREI--EAVIP--------SLLEfaRLESKADARV----SDLSGGMKR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1200 RIAIARALIRQPRILLLDEATSALDTESEKIVQEALDK--AReGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQ 1276
Cdd:PRK13536 180 RLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHA 258
|
....*
gi 2024474312 1277 LLAEK 1281
Cdd:PRK13536 259 LIDEH 263
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1052-1270 |
2.27e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLdGRNTKtlniqwlraqIG 1131
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFDC--TIAENIA-YGDNSREVSheeivsaakaanIHSFIESL---PKKYNTRVGDkgaqLSGGQKQRIAIAR 1205
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRdGAPGGTEQE------------VRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDkAREGrTCIVIAH-R--LSTIqnADKIAVIQNGKVIE 1270
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1055-1293 |
2.43e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.18 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1055 KDVAFKYPTRPE-VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWL----RAQ 1129
Cdd:PRK10535 8 KDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1130 IGIVSQE-PILFDCTIAENI----AYGDNSRevsheeivsAAKAANIHSFIESLpkKYNTRVGDKGAQLSGGQKQRIAIA 1204
Cdd:PRK10535 88 FGFIFQRyHLLSHLTAAQNVevpaVYAGLER---------KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1205 RALIRQPRILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVIQNGKVIEQGTHQQLLAEKGF 1283
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGG 236
|
250
....*....|
gi 2024474312 1284 YYSLVNVQSG 1293
Cdd:PRK10535 237 TEPVVNTASG 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1048-1280 |
2.46e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.85 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1048 FGGNITFKDVAFKYPTRP--EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRN-----TKT 1120
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanlKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1121 LNIQWLRAQIGIVSQEP--ILFDCTIAENIAYGDNSREVSHEEIVSaaKAANIHSFIeSLPKKYNTRvgdKGAQLSGGQK 1198
Cdd:PRK13645 83 KEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYK--KVPELLKLV-QLPEDYVKR---SPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1199 QRIAIARALIRQPRILLLDEATSALDTESEKIVQ---EALDKaREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQG-- 1272
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFInlfERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGsp 235
|
250
....*....|..
gi 2024474312 1273 ----THQQLLAE 1280
Cdd:PRK13645 236 feifSNQELLTK 247
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
413-639 |
2.48e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.64 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYpaRPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEP--VLFATTIAENIRYGREDVTMEE------IERATKEANAYDFIMKLPKkfetvvgergaQMSGGQKQRIAIAR 564
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQ 639
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
413-631 |
2.58e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDIK--------ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYdPKEGTITIDGQDLKSLNV 484
Cdd:PRK15134 276 LDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 485 RYL---REIIGVVNQEP---------VLfaTTIAENIRYGREDVTMEEIERATKEAnaydfiMKlpkkfetvvgERG--- 549
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------ME----------EVGldp 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 550 -------AQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTI--LVIAHRLSTVRN-ADLI 619
Cdd:PRK15134 417 etrhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQV 496
|
250
....*....|..
gi 2024474312 620 AAFENGVITEQG 631
Cdd:PRK15134 497 IVLRQGEVVEQG 508
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1006-1279 |
3.06e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.16 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1006 GQSTSFTPDYAKAKMSAAHLFLlfervplidsyseegekpkMFGGNITFKDVAFKYPTRPevkvlqglnievekgqTLAL 1085
Cdd:PRK14271 8 GQSGAADVDAAAPAMAAVNLTL-------------------GFAGKTVLDQVSMGFPARA----------------VTSL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1086 VGSSGCGKSTVVQLLERFYDPLSG-----EVLLDGRNT-KTLNIQWLRAQIGIVSQEPILFDCTIAENIAYGDNSRE-VS 1158
Cdd:PRK14271 53 MGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKlVP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1159 HEEIVSAAKAANIHSfieSLPKKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKA 1238
Cdd:PRK14271 133 RKEFRGVAQARLTEV---GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2024474312 1239 REGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK14271 210 ADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
431-608 |
3.17e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 94.07 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLreiigVVNQEPVLFA-TTIAENI 509
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 RYGREDVtMEEIERATKEANAYDFImklpkkfeTVVG------ERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:TIGR01184 76 ALAVDRV-LPDLSKSERRAIVEEHI--------ALVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 2024474312 584 TESESVVQAALDKI--RKGRTILVIAH 608
Cdd:TIGR01184 147 ALTRGNLQEELMQIweEHRVTVLMVTH 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
421-617 |
3.61e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 421 SYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGqdlkSLNVRYLREIIGVVNQEPVl 500
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 501 fatTIAENI------------RYGREDvtMEEIERATKEANAYDFimklpkkfetvVGERGAQMSGGQKQRIAIARALVR 568
Cdd:NF040873 73 ---TVRDLVamgrwarrglwrRLTRDD--RAAVDDALERVGLADL-----------AGRQLGELSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTVRNAD 617
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRAD 186
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
430-638 |
3.99e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.14 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK-----EGTITIDGQDLKSLNVR--YLREIIGVVNQEPVLFA 502
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 503 -TTIAENIRYG--------REDVTMEEIERATKEANAYDfimklpkKFETVVGERGAQMSGGQKQRIAIARALVRNPKIL 573
Cdd:PRK14267 99 hLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWD-------EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 574 LLDEATSALDTESESVVQAALDKIRKGRTILVIAHR-LSTVRNADLIAAFENGVITEQGTHDELME 638
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
413-641 |
4.31e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.44 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSlNVRYLREIIG 492
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVL-FATTIAEN-IRYGRE-DVTMEEIERATkeANAYDFiMKLPKKFETvvgeRGAQMSGGQKQRIAIARALVRN 569
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRYfGMSTREIEAVI--PSLLEF-ARLESKADA----RVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 570 PKILLLDEATSALDTESESVVQAALDK-IRKGRTILVIAHRLSTV-RNADLIAAFENGV-ITEQGTHDELMEQKG 641
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRkIAEGRPHALIDEHIG 265
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1068-1277 |
4.56e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 95.93 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1068 KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRN-TKTLNIQWL--RAQIGIVSQEPILF---D 1141
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDlLGMKDDEWRavRSDIQMIFQDPLASlnpR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1142 CTIAENIA------YGDNSREVSHEEiVSA--AKAANIHSFIESLPKKYntrvgdkgaqlSGGQKQRIAIARALIRQPRI 1213
Cdd:PRK15079 115 MTIGEIIAeplrtyHPKLSRQEVKDR-VKAmmLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1214 LLLDEATSALDTESEKIVQEALDK-ARE-GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQL 1277
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1069-1252 |
5.89e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.34 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQW---LRAQ-IGIVSQ-EPILFDCT 1143
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIAY----GDNSREVSHEEIVSAAKAAnihsfieSLPKKYNTRvgdkGAQLSGGQKQRIAIARALIRQPRILLLDEA 1219
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLAAV-------GLEHRANHR----PSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2024474312 1220 TSALDTESEKIVQEALDK--AREGRTCIVIAHRLS 1252
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
427-631 |
7.78e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 92.28 E-value: 7.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLReiIGVVNQEPVLFAT-TI 505
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--IGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 506 AENIRYGRE--DVTMEEIERATKEANAYDFIMKLPKKFetvvgergaqmSGGQKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:cd03268 90 RENLRLLARllGIRKKRIDEVLDVVGLKDSAKKKVKGF-----------SLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024474312 584 TESESVVQAALDKIRK-GRTILVIAHRLSTVRN-ADLIAAFENGVITEQG 631
Cdd:cd03268 159 PDGIKELRELILSLRDqGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1036-1292 |
8.03e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 100.09 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1036 DSYSEEgEKPKMFGGnITFKDVA--FKYPTRPEVkvlQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLL 1113
Cdd:TIGR01257 915 DSFFER-ELPGLVPG-VCVKNLVkiFEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1114 DGRNTKTlNIQWLRAQIGIVSQEPILFD-CTIAENIAYGDNSREVSHEEivsaaKAANIHSFIES--LPKKYNTRVGDkg 1190
Cdd:TIGR01257 990 GGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEE-----AQLEMEAMLEDtgLHHKRNEEAQD-- 1061
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1191 aqLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVI 1269
Cdd:TIGR01257 1062 --LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLY 1139
|
250 260
....*....|....*....|....*....
gi 2024474312 1270 EQGTHQQL--LAEKGFYYSLV----NVQS 1292
Cdd:TIGR01257 1140 CSGTPLFLknCFGTGFYLTLVrkmkNIQS 1168
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
417-669 |
8.08e-21 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 94.15 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 417 NVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlkslnvrylreiIGVVNQ 496
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 497 EPVLFATTIAENIRYGredVTMEEI--ERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILL 574
Cdd:cd03291 106 FSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 575 LDEATSALD--TESEsVVQAALDKIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGTHDELMEQKGVYYKLvnMQAS 652
Cdd:cd03291 183 LDSPFGYLDvfTEKE-IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSK--LMGY 259
|
250
....*....|....*..
gi 2024474312 653 ETEDQLQEEGNASSVSE 669
Cdd:cd03291 260 DTFDQFSAERRNSILTE 276
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1066-1279 |
8.73e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.49 E-value: 8.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTL-------------NIQWLRAQIGI 1132
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1133 VSQEPILFD-CTIAENIAYgdnsrevSHEEIVSAAKAANIHSFIeslpkKYNTRVG-DKGAQ------LSGGQKQRIAIA 1204
Cdd:PRK10619 97 VFQHFNLWShMTVLENVME-------APIQVLGLSKQEARERAV-----KYLAKVGiDERAQgkypvhLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1205 RALIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
413-610 |
1.12e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.23 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNV---FFsyPARPD-IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVrYLR 488
Cdd:COG1101 2 LELKNLsktFN--PGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 489 -EIIGVVNQEPVL---FATTIAENI--------RYG-REDVTMEEIERATKEANAYDfiMKLPKKFETVVGergaQMSGG 555
Cdd:COG1101 79 aKYIGRVFQDPMMgtaPSMTIEENLalayrrgkRRGlRRGLTKKRRELFRELLATLG--LGLENRLDTKVG----LLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 556 QKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAHRL 610
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
416-638 |
1.33e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.93 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 416 QNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVR-YLREIIGVV 494
Cdd:PRK10575 15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 495 NQEPVLFATTIAENI------------RYGREDvtMEEIERATKEANAYDFIMKLPKkfetvvgergaQMSGGQKQRIAI 562
Cdd:PRK10575 92 QQLPAAEGMTVRELVaigrypwhgalgRFGAAD--REKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 563 ARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRTILVIA--HRLS-TVRNADLIAAFENGVITEQGTHDELME 638
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
430-609 |
1.77e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.19 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDgQDLKSLnvrylreiigVVNQEPVLFATTIAENI 509
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP-AGARVL----------FLPQRPYLPLGTLREAL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 RY--GREDVTMEEIERATKEANAYDFIMKLpkkfeTVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 587
Cdd:COG4178 447 LYpaTAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
170 180
....*....|....*....|..
gi 2024474312 588 SVVQAALDKIRKGRTILVIAHR 609
Cdd:COG4178 522 AALYQLLREELPGTTVISVGHR 543
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
718-1218 |
1.89e-20 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 96.79 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 718 IMKLNKTEWPYFVVGTLCAIINGALQPIFSVMISDVIgmfvekgkAAIRETNSTYALLFLGFGLISFVTFFLQGFTFGKA 797
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLANAGLIALINQAL--------NATGAALARLLLLFAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 798 GEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATgSRLALVAQNIANlgtgIVLSLIY-GWQLTL 876
Cdd:COG4615 76 GQHAVARLRLRLSRRILAAPLERLE--RIGAARLLAALTEDVRTISQAF-VRLPELLQSVAL----VLGCLAYlAWLSPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 877 LLLAIVPIIAITGMIQMKMLaghaKKDKKELETLGKVASEAIENIRTVV------ALTQERKfEYMYGQNLQVS---YRN 947
Cdd:COG4615 149 LFLLTLVLLGLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFRALLegfkelKLNRRRR-RAFFDEDLQPTaerYRD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 948 SIKKAH-IFGFTFAFTQAIMYFTYAGCFrfgAYLVKNGHMRFKDVLLVFSAIVFGAMALGQSTSFTPDYAKAKMSA---A 1023
Cdd:COG4615 224 LRIRADtIFALANNWGNLLFFALIGLIL---FLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALrkiE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1024 HLFLLFERVPLIDSYSEEGEKPKMFGGnITFKDVAFKYPTRPEVK--VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLE 1101
Cdd:COG4615 301 ELELALAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1102 RFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDctiaenIAYGdnsrevsheeIVSAAKAANIHSFIESLPKK 1181
Cdd:COG4615 380 GLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD------RLLG----------LDGEADPARARELLERLELD 443
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024474312 1182 YNTRVgDKGA----QLSGGQKQRIAIARALIRQPRILLLDE 1218
Cdd:COG4615 444 HKVSV-EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1063-1270 |
1.93e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 96.40 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1063 TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYdP---LSGEVLLDGRNTKTLNI-QWLRAQIGIVSQE-- 1136
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKDIrDSEALGIVIIHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1137 --PILfdcTIAENIAYGDnsrEVSHEEIVSAaKAANIHSfiESLPKKY------NTRVGDKGAqlsgGQKQRIAIARALI 1208
Cdd:NF040905 89 liPYL---SIAENIFLGN---ERAKRGVIDW-NETNRRA--RELLAKVgldespDTLVTDIGV----GKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1209 RQPRILLLDEATSAL-DTESEKIVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIE 1270
Cdd:NF040905 156 KDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
163-383 |
2.13e-20 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 92.88 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 163 RQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTGFIVGFTKGWKLTLVILAL 242
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 243 SPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDAKRMGIQKAISANISMGV 322
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 323 SFFLIYGSYALAFWYGTILVLSEDYTIGKV--FTVFFSILVGAfsVGQAAPSMEAFANARGAA 383
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLvaFLLYLFQLITP--LSQLSSFFTQLQKALGAL 286
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1054-1269 |
2.34e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1054 FKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRntktlniqwlrAQIGIV 1133
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1134 SQEPILFD-CTIAENIAYGDNS--------REVSH---EEIVSAAKAANIHSFIESL-------------------PKKY 1182
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAElraleaelEELEAklaEPDEDLERLAELQEEFEALggweaearaeeilsglgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1183 NTRVGDkgaqLSGGQKQRIAIARALIRQPRILLLDEATSALDTESekiVQ--EALDKAREGrTCIVIAH-R--LSTIqnA 1257
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV--A 216
|
250
....*....|..
gi 2024474312 1258 DKIAVIQNGKVI 1269
Cdd:COG0488 217 TRILELDRGKLT 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1052-1280 |
2.56e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.41 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPT--RPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEV----------------LL 1113
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1114 DGRNTKtlniqwlraQIGIVSQEPILF-DCTIAENI--AYG-DNSREVSHEEIVSAAKAAnihSFIESLPKKYNTRVGDk 1189
Cdd:TIGR03269 360 RGRAKR---------YIGILHQEYDLYpHRTVLDNLteAIGlELPDELARMKAVITLKMV---GFDEEKAEEILDKYPD- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1190 gaQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNG 1266
Cdd:TIGR03269 427 --ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDG 504
|
250
....*....|....
gi 2024474312 1267 KVIEQGTHQQLLAE 1280
Cdd:TIGR03269 505 KIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
413-636 |
2.75e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.78 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDI--KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDL----KSLNVRY 486
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 487 LREIIGVVNQ--EPVLFATTIAENIRYGRED--VTMEEIERATKEAnaydfiMKLPKKFETVVGERGAQMSGGQKQRIAI 562
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREM------IELVGLPEELLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 563 ARALVRNPKILLLDEATSALDTESESVVQ---AALDKiRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1025-1279 |
2.95e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.89 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1025 LFLLFERVpLIDSYSEEGEKPKmfggnITFKDVAFKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFY 1104
Cdd:PLN03130 594 LLLAEERV-LLPNPPLEPGLPA-----ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1105 DPLSGEVLLdgrntktlniqwLRAQIGIVSQEPILFDCTIAENIAYGDNSREVSHEEivsAAKAANIHSFIESLPKKYNT 1184
Cdd:PLN03130 668 PPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYER---AIDVTALQHDLDLLPGGDLT 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1185 RVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVI 1263
Cdd:PLN03130 733 EIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILV 812
|
250
....*....|....*.
gi 2024474312 1264 QNGKVIEQGTHQQLLA 1279
Cdd:PLN03130 813 HEGMIKEEGTYEELSN 828
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
426-614 |
4.38e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.48 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 426 PDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-IGVVNQEPVLFAT- 503
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENIRYGREDVT-----MEEIERATKE-ANAYDFIMKLpkkfETVVGergaQMSGGQKQRIAIARALVRNPKILLLDE 577
Cdd:COG3845 96 TVAENIVLGLEPTKggrldRKAARARIRElSERYGLDVDP----DAKVE----DLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024474312 578 ATSAL-DTESESVVqAALDKIRK-GRTILVIAHRLSTVR 614
Cdd:COG3845 168 PTAVLtPQEADELF-EILRRLAAeGKSIIFITHKLREVM 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
413-643 |
4.79e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.61 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNV--FFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITID----GQDL------- 479
Cdd:PRK13631 22 LRVKNLycVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKnnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 480 -----KSLNVRYLREIIGVVNQEP--VLFATTIAENIRYGREDVTMEEIErATKEANAYDFIMKLPKKFEtvvgERGA-Q 551
Cdd:PRK13631 102 npyskKIKNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLDDSYL----ERSPfG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 552 MSGGQKQRIAIARALVRNPKILLLDEATSALDTESES-VVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITE 629
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILK 256
|
250
....*....|....
gi 2024474312 630 QGTHDELMEQKGVY 643
Cdd:PRK13631 257 TGTPYEIFTDQHII 270
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
412-583 |
5.22e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.37 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 412 NLEFQNVFFSYPArpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlkslnvrylreii 491
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 gVVNQ-EP------VLFAT-------TIAENIRYGREDVTM--EEIERATKEANAydfIMKLpkkfETVVGERGAQMSGG 555
Cdd:PRK11650 67 -VVNElEPadrdiaMVFQNyalyphmSVRENMAYGLKIRGMpkAEIEERVAEAAR---ILEL----EPLLDRKPRELSGG 138
|
170 180
....*....|....*....|....*...
gi 2024474312 556 QKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1031-1272 |
5.36e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.08 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1031 RVPLI-----DSYSEEGEKPKMFGGN--ITFKDVAFKYPTRP--------EVKVLQGLNIEVEKGQTLALVGSSGCGKST 1095
Cdd:PRK10261 286 RFPLIslehpAKQEPPIEQDTVVDGEpiLQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKST 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1096 VVQLLERFYDPLSGEVLLDGRNTKTLN---IQWLRAQIGIVSQEPIlfdCTIAENIAYGDNSRE--VSHEEIVSAAKAAN 1170
Cdd:PRK10261 366 TGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY---ASLDPRQTVGDSIMEplRVHGLLPGKAAAAR 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1171 IHSFIEslpkkyntRVGDKGA-------QLSGGQKQRIAIARALIRQPRILLLDEATSALDTE-SEKIVQEALDKARE-G 1241
Cdd:PRK10261 443 VAWLLE--------RVGLLPEhawryphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfG 514
|
250 260 270
....*....|....*....|....*....|..
gi 2024474312 1242 RTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:PRK10261 515 IAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
413-639 |
5.42e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVR---YLRE 489
Cdd:COG4152 2 LELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 iigvvnqEPVLFA-TTIAENIRY-GR-EDVTMEEIERATKEanaydfimkLPKKFEtvVGERGA----QMSGGQKQRIAI 562
Cdd:COG4152 79 -------ERGLYPkMKVGEQLVYlARlKGLSKAEAKRRADE---------WLERLG--LGDRANkkveELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 563 ARALVRNPKILLLDEATSALDTES-ESVVQAALDKIRKGRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELMEQ 639
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1052-1278 |
6.24e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.75 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFkypTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:PRK09536 4 IDVSDLSV---EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPIL-FDCTIAENIAYGdnsrEVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKG-AQLSGGQKQRIAIARALIR 1209
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMG----RTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPvTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1210 QPRILLLDEATSALDTESE-KIVQEALDKAREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1065-1280 |
6.57e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.98 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQ-WLRAQIGIVSQEPILF-DC 1142
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1143 TIAENIAYGD--NSREVSHE-EIVSAAKAANIHSFIESLPkkyNTRVGDkgaqLSGGQKQRIAIARALIRQPRILLLDEA 1219
Cdd:PRK11288 95 TVAENLYLGQlpHKGGIVNRrLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1220 TSALDT-ESE---KIVQEALDkarEGRTCIVIAHRLSTI-QNADKIAVIQNGKVIE------QGTHQQLLAE 1280
Cdd:PRK11288 168 TSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRDQLVQA 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1059-1272 |
9.01e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.51 E-value: 9.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1059 FKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRntktlnIQW-LRAQIGIVSQ-- 1135
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPElt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1136 --EPILFDCTIaeniaYGdnsreVSHEEIvsAAKAANIHSFIEsLPKKYNTRVGdkgaQLSGGQKQRIAIARALIRQPRI 1213
Cdd:cd03220 101 grENIYLNGRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1214 LLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQG 1272
Cdd:cd03220 164 LLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
729-986 |
9.08e-20 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 91.32 E-value: 9.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQpifsVMISDVIGMFVEkgkaAIRETNST------YALLFLGFGLISFVTFFLQGFTFGKAGEILT 802
Cdd:cd18541 1 YLLGILFLILVDLLQ----LLIPRIIGRAID----ALTAGTLTasqllrYALLILLLALLIGIFRFLWRYLIFGASRRIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 803 MRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIV 882
Cdd:cd18541 73 YDLRNDLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 883 PIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFT 962
Cdd:cd18541 151 PLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLI 230
|
250 260
....*....|....*....|....
gi 2024474312 963 QAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18541 231 GLLIGLSFLIVLWYGGRLVIRGTI 254
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1068-1281 |
9.90e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.46 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1068 KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLL----------ERFYDPLSGEVLLDGRNTKtlNIQWLRAQIGIVSQEP 1137
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLAR--DIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 ILFD-CTIAENIAYGDNSREVSHEEIVSAAKAANIHSFIESLpkkynTRVG------DKGAQLSGGQKQRIAIARALIRQ 1210
Cdd:PRK09984 96 NLVNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1211 PRILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQLLAEK 1281
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1052-1265 |
1.20e-19 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 87.21 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPT-RPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNtktlniqwlraQI 1130
Cdd:cd03223 1 IELENLSLATPDgRV---LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEPILFDCTIAENIAY--GDNsrevsheeivsaakaanihsfieslpkkyntrvgdkgaqLSGGQKQRIAIARALI 1208
Cdd:cd03223 67 LFLPQRPYLPLGTLREQLIYpwDDV---------------------------------------LSGGEQQRLAFARLLL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1209 RQPRILLLDEATSALDTESEKIVQEALDKarEGRTCIVIAHRLSTIQNADKIAVIQN 1265
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1053-1273 |
1.46e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.37 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1053 TFKDVAF--KYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRntktlnIQWLraqI 1130
Cdd:COG1134 23 SLKELLLrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GI-VSQEPILfdcTIAENI-----AYGDNSREVSH--EEIVSAAkaaNIHSFIEsLP-KKYntrvgdkgaqlSGGQKQRI 1201
Cdd:COG1134 94 ELgAGFHPEL---TGRENIylngrLLGLSRKEIDEkfDEIVEFA---ELGDFID-QPvKTY-----------SSGMRARL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1202 AIARALIRQPRILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGT 1273
Cdd:COG1134 156 AFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
749-1011 |
1.48e-19 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 90.62 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 749 MISDVIGMFVEKGKAAIRETNSTYALLFL-----GFGLISFVTFFLqgftFGKAGEILTMRLRSMAFRAILRQEISWFDe 823
Cdd:cd18575 14 ALGQGLRLLIDQGFAAGNTALLNRAFLLLlavalVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 824 pKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKD 903
Cdd:cd18575 89 -TTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 904 KKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTqaimyftyagcfrfgaylvkn 983
Cdd:cd18575 168 QDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALV--------------------- 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 2024474312 984 ghmrfkdVLLVFSAIVF-----------GAMALGQSTSF 1011
Cdd:cd18575 227 -------IFLVFGAIVFvlwlgahdvlaGRMSAGELSQF 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
413-639 |
2.02e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIdGQDLKslnvrylreiIG 492
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFAT--TIAENIRYGREDVTmeeieraTKEANAY--DFIMKlPKKFETVVGErgaqMSGGQKQRIAIARALVR 568
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGT-------EQEVRGYlgRFLFS-GDDAFKPVGV----LSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKIrKGrTILVIAH-R--LSTVrnADLIAAFENGVITE-QGTHDELMEQ 639
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDDYLEK 520
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
130-350 |
2.56e-19 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 90.06 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 130 EEMTRYAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGE 209
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 210 KIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFG 289
Cdd:cd18784 113 NLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 290 GQRKETERYQKNLEDAKRMGIQKAIS-ANISMGVSFFLIyGSYALAFWYGTILVLSEDYTIG 350
Cdd:cd18784 193 NEDGEANRYSEKLKDTYKLKIKEALAyGGYVWSNELTEL-ALTVSTLYYGGHLVITGQISGG 253
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
412-636 |
2.86e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 412 NLEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKslNVRYLREII 491
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFA-TTIAENIRYGREDVTMEEIERATKEANAYDfIMKLPKKFEtvvgERGAQMSGGQKQRIAIARALVRNP 570
Cdd:PRK11000 78 GMVFQSYALYPhLSVAENMSFGLKLAGAKKEEINQRVNQVAE-VLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 571 KILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAH-RLSTVRNADLIAAFENGVITEQGTHDEL 636
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1052-1279 |
2.95e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.25 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTlNIQWLRAQIG 1131
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQ----EPilfDCTIAENI-AYGdnsrevSHEEIVSAAKAANIHSFIE--SLPKKYNTRVGDkgaqLSGGQKQRIAIA 1204
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLlVFG------RYFGLSAAAARALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1205 RALIRQPRILLLDEATSALDTESEKIVQEALDK--AReGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
413-625 |
2.97e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.07 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPArpdIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYdPK---EGTITIDGQDLKSLNVRYLRE 489
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 I-IGVVNQEPVLFAT-TIAENIRYGREDVTMEEIERATKEANAYDFIMKLpkKFETVVGERGAQMSGGQKQRIAIARALV 567
Cdd:PRK13549 82 AgIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 568 RNPKILLLDEATSALdTESEsvVQAALDKIR----KGRTILVIAHRLSTVRN-ADLIAAFENG 625
Cdd:PRK13549 160 KQARLLILDEPTASL-TESE--TAVLLDIIRdlkaHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
430-610 |
3.13e-19 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 89.14 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDpKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTIAENI 509
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 R-YGREdvTMEEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESES 588
Cdd:cd03289 98 DpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175
|
170 180
....*....|....*....|..
gi 2024474312 589 VVQAALDKIRKGRTILVIAHRL 610
Cdd:cd03289 176 VIRKTLKQAFADCTVILSEHRI 197
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
427-639 |
3.31e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 87.20 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK--EGTITIDGQDLKSLNV--RyLREIIGVVNQEPVLFa 502
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPeeR-ARLGIFLAFQYPPEI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 503 ttiaenirygrEDVTMEeieratkeanayDFIMKLPKKFetvvgergaqmSGGQKQRIAIARALVRNPKILLLDEATSAL 582
Cdd:cd03217 90 -----------PGVKNA------------DFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 583 DTESESVVQAALDKIR-KGRTILVIAH--RLSTVRNADLIAAFENGVITEQGThDELMEQ 639
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
413-639 |
3.42e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 92.67 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPArpdIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVR-YLREII 491
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQE----PVLfatTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKF--ETVVGErgaqMSGGQKQRIAIARA 565
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIdpDTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 566 LVRNPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAHRLSTV-RNADLIAAFENG--VIT----EQGTHDELM 637
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRaEGRVILYVSHRMEEIfALCDAITVFKDGryVATfddmAQVDRDQLV 234
|
..
gi 2024474312 638 EQ 639
Cdd:PRK11288 235 QA 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1068-1268 |
3.86e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 86.33 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1068 KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNI-QWLRAQIGIVSQEP----ILFDC 1142
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1143 TIAENIAYGdnsrevsheeivsaakaanihsfieslpkkyntrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSA 1222
Cdd:cd03215 94 SVAENIALS---------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1223 LDTES-EKIVQEALDKAREGRTCIVIahrlST-----IQNADKIAVIQNGKV 1268
Cdd:cd03215 135 VDVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
745-986 |
4.30e-19 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 89.53 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 745 IFSVMISDVIGMFVEKGKAAIRETNSTYALLFLGFGLISFVTFFLQG-FTF------GKAGEILTMRLRSMAFRAILRQE 817
Cdd:cd18574 10 LVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 818 ISWFDepKNSTGELITRLANDASQVKGATGSrlaLVAQNIANL----GTGIVLSLIYGwQLTLLLLAIVPIIAITGMIQM 893
Cdd:cd18574 90 IAFFD--THRTGELVNRLTADVQEFKSSFKQ---CVSQGLRSVtqtvGCVVSLYLISP-KLTLLLLVIVPVVVLVGTLYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 894 KMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKkahiFGFTFAFTQAIMYFTYAG- 972
Cdd:cd18574 164 SFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK----LGLGIGIFQGLSNLALNGi 239
|
250
....*....|....*..
gi 2024474312 973 ---CFRFGAYLVKNGHM 986
Cdd:cd18574 240 vlgVLYYGGSLVSRGEL 256
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1069-1278 |
4.33e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.50 E-value: 4.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPIL-FDCTIAEN 1147
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1148 IAYG--------DNSREVSHEEIVSAAKAANIhsfieslpkkynTRVGDKGAQ-LSGGQKQRIAIARALIRQPRILLLDE 1218
Cdd:PRK10253 102 VARGryphqplfTRWRKEDEEAVTKAMQATGI------------THLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1219 ATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
413-642 |
4.38e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.01 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSL-NVRYLREII 491
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFA-TTIAENIRYG----REDVTMEEIERAtkeanaYDFimkLPKKFETVVgERGAQMSGGQKQRIAIARAL 566
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGgffaERDQFQERIKWV------YEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 567 VRNPKILLLDEATSALdteSESVVQAALDKIRK----GRTILVIAHRLS-TVRNADLIAAFENGVITEQGTHDELMEQKG 641
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
.
gi 2024474312 642 V 642
Cdd:PRK11614 230 V 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
413-638 |
4.98e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSlNVRYLREIIG 492
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VV----NQEPVLfatTIAENIR-YGRE-DVTMEEIERATkeANAYDFiMKLPKKFETVVGErgaqMSGGQKQRIAIARAL 566
Cdd:PRK13537 84 VVpqfdNLDPDF---TVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 567 VRNPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELME 638
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
413-642 |
5.35e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQ--DLKSLNVRYLREI 490
Cdd:PRK13638 2 LATSDLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEP--VLFATTIAENIRYGRED--VTMEEIERATKEAnaydfimklpkkfETVVGERGAQ------MSGGQKQRI 560
Cdd:PRK13638 79 VATVFQDPeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEA-------------LTLVDAQHFRhqpiqcLSHGQKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 561 AIARALVRNPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQG------T 632
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevfA 225
|
250
....*....|
gi 2024474312 633 HDELMEQKGV 642
Cdd:PRK13638 226 CTEAMEQAGL 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1059-1279 |
5.56e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.31 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1059 FKYPT----RPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVS 1134
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1135 QEPI-----------LFDCTIAENIAYGDNSREvshEEIVSAAKAANIhsfiesLPKKYNTRvgdkGAQLSGGQKQRIAI 1203
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLNTDLEPEQRE---KQIIETLRQVGL------LPDHASYY----PHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1204 ARALIRQPRILLLDEATSALD-TESEKIVQEALD-KAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
413-625 |
5.75e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 84.81 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDgqdlKSLNVRYLreiig 492
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 vvnqepvlfattiaenirygredvtmeeieratkeanaydfimklpkkfetvvgergAQMSGGQKQRIAIARALVRNPKI 572
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 573 LLLDEATSALDTESESVVQAALDKIRkgRTILVIAH-R--LSTVrnADLIAAFENG 625
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
413-637 |
5.92e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPArpdIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-I 491
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFAT-TIAENIRYG--REDVTMEEIERATKEANAYdfiMKLPKKFETV-VGERgaqmsggqkQRIAIARALV 567
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 568 RNPKILLLDEATSALdTESEsvVQAALDKIR----KGRTILVIAHRLSTVRN-ADLIAAFENGVI-----TEQGTHDELM 637
Cdd:PRK15439 157 RDSRILILDEPTASL-TPAE--TERLFSRIRellaQGVGIVFISHKLPEIRQlADRISVMRDGTIalsgkTADLSTDDII 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
413-631 |
6.32e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 86.57 E-value: 6.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNvrylREIIG 492
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLF-ATTIAENIRY-GR-EDVTMEEI-ERATKEANAYDFIMKLPKKFEtvvgergaQMSGGQKQRIAIARALVR 568
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQlKGLKKEEArRRIDEWLERLELSEYANKRVE--------ELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTV-RNADLIAAFENGVITEQG 631
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1068-1254 |
6.99e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1068 KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNT---KTLNIQWLRAQIGIVSQEP-ILFDCT 1143
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIAYgdnsrevshEEIVSAAKAANIHSFIESLPKKyntrVG--DKGA----QLSGGQKQRIAIARALIRQPRILLLD 1217
Cdd:PRK10908 96 VYDNVAI---------PLIIAGASGDDIRRRVSAALDK----VGllDKAKnfpiQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024474312 1218 EATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTI 1254
Cdd:PRK10908 163 EPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
413-637 |
7.09e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 87.97 E-value: 7.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSY------PARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRY 486
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 487 LREIIGVVNQEPvlfATTIAENIRYG-------REDVTMEEIERATKeanaydfImklpkkFETV--VGERGAQ------ 551
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTAEEREER-------I------FATLrlVGLLPEHanfyph 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 552 -MSGGQKQRIAIARALVRNPKILLLDEATSALDTESES-VVQAALD-KIRKGRTILVIAHRLSTVRN-ADLIAAFENGVI 627
Cdd:COG4167 149 mLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEV 228
|
250
....*....|
gi 2024474312 628 TEQGTHDELM 637
Cdd:COG4167 229 VEYGKTAEVF 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1052-1267 |
9.42e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 84.04 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTktlniqwlraqig 1131
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 ivsqepilfdctiaenIAYgdnsrevsheeivsaakaanihsFieslpkkyntrvgdkgAQLSGGQKQRIAIARALIRQP 1211
Cdd:cd03221 65 ----------------IGY-----------------------F----------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALdKAREGrTCIVIAHRLSTIQN-ADKIAVIQNGK 1267
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
771-986 |
1.56e-18 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 87.45 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 771 TYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGA--TGS 848
Cdd:cd18548 40 RTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFvmMLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 849 RLALVAqnIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALT 928
Cdd:cd18548 118 RMLVRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFN 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 929 QE----RKFEymygqnlQVS---YRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18548 196 REdyeeERFD-------KANddlTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSL 253
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1052-1277 |
1.72e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.13 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFkypTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWL---RA 1128
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1129 QIGIVSQEPILF-DCTIAENIAYgdNSREvsHEEIVSAAKAANIHSFIESlpkkyntrVGDKGA------QLSGGQKQRI 1201
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAY--PLRE--HTQLPAPLLHSTVMMKLEA--------VGLRGAaklmpsELSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1202 AIARALIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQL 1277
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
779-986 |
2.48e-18 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 86.98 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 779 FGLISFVTFFLQG-----FTFGKAGeiLTMRLRSMAFRAILRQEISWFDEPKnsTGELITRLANDASQVKGATGSRLALV 853
Cdd:cd18784 42 MGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFDTVK--TGDITSRLTSDTTTMSDTVSLNLNIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 854 AQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKF 933
Cdd:cd18784 118 LRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 934 EYMYGQNLQVSYRNSIKKAHIFG--------FTFAFTQAIMYftyagcfrFGAYLVKNGHM 986
Cdd:cd18784 198 ANRYSEKLKDTYKLKIKEALAYGgyvwsnelTELALTVSTLY--------YGGHLVITGQI 250
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
427-631 |
2.52e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVL-FATTI 505
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 506 AENIRYGRE------DVTMEEIERATKEA-NAYDFIMKLPKKFETVvgergaqmSGGQKQRIAIARALVRNPKILLLDEA 578
Cdd:PRK09536 95 RQVVEMGRTphrsrfDTWTETDRAAVERAmERTGVAQFADRPVTSL--------SGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 579 TSALDTESE-SVVQAALDKIRKGRTILVIAHRLS-TVRNADLIAAFENGVITEQG 631
Cdd:PRK09536 167 TASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1060-1279 |
3.96e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.08 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1060 KYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVvqllerFY------DPLSGEVLLDGRNTKTLNIqWLRAQIGI- 1132
Cdd:COG1137 12 SYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1133 -VSQEPILF-DCTIAENIAYGDNSREVSHEEIvsAAKAAN-IHSF-IESLPKKyntrvgdKGAQLSGGQKQRIAIARALI 1208
Cdd:COG1137 82 yLPQEASIFrKLTVEDNILAVLELRKLSKKER--EERLEElLEEFgITHLRKS-------KAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1209 RQPRILLLDEATSALD----TESEKIVQEALDK----------AREgrtciviahrlsTIQNADKIAVIQNGKVIEQGTH 1274
Cdd:COG1137 153 TNPKFILLDEPFAGVDpiavADIQKIIRHLKERgigvlitdhnVRE------------TLGICDRAYIISEGKVLAEGTP 220
|
....*
gi 2024474312 1275 QQLLA 1279
Cdd:COG1137 221 EEILN 225
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
130-361 |
4.12e-18 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 86.31 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 130 EEMTRYAYYYSGIGAGVLFAAYIQvSFWTLAAGRQI-KRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIG 208
Cdd:cd18541 37 SQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 209 EKIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAF 288
Cdd:cd18541 116 PGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAF 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 289 GGQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKV--FTVFFSILV 361
Cdd:cd18541 196 VQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLvaFNSYLGMLI 270
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
729-986 |
4.13e-18 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 86.30 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAAIRETNS---TYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRL 805
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSgllRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 806 RSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPII 885
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 886 AITgmiqMKMLAGHAKKD-KKELETLGKVAS---EAIENIRTVVALTQE----RKFEYMygqNLQvsYRNSIKKAHIF-G 956
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELNGyieEMISGQKVVKAFNREeeaiEEFDEI---NEE--LYKASFKAQFYsG 229
|
250 260 270
....*....|....*....|....*....|
gi 2024474312 957 FTFAFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18547 230 LLMPIMNFINNLGYVLVAVVGGLLVINGAL 259
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1025-1270 |
4.56e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 89.26 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1025 LFLLFERVPLI------------------------DSYSEEGEKPKMFGG--NITFKDVAFKYPTRP-EVKvlqGLNIEV 1077
Cdd:PRK10522 270 LTLLFLRTPLLsavgalptllsaqvafnklnklalAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNGfSVG---PINLTI 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1078 EKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCTIaeniayGDNSREv 1157
Cdd:PRK10522 347 KRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEGKP- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1158 sheeivsaAKAANIHSFIESLPKKYNTRVGD---KGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIV-QE 1233
Cdd:PRK10522 420 --------ANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQV 491
|
250 260 270
....*....|....*....|....*....|....*...
gi 2024474312 1234 ALDKARE-GRTCIVIAHRLSTIQNADKIAVIQNGKVIE 1270
Cdd:PRK10522 492 LLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1052-1279 |
4.99e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.09 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERF--YDPLSGEVL----------------L 1113
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1114 DGRNTK----TLNIQ----W---------LRAQIGIVSQEPILF--DCTIAENIAYGDNSREVSHEEIVSaaKAANIhsf 1174
Cdd:TIGR03269 78 VGEPCPvcggTLEPEevdfWnlsdklrrrIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVG--RAVDL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1175 IESLpkKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKA--REGRTCIVIAHRLS 1252
Cdd:TIGR03269 153 IEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*...
gi 2024474312 1253 TIQN-ADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:TIGR03269 231 VIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
428-640 |
5.95e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.29 E-value: 5.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSL------------------------N 483
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 484 VRYLREIIGVVNQ--EPVLFATTIAENIRYGREDVTMEEiERATKEANAYDFIMKLPKKFEtvvgERGA-QMSGGQKQRI 560
Cdd:PRK13651 100 IKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 561 AIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTV-RNADLIAAFENG-VITEQGTHDELM 637
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVlEWTKRTIFFKDGkIIKDGDTYDILS 254
|
...
gi 2024474312 638 EQK 640
Cdd:PRK13651 255 DNK 257
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1067-1272 |
9.26e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 9.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1067 VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwLRAQIGI--VSQEPILF-DCT 1143
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIAYGDNSREVSHEEIVSAAKAANIHSFIESlpkkyntrvgdKGAQLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1224 D-TESEKI---VQEALDKareGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQG 1272
Cdd:PRK15439 172 TpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1064-1263 |
1.03e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 82.93 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1064 RPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCT 1143
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIAY--GDNSREvsheEIVSAAKAANIHSFiESLPkkyntrvgdkGAQLSGGQKQRIAIARALIRQPRILLLDEATS 1221
Cdd:cd03231 90 VLENLRFwhADHSDE----QVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024474312 1222 ALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVI 1263
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
430-627 |
1.50e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.96 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLnvrylREIIGVVNQEPVLFA-TTIAEN 508
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 509 IRYGREDVTMEEIERATKEANaydfimklpkkFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESES 588
Cdd:PRK11247 102 VGLGLKGQWRDAALQALAAVG-----------LADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024474312 589 VVQAALDKI--RKGRTILVIAHRLS-TVRNADLIAAFENGVI 627
Cdd:PRK11247 171 EMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
413-610 |
1.82e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 87.37 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPArpdIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-I 491
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 GVVNQEPVLFAT-TIAENIRYGREDVT-MEEIERATKEANAYDFIMKLPKKF--ETVVGErgaqMSGGQKQRIAIARALV 567
Cdd:PRK10762 82 GIIHQELNLIPQlTIAENIFLGREFVNrFGRIDWKKMYAEADKLLARLNLRFssDKLVGE----LSIGEQQMVEIAKVLS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024474312 568 RNPKILLLDEATSAL-DTESESVVQAALDKIRKGRTILVIAHRL 610
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
414-637 |
2.12e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.21 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 414 EFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGV 493
Cdd:COG4604 3 EIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 494 VNQEPVlFAT--TIAENIRYGR----------EDvtmeeiERATKEANAYdfiMKLpkkfETVVGERGAQMSGGQKQRIA 561
Cdd:COG4604 80 LRQENH-INSrlTVRELVAFGRfpyskgrltaED------REIIDEAIAY---LDL----EDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 562 IARALVRNPKILLLDEATSALDTeSESV-----VQAALDKirKGRTILVIAHRLstvrN-----ADLIAAFENGVITEQG 631
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDM-KHSVqmmklLRRLADE--LGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQG 218
|
....*.
gi 2024474312 632 THDELM 637
Cdd:COG4604 219 TPEEII 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1046-1278 |
2.27e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.44 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1046 KMFGGNITFKDVAFK-YPtrpevkvlqglnievekGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQ 1124
Cdd:PRK11701 14 KLYGPRKGCRDVSFDlYP-----------------GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1125 WL---------RAQIGIVSQEP---ILFDCTIAENIA----------YGDNSREVSH----EEIVSAakaanihsfiesl 1178
Cdd:PRK11701 77 ALseaerrrllRTEWGFVHQHPrdgLRMQVSAGGNIGerlmavgarhYGDIRATAGDwlerVEIDAA------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1179 pkkyntRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTEsekiVQ-EALDKARE-----GRTCIVIAHRLS 1252
Cdd:PRK11701 144 ------RIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLA 213
|
250 260
....*....|....*....|....*..
gi 2024474312 1253 TIQN-ADKIAVIQNGKVIEQGTHQQLL 1278
Cdd:PRK11701 214 VARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1043-1278 |
3.62e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.91 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1043 EKPKMFGGNITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN 1122
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1123 IQWLRAQIGIVSQE-PILFDCTIAENIA------------YGDNSREVSHEEIVSAAKAANIHSFIESlpkkyntrvgdk 1189
Cdd:PRK10575 80 SKAFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDS------------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1190 gaqLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAhRLSTIQNA----DKIAVIQN 1265
Cdd:PRK10575 148 ---LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRG 223
|
250
....*....|...
gi 2024474312 1266 GKVIEQGTHQQLL 1278
Cdd:PRK10575 224 GEMIAQGTPAELM 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
428-583 |
3.72e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.13 E-value: 3.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVR---YLR-EIIGVVNQEPVLFAT 503
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAenirygREDVTMEEIERATKEANAYDFIMKLPKKFEtvVGER----GAQMSGGQKQRIAIARALVRNPKILLLDEAT 579
Cdd:PRK10584 103 LNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
....
gi 2024474312 580 SALD 583
Cdd:PRK10584 175 GNLD 178
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
413-631 |
3.81e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQD--LKSLNVRYLREI 490
Cdd:PRK10895 4 LTAKNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 iGVVNQEPVLFAT-TIAENIRYG---REDVTMEEIERATKEANAYDFIMKLPKKFetvvgerGAQMSGGQKQRIAIARAL 566
Cdd:PRK10895 81 -GYLPQEASIFRRlSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 567 VRNPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAHrlsTVRnaDLIAAFENGVITEQG 631
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDH---NVR--ETLAVCERAYIVSQG 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
411-646 |
4.06e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 411 GNLEFQNVFFSYPARP--DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTiTIDGQ-----DLKSLN 483
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDyaipaNLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 484 -VRYLREIIGVVNQEP--VLFATTIAENIRYGREDVTMEEIERATKEANAYDFImKLPKKFetvVGERGAQMSGGQKQRI 560
Cdd:PRK13645 84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 561 AIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELM 637
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIF 239
|
....*....
gi 2024474312 638 EQKGVYYKL 646
Cdd:PRK13645 240 SNQELLTKI 248
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
413-609 |
4.09e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.28 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPArpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDlkslNVRYLreiig 492
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLLFL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 vvNQEPVLFATTIAENIRYGREDVtmeeieratkeanaydfimklpkkfetvvgergaqMSGGQKQRIAIARALVRNPKI 572
Cdd:cd03223 70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024474312 573 LLLDEATSALDTESESVVQAALDKirKGRTILVIAHR 609
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
430-611 |
4.42e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI----IGVVNQEPVLFATTI 505
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 506 AenirygREDVTMEEI--ERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:PRK11629 104 A------LENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 2024474312 584 TESESVVQAALDKI--RKGRTILVIAHRLS 611
Cdd:PRK11629 178 ARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
431-613 |
4.76e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.46 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQD---LKSLNVRYLREIIGVVNQEP-VLFATTIA 506
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 507 ENIRYGR--EDVTMEEIERATKEANAYDFIMKLPKKFETvvgergaQMSGGQKQRIAIARALVRNPKILLLDEATSALDT 584
Cdd:PRK10908 98 DNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190
....*....|....*....|....*....|
gi 2024474312 585 E-SESVVQAALDKIRKGRTILVIAHRLSTV 613
Cdd:PRK10908 171 AlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
729-984 |
4.78e-17 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 83.21 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAAIRETNsTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSM 808
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLL-LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 809 AFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAIT 888
Cdd:cd18544 80 LFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 889 GMIqmkmlagHAKKDKK-ELETLGKVA------SEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAF 961
Cdd:cd18544 158 TYL-------FRKKSRKaYREVREKLSrlnaflQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPL 230
|
250 260
....*....|....*....|...
gi 2024474312 962 TQAIMYFTYAGCFRFGAYLVKNG 984
Cdd:cd18544 231 VELLSSLALALVLWYGGGQVLSG 253
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1065-1269 |
5.09e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTkTLN--IQWLRAQIGIVSQEPILFD- 1141
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNgpKSSQEAGIGIIHQELNLIPq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1142 CTIAENIAYGdnsrevshEEIVSAAKAAN---IHSFIESLPKKYN------TRVGDkgaqLSGGQKQRIAIARALIRQPR 1212
Cdd:PRK10762 94 LTIAENIFLG--------REFVNRFGRIDwkkMYAEADKLLARLNlrfssdKLVGE----LSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1213 ILLLDEATSAL-DTESE---KIVQEALDkarEGRTCIVIAHRLSTI-QNADKIAVIQNGKVI 1269
Cdd:PRK10762 162 VIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQFI 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
413-577 |
5.74e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.61 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTT----VQLIQrfydPKEGTITIDGQDLKSLNVrYLR 488
Cdd:COG1137 4 LEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLPM-HKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 489 EI--IGVVNQEPVLFAT-TIAENIRygredVTMEEIERATKEANaydfimklpKKFETVVGE---------RGAQMSGGQ 556
Cdd:COG1137 76 ARlgIGYLPQEASIFRKlTVEDNIL-----AVLELRKLSKKERE---------ERLEELLEEfgithlrksKAYSLSGGE 141
|
170 180
....*....|....*....|.
gi 2024474312 557 KQRIAIARALVRNPKILLLDE 577
Cdd:COG1137 142 RRRVEIARALATNPKFILLDE 162
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1072-1277 |
5.85e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1072 GLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLrAQIGIVS--QEPILF-DCTIAENI 1148
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 --------------------AYgdnsREVSHEEIVSAAkaanihSFIE--SLPKKYNTRVGDkgaqLSGGQKQRIAIARA 1206
Cdd:PRK11300 102 lvaqhqqlktglfsgllktpAF----RRAESEALDRAA------TWLErvGLLEHANRQAGN----LAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1207 LIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQL 1277
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
441-638 |
6.43e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.06 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 441 GQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN---VRYLREIIGVVNQEPvlFAT---------TIAEN 508
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP--YASldprqtvgdSIMEP 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 509 IRY--------GREDVTmEEIER-ATKEANAYDFimklPKKFetvvgergaqmSGGQKQRIAIARALVRNPKILLLDEAT 579
Cdd:PRK10261 428 LRVhgllpgkaAAARVA-WLLERvGLLPEHAWRY----PHEF-----------SGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 580 SALDTESES-VVQAALDKIRK-GRTILVIAHRLSTV-RNADLIAAFENGVITEQGTHDELME 638
Cdd:PRK10261 492 SALDVSIRGqIINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
141-365 |
7.08e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 82.95 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 141 GIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVAT 220
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 221 FFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERY-- 298
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFar 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 299 --QKNLEDAKRmgiQKAISANISMGVSfFLIYGSYALAFWYGTILVLSEDYTIGKVfTVFFSILVGAFS 365
Cdd:cd18564 222 enRKSLRAGLR---AARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPGDL-LVFLAYLKNLYK 285
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1058-1272 |
1.12e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.84 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1058 AFKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRaQIGIV--SQ 1135
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1136 EPILFDCTIAENIAYgdnsrevsHEEI--VSAAKA-ANIHSFIESLPKkynTRVGDKGA-QLSGGQKQRIAIARALIRQP 1211
Cdd:cd03267 104 TQLWWDLPVIDSFYL--------LAAIydLPPARFkKRLDELSELLDL---EELLDTPVrQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALDKAREGR--TCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
430-636 |
1.13e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYdPK------EGTITIDGQDLKSLNVRYLREI----IGVVNQEPV 499
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 500 lfattIAENIRYGREDVTME--EIERAT-KEANAYDFIMKLPKkfetvVGERGA---------QMSGGQKQRIAIARALV 567
Cdd:PRK15134 103 -----VSLNPLHTLEKQLYEvlSLHRGMrREAARGEILNCLDR-----VGIRQAakrltdyphQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 568 RNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1064-1284 |
1.29e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1064 RPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLErFYDP----LSGEVLLDGRntkTLNIQWLRAQIGIVSQEPIL 1139
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1140 F-DCTIAENIAYGDNSRevSHEEIVSAAKAANIHSFIE--SLPKKYNTRVGDKGAQ--LSGGQKQRIAIARALIRQPRIL 1214
Cdd:TIGR00955 111 IpTLTVREHLMFQAHLR--MPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1215 LLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLST--IQNADKIAVIQNGKVIEQGTHQQL---LAEKGFY 1284
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAvpfFSDLGHP 264
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1055-1269 |
1.82e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1055 KDVAFKYPTRP--------EVK------VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLerF--YDPLSGEVLLDGRNT 1118
Cdd:COG1129 239 RELEDLFPKRAaapgevvlEVEglsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDGKPV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1119 KTLNI-QWLRAQIGIVS----QEPILFDCTIAENIAYGdNSREVSHEEIVSAAKAANIhsfIESLPKKYNTRVGDKGA-- 1191
Cdd:COG1129 317 RIRSPrDAIRAGIAYVPedrkGEGLVLDLSIRENITLA-SLDRLSRGGLLDRRRERAL---AEEYIKRLRIKTPSPEQpv 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1192 -QLSGGQKQRIAIARALIRQPRILLLDEATSALD--TESE--KIVQEAldkAREGRTCIVIahrlST-----IQNADKIA 1261
Cdd:COG1129 393 gNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRIL 465
|
....*...
gi 2024474312 1262 VIQNGKVI 1269
Cdd:COG1129 466 VMREGRIV 473
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1052-1273 |
2.08e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.51 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG 1131
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEP-ILFDCTIAENIAYG------------DnsrevshEEIVSAAkaanIHSF-IESLPKKYNTrvgdkgaQLSGGQ 1197
Cdd:COG4604 79 ILRQENhINSRLTVRELVAFGrfpyskgrltaeD-------REIIDEA----IAYLdLEDLADRYLD-------ELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1198 KQRIAIARALIRQPRILLLDEATSALD----TESEKIVQEAldkARE-GRTCIVIAHRLstiqN-----ADKIAVIQNGK 1267
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGR 213
|
....*.
gi 2024474312 1268 VIEQGT 1273
Cdd:COG4604 214 VVAQGT 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1052-1279 |
2.25e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.92 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPtrpEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRN-TKTLNIQWLRAQI 1130
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEPILFD-CTIAENIAYGD--NSREVSHEEIVSAakaanihsfIESLPKKYNTRVGDKGAqLSGGQKQRIAIARAL 1207
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1208 IRQPRILLLDEATSALdteSEKIVQEALDKAR----EGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
404-631 |
2.98e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 79.11 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 404 YKLDHVKGN-LEFQNVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlksl 482
Cdd:cd03220 10 YPTYKGGSSsLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 483 nVRYLREIIGVVNQEpvlfaTTIAENIR-----YGREDVTMEEIERATKEanaydfIMKLPKKFETVVGErgaqMSGGQK 557
Cdd:cd03220 85 -VSSLLGLGGGFNPE-----LTGRENIYlngrlLGLSRKEIDEKIDEIIE------FSELGDFIDLPVKT----YSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 558 QRIAIARALVRNPKILLLDEATSALDtesESVVQAALDKIR----KGRTILVIAHRLSTVRN-ADLIAAFENGVITEQG 631
Cdd:cd03220 149 ARLAFAIATALEPDILLIDEVLAVGD---AAFQEKCQRRLRellkQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1051-1277 |
3.20e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1051 NITFKDvafkypTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEV-----LLDGRNTKTLNI-- 1123
Cdd:PRK10261 19 NIAFMQ------EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRQVIELse 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1124 ------QWLR-AQIGIVSQEPI-----LFdcTIAENIAYGDNSRE-VSHEEIVSAAKA-------ANIHSFIESLPKkyn 1183
Cdd:PRK10261 93 qsaaqmRHVRgADMAMIFQEPMtslnpVF--TVGEQIAESIRLHQgASREEAMVEAKRmldqvriPEAQTILSRYPH--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1184 trvgdkgaQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESE-------KIVQEALDKAregrtCIVIAHRLSTIQN 1256
Cdd:PRK10261 168 --------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAE 234
|
250 260
....*....|....*....|..
gi 2024474312 1257 -ADKIAVIQNGKVIEQGTHQQL 1277
Cdd:PRK10261 235 iADRVLVMYQGEAVETGSVEQI 256
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
425-611 |
3.28e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 425 RPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQrFYDPK----EGTITIDGqdlKSLNVRYLREIIGVVNQEPVL 500
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 501 FAT-TIAENI------RYGREDVTMEEIERATKEANAydfiMKLPKKFETVVGERGAQ--MSGGQKQRIAIARALVRNPK 571
Cdd:TIGR00955 111 IPTlTVREHLmfqahlRMPRRVTKKEKRERVDEVLQA----LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024474312 572 ILLLDEATSALDTES-ESVVQAALDKIRKGRTILVIAHRLS 611
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPS 227
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
130-354 |
3.65e-16 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 80.51 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 130 EEMTRYAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGE 209
Cdd:cd18544 38 QGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 210 KIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFG 289
Cdd:cd18544 118 GLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFN 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 290 GQRKETERYQKNLEDAKRMGIqKAISAN-ISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVFT 354
Cdd:cd18544 198 REKREFEEFDEINQEYRKANL-KSIKLFaLFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
162-354 |
5.44e-16 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 80.21 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 162 GRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTGFIVGFTKGWKLTLVILA 241
Cdd:cd18589 65 SRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 242 LSPVLgfssALWAKIISTFtNKELT-----AYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDAKRMGIQKAISA 316
Cdd:cd18589 145 GLPLL----LLVPKFVGKF-QQSLAvqvqkSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAY 219
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024474312 317 NISMGVSFFliyGSYALA---FWYGTILVLSEDYTIGKVFT 354
Cdd:cd18589 220 AVSMWTSSF---SGLALKvgiLYYGGQLVTAGTVSSGDLVT 257
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1064-1248 |
5.77e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 77.78 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1064 RPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPILFDCT 1143
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIA-YGDNSRevSHEEIVSAAKAANIHSFIESLPkkyntrvgdkGAQLSGGQKQRIAIARALIRQPRILLLDEATSA 1222
Cdd:TIGR01189 90 ALENLHfWAAIHG--GAQRTIEDALAAVGLTGFEDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 2024474312 1223 LDTESEKIVQEALDkAREGRTCIVIA 1248
Cdd:TIGR01189 158 LDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1084-1272 |
7.28e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1084 ALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR----NTKTLNIQWLRAQIGIVSQEPILF-DCTIAENIAYG-DNSREV 1157
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdAEKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1158 SHEEIVSAAKaanihsfIESLPKKYNtrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDK 1237
Cdd:PRK11144 108 QFDKIVALLG-------IEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024474312 1238 -AREGRTCIV-IAHRLSTI-QNADKIAVIQNGKVIEQG 1272
Cdd:PRK11144 174 lAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1063-1248 |
7.57e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1063 TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNiqwLRAQIGIVSQ----EPI 1138
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEACHYLGHrnamKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 LfdcTIAENIAYGDNSREVSHEEIVSAAKAANIHSfIESLPKKYntrvgdkgaqLSGGQKQRIAIARALIRQPRILLLDE 1218
Cdd:PRK13539 88 L---TVAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|
gi 2024474312 1219 ATSALDTESEKIVQEALdKAREGRTCIVIA 1248
Cdd:PRK13539 154 PTAALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
426-614 |
8.09e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 426 PDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-IGVVNQE-PVLFAT 503
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENIRYGRE------DVTMEEIERATKEANAYDFIMKLPKKFETVVGErgaqMSGGQKQRIAIARALVRNPKILLLDE 577
Cdd:PRK09700 96 TVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024474312 578 ATSALDTESESVVQAALDKIRK-GRTILVIAHRLSTVR 614
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIR 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1065-1266 |
8.45e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQwLRAQ--IGIVSQEPILFD- 1141
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQELSVIDe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1142 CTIAENIAYGDN-SREVSHEEIVSAAKA---ANIHSFIESLPKKYNTRVGDkgaqLSGGQKQRIAIARALIRQPRILLLD 1217
Cdd:PRK09700 95 LTVLENLYIGRHlTKKVCGVNIIDWREMrvrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1218 EATSAL-DTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNG 1266
Cdd:PRK09700 171 EPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
156-352 |
1.84e-15 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 78.53 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 156 FWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQA-VATFFT-GFIVGFTkgW 233
Cdd:cd18590 59 LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSlVKTLGMlGFMLSLS--W 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 234 KLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLEDAKRMGIQKA 313
Cdd:cd18590 137 QLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRD 216
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024474312 314 ISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKV 352
Cdd:cd18590 217 TVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSL 255
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1066-1283 |
2.01e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.37 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERF--YDPLSGEVLLDGRNTKTLNIQwLRAQIGI----------- 1132
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1133 -VSQEPILfdctiaeNIAYgdNSREVSHEEivsaaKAANIHSFIESLPKKYN---------TRVGDKGaqLSGGQKQRIA 1202
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSKRKFQGL-----PELDPLEFLEIINEKLKlvgmdpsflSRNVNEG--FSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1203 IARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGRTCIV-IAH--RLSTIQNADKIAVIQNGKVIEQGTHQ--QL 1277
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKE 241
|
....*.
gi 2024474312 1278 LAEKGF 1283
Cdd:CHL00131 242 LEKKGY 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
434-632 |
2.31e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.98 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 434 LNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSlNVRYLREIIGVVNQEPVLFA-TTIAENIRYG 512
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 513 REdVTMEEIERATKEANAydfiMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQA 592
Cdd:TIGR01257 1028 AQ-LKGRSWEEAQLEMEA----MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024474312 593 ALDKIRKGRTILVIAHRLStvrNADL----IAAFENGVITEQGT 632
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
427-625 |
2.40e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYdPK---EGTITIDGQDLKSLNVRYL-REIIGVVNQEPVLFA 502
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 503 T-TIAENIRYGREdVTME----EIERATKEANAYDFIMKLPKKFET-VVGERGaqmsGGQKQRIAIARALVRNPKILLLD 576
Cdd:TIGR02633 92 ElSVAENIFLGNE-ITLPggrmAYNAMYLRAKNLLRELQLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 577 EATSALdTESEsvVQAALDKIR----KGRTILVIAHRLSTVRN-ADLIAAFENG 625
Cdd:TIGR02633 167 EPSSSL-TEKE--TEILLDIIRdlkaHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
427-661 |
3.30e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 80.23 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRF--YDPKEGTI----------------TIDGQ----------- 477
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 478 ---DLKSLNVRYLREIigvVNQEPVLFATTIAeniRYGREDV------TMEEIERATKEA--NAYDFIMKLpkKFETVVG 546
Cdd:TIGR03269 92 eevDFWNLSDKLRRRI---RKRIAIMLQRTFA---LYGDDTVldnvleALEEIGYEGKEAvgRAVDLIEMV--QLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 547 ERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDK--IRKGRTILVIAHRLSTVRN-ADLIAAFE 623
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKAIWLE 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 2024474312 624 NGVITEQGTHDELMEqkgVYYKLVNMQASETEDQLQEE 661
Cdd:TIGR03269 244 NGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGEP 278
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
424-587 |
3.41e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.61 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 424 ARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFAT 503
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENIRYGREDVTMEEIERATKEANAydfimklpKKFETVVGergAQMSGGQKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
....
gi 2024474312 584 TESE 587
Cdd:cd03231 158 KAGV 161
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1052-1266 |
3.74e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 75.36 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEVK-VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLL-ERFYDPL-SGEVLLDGR-NTKTLNIqwlr 1127
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRpLDKNFQR---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 aQIGIVSQEPILFDC-TIAENIAYGDNSREVSHEeivsaakaanihsfieslpkkyntrvgdkgaqlsggQKQRIAIARA 1206
Cdd:cd03232 80 -STGYVEQQDVHSPNlTVREALRFSALLRGLSVE------------------------------------QRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1207 LIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLS--TIQNADKIAVIQNG 1266
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
428-639 |
4.29e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.85 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTI-----------TIDGQDLKSLNVRYlreiIGVVNQ 496
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPDGRGRAKRY----IGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 497 EPVLFA-TTIAENIRygrEDVTMEEIERATKEANAYDFIMK--LPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKIL 573
Cdd:TIGR03269 373 EYDLYPhRTVLDNLT---EAIGLELPDELARMKAVITLKMVgfDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 574 LLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQ 639
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
433-636 |
5.17e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.57 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 433 GLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSL---------------NVRYLREIIGVVN-- 495
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfqHVRLFREMTVIENll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 --QE--------PVLFATTiaeniRYGREDvtMEEIERAtkeANAYDFIMKLPkkfetvVGERGA-QMSGGQKQRIAIAR 564
Cdd:PRK11300 103 vaQHqqlktglfSGLLKTP-----AFRRAE--SEALDRA---ATWLERVGLLE------HANRQAgNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 565 ALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
404-648 |
6.00e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 404 YKLDHVKGNLEFQNVFFSYPARPDIK-ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGqdlksl 482
Cdd:COG1134 14 YRLYHEPSRSLKELLLRRRRTRREEFwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 483 NVRYLREIIGVVNQEpvlfaTTIAENIR-----YGredVTMEEIERATKEANAY----DFImKLPKKFetvvgergaqMS 553
Cdd:COG1134 88 RVSALLELGAGFHPE-----LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-DQPVKT----------YS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 554 GGQKQRIAIARALVRNPKILLLDEATSALDtesESVVQAALDKIR----KGRTILVIAHRLSTVRN-ADLIAAFENGVIT 628
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGD---AAFQKKCLARIRelreSGRTVIFVSHSMGAVRRlCDRAIWLEKGRLV 225
|
250 260
....*....|....*....|
gi 2024474312 629 EQGTHDELMEQkgvYYKLVN 648
Cdd:COG1134 226 MDGDPEEVIAA---YEALLA 242
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
430-637 |
7.49e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEpvlfATTIAeni 509
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN----ATTPG--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 rygreDVTMEEI------------ERATKE-ANAYDFIMKlPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLD 576
Cdd:PRK10253 95 -----DITVQELvargryphqplfTRWRKEdEEAVTKAMQ-ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 577 EATSALDTESESVVQAALDKI--RKGRTILVIAHRLS-TVRNADLIAAFENGVITEQGTHDELM 637
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
63-358 |
1.61e-14 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 75.90 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 63 LLMVLGTTMAVLhgasLPLMMivfGDMTDTFIASENTTYPANFSLLnstsvnfsmefFSYLILgeleeemtryayyYSGI 142
Cdd:cd18547 6 ILAIISTLLSVL----GPYLL---GKAIDLIIEGLGGGGGVDFSGL-----------LRILLL-------------LLGL 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 143 GAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFF 222
Cdd:cd18547 55 YLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 223 TGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNL 302
Cdd:cd18547 135 GTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEIN 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 303 EDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGkVFTVFFS 358
Cdd:cd18547 215 EELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVG-VIQAFLQ 269
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
424-608 |
2.28e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.16 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 424 ARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFAT 503
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENIRYGREDVTMEE--IERATKEANAYDFiMKLPkkfetvvgerGAQMSGGQKQRIAIARALVRNPKILLLDEATSA 581
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQrtIEDALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*...
gi 2024474312 582 LDTESESVVQAALDK-IRKGRTILVIAH 608
Cdd:TIGR01189 158 LDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
771-986 |
2.55e-14 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 75.07 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 771 TYALLFLG-FGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVkgatgSR 849
Cdd:cd18590 36 TSAIGLMClFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLM-----SR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 850 laLVAQN--------IANLGT-GIVLSLiyGWQLTLLLLAIVPIIAITgmiqMKMLAGHAKKDKKELE----TLGKVASE 916
Cdd:cd18590 109 --SVALNanvllrslVKTLGMlGFMLSL--SWQLTLLTLIEMPLTAIA----QKVYNTYHQKLSQAVQdsiaKAGELARE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 917 AIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18590 181 AVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
445-636 |
2.99e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 445 ALVGGSGCGKSTTVQLIQRFYDP-----KEGTITIDGQDLKSL-NVRYLREIIGVVNQEPVLFATTIAENIRYGREDVTM 518
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 519 EEIERATKEANAYDFIMKLPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIR 598
Cdd:PRK14271 131 VPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024474312 599 KGRTILVIAHRLS-TVRNADLIAAFENGVITEQGTHDEL 636
Cdd:PRK14271 211 DRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1056-1295 |
3.23e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.53 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1056 DVAFKYPTrPEVKVLQGLNIEVEKGQTLALVGSSGCGKS-TVVQLLERFYDP--LSGEVLLDGRN-----TKTLNIqwLR 1127
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilnlpEKELNK--LR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1128 A-QIGIVSQEPIlfdCTIAENIAYGDNSREV--SHEEIvSAAKAanihsFIES--------LPKKyNTRVGDKGAQLSGG 1196
Cdd:PRK09473 96 AeQISMIFQDPM---TSLNPYMRVGEQLMEVlmLHKGM-SKAEA-----FEESvrmldavkMPEA-RKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALD-TESEKIVQEALDKAREGRTCIV-IAHRLSTIQN-ADKIAVIQNGKVIEQGT 1273
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDvTVQAQIMTLLNELKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
250 260
....*....|....*....|..
gi 2024474312 1274 HQQLLAEKGFYYSLVNVQSGPR 1295
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPR 267
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
413-638 |
3.51e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.42 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSypaRPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYL---RE 489
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQEPVLFA-TTIAENIRYG-REDVTM-EEIERATkeanaydFIMKLpkkfeTVVGERGA------QMSGGQKQRI 560
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPlREHTQLpAPLLHST-------VMMKL-----EAVGLRGAaklmpsELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 561 AIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHR----LSTVRNADLIAafENGVITEqGTHD 634
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVA--DKKIVAH-GSAQ 229
|
....
gi 2024474312 635 ELME 638
Cdd:PRK11831 230 ALQA 233
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
729-986 |
3.72e-14 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 74.44 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVI-GMFVEKGKAAIretnSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRS 807
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdGPIAHGDRSAL----WPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 808 MAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATgSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAI 887
Cdd:cd18543 77 DLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFL-AFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 888 TGMIQMKML--AGHAKKDKkeletLGKVASEAIEN---IRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFT 962
Cdd:cd18543 154 VARRFRRRYfpASRRAQDQ-----AGDLATVVEESvtgIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLL 228
|
250 260
....*....|....*....|....
gi 2024474312 963 QAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18543 229 EALPELGLAAVLALGGWLVANGSL 252
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
427-648 |
3.78e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.91 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLI--QRFYDPKEGTITIDGQDLKS------------LNVRYLREIIG 492
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDlepeerahlgifLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEpvlFATTIAENIRYGREDVTMEEIEratkeanAYDFIM-KLPK-KFETVVGERGAQ--MSGGQKQRIAIARALVR 568
Cdd:CHL00131 99 VSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeKLKLvGMDPSFLSRNVNegFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAH--RLSTVRNADLIAAFENGVITEQGTHD--ELMEQKGvy 643
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKG-- 246
|
....*
gi 2024474312 644 YKLVN 648
Cdd:CHL00131 247 YDWLK 251
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
144-358 |
4.98e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 74.47 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 144 AGVLFAAYIQVSF--W------TLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFF 215
Cdd:cd18563 46 VLGLAGAYVLSALlgIlrgrllARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 216 QAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKET 295
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREI 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 296 ERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGkVFTVFFS 358
Cdd:cd18563 206 KRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLS 267
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
422-631 |
6.11e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 422 YPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDP----KEGTITIDGQDLKSLNVRylREIIGVVNQE 497
Cdd:PRK10418 13 QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 498 P-------------------VLFATTIAENIRYGREDVTMEEIERATKeanAYDFimklpkkfetvvgergaQMSGGQKQ 558
Cdd:PRK10418 88 PrsafnplhtmhtharetclALGKPADDATLTAALEAVGLENAARVLK---LYPF-----------------EMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 559 RIAIARALVRNPKILLLDEATSALDteseSVVQA-ALDKI-----RKGRTILVIAHRLSTV-RNADLIAAFENGVITEQG 631
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLD----VVAQArILDLLesivqKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1066-1250 |
7.18e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 7.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFY--DPLSGEVLLDgrntktlNIQWLRaqigivsqepilfDCT 1143
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP-------DNQFGR-------------EAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENIAYGDNSREVSheEIVSAAKAANIHSFIeslpKKYntrvgdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:COG2401 102 LIDAIGRKGDFKDAV--ELLNAVGLSDAVLWL----RRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180
....*....|....*....|....*....
gi 2024474312 1224 DTESEKIVQEALDKA--REGRTCIVIAHR 1250
Cdd:COG2401 168 DRQTAKRVARNLQKLarRAGITLVVATHH 196
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
413-631 |
7.88e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 71.51 E-value: 7.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYP-ARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQ-LIQRFYDPK-EGTITIDGQDLKSlnvrYLRE 489
Cdd:cd03232 4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILINGRPLDK----NFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 490 IIGVVNQEPVLFAT-TIAENIRygredvtmeeieratkeanaydFIMKLpkkfetvvgeRGaqMSGGQKQRIAIARALVR 568
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLStvrnADLIAAFENGVITEQG 631
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPS----ASIFEKFDRLLLLKRG 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1031-1279 |
7.95e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.07 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1031 RVPLIDSYSEEGEKPKMFGGNITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLE-RFY-DPLS 1108
Cdd:PLN03211 48 RVKFENMKNKGSNIKRILGHKPKISDETRQIQER---TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1109 GEVLLDGRNtktLNIQWLRaQIGIVSQEPILF-DCTIAENIAYGDNSR---EVSHEEIVSAAKaanihSFIESL--PKKY 1182
Cdd:PLN03211 125 GTILANNRK---PTKQILK-RTGFVTQDDILYpHLTVRETLVFCSLLRlpkSLTKQEKILVAE-----SVISELglTKCE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1183 NTRVGDKGAQ-LSGGQKQRIAIARALIRQPRILLLDEATSALD-TESEKIVQEALDKAREGRTCIVIAHRLST--IQNAD 1258
Cdd:PLN03211 196 NTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFD 275
|
250 260
....*....|....*....|.
gi 2024474312 1259 KIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PLN03211 276 SVLVLSEGRCLFFGKGSDAMA 296
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1067-1269 |
1.04e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1067 VKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLL--ERfyDPLSGEVLLDGRNTKTLNI-QWLRAQIGIVSQEP-----I 1138
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPEDRlgrglV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 LfDCTIAENIAYGD-NSREVSHEEIVSAAKaanIHSFIESLPKKYNTRVGDKGA---QLSGGQKQRIAIARALIRQPRIL 1214
Cdd:COG3845 349 P-DMSVAENLILGRyRRPPFSRGGFLDRKA---IRAFAEELIEEFDVRTPGPDTparSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1215 LLDEATSALDTES-EKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVI 1269
Cdd:COG3845 425 IAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
729-986 |
1.41e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 72.93 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQ---PIFSVMISDVIgmFVEKGKAAIRETNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRL 805
Cdd:cd18563 1 LILGFLLMLLGTALGlvpPYLTKILIDDV--LIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 806 RSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANL-GTGIVLsLIYGWQLTLLLLAIVPI 884
Cdd:cd18563 79 RRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIiGIGVVL-FSLNWKLALLVLIPVPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 885 IAI-TGMIQMKMLAGHAKKDKKELEtLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFtfaFTQ 963
Cdd:cd18563 156 VVWgSYFFWKKIRRLFHRQWRRWSR-LNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWAT---FFP 231
|
250 260
....*....|....*....|....*.
gi 2024474312 964 AIMYFTYAGCF---RFGAYLVKNGHM 986
Cdd:cd18563 232 LLTFLTSLGTLivwYFGGRQVLSGTM 257
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
441-632 |
1.43e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 69.32 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 441 GQTVALVGGSGCGKSTTVQLIQRFYDPKEGT-ITIDGQDLKSLNVRYLREIIgvvnqepvlfattiaenirygredvtme 519
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 520 eieratkeanaydfimklpkkfetvVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALD---- 595
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024474312 596 ---KIRKGRTILVIAHRLSTVRNADLIAAFENGVITEQGT 632
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1073-1280 |
2.14e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1073 LNIEVEKGQTLALVGSSGCGKSTvvqLLERFYD--PLSGEVLLDGRNTKTLNIQWLRAQIGIVSQE---PILFDCtiaen 1147
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtpPFAMPV----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1148 IAYGDNSRevsHEEIVSAAKAANIHSFIESLpkkyntRVGDKGA----QLSGGQKQRIAIArALIRQ--PRI------LL 1215
Cdd:PRK03695 87 FQYLTLHQ---PDKTRTEAVASALNEVAEAL------GLDDKLGrsvnQLSGGEWQRVRLA-AVVLQvwPDInpagqlLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1216 LDEATSALDtesekIVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK03695 157 LDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1043-1291 |
2.19e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.81 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1043 EKPKMFGGniTFKDVaFKyPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN 1122
Cdd:COG4586 15 EKEPGLKG--ALKGL-FR-REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1123 IQWLRaQIGIV----SQepILFDCTIAENIAYgdnsrevsHEEI--VSAAKAA-NIHSFIE--SLPKKYNTRVgdkgAQL 1193
Cdd:COG4586 91 KEFAR-RIGVVfgqrSQ--LWWDLPAIDSFRL--------LKAIyrIPDAEYKkRLDELVEllDLGELLDTPV----RQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1194 SGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIE 1270
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIY 235
|
250 260
....*....|....*....|.
gi 2024474312 1271 QGTHQQLLaEKGFYYSLVNVQ 1291
Cdd:COG4586 236 DGSLEELK-ERFGPYKTIVLE 255
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
431-625 |
2.88e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 69.38 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREI-IGVV----NQEPVLFATTI 505
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 506 AENIRYGRedvtmeeieratkeanaydfimklpkkfetvvgergaQMSGGQKQRIAIARALVRNPKILLLDEATSALDTE 585
Cdd:cd03215 96 AENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024474312 586 SESVVQAALDKIR-KGRTILVIAHRLSTV-RNADLIAAFENG 625
Cdd:cd03215 139 AKAEIYRLIRELAdAGKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
132-356 |
3.36e-13 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 71.73 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 132 MTRYAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINE----GI 207
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDllsnGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 208 GEKIAMFFQAVATfftgFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVA 287
Cdd:cd18545 119 INLIPDLLTLVGI----VIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQS 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 288 FgGQRKETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYG-SYALAFWYGTILVLSEDYTIGkVFTVF 356
Cdd:cd18545 195 F-AREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG-VLVAF 262
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
429-625 |
3.82e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.20 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 429 KILKGLNLKVNCGQTVALVGGSGCGKSTTVQ----LIQRFYDPkEGTITIDGQDLK-----SLNVRYLREIIGVVNQEPV 499
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSA-GSHIELLGRTVQregrlARDIRKSRANTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 500 LF-ATTIAENIRYGREDVT------MEEIERATKEaNAYDFIMKLpkKFETVVGERGAQMSGGQKQRIAIARALVRNPKI 572
Cdd:PRK09984 97 LVnRLSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 573 LLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLS-TVRNADLIAAFENG 625
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQG 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1065-1269 |
4.36e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.23 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1065 PEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGR--NTKTLNiQWLRAQIGIVSQE-PILFD 1141
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSK-EALENGISMVHQElNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1142 CTIAENIAYGDNSRE---VSHEEIVSAAKAANIHSFIESLPKkyntrvgDKGAQLSGGQKQRIAIARALIRQPRILLLDE 1218
Cdd:PRK10982 88 RSVMDNMWLGRYPTKgmfVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1219 ATSALdTESE-----KIVQEALDKareGRTCIVIAHRLSTI-QNADKIAVIQNGKVI 1269
Cdd:PRK10982 161 PTSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
430-607 |
5.93e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQ-EPVLfatTIAEN 508
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL---TVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 509 IR-----YGREDvtmEEIERATkEANAYDFIMKLPKKFetvvgergaqMSGGQKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:PRK13539 94 LEfwaafLGGEE---LDIAAAL-EAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180
....*....|....*....|....
gi 2024474312 584 TESESVVQAALDKIRKGRTILVIA 607
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAA 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
434-639 |
6.40e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 434 LNLKVNCGQTVALVGGSGCGKSTtvqLIQRFYD--PKEGTITIDGQDLKSLNVR-------YLreiigvVNQEPVLFATT 504
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAelarhraYL------SQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 505 I--------AENIRYGREDVTMEEIERAtkeanaydfiMKLPKKFETVVGergaQMSGGQKQRIAIARALVR-----NP- 570
Cdd:PRK03695 86 VfqyltlhqPDKTRTEAVASALNEVAEA----------LGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 571 -KILLLDEATSALDTESesvvQAALDKI-----RKGRTILVIAHRLS-TVRNADLIAAFENGVITEQGTHDELMEQ 639
Cdd:PRK03695 152 gQLLLLDEPMNSLDVAQ----QAALDRLlselcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1061-1272 |
6.70e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.11 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1061 YPTRPEVKvlqGLNIEVEKGQTLALVGSSGCGKS----TVVQLLERFYDPLSGEVLLDGrntKTLNIQWLRAQ-IGIVSQ 1135
Cdd:PRK10418 13 QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG---KPVAPCALRGRkIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1136 EP--------ILFDCTIAENIAYGDNSREVSHEEIVSAAKAANIHSFIESLPkkyntrvgdkgAQLSGGQKQRIAIARAL 1207
Cdd:PRK10418 87 NPrsafnplhTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1208 IRQPRILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQG 1272
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
420-608 |
8.89e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 69.28 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 420 FSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPV 499
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 500 L-FATTIAENIRYGREDVTMEEIERATKEANAYDfIMKLPKKFETVVgergAQMSGGQKQRIAIARALVRNPKILLLDEA 578
Cdd:cd03267 106 LwWDLPVIDSFYLLAAIYDLPPARFKKRLDELSE-LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190
....*....|....*....|....*....|..
gi 2024474312 579 TSALDTESESVVQAALDKIRKGR--TILVIAH 608
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERgtTVLLTSH 212
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
434-583 |
1.32e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.67 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 434 LNLKVNC-----GQTvALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDL----KSLNVRYLREIIGVVNQEPVLFA-T 503
Cdd:PRK11144 13 LCLTVNLtlpaqGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFPhY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENIRYGredvtMEEIERAtkeanaydfimklpkKFETVVGERG---------AQMSGGQKQRIAIARALVRNPKILL 574
Cdd:PRK11144 92 KVRGNLRYG-----MAKSMVA---------------QFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPELLL 151
|
....*....
gi 2024474312 575 LDEATSALD 583
Cdd:PRK11144 152 MDEPLASLD 160
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
427-639 |
1.81e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 68.66 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKST-TVQLIQRF-YDPKEGTITIDGQDLKSLN------------VRYLREIIG 492
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSpedragegifmaFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQepvLFATTIAENIRYGREdvtMEEIERATKEanayDFI------MKLPKKFETVVGERGaqMSGGQKQRIAIARAL 566
Cdd:PRK09580 93 VSNQ---FFLQTALNAVRSYRG---QEPLDRFDFQ----DLMeekialLKMPEDLLTRSVNVG--FSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 567 VRNPKILLLDEATSALDTESESVVQAALDKIRKG-RTILVIAH--RLSTVRNADLIAAFENGVITEQGTHD---ELMEQ 639
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTlvkQLEEQ 239
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
419-603 |
1.99e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 67.67 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 419 FFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK---EGTITIDGQDLKSLNVRYLREIIgVVN 495
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEII-YVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 QEPVLFATtiaenirygredVTMEEIERATKEANAYDFImklpkkfetvvgeRGaqMSGGQKQRIAIARALVRNPKILLL 575
Cdd:cd03233 90 EEDVHFPT------------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCW 142
|
170 180
....*....|....*....|....*...
gi 2024474312 576 DEATSALDTESesvvqaALDKIRKGRTI 603
Cdd:cd03233 143 DNSTRGLDSST------ALEILKCIRTM 164
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
428-639 |
2.60e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.55 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKeGTITID-----GQDLKSLNVRYLREIIG----VVNQEP 498
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN-WHVTADrfrwnGIDLLKLSPRERRKIIGreiaMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 499 VLF---ATTIAENIrygredvtMEEIERAT-------------KEANA---------YDFIMK-LPKkfetvvgergaQM 552
Cdd:COG4170 99 SSCldpSAKIGDQL--------IEAIPSWTfkgkwwqrfkwrkKRAIEllhrvgikdHKDIMNsYPH-----------EL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 553 SGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTV-RNADLIAAFENGVITE 629
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESIsQWADTITVLYCGQTVE 239
|
250
....*....|
gi 2024474312 630 QGTHDELMEQ 639
Cdd:COG4170 240 SGPTEQILKS 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
441-634 |
2.85e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.41 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 441 GQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNV---------RYLREIIGVVNQEP-------VLFATT 504
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrRLLRTEWGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 505 IAE-----------NIRYGREDvTMEEIERATkeanayDFIMKLPKKFetvvgergaqmSGGQKQRIAIARALVRNPKIL 573
Cdd:PRK11701 112 IGErlmavgarhygDIRATAGD-WLERVEIDA------ARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 574 LLDEATSALDTEsesvVQAA-LDKIRK-----GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHD 634
Cdd:PRK11701 174 FMDEPTGGLDVS----VQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTD 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
429-609 |
3.30e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 429 KILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKslnvrylreiigvVNQEpvlfaTTIAEN 508
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------------FGRE-----ASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 509 IryGREDVTMEEIER--ATKEANAYDFImklpKKFetvvgergAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTES 586
Cdd:COG2401 106 I--GRKGDFKDAVELlnAVGLSDAVLWL----RRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*
gi 2024474312 587 ESVVQAALDKI--RKGRTILVIAHR 609
Cdd:COG2401 172 AKRVARNLQKLarRAGITLVVATHH 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
416-613 |
3.37e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.83 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 416 QNVFFSYPARpdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlkslnvryLReiIGVVN 495
Cdd:PRK09544 8 ENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 QEPVLFAT---TIAENIRYgREDVTMEEIERATKEANAYDFIMKLPKKfetvvgergaqMSGGQKQRIAIARALVRNPKI 572
Cdd:PRK09544 74 QKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024474312 573 LLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTV 613
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
425-636 |
3.52e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 425 RPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLN--VRYLREI------------ 490
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 IGVVNQEPV-----LFAT--TIAENIR----YGREDvTMEEIERATKEanaydfiMKLPKKfETVVGERGAQMSGGQKQR 559
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREE-AMVEAKRMLDQ-------VRIPEA-QTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 560 IAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRKGRT--ILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1062-1279 |
4.58e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1062 PTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYD-PLSGEVLLDGRNTKTLN-IQWLRAQIGIVSQEP-- 1137
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 --ILFDCTIAENIAYGDNSREVSHEEIVSAAKAANIHSFIESLpkKYNTRVGDKG-AQLSGGQKQRIAIARALIRQPRIL 1214
Cdd:TIGR02633 348 hgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 1215 LLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKV----IEQG-THQQLLA 1279
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLkgdfVNHAlTQEQVLA 497
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
425-588 |
5.48e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.51 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 425 RPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPvlfATT 504
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 505 IAENIRYG-------REDVTMEEIERATKEANAYDFIMKLPKKfetvVGERGAQMSGGQKQRIAIARALVRNPKILLLDE 577
Cdd:PRK15112 100 LNPRQRISqildfplRLNTDLEPEQREKQIIETLRQVGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170
....*....|.
gi 2024474312 578 ATSALDTESES 588
Cdd:PRK15112 176 ALASLDMSMRS 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1064-1249 |
6.01e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1064 RPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTL------NIQWLRAQIGIVSqep 1137
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKT--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 ilfDCTIAENIA-YGDNSREVSHEEIVSAAKAANIHSFiESLPkkyntrvgdkGAQLSGGQKQRIAIARALIRQPRILLL 1216
Cdd:PRK13538 88 ---ELTALENLRfYQRLHGPGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....
gi 2024474312 1217 DEATSALDTESEKIVQEALDK-AREGRTCIVIAH 1249
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1031-1252 |
6.76e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 70.16 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1031 RVPLIDSYSEEGEKPKMF--GGNITFKDVAFKYPTRPEV-----KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERF 1103
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVpgRGIVEYQDNGIKFENIPLVtpngdVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1104 YdPLSGevlldGRNTKTLniqwlRAQIGIVSQEPILFDCTIAENIAYGDNS-----REVSHEEIVSAAKAANIHSFIEsl 1178
Cdd:TIGR00954 502 W-PVYG-----GRLTKPA-----KGKLFYVPQRPYMTLGTLRDQIIYPDSSedmkrRGLSDKDLEQILDNVQLTHILE-- 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1179 pkkyntR------VGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAreGRTCIVIAHRLS 1252
Cdd:TIGR00954 569 ------ReggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1052-1251 |
6.85e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRntktlniqwLRaqIG 1131
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEpILFDCTIAENIAYGDNSRE-VSHEEIVSAAKAANIHSFIESLPKKyntrvgdkgaqLSGGQKQRIAIARALIRQ 1210
Cdd:PRK09544 71 YVPQK-LYLDTTLPLTVNRFLRLRPgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024474312 1211 PRILLLDEATSALDTESEKIVQEALDKAREGRTCIV--IAHRL 1251
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
771-986 |
8.28e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 67.49 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 771 TYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGA-TGSR 849
Cdd:cd18545 41 IIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLlSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 850 LALVAQNIANLGTGIVLsLIYGWQLTLLLLAIVPI-IAITGMIQMKMLAGHAKKDKKELETLGKVAsEAIENIRTVVALT 928
Cdd:cd18545 119 INLIPDLLTLVGIVIIM-FSLNVRLALVTLAVLPLlVLVVFLLRRRARKAWQRVRKKISNLNAYLH-ESISGIRVIQSFA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 929 QE----RKFEYMYGQNLQvSYRNSIKKAHIFG----FTFAFTQAIMYFtyagcfrFGAYLVKNGHM 986
Cdd:cd18545 197 REdeneEIFDELNRENRK-ANMRAVRLNALFWplveLISALGTALVYW-------YGGKLVLGGAI 254
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
63-364 |
8.58e-12 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 67.42 E-value: 8.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 63 LLMVLGTTMAVLhgasLPLMMivfGDMTDTFIASENTTYPANFSLLnstsvnfsMEFFSYLILGeleeemtryayyySGI 142
Cdd:cd18548 6 LFKLLEVLLELL----LPTLM---ADIIDEGIANGDLSYILRTGLL--------MLLLALLGLI-------------AGI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 143 GAGVlFAAYIQVSFwtlaagrqIKRIRQEFFHAVMR---QEIGWFDVNDvceLNTRIVDDISKINEGIGEKIAMFFQAVA 219
Cdd:cd18548 58 LAGY-FAAKASQGF--------GRDLRKDLFEKIQSfsfAEIDKFGTSS---LITRLTNDVTQVQNFVMMLLRMLVRAPI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 220 TFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQ 299
Cdd:cd18548 126 MLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFD 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 300 KNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKV-------FTVFFSILVGAF 364
Cdd:cd18548 206 KANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
426-619 |
1.01e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.05 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 426 PDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYdPK---EGTITIDGQdlkslnVRYLREI-------IGVVN 495
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGE------VCRFKDIrdsealgIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 QE----PVLfatTIAENIRYGREDVTMEEIERATKEANAYDFIMK--LPKKFETVVGERGAqmsgGQKQRIAIARALVRN 569
Cdd:NF040905 85 QElaliPYL---SIAENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALSKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 570 PKILLLDEATSALDtESESvvQAALDKIR----KGRTILVIAHRLSTVRN-ADLI 619
Cdd:NF040905 158 VKLLILDEPTAALN-EEDS--AALLDLLLelkaQGITSIIISHKLNEIRRvADSI 209
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
773-997 |
1.06e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 67.54 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 773 ALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLAL 852
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVSGVLP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 853 VAQNIANLG--TGIVLSLiyGWQLTLLLLAIVPIIAITgMIQMKMLAGHAKKDKKELE-TLGKVASEAIENIRTVVALTQ 929
Cdd:cd18564 135 LLTNLLTLVgmLGVMFWL--DWQLALIALAVAPLLLLA-ARRFSRRIKEASREQRRREgALASVAQESLSAIRVVQAFGR 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 930 E----RKFEymyGQNLQvSYRNSIKKAHI-------FGFTFAFTQAIMYFtyagcfrFGAYLVKNGHMRFKDvLLVFSA 997
Cdd:cd18564 212 EeheeRRFA---RENRK-SLRAGLRAARLqallspvVDVLVAVGTALVLW-------FGAWLVLAGRLTPGD-LLVFLA 278
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1079-1255 |
1.19e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.93 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1079 KGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVlldgrntktlniqwlraqigivsqepILFDCtiaeniaygDNSREVS 1158
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDG---------EDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1159 HEEIvsaakaanihsfieslpkkYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALD-- 1236
Cdd:smart00382 46 LDQL-------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....
gi 2024474312 1237 -----KAREGRTCIVIAHRLSTIQ 1255
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLG 130
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1076-1273 |
1.23e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.46 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1076 EVEKGQTLALVGSSGCGKST---VVQLLERFYDPLSGEVL-LDGRNTKTLNIQWLR----AQIGIVSQEPI--LFDC--- 1142
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVsslAIMGLIDYPGRVMAEKLeFNGQDLQRISEKERRnlvgAEVAMIFQDPMtsLNPCytv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1143 --TIAENI-AYGDNSREVSHEEIVSAAKAANI---HSFIESLPKkyntrvgdkgaQLSGGQKQRIAIARALIRQPRILLL 1216
Cdd:PRK11022 109 gfQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPH-----------QLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1217 DEATSALD-TESEKIVQEALD-KAREGRTCIVIAHRLSTI-QNADKIAVIQNGKVIEQGT 1273
Cdd:PRK11022 178 DEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1052-1281 |
1.58e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRpevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNI-QWLRAQI 1130
Cdd:PRK10895 4 LTAKNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1131 GIVSQEPILFD-CTIAENIA-----YGDNSREVSHEEIVSAAKAANIHSFIESLpkkyntrvgdkGAQLSGGQKQRIAIA 1204
Cdd:PRK10895 81 GYLPQEASIFRrLSVYDNLMavlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1205 RALIRQPRILLLDEATSALDTES----EKIVQEALDKareGRTCIVIAHRL-STIQNADKIAVIQNGKVIEQGTHQQLLA 1279
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
..
gi 2024474312 1280 EK 1281
Cdd:PRK10895 227 DE 228
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
424-637 |
1.73e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.39 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 424 ARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQ-LIQRFYDPKE-------GTITIDGQDLKSLNVRYLREIIGVVN 495
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 496 Q--EPVlFATTIAENIRYGR----------EDVTMEEIERATKEANAydfimklpkkfETVVGERGAQMSGGQKQRIAIA 563
Cdd:PRK13547 90 QaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 564 RAL---------VRNPKILLLDEATSALDTESEsvvQAALDKIRK-GRT----ILVIAHRLS-TVRNADLIAAFENGVIT 628
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQ---HRLLDTVRRlARDwnlgVLAIVHDPNlAARHADRIAMLADGAIV 234
|
....*....
gi 2024474312 629 EQGTHDELM 637
Cdd:PRK13547 235 AHGAPADVL 243
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
773-986 |
1.76e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 66.36 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 773 ALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLAL 852
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 853 VAQNIANL-GTGIVLsLIYGWQLTLLLLAIVPIIAITGMIQMKmLAGHAKKDKKelETLGKVAS---EAIENIRTVVALT 928
Cdd:cd18546 120 LVVSLLTLvGIAVVL-LVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRAR--ERIAAVNAdlqETLAGIRVVQAFR 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 929 QERKFEYMYGQnLQVSYRNSIKKAH-IFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18546 196 RERRNAERFAE-LSDDYRDARLRAQrLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTL 253
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
770-986 |
1.81e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 66.45 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 770 STYALLFLGFGLISFVTFFLQGF---TFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLaNDASQVKGAT 846
Cdd:cd18566 39 PTLQVLVIGVVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERL-NSLEQIREFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 847 GSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVA 926
Cdd:cd18566 116 TGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 927 LTQE----RKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAgcfrFGAYLVKNGHM 986
Cdd:cd18566 196 MAMEpqmlRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVA----FGALLVINGDL 255
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
394-623 |
2.11e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 394 PQIDSSSNAGYKLDHVKGN----LEFQNVFFSYPARPDIK-ILKGLNLKVNCGQTVALVGGSGCGKSTTVQ-LIQRFYDP 467
Cdd:TIGR00956 737 DLTDESDDVNDEKDMEKESgediFHWRNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERVTTG 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 468 --KEGTITIDGQDLKSLNVRylreIIGVVNQEPVLFAT-TIAENIRYGREDVTMEEIERatKEANAY-DFIMKL---PKK 540
Cdd:TIGR00956 817 viTGGDRLVNGRPLDSSFQR----SIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESY 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 541 FETVVGERGAQMSGGQKQRIAIARALVRNPKILL-LDEATSALDTESE-SVVQAaldkIRK----GRTILVIAHRLStvr 614
Cdd:TIGR00956 891 ADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAwSICKL----MRKladhGQAILCTIHQPS--- 963
|
....*....
gi 2024474312 615 nADLIAAFE 623
Cdd:TIGR00956 964 -AILFEEFD 971
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1069-1283 |
2.92e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.20 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLL--ERFYDPLSGEVLLDGRNTKTLNIQwLRAQIGI--VSQEPI------ 1138
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 -LFDCTIAENIAygdnsREVSHEEivsAAKAANIHSFIE------SLPKKYNTRVGDKGaqLSGGQKQRIAIARALIRQP 1211
Cdd:PRK09580 95 nQFFLQTALNAV-----RSYRGQE---PLDRFDFQDLMEekiallKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1212 RILLLDEATSALDTESEKIVQEALDKAREG-RTCIVIAH--RLSTIQNADKIAVIQNGKVIEQGTHQ--QLLAEKGF 1283
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTlvKQLEEQGY 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
431-613 |
3.55e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlkSLNVRYLREIIGVVNQE-------PVLFAT 503
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ---PTRQALQKNLVAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENiRYGRedvtMEEIERATKE-----ANAYDFIMKLPKKFETVvgergAQMSGGQKQRIAIARALVRNPKILLLDEA 578
Cdd:PRK15056 100 VVMMG-RYGH----MGWLRRAKKRdrqivTAALARVDMVEFRHRQI-----GELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024474312 579 TSALDTESESVVQAALDKIR-KGRTILVIAHRLSTV 613
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
771-986 |
3.65e-11 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 65.54 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 771 TYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDEPKnsTGELITRLaNDASQVKGA-TGSR 849
Cdd:cd18570 43 IISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRK--TGEIISRF-NDANKIREAiSSTT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 850 LALVAQNIANLGTGIVLsLIYGWQLTLLLLAIVPIIAITGMIQMKMLaghAKKDKKELETLGKVAS---EAIENIRTVVA 926
Cdd:cd18570 120 ISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYILIILLFNKPF---KKKNREVMESNAELNSyliESLKGIETIKS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 927 LTQERKFeymyGQNLQVSYRNSIKKAHIFG----FTFAFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18570 196 LNAEEQF----LKKIEKKFSKLLKKSFKLGklsnLQSSIKGLISLIGSLLILWIGSYLVIKGQL 255
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1062-1279 |
3.98e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1062 PTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYD-PLSGEVLLDGRNTKTLN-IQWLRAQIGIVSQEP-- 1137
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDRkr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 --ILFDCTIAENIAYGDNSREVSHEEIVSAAKAANIHSFIESLPKKYNT---RVGdkgaQLSGGQKQRIAIARALIRQPR 1212
Cdd:PRK13549 350 dgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1213 ILLLDEATSALDT----ESEKIVQEAldkAREGRTCIVIAHRLSTIQN-ADKIAVIQNGK-----VIEQGTHQQLLA 1279
Cdd:PRK13549 426 ILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKlkgdlINHNLTQEQVME 499
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
413-617 |
4.28e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFATTIAEN----IRYGREDVTMEEIERATKEANAYDFIMKLpkkfetvvgergaqMSGGQKQRIAIARALVR 568
Cdd:PRK13540 79 VGHRSGINPYLTLRENclydIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2024474312 569 NPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAHRLSTVRNAD 617
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
417-613 |
4.55e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 417 NVFFSYPaRPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK---EGTITIDGQDLKSLNVRYLREI--- 490
Cdd:PRK09473 19 RVTFSTP-DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 -IGVVNQEP----------------VLF-------ATTIAENIRYgREDVTMEEierATKEANAYdfimklPKKFetvvg 546
Cdd:PRK09473 98 qISMIFQDPmtslnpymrvgeqlmeVLMlhkgmskAEAFEESVRM-LDAVKMPE---ARKRMKMY------PHEF----- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 547 ergaqmSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTV 613
Cdd:PRK09473 163 ------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVV 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
430-1266 |
4.67e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.83 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVG--GSGCG---KSTTVQLIQrFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQE---PVLf 501
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGrpGSGCStllKTIASNTDG-FHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDvhfPHL- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 502 atTIAENIRYG--------REDVTMEEiERATKEANAYDFIMKLPKKFETVVGE---RGaqMSGGQKQRIAIARALVRNP 570
Cdd:TIGR00956 154 --TVGETLDFAarcktpqnRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 571 KILLLDEATSALDTESesvvqaALDKIRKGRTILVIAHRLSTV------RNA-----DLIAAFENGVI------------ 627
Cdd:TIGR00956 229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfdKVIVLYEGYQIyfgpadkakqyf 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 628 --------TEQGTHD---------------------------------------ELMEQKGVYYKLVNmqaSETEDQLQE 660
Cdd:TIGR00956 303 ekmgfkcpDRQTTADfltsltspaerqikpgyekkvprtpqefetywrnspeyaQLMKEIDEYLDRCS---ESDTKEAYR 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 661 EGNASSVSEEALNGSVLTGQKRQSTRKSIKR--VRIQNDE---LDVKADQLDKNMPPSSFFKIMKLNKTEWpYFVVGTLC 735
Cdd:TIGR00956 380 ESHVAKQSKRTRPSSPYTVSFSMQVKYCLARnfLRMKGNPsftLFMVFGNIIMALILSSVFYNLPKNTSDF-YSRGGALF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 736 -AIINGALQPifsvmISDVIGMF-----VEKGKA---------AIRETNSTYALLFLGFGLISFVTFFLQGF-----TFG 795
Cdd:TIGR00956 459 fAILFNAFSS-----LLEIASMYearpiVEKHRKyalyhpsadAIASIISEIPFKIIESVVFNIILYFMVNFrrtagRFF 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 796 KAGEILTMRLRSMA--FRAIlrqeiswfdepknstgelitrlandasqvkGATGSRLALvaqniANLGTGIVLSLiygwq 873
Cdd:TIGR00956 534 FYLLILFICTLAMShlFRSI------------------------------GAVTKTLSE-----AMTPAAILLLA----- 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 874 LTLLLLAIVPIIAITG-----------------MIQMKMLAGHAkkDKKELETLGKvASEAIENIRTVVALTQERKFE-Y 935
Cdd:TIGR00956 574 LSIYTGFAIPRPSMLGwskwiyyvnplayafesLMVNEFHGRRF--ECSQYVPSGG-GYDNLGVTNKVCTVVGAEPGQdY 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 936 MYGQN---LQVSYRNSiKKAHIFGFTFAFTqAIMYFTYAGCFRF-------GAYLVK-NGHMRFKDVLLVFSAIVFGAMA 1004
Cdd:TIGR00956 651 VDGDDylkLSFQYYNS-HKWRNFGIIIGFT-VFFFFVYILLTEFnkgakqkGEILVFrRGSLKRAKKAGETSASNKNDIE 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1005 LGQSTSFTPDYAKAKMsaahlfllfervplidsYSEEGEKPKMFGGNITF-KDVAFKYPTRPEVKV-LQGLNIEVEKGQT 1082
Cdd:TIGR00956 729 AGEVLGSTDLTDESDD-----------------VNDEKDMEKESGEDIFHwRNLTYEVKIKKEKRViLNNVDGWVKPGTL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1083 LALVGSSGCGKSTVVQLL-ERFYDPL--SGEVLLDGRntkTLNIQWLRAqIGIVSQEPI-LFDCTIAENI---AYGDNSR 1155
Cdd:TIGR00956 792 TALMGASGAGKTTLLNVLaERVTTGVitGGDRLVNGR---PLDSSFQRS-IGYVQQQDLhLPTSTVRESLrfsAYLRQPK 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1156 EVSHEEivsaaKAANIHSFIESLP-KKY-NTRVGDKGAQLSGGQKQRIAIARALIRQPRILL-LDEATSALDTESEKIVQ 1232
Cdd:TIGR00956 868 SVSKSE-----KMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIC 942
|
970 980 990
....*....|....*....|....*....|....*..
gi 2024474312 1233 EALDK-AREGRTCIVIAHRLSTI--QNADKIAVIQNG 1266
Cdd:TIGR00956 943 KLMRKlADHGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
726-986 |
5.20e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 65.19 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 726 WPYFVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAairETNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRL 805
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTL---DGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 806 RSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPII 885
Cdd:cd18540 78 RKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 886 AITGMI-QMKMLAGHaKKDKKELETLGKVASEAIENIRTVVALTQErkfEYMYGQNLQVS---YRNSIKKAHIFGFTFAF 961
Cdd:cd18540 156 AVVSIYfQKKILKAY-RKVRKINSRITGAFNEGITGAKTTKTLVRE---EKNLREFKELTeemRRASVRAARLSALFLPI 231
|
250 260
....*....|....*....|....*
gi 2024474312 962 TQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18540 232 VLFLGSIATALVLWYGGILVLAGAI 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
413-628 |
5.27e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVffSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLI--QRfyDPKEGTITIDGQDLKSLNVRYLREI 490
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 491 -IGVVNQEPVLFAT----TIAENI---RYGREDVT------MEEIERATKEA-NAYDfImkLPKKFETVVGergaQMSGG 555
Cdd:COG3845 334 gVAYIPEDRLGRGLvpdmSVAENLilgRYRRPPFSrggfldRKAIRAFAEELiEEFD-V--RTPGPDTPAR----SLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 556 QKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAHRLSTVRN-ADLIAAFENGVIT 628
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
771-952 |
6.15e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 64.80 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 771 TYALLFLGF-GLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSR 849
Cdd:cd18589 36 TAAITVMSLlTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSEN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 850 LALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQ 929
Cdd:cd18589 114 LSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFAN 193
|
170 180
....*....|....*....|...
gi 2024474312 930 ERKFEYMYGQNLQVSYRNSIKKA 952
Cdd:cd18589 194 EEGEAQRYRQRLQKTYRLNKKEA 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
437-636 |
7.07e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 65.15 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 437 KVNCGQTVALVGGSGCGKSTTVQLIQRFYD-PKEGT---ITIDGQDLKSLNVRYLREIIG----VVNQEPVlfaTTIAEN 508
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMaekLEFNGQDLQRISEKERRNLVGaevaMIFQDPM---TSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 509 IRYGREdvTMEEIE------RATKEANAYDFImklpkkfeTVVG-----ER----GAQMSGGQKQRIAIARALVRNPKIL 573
Cdd:PRK11022 106 YTVGFQ--IMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSRldvyPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 574 LLDEATSALD-TESESVVQAALDKIRKGRTILV-IAHRLSTV-RNADLIAAFENGVITEQGTHDEL 636
Cdd:PRK11022 176 IADEPTTALDvTIQAQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1070-1268 |
7.22e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLN-----------IQWLRAQIGIVSQEPI 1138
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 LFDCTIAENIAYGDNSREVSHEEIVSaakaaNIHSFIESLPKK---YNTRVGdkgaQLSGGQKQRIAIARALIRQPRILL 1215
Cdd:PRK10982 344 GFNSLISNIRNYKNKVGLLDNSRMKS-----DTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1216 LDEATSALDTESE-KIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVIQNGKV 1268
Cdd:PRK10982 415 LDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1047-1272 |
8.30e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1047 MFGGNITFKDVAFKYptRPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWL 1126
Cdd:PRK15056 2 MQQAGIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1127 RAQIGiVSQE-----PILFDCTIAENiAYGDNS---REVSHE-EIVSAAKAAnihsfIESLPKKYNtRVGdkgaQLSGGQ 1197
Cdd:PRK15056 80 VAYVP-QSEEvdwsfPVLVEDVVMMG-RYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1198 KQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQNADKIAVIQNGKVIEQG 1272
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1069-1273 |
9.04e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLE-RFYDP-------LSGEVLLDGRNTKTLNIQWL---RAQIGIVSQEP 1137
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 ILFdcTIAENIAYG-----DNSREVSHE--EIVSAAKAAnihsfieslpKKYNTRVGDKGAQLSGGQKQRIAIARAL--- 1207
Cdd:PRK13547 96 FAF--SAREIVLLGryphaRRAGALTHRdgEIAWQALAL----------AGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1208 ------IRQPRILLLDEATSALD-TESEKIVQEALDKAREGRT-CIVIAHRLS-TIQNADKIAVIQNGKVIEQGT 1273
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
413-629 |
9.57e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 9.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIG 492
Cdd:PRK10522 323 LELRNVTFAYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQEPVLFATTIAEnirygredvtmEEIERATKEANAYDFIMKLPKKFETVVGE-RGAQMSGGQKQRIAIARALVRNPK 571
Cdd:PRK10522 401 AVFTDFHLFDQLLGP-----------EGKPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 572 ILLLDEATSALDTESESVV-QAALDKIR-KGRTILVIAHRLSTVRNADLIAAFENGVITE 629
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
729-1000 |
1.55e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 64.12 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINgalqPIFSVMISDVIGMFVEkgkAAIRETNSTYALL------------FLGFGLISFVTF-------FL 789
Cdd:cd18565 1 LVLGLLASILN----RLFDLAPPLLIGVAID---AVFNGEASFLPLVpaslgpadprgqLWLLGGLTVAAFlleslfqYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 790 QGFTFGKAGEILTMRLRSMAFRAILRQEISWFDEpkNSTGELITRLANDASQV-----KGATGS-RLALVAqnianLGTG 863
Cdd:cd18565 74 SGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLerfldDGANSIiRVVVTV-----LGIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 864 IVLsLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERkFEYMYGQNLQV 943
Cdd:cd18565 147 AIL-FYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAED-FERERVADASE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 944 SYRNSIKKAHIFGFTF-AFTQAIMYFTYAGCFRFGAYLVKNGHMRFKDVLLV--FSAIVF 1000
Cdd:cd18565 225 EYRDANWRAIRLRAAFfPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTVgtLVTFLF 284
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
166-364 |
1.73e-10 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 63.62 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 166 KRIRQEFFHAVMRQEIGWFDVNDVCELNTRIvDDISKINEGIGEKIAMFFQAVATFFTGFIVGFTKGWKLTLVILALSPV 245
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 246 LGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQR---KETE-RYQKNLEDAKRMGIQKAISANISMG 321
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEqflKKIEkKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024474312 322 VSFFLIygsyALAFWYGTILVLSEDYTIGKVFTvfFSILVGAF 364
Cdd:cd18570 234 ISLIGS----LLILWIGSYLVIKGQLSLGQLIA--FNALLGYF 270
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1068-1280 |
1.73e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1068 KVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNT---------KTLNIQWLRAQIGIVSQEPI 1138
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHItrlsfeqlqKLVSDEWQRNNTDMLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 LFDCTIAENIaygdnsREVSHEEIVSAAKAANIHsfIESL---PKKYntrvgdkgaqLSGGQKQRIAIARALIRQPRILL 1215
Cdd:PRK10938 97 DTGRTTAEII------QDEVKDPARCEQLAQQFG--ITALldrRFKY----------LSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1216 LDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
211-577 |
1.94e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 65.20 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 211 IAMFFQAVATFFTGFIVGFtkgwkLTLVILA-LSPVLGFSSALWAKIISTFTNKEL-TAYAKAGAVAEE---VLAAVRTV 285
Cdd:COG4615 118 ISQAFVRLPELLQSVALVL-----GCLAYLAwLSPPLFLLTLVLLGLGVAGYRLLVrRARRHLRRAREAedrLFKHFRAL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 286 VafGGqRKE------------TERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGK-V 352
Cdd:COG4615 193 L--EG-FKElklnrrrrraffDEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGfV 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 353 FTVFFsiLVGAfsVGQAAPSMEAFANARGAAYAIFNIIDNEPQIDSSSNAGYKLDHVKG--NLEFQNVFFSYPARPDIK- 429
Cdd:COG4615 270 LVLLF--LRGP--LSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEg 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 -ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIIGVVNQEPVLFATTiaen 508
Cdd:COG4615 346 fTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL---- 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 509 irYGREDVTMEEieratkEANAYDFIMKLPKK-------FETVvgergaQMSGGQKQRIAIARALVRNPKILLLDE 577
Cdd:COG4615 422 --LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
141-361 |
1.94e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 63.27 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 141 GIGAGVLFAAYIQVSFwTLAAGRQIkRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGeKIAMFFQAVAT 220
Cdd:cd18543 49 GVAEAVLSFLRRYLAG-RLSLGVEH-DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 221 FFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTnkeLTAYAKAGAVA---EEVLAAVRTVVAFGGQRKETER 297
Cdd:cd18543 126 LVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVKAFGRERRELDR 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 298 YQKNLEDAKRMGIQKA-ISANISMGVSfFLIYGSYALAFWYGTILVLSEDYTIGkVFTVFFSILV 361
Cdd:cd18543 203 FEAAARRLRATRLRAArLRARFWPLLE-ALPELGLAAVLALGGWLVANGSLTLG-TLVAFSAYLT 265
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1070-1281 |
4.24e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVQLLerfydplSGEVLLD-GRntktLNIqwlrAQIGIVS---QEP------IL 1139
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGR----IIY----EQDLIVArlqQDPprnvegTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1140 FDcTIAENIA--------YGDNSREVSHE-------------EIVSAAKA----ANIHSFIESLPKKYNTRVGDkgaqLS 1194
Cdd:PRK11147 84 YD-FVAEGIEeqaeylkrYHDISHLVETDpseknlnelaklqEQLDHHNLwqleNRINEVLAQLGLDPDAALSS----LS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1195 GGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALdKAREGrTCIVIAHRLSTIQN-ADKIAVIQNGKVIE-QG 1272
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLVSyPG 236
|
....*....
gi 2024474312 1273 THQQLLAEK 1281
Cdd:PRK11147 237 NYDQYLLEK 245
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
770-887 |
8.53e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 61.34 E-value: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 770 STYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDEPKnsTGELITRLANDASQVKGATGSR 849
Cdd:cd18550 39 VLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGT 116
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024474312 850 LALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAI 887
Cdd:cd18550 117 LTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
431-689 |
1.25e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQ-DLKSLNVRYLREIIGVVNQEpvlfattiAENI 509
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAISSGLNGQLTGIENIE--------LKGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 RYGredVTMEEIERATKE----ANAYDFIMKLPKKFetvvgergaqmSGGQKQRIAIARALVRNPKILLLDEATSALDte 585
Cdd:PRK13545 112 MMG---LTKEKIKEIIPEiiefADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 586 sESVVQAALDKI----RKGRTILVIAHRLSTVRNADLIAAF-ENGVITEQGTHDELMEQKGVYYKLVNMQASETEDQLQE 660
Cdd:PRK13545 176 -QTFTKKCLDKMnefkEQGKTIFFISHSLSQVKSFCTKALWlHYGQVKEYGDIKEVVDHYDEFLKKYNQMSVEERKDFRE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2024474312 661 E-----------GNASSVSEealNGSVLTGQKRQSTRKSI 689
Cdd:PRK13545 255 EqisqfqhgllqEDQTGRER---KRKKGKKTSRKFKKKRV 291
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1052-1268 |
1.32e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLldgRNTKTlniqwlraQIG 1131
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAKV--------RMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEpilfdctiaeniaygdnsrEVSHEEIVSAAKAANIHSFIESLPKKYNTRVGDKGAQ----------LSGGQKQRI 1201
Cdd:PLN03073 576 VFSQH-------------------HVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRV 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 1202 AIARALIRQPRILLLDEATSALDTES-EKIVQEALdkAREGRTCIViAHRLSTIQNA-DKIAVIQNGKV 1268
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV--LFQGGVLMV-SHDEHLISGSvDELWVVSEGKV 702
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
426-610 |
1.44e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 426 PDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRY-LREIIGVVNQE-PVLFAT 503
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 504 TIAENIRYGRED-----VTMEEIERATKEANAYDFIMKLPKkfetvvgERGAQMSGGQKQRIAIARALVRNPKILLLDEA 578
Cdd:PRK10982 89 SVMDNMWLGRYPtkgmfVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024474312 579 TSALdTESEsvVQAALDKIRK----GRTILVIAHRL 610
Cdd:PRK10982 162 TSSL-TEKE--VNHLFTIIRKlkerGCGIVYISHKM 194
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
142-362 |
1.86e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 60.57 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 142 IGAGVLFAA--YIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVA 219
Cdd:cd18550 46 VAVAVASALlgVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 220 TFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAA-----VRTvvaFGGQRKE 294
Cdd:cd18550 126 TLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgallVKL---FGREDDE 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 295 TERYQKNLEDAKRMGIQKAIsanisMGVSFFLIYGSY-----ALAFWYGTILVLSEDYTIGKVftVFFSILVG 362
Cdd:cd18550 203 AARFARRSRELRDLGVRQAL-----AGRWFFAALGLFtaigpALVYWVGGLLVIGGGLTIGTL--VAFTALLG 268
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
729-995 |
1.89e-09 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 60.54 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVIGMFVEKGkaAIRETNSTYALLFLGFGLISFVTFFLQGFtfgkaGEILTMR---- 804
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSK--NLRLILIIGAILLALYILRTLLNYFVTYW-----GHVMGARietd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 805 LRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVkgatgSRLA------LVAQNIANLGTGIVLSLIYgWQLTLLL 878
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDI-----SELAhhgpedLFISIITIIGSFIILLTIN-VPLTLIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 879 LAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQE----RKFEYmYGQNLQVSYRNSIKK-AH 953
Cdd:cd18549 149 FALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEeyeiEKFDE-GNDRFLESKKKAYKAmAY 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2024474312 954 IFGFTFAFTQAIMYFTYAgcfrFGAYLVKNGHMRFKDvLLVF 995
Cdd:cd18549 228 FFSGMNFFTNLLNLVVLV----AGGYFIIKGEITLGD-LVAF 264
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1059-1258 |
2.17e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1059 FKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVSQEPI 1138
Cdd:PRK13540 9 FDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 LFDCTIAENIAYG--DNSREVSHEEIVSAAKAANIHSFIESLpkkyntrvgdkgaqLSGGQKQRIAIARALIRQPRILLL 1216
Cdd:PRK13540 86 NPYLTLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2024474312 1217 DEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1258
Cdd:PRK13540 152 DEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1031-1285 |
2.26e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1031 RVPLIDSYSEEGEKPK--MFGGNIT----FKDVAFKYP--TRPEVkvlQGLNIEVEKGQTLALVGSSGCGKSTVVQLLER 1102
Cdd:TIGR01257 1911 KEPIFDEDDDVAEERQriISGGNKTdilrLNELTKVYSgtSSPAV---DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1103 FYDPLSGEVLLDGRNTKTlNIQWLRAQIGIVSQEPILFDC-TIAENIAYGDNSREVSHEEIvsaAKAAN--IHSFIESLp 1179
Cdd:TIGR01257 1988 DTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLlTGREHLYLYARLRGVPAEEI---EKVANwsIQSLGLSL- 2062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1180 kkYNTRVGdkgAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEAL-DKAREGRTCIVIAHRLSTIQN-A 1257
Cdd:TIGR01257 2063 --YADRLA---GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlC 2137
|
250 260
....*....|....*....|....*...
gi 2024474312 1258 DKIAVIQNGKVIEQGTHQQLLAEKGFYY 1285
Cdd:TIGR01257 2138 TRLAIMVKGAFQCLGTIQHLKSKFGDGY 2165
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1050-1236 |
2.27e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1050 GNITF--KDVAFKYPTRPEVKvlqGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVlldGRNTKtLNIQWL- 1126
Cdd:PRK11147 316 GKIVFemENVNYQIDGKQLVK---DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI---HCGTK-LEVAYFd 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1127 --RAQIgivsqEPilfDCTIAENIAYGDnsrevshEEIVSAAKAANIHSFIESL---PKKYNTRVgdkgAQLSGGQKQRI 1201
Cdd:PRK11147 389 qhRAEL-----DP---EKTVMDNLAEGK-------QEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRL 449
|
170 180 190
....*....|....*....|....*....|....*
gi 2024474312 1202 AIARALIRQPRILLLDEATSALDTESEKIVQEALD 1236
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
142-364 |
2.31e-09 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 60.16 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 142 IGAGVLFAAYI-------QVSFWTLAAGRQIKR-IRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEgigekIA- 212
Cdd:cd18549 43 IIGAILLALYIlrtllnyFVTYWGHVMGARIETdMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISE-----LAh 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 213 ----MFFQAVATFFTGFIVGFTKGWKLTLVILALSPVLGfssalwakIISTFTNKELTA-----YAKAG---AVAEEVLA 280
Cdd:cd18549 118 hgpeDLFISIITIIGSFIILLTINVPLTLIVFALLPLMI--------IFTIYFNKKMKKafrrvREKIGeinAQLEDSLS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 281 AVRTVVAFGGQRKETERYQKN---LEDAKRMGIqKAISANISmGVSFF--LIYGSyALAFwyGTILVLSEDYTIGKVFTv 355
Cdd:cd18549 190 GIRVVKAFANEEYEIEKFDEGndrFLESKKKAY-KAMAYFFS-GMNFFtnLLNLV-VLVA--GGYFIIKGEITLGDLVA- 263
|
....*....
gi 2024474312 356 fFSILVGAF 364
Cdd:cd18549 264 -FLLYVNVF 271
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1053-1227 |
3.90e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.72 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1053 TFKDVAFKYPtrPEVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLL-DGRNtktlniqwlraqIG 1131
Cdd:TIGR03719 6 TMNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIK------------VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1132 IVSQEPILFDC-TIAENI-------------------AYGDNSREVSH--------EEIVSAAKAANIHSFIE------S 1177
Cdd:TIGR03719 72 YLPQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDKlaaeqaelQEIIDAADAWDLDSQLEiamdalR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1178 LPKkyntrvGD-KGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTES 1227
Cdd:TIGR03719 152 CPP------WDaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
430-612 |
3.90e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 430 ILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQ-RFYDPK-EGTITIDGQDLKSLNVRYlreiIGVVNQEPVLFA-TTIA 506
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILKR----TGFVTQDDILYPhLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 507 ENIRYGREDVTMEEIERATKEANAYDFI--MKLPKKFETVVGE---RGaqMSGGQKQRIAIARALVRNPKILLLDEATSA 581
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190
....*....|....*....|....*....|..
gi 2024474312 582 LD-TESESVVQAALDKIRKGRTILVIAHRLST 612
Cdd:PLN03211 237 LDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
142-362 |
3.98e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 59.53 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 142 IGAGVLFAAYIQVSF-------WTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIvDDISKINEGI-GEKIAM 213
Cdd:cd18782 44 IGVVMLVAALLEAVLtalrtylFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLtGTALTT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 214 FFQAVATFFTgFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRK 293
Cdd:cd18782 123 LLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELK 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 294 ETERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVFTvfFSILVG 362
Cdd:cd18782 202 ARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIA--FRILSG 268
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1059-1249 |
4.99e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.57 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1059 FKYPTRpeVKVLQGLNIEVEKG-----QTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDgRNTKTLNIQWLRA-QIGI 1132
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKAdYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1133 VSQepILFDCTiaeNIAYGDNSREVsheEIVSAAKaanihsfIESLpkkYNTRVGDkgaqLSGGQKQRIAIARALIRQPR 1212
Cdd:cd03237 78 VRD--LLSSIT---KDFYTHPYFKT---EIAKPLQ-------IEQI---LDREVPE----LSGGELQRVAIAACLSKDAD 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024474312 1213 ILLLDEATSALDTESEKIVQEALDKAREG--RTCIVIAH 1249
Cdd:cd03237 136 IYLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH 174
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
420-608 |
6.18e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.19 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 420 FSYPARpdIKILKGLNLKV-----NCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDlkslnVRYLREIIgvv 494
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEVeggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----VSYKPQYI--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 495 nqEPVlFATTIaenirygrEDVTMEEIERATKEANAYDFIMKlPKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILL 574
Cdd:cd03237 71 --KAD-YEGTV--------RDLLSSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 2024474312 575 LDEATSALDTESESVVQAALDKI--RKGRTILVIAH 608
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFaeNNEKTAFVVEH 174
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
440-611 |
6.95e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.15 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 440 CGQTVALVGGSGCGKSTTVQLIQ--------RFYDPKEGTITID---GQDLKSLNVRYLREIIGV------VNQEPVLFA 502
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 503 TTIAENIRygredvtmeeierATKEANAYDFIMKLpKKFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSAL 582
Cdd:cd03236 105 GKVGELLK-------------KKDERGKLDELVDQ-LELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|
gi 2024474312 583 DTESE-SVVQAALDKIRKGRTILVIAHRLS 611
Cdd:cd03236 171 DIKQRlNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
395-667 |
7.91e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 395 QIDSSSNAGykldhvKGNLEFQNVFFSYParpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITI 474
Cdd:PRK11147 308 QVEEASRSG------KIVFEMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 475 DGQdlksLNVRYL---REIIgvvnqEPvlfATTIAENIRYGREDVTMEEIERatkEANAY--DFIMKlPKKFETVVgerg 549
Cdd:PRK11147 379 GTK----LEVAYFdqhRAEL-----DP---EKTVMDNLAEGKQEVMVNGRPR---HVLGYlqDFLFH-PKRAMTPV---- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 550 AQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIrKGrTILVIAHRLSTVRNA---DLIaaFE-NG 625
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY-QG-TVLLVSHDRQFVDNTvteCWI--FEgNG 514
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2024474312 626 VITE--QGTHDElmEQKGVYYKLVNMQASETEDQLQEEGNASSV 667
Cdd:PRK11147 515 KIGRyvGGYHDA--RQQQAQYLALKQPAVKKKEEAAAPKAETVK 556
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
145-350 |
8.65e-09 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 58.33 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 145 GVLFAAYIqvSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISK--------INEGIgekiamffQ 216
Cdd:cd18574 56 SLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 217 AVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETE 296
Cdd:cd18574 126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 297 RYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIG 350
Cdd:cd18574 206 LYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAG 259
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
729-931 |
1.08e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 57.93 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISDVIGMFVEKGKAAIRETnsTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSM 808
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLL--GLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 809 AFRAILRQEISWFDepKNSTGELITRLANDASQVKgatgsRLAL--VAQNIAN----LGTGIVLSLIyGWQLTLLLLAIV 882
Cdd:cd18778 79 LYDKLQRLSLRYFD--DRQTGDLMSRVINDVANVE-----RLIAdgIPQGITNvltlVGVAIILFSI-NPKLALLTLIPI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2024474312 883 PIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQER 931
Cdd:cd18778 151 PFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREE 199
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
428-608 |
1.59e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.79 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQ----LIQrfydPKEGTITIDGQDLKSLNVRYLREIiGVV----NQ--- 496
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgILV----PTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 497 -EPVLfattiaENIRYGRE--DVTMEEIERATKEanaYDFIMKLPKKFETVVgeRgaQMSGGQKQRIAIARALVRNPKIL 573
Cdd:COG4586 110 dLPAI------DSFRLLKAiyRIPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024474312 574 LLDEATSALDTESESVVQAALDKI--RKGRTILVIAH 608
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSH 213
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
768-887 |
1.76e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 57.48 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 768 TNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATG 847
Cdd:cd18606 33 SQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD--TTPLGRILNRFSKDTDVLDNELP 110
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2024474312 848 SRLALVAQNIANLGTGIVLSLIYgwqLTLLLLAIVPIIAI 887
Cdd:cd18606 111 DSLRMFLYTLSSIIGTFILIIIY---LPWFAIALPPLLVL 147
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1051-1254 |
1.83e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1051 NITFKDVAFKYPTRPE---------------VKVLQGLNIEVE-----KGQTLALVGSSGCGKSTVVQLLERFYDPLSGE 1110
Cdd:PRK13409 316 NMRIRPEPIEFEERPPrdeseretlveypdlTKKLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1111 VLLDGRntktlniqwlraqigiVSQEPilfdctiaeniAYGDNSREVSHEEIVSAAKAANIHSFIES-------LPKKYN 1183
Cdd:PRK13409 396 VDPELK----------------ISYKP-----------QYIKPDYDGTVEDLLRSITDDLGSSYYKSeiikplqLERLLD 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1184 TRVGDkgaqLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAREGR--TCIVIAHRLSTI 1254
Cdd:PRK13409 449 KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
393-611 |
1.98e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.61 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 393 EPQIDSSSNAGYKLDHVKGN---------LEFQNVFFSYPArpDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQR 463
Cdd:TIGR00954 423 VEEIESGREGGRNSNLVPGRgiveyqdngIKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 464 FYDPKEGTITIDGQDlkslNVRYlreiigvVNQEPVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFET 543
Cdd:TIGR00954 501 LWPVYGGRLTKPAKG----KLFY-------VPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILER 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 544 VVGERGAQ-----MSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDkiRKGRTILVIAHRLS 611
Cdd:TIGR00954 570 EGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR--EFGITLFSVSHRKS 640
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1047-1278 |
2.68e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1047 MFGGNITfkDVaFKYPTRP------EVKVLQG------LNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLD 1114
Cdd:PRK11288 237 MVGREIG--DI-YGYRPRPlgevrlRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLD 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1115 GrntKTLNIQWLRAQI--GIV------SQEPILFDCTIAENIAYGDNSREVSHEEIVSAAK-AANIHSFIESLPKKynTR 1185
Cdd:PRK11288 314 G---KPIDIRSPRDAIraGIMlcpedrKAEGIIPVHSVADNINISARRHHLRAGCLINNRWeAENADRFIRSLNIK--TP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1186 VGD-KGAQLSGGQKQRIAIARALIRQPRILLLDEATSALD--TESEkIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIA 1261
Cdd:PRK11288 389 SREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIV 467
|
250 260
....*....|....*....|..
gi 2024474312 1262 VIQNGKVI-----EQGTHQQLL 1278
Cdd:PRK11288 468 VMREGRIAgelarEQATERQAL 489
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1070-1273 |
2.70e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.47 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVqlLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIG---IVSQEPI-------- 1138
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIgrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1139 -----LFD------CTIAENIAYGDNSREVSHeeivsaaKAANIH-----------SFIESLPKKYNT------------ 1184
Cdd:cd03271 89 atytgVFDeirelfCEVCKGKRYNRETLEVRY-------KGKSIAdvldmtveealEFFENIPKIARKlqtlcdvglgyi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1185 RVGDKGAQLSGGQKQRIAIARALIRQPR---ILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKI 1260
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
250
....*....|....*....
gi 2024474312 1261 AVI------QNGKVIEQGT 1273
Cdd:cd03271 242 IDLgpeggdGGGQVVASGT 260
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
421-608 |
3.33e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 421 SYParPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQlIQRFYDpKEgtitIDGQDLKSLNVRylreiIGVVNQEPVL 500
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVD-KD----FNGEARPQPGIK-----VGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 501 FAT-TIAENIRYGredvtMEEIERATKEANA-----------YDFIMKLPKKFETVVGERGA------------------ 550
Cdd:TIGR03719 80 DPTkTVRENVEEG-----VAEIKDALDRFNEisakyaepdadFDKLAAEQAELQEIIDAADAwdldsqleiamdalrcpp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 551 ------QMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIrKGrTILVIAH 608
Cdd:TIGR03719 155 wdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1062-1279 |
3.46e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1062 PTRPEVKVLQGLNIE-----VEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQ-WLRAQIGIVSQ 1135
Cdd:PRK10762 255 EVRLKVDNLSGPGVNdvsftLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1136 EP----ILFDCTIAENI---AYGDNSREVSHeeIVSAAKAANIHSFIESLPKKYNTRVGDKGaQLSGGQKQRIAIARALI 1208
Cdd:PRK10762 335 DRkrdgLVLGMSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1209 RQPRILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQN-ADKIAVIQNGKV-----IEQGTHQQLLA 1279
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1041-1282 |
3.92e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1041 EGEKpKMFGGNITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVlldgrntkt 1120
Cdd:PRK15064 310 EQDK-KLHRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1121 lniQWL-RAQIGIVSQEP--------ILFDCtIAENIAYGDNSREV---------SHEEIVSAAKAanihsfieslpkky 1182
Cdd:PRK15064 377 ---KWSeNANIGYYAQDHaydfendlTLFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVKV-------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1183 ntrvgdkgaqLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKArEGrTCIVIAH-R--LSTIqnADK 1259
Cdd:PRK15064 439 ----------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdRefVSSL--ATR 504
|
250 260
....*....|....*....|....
gi 2024474312 1260 IAVIQNGKVIE-QGTHQQLLAEKG 1282
Cdd:PRK15064 505 IIEITPDGVVDfSGTYEEYLRSQG 528
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
431-638 |
5.24e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVR--------YL---REIIGVVNQEPv 499
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdairagiaYVpedRKGEGLVLDLS- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 500 lfattIAENI------RYGREDVtmeeIERATKEANAYDFIMKL---PKKFETVVGergaQMSGGQKQRIAIARALVRNP 570
Cdd:COG1129 347 -----IRENItlasldRLSRGGL----LDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 571 KILLLDEATSALDTESESVVQAALDKI-RKGRTILVIahrlST-----VRNADLIAAFENGVIT-----EQGTHDELME 638
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVI----SSelpelLGLSDRILVMREGRIVgeldrEEATEEAIMA 488
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
433-608 |
6.20e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 433 GLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREII------GVvnqEPVLfatTIA 506
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGI---KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 507 ENIRY---GREDVTMEEIERAtkeanaydfimkLPKkfetvVGERG------AQMSGGQKQRIAIARALVRNPKILLLDE 577
Cdd:PRK13538 93 ENLRFyqrLHGPGDDEALWEA------------LAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|..
gi 2024474312 578 ATSALDTESESVVQAALDK-IRKGRTILVIAH 608
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1085-1227 |
6.79e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1085 LVGSSGCGKSTVVQLLERFYDPLSGE-VLLDGrntktlniqwlrAQIGIVSQEPIL-FDCTIAENI-------------- 1148
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG------------IKVGYLPQEPQLdPEKTVRENVeegvaevkaaldrf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 -----AYGDNSREVSH--------EEIVSAAKAANIHSFIE------SLPKkyntrvGD-KGAQLSGGQKQRIAIARALI 1208
Cdd:PRK11819 106 neiyaAYAEPDADFDAlaaeqgelQEIIDAADAWDLDSQLEiamdalRCPP------WDaKVTKLSGGERRRVALCRLLL 179
|
170
....*....|....*....
gi 2024474312 1209 RQPRILLLDEATSALDTES 1227
Cdd:PRK11819 180 EKPDMLLLDEPTNHLDAES 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
413-591 |
9.30e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 9.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdiKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTI--------------TIDGQD 478
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 479 LKSLNVRYL-REIIGVVNQEpvlfattiaenIRygredvtmeeieratkeANAYDFimklpkkfeTVVGERGAQ----MS 553
Cdd:PLN03073 587 LSSNPLLYMmRCFPGVPEQK-----------LR-----------------AHLGSF---------GVTGNLALQpmytLS 629
|
170 180 190
....*....|....*....|....*....|....*....
gi 2024474312 554 GGQKQRIAIARALVRNPKILLLDEATSALDTES-ESVVQ 591
Cdd:PLN03073 630 GGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
140-350 |
1.23e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 54.80 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 140 SGIGAGVLFAAYIQVSFWTLAAGRQIKRI----RQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFF 215
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLlydlRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 216 QAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSaLWAKIISTFtnkeltAYAKA-GAVAE------EVLAAVRTVVAF 288
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT-RWFRRRSSR------AYRRArERIAAvnadlqETLAGIRVVQAF 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 289 GGQRKETERYQKNLED--AKRMGIQKAISanISMGVSFFLIYGSYALAFWYGTILVLSEDYTIG 350
Cdd:cd18546 195 RRERRNAERFAELSDDyrDARLRAQRLVA--IYFPGVELLGNLATAAVLLVGAWRVAAGTLTVG 256
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1069-1252 |
1.43e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIeVEKGQTLALVGSSGCGKSTVVQLLE--------RFYDPLS-GEVLLDGRNT-------KTLNIQwLRAQIGI 1132
Cdd:cd03236 16 KLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDwDEILDEFRGSelqnyftKLLEGD-VKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1133 --VSQEPILFDCTIAENIAYGDNSREVshEEIVSAAKAANIhsfieslpkkyntrVGDKGAQLSGGQKQRIAIARALIRQ 1210
Cdd:cd03236 94 qyVDLIPKAVKGKVGELLKKKDERGKL--DELVDQLELRHV--------------LDRNIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024474312 1211 PRILLLDEATSALDT----ESEKIVQEAldkAREGRTCIVIAHRLS 1252
Cdd:cd03236 158 ADFYFFDEPSSYLDIkqrlNAARLIREL---AEDDNYVLVVEHDLA 200
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
431-619 |
1.78e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.16 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQ------LIQRFYDPKEGTITIDGQDlkslNVRYLREIIgVVNQEPV----- 499
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHLKKEQPGNHDRIE----GLEHIDKVI-VIDQSPIgrtpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 500 --------LFaTTIAE-------NIRYGRE---------------DVTMEEieratkeanAYDFIMKLPK---KFETVV- 545
Cdd:cd03271 86 snpatytgVF-DEIRElfcevckGKRYNREtlevrykgksiadvlDMTVEE---------ALEFFENIPKiarKLQTLCd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 546 --------GERGAQMSGGQKQRIAIARALVR---NPKILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAHRLSTV 613
Cdd:cd03271 156 vglgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVI 235
|
....*.
gi 2024474312 614 RNADLI 619
Cdd:cd03271 236 KCADWI 241
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1066-1257 |
2.31e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1066 EVKVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLdgRNTKTLNIQ-----WLRAQIGIVSqepilf 1140
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAkpyctYIGHNLGLKL------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1141 DCTIAENIAYGdnSREVSHEEIVSAAkaanIHSFieslpkKYNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEAT 1220
Cdd:PRK13541 84 EMTVFENLKFW--SEIYNSAETLYAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVE 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024474312 1221 SALDTESEKIVQEALD-KAREGRTCIVIAHRLSTIQNA 1257
Cdd:PRK13541 152 TNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
141-364 |
2.62e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 53.67 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 141 GIGAGVLFAAYIQVSF---WTLA--AGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIvDDISKINEGIGEKIAMFF 215
Cdd:cd18555 45 GIGILILFLLYGLFSFlrgYIIIklQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 216 QAVATFFTGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKET 295
Cdd:cd18555 124 IDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIY 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 296 ERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVFTvfFSILVGAF 364
Cdd:cd18555 204 KKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIA--FSSLAGSF 270
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1052-1258 |
2.76e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPevkVLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLE----RFYdplSGEVLLDGRNTKTLNIQW-L 1126
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY---SNDLTLFGRRRGSGETIWdI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1127 RAQIGIVSQEPIL---FDCTIAENIAYG--DN---SREVSHEEIVSAAKAANIHSFieslpkkyNTRVGDKGAQ-LSGGQ 1197
Cdd:PRK10938 335 KKHIGYVSSSLHLdyrVSTSVRNVILSGffDSigiYQAVSDRQQKLAQQWLDILGI--------DKRTADAPFHsLSWGQ 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1198 kQRIA-IARALIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRT--------------CivIAHRLSTIQNAD 1258
Cdd:PRK10938 407 -QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLEFVPDGD 480
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
431-639 |
2.90e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQ-DLKSLNVRYLREIIGVVNQEPVLFATTIaeni 509
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGIENIEFKMLCMGF---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 rygredvTMEEIERATKEANAY----DFIMKLPKKFetvvgergaqmSGGQKQRIAIARALVRNPKILLLDEATSALDte 585
Cdd:PRK13546 116 -------KRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD-- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024474312 586 sESVVQAALDKI----RKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQ 639
Cdd:PRK13546 176 -QTFAQKCLDKIyefkEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1076-1254 |
3.92e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1076 EVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVlldgrnTKTLNI----QWLRAQigivsqepilFDCTIAENIayg 1151
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKIsykpQYISPD----------YDGTVEEFL--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1152 dnsREVSHEEIVSaakaanihSFIES-------LPKKYNTRVGDkgaqLSGGQKQRIAIARALIRQPRILLLDEATSALD 1224
Cdd:COG1245 423 ---RSANTDDFGS--------SYYKTeiikplgLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190
....*....|....*....|....*....|..
gi 2024474312 1225 TESEKIVQEALDKAREGR--TCIVIAHRLSTI 1254
Cdd:COG1245 488 VEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI 519
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
770-986 |
4.41e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 53.28 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 770 STYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRlANDASQVKGATGSR 849
Cdd:cd18555 42 NVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE--NRSSGDLLFR-ANSNVYIRQILSNQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 850 LALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLaghAKKDKKELETLGKVAS---EAIENIRTVVA 926
Cdd:cd18555 119 VISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKI---KKLNQEEIVAQTKVQSyltETLYGIETIKS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 927 LTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18555 196 LGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
550-661 |
5.03e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 550 AQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALdKIRKGrTILVIAHRLSTVRN-ADLIAAFENGVIT 628
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
90 100 110
....*....|....*....|....*....|....*
gi 2024474312 629 E-QGTHDELMEQKGVYYKLVNMQASETEDQL-QEE 661
Cdd:PRK11147 233 SyPGNYDQYLLEKEEALRVEELQNAEFDRKLaQEE 267
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
160-383 |
6.92e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 52.54 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 160 AAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFFTGFIVGFTKGWKLTLVI 239
Cdd:cd18778 67 AEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 240 LALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETER--------YQKNLEDAKRMGIQ 311
Cdd:cd18778 147 LIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRfealsrryRKAQLRAMKLWAIF 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 312 kaisaniSMGVSFFLIYGsYALAFWYGTILVLSEDYTIGKVftVFFSILVGAF--SVGQAAPSMEAFANARGAA 383
Cdd:cd18778 227 -------HPLMEFLTSLG-TVLVLGFGGRLVLAGELTIGDL--VAFLLYLGLFyePITSLHGLNEMLQRALAGA 290
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
413-642 |
6.97e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIdgqdlkslnvrylreiig 492
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------------------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 vvnqepvlfattiAEN--IRYGREDVTmEEIEratKEANAYDFI--MKLPKKFETVVgeRGA----------------QM 552
Cdd:PRK15064 379 -------------SENanIGYYAQDHA-YDFE---NDLTLFDWMsqWRQEGDDEQAV--RGTlgrllfsqddikksvkVL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 553 SGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKIrKGRTILVIAHR-----LSTvrnaDLIAAFENGVI 627
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EGTLIFVSHDRefvssLAT----RIIEITPDGVV 514
|
250
....*....|....*
gi 2024474312 628 TEQGTHDELMEQKGV 642
Cdd:PRK15064 515 DFSGTYEEYLRSQGI 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
434-658 |
7.59e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 434 LNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSlNVRYLREIIGVVNQEPVLfattiaENIRYGR 513
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 514 ED---------VTMEEIERATKEAnaydfIMKLPKkfeTVVGERGA-QMSGGQKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:TIGR01257 2031 EHlylyarlrgVPAEEIEKVANWS-----IQSLGL---SLYADRLAgTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 584 TESESVV-QAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQKGVYYkLVNMQASETEDQL 658
Cdd:TIGR01257 2103 PQARRMLwNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFGDGY-IVTMKIKSPKDDL 2178
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1182-1272 |
9.52e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1182 YNTRVGD---KGaqLSGGQKQRIAIARALIRQPRILLLDEATSALDTESekivqeALDKAREGRTCIVIAHRLSTI---- 1254
Cdd:TIGR00956 198 RNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyq 269
|
90 100
....*....|....*....|....
gi 2024474312 1255 --QNA----DKIAVIQNGKVIEQG 1272
Cdd:TIGR00956 270 csQDAyelfDKVIVLYEGYQIYFG 293
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1046-1253 |
1.01e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.02 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1046 KMFGGNITFKDVAFKYPtrpevkvlqglnieveKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLdGRNTKtlniqw 1125
Cdd:TIGR03719 330 KAFGDKLLIDDLSFKLP----------------PGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK------ 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1126 lraqIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVSAAkaanihsfieslpkkYNTRVGDKGA-------QLSGG 1196
Cdd:TIGR03719 387 ----LAYVDQsrDALDPNKTVWEEISGGLDIIKLGKREIPSRA---------------YVGRFNFKGSdqqkkvgQLSGG 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKAreGRTCIVIAH------RLST 1253
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
413-613 |
1.01e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK-EGTITIDGqdlKSLNVRYLREII 491
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFING---KPVDIRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 --------------GVVNQEPVLFATTIAENIRY---GREDVTMEE--IERATKEANAYDFIMKLPKkfetvvgergAQM 552
Cdd:TIGR02633 335 ragiamvpedrkrhGIVPILGVGKNITLSVLKSFcfkMRIDAAAELqiIGSAIQRLKVKTASPFLPI----------GRL 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 553 SGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTV 613
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEV 466
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1192-1279 |
1.12e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.11 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1192 QLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTI-QNADKIAVIQNGKV 1268
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 2024474312 1269 IEQGTHQQLLA 1279
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1070-1272 |
1.34e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVQllERFYDplSGEVLLDGR-----NTKTLNIQWLRAQIGIvsqepilfdcti 1144
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA--SGKARLISFlpkfsRNKLIFIDQLQFLIDV------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1145 aeNIAYgdnsrevsheeivsaakaanihsfieslpkkynTRVGDKGAQLSGGQKQRIAIARALIRQPR--ILLLDEATSA 1222
Cdd:cd03238 75 --GLGY---------------------------------LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 1223 LDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQNADKI------AVIQNGKVIEQG 1272
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
418-583 |
1.36e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 418 VFFSYPARPDIKIL-KGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQdlkslnvrylrEIIGVVNQ 496
Cdd:PRK10636 3 VFSSLQIRRGVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-----------WQLAWVNQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 497 E-PVLFATTIAENIRYGREDVTMEEIERATKEANAYDFIMKLPKKFETV----VGERGAQM------------------S 553
Cdd:PRK10636 72 EtPALPQPALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdfS 151
|
170 180 190
....*....|....*....|....*....|
gi 2024474312 554 GGQKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:PRK10636 152 GGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1192-1274 |
1.72e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 49.28 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1192 QLSGGQKQRIAIARALI---RQPRIL-LLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQNADKIAVIqnG 1266
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHI--K 154
|
....*...
gi 2024474312 1267 KVIEQGTH 1274
Cdd:cd03227 155 KVITGVYK 162
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
731-1005 |
2.05e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 50.95 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 731 VGTLCAIINGALQPIFSVMISDVIGmFVEKGKAAIRETNSTYALLFLGFGLISfvTFFLQGFTFGkaGEILTMRLRS--- 807
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLIS-YLSSYPDEPLSEGYLLALALFLVSLLQ--SLLLHQYFFL--SFRLGMRVRSals 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 808 -MAFRAILRqeISWFDEPKNSTGELITRLANDAsqvkgatgSRLALVAQNIANLGTG---IVLSLIYGWQLT-------- 875
Cdd:cd18579 76 sLIYRKALR--LSSSARQETSTGEIVNLMSVDV--------QRIEDFFLFLHYLWSAplqIIVALYLLYRLLgwaalagl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 876 LLLLAIVPIIAITGMIQMKMLAGHAK-KDKKeletlGKVASEAIENIRTVvaltqerKF---EYMYGQNLQvSYRNS-IK 950
Cdd:cd18579 146 GVLLLLIPLQAFLAKLISKLRKKLMKaTDER-----VKLTNEILSGIKVI-------KLyawEKPFLKRIE-ELRKKeLK 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 951 KAHIFGFTFAFTQAIMYFT--YAGCFRFGAYLVKNGHMRfkdvllvfSAIVFGAMAL 1005
Cdd:cd18579 213 ALRKFGYLRALNSFLFFSTpvLVSLATFATYVLLGNPLT--------AAKVFTALSL 261
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
413-583 |
2.06e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPK-EGTITIDGQDLKslnVRYLREII 491
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVK---IRNPQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 492 --------------GVVNQEPVLFATTIAENIRYGREDVtmeeIERATKEANAYDFIMKLpkKFETVVGE-RGAQMSGGQ 556
Cdd:PRK13549 337 aqgiamvpedrkrdGIVPVMGVGKNITLAALDRFTGGSR----IDDAAELKTILESIQRL--KVKTASPElAIARLSGGN 410
|
170 180
....*....|....*....|....*..
gi 2024474312 557 KQRIAIARALVRNPKILLLDEATSALD 583
Cdd:PRK13549 411 QQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
143-344 |
2.28e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 51.03 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 143 GAGVLFAaYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMFFQAVATFF 222
Cdd:cd18565 65 LLESLFQ-YLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 223 TGFIVGFTKGWKLTLVILALSPVLGFSSALWAKIIStftnkeltayAKAGAVAEEV----------LAAVRTVVAFGGQR 292
Cdd:cd18565 144 GIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIE----------PRYRAVREAVgdlnarlennLSGIAVIKAFTAED 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024474312 293 KETERyqknLEDAKRMGIQKAISAnISMGVSFF-----LIYGSYALAFWYGTILVLS 344
Cdd:cd18565 214 FERER----VADASEEYRDANWRA-IRLRAAFFpvirlVAGAGFVATFVVGGYWVLD 265
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
740-986 |
2.31e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 51.05 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 740 GALQPIFSVMISDVIGMFVEKGkaaireTNSTYALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEIS 819
Cdd:cd18782 18 GLANPLLFQVIIDKVLVQQDLA------TLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 820 WFDepKNSTGELITRLaNDASQVKG-ATGSRLALVAQNIANLGTGIVLsLIYGWQLTLLLLAIVPIIAITGMIQMKMLAG 898
Cdd:cd18782 92 FFD--KRPVGELSTRI-SELDTIRGfLTGTALTTLLDVLFSVIYIAVL-FSYSPLLTLVVLATVPLQLLLTFLFGPILRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 899 HAkkdKKELETLGKVAS---EAIENIRTVVALTQE----RKFEYMYGQNLQVSYRNSIKKAhIFGFTFAF----TQAIMY 967
Cdd:cd18782 168 QI---RRRAEASAKTQSylvESLTGIQTVKAQNAElkarWRWQNRYARSLGEGFKLTVLGT-TSGSLSQFlnklSSLLVL 243
|
250
....*....|....*....
gi 2024474312 968 FtyagcfrFGAYLVKNGHM 986
Cdd:cd18782 244 W-------VGAYLVLRGEL 255
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1187-1282 |
2.31e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1187 GDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSALDTESE-KIVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVIQ 1264
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*...
gi 2024474312 1265 NGKVIEQGTHQQLLAEKG 1282
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
469-619 |
2.37e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.32 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 469 EGTITIDGQDLKSLNV--------RYLREIIgvvnqEPVLFATTIAENIrygreDVTMEEieratkeanAYDFIMKLPK- 539
Cdd:TIGR00630 746 DGVIKIEMHFLPDVYVpcevckgkRYNRETL-----EVKYKGKNIADVL-----DMTVEE---------AYEFFEAVPSi 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 540 --KFETVV---------GERGAQMSGGQKQRIAIARALVR---NPKILLLDEATSALDTES----ESVVQAALDKirkGR 601
Cdd:TIGR00630 807 srKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDikklLEVLQRLVDK---GN 883
|
170
....*....|....*...
gi 2024474312 602 TILVIAHRLSTVRNADLI 619
Cdd:TIGR00630 884 TVVVIEHNLDVIKTADYI 901
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
413-623 |
3.01e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.47 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 413 LEFQNVFFSYPARPdikILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIdGQDLKslnvrylreiIG 492
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQ--EPVLFATTIAENIRYGredvtMEEIERATKEAN--AY--DFIMKLP---KKfetvVGergaQMSGGQKQRIAIA 563
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGG-----LDIIKLGKREIPsrAYvgRFNFKGSdqqKK----VG----QLSGGERNRVHLA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 564 RALVRNPKILLLDEATSALDTESESVVQAALDKIrkGRTILVIAH-RLSTVRNADLIAAFE 623
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdRWFLDRIATHILAFE 514
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
428-633 |
4.35e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLI--QRFYDPKEGTITIDG-----------------QDLKS--LNVR- 485
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqetfarisgyceqNDIHSpqVTVRe 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 486 ------YLREIIGVVNQEPVLFAttiaenirygreDVTMEEIERAtkeaNAYDFIMKLPKkfetVVGergaqMSGGQKQR 559
Cdd:PLN03140 973 sliysaFLRLPKEVSKEEKMMFV------------DEVMELVELD----NLKDAIVGLPG----VTG-----LSTEQRKR 1027
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 560 IAIARALVRNPKILLLDEATSALDTESESVVQAAL-DKIRKGRTILVIAHRLSTvrnaDLIAAFENGVITEQGTH 633
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1185-1277 |
4.47e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.17 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1185 RVGDKGAQLSGGQKQRIAIARALIRQ---PRILLLDEATSALDTESEK----IVQEALDKareGRTCIVIAHRLSTIQNA 1257
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTA 898
|
90 100
....*....|....*....|....*.
gi 2024474312 1258 DKIAVI------QNGKVIEQGTHQQL 1277
Cdd:TIGR00630 899 DYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1069-1253 |
4.88e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIeVEKGQTLALVGSSGCGKSTVVQLLerfydplSGEvlldgrntktlniqwLRAQIGIVSQEPilfdcTIAENI 1148
Cdd:COG1245 89 RLYGLPV-PKKGKVTGILGPNGIGKSTALKIL-------SGE---------------LKPNLGDYDEEP-----SWDEVL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 AY------GDNSREVSHEEIvsaaKAANIHSFIESLPKKYNTRVGD-------KGA-------------------QLSGG 1196
Cdd:COG1245 141 KRfrgtelQDYFKKLANGEI----KVAHKPQYVDLIPKVFKGTVREllekvdeRGKldelaeklglenildrdisELSGG 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALD----TESEKIVQEAldkAREGRTCIVIAHRLST 1253
Cdd:COG1245 217 ELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAI 274
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
773-986 |
4.95e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 49.87 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 773 ALLFLGFG--LISFVTFFLQGFTFGKageiLTMRLRSMAFRAILRQEISWFDepKNSTGELITRLA-NDASQvkgATGSR 849
Cdd:cd18568 47 GLLIVGIFqiLLSAVRQYLLDYFANR----IDLSLLSDFYKHLLSLPLSFFA--SRKVGDIITRFQeNQKIR---RFLTR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 850 LALvaQNIANLGTGIV---LSLIYGWQLTLLLLAIVPIIAITGMI---QMKMLAghakkdKKELETLGKVAS---EAIEN 920
Cdd:cd18568 118 SAL--TTILDLLMVFIylgLMFYYNLQLTLIVLAFIPLYVLLTLLsspKLKRNS------REIFQANAEQQSflvEALTG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 921 IRTVVALTQERKF----EYMYGQNLQVSYRN---SIKKAHIFGFTFAFTQAIMYFtyagcfrFGAYLVKNGHM 986
Cdd:cd18568 190 IATIKALAAERPIrwrwENKFAKALNTRFRGqklSIVLQLISSLINHLGTIAVLW-------YGAYLVISGQL 255
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1073-1268 |
5.20e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.82 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1073 LNIEVEKGQTLALVGSSGCGKStvvQLLERFY---DPLSGEVLLDGRNTKTLNIQwLRAQIGIV-----SQEPILF-DCT 1143
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAENI---AYGDNSREvsheeIVSAAKAANIHSFIESLPKKYNTrvGDKGAQ-LSGGQKQRIAIARALIRQPRILLLDEA 1219
Cdd:PRK15439 358 LAWNVcalTHNRRGFW-----IKPARENAVLERYRRALNIKFNH--AEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1220 TSALDTESEK-IVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVIQNGKV 1268
Cdd:PRK15439 431 TRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
426-608 |
5.79e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 426 PDI-KILKGLNLKV-----NCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDgqdlksLNVRYLREIIGVvnqepv 499
Cdd:PRK13409 344 PDLtKKLGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKISYKPQYIKP------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 500 lfattiaenirygREDVTMEEIERATKEANAYDFI-------MKLPKKFETVVGErgaqMSGGQKQRIAIARALVRNPKI 572
Cdd:PRK13409 412 -------------DYDGTVEDLLRSITDDLGSSYYkseiikpLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADL 474
|
170 180 190
....*....|....*....|....*....|....*...
gi 2024474312 573 LLLDEATSALDTESESVVQAALDKI--RKGRTILVIAH 608
Cdd:PRK13409 475 YLLDEPSAHLDVEQRLAVAKAIRRIaeEREATALVVDH 512
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
483-641 |
8.77e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 483 NVRYLREIIGVvnQEPVLFATTIAENiryGREDVTM----EEIERATKEANAYDFIMKLpkKFETVVGERGAQMSGGQKQ 558
Cdd:NF000106 79 NRRALRRTIG*--HRPVR*GRRESFS---GRENLYMigr*LDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 559 RIAIARALVRNPKILLLDEATSALDTESESVV-QAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:NF000106 152 RLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDEL 231
|
....*
gi 2024474312 637 MEQKG 641
Cdd:NF000106 232 KTKVG 236
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
729-892 |
1.08e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 48.65 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 729 FVVGTLCAIINGALQPIFSVMISdvigMFVEKGKAAIRETNSTYALLFLGFGLISFVTF-FLQGFTFGKAGEILTMRLRS 807
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLD----WWSSDWSSSPNSSSGYYLGVYAALLVLASVLLvLLRWLLFVLAGLRASRRLHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 808 MAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWqltLLLLAIVPIIAI 887
Cdd:cd18580 77 KLLRSVLRAPMSFFD--TTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP---YFLIVLPPLLVV 151
|
....*
gi 2024474312 888 TGMIQ 892
Cdd:cd18580 152 YYLLQ 156
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
414-647 |
1.09e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 414 EFQNVffsypARPDIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLK-SLNVRYLREIIG 492
Cdd:PRK09700 267 EVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 VVNQ---EPVLFAT-TIAENI------RYGREDVTM----EEIERATKEANAYDFIMKLpkkfeTVVGERGAQMSGGQKQ 558
Cdd:PRK09700 342 YITEsrrDNGFFPNfSIAQNMaisrslKDGGYKGAMglfhEVDEQRTAENQRELLALKC-----HSVNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 559 RIAIARALVRNPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTVRNA-DLIAAFENGVITEQGTH-DE 635
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNrDD 496
|
250
....*....|..
gi 2024474312 636 LMEQKGVYYKLV 647
Cdd:PRK09700 497 MSEEEIMAWALP 508
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
551-610 |
1.15e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 1.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 551 QMSGGQKQRIAIARALVRNPKILLLDEATSALDtesesVVQ--AALDKIR---KGRTILVIAHRL 610
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-----IRQrlNVARLIRelaEGKYVLVVEHDL 271
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
431-619 |
1.20e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 431 LKGLNLKVNCGQTVALVGGSGCGKSTTVQliqrfydpkEGTITIDGQDLKSLNVRYLREIIGVVNQepvlFATTIAENIR 510
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFIDQ----LQFLIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 511 YgredvtmeeieratkeanaydfiMKLPKKFETvvgergaqMSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESES 588
Cdd:cd03238 78 Y-----------------------LTLGQKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|..
gi 2024474312 589 VVQAALDKIR-KGRTILVIAHRLSTVRNADLI 619
Cdd:cd03238 127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWI 158
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
773-986 |
1.72e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 48.23 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 773 ALLFLGFGLISFVTFFLQGFTFGKAGEILTMRLRSMAFRAILRQEISWFDepKNSTGELITRLaNDASQVKGA-TGSRLA 851
Cdd:cd18567 45 AIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFE--KRHLGDIVSRF-GSLDEIQQTlTTGFVE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 852 LVAQNIANLGTGIVLsLIYGWQLTLLLLAIVPIIAItgmiqMKMLAGHAKKDKKE--LETLGKVASEAIENIRTVVAL-- 927
Cdd:cd18567 122 ALLDGLMAILTLVMM-FLYSPKLALIVLAAVALYAL-----LRLALYPPLRRATEeqIVASAKEQSHFLETIRGIQTIkl 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024474312 928 ---TQERKFEYmygQNLQVSYRNSIKKAHIFGFTF-AFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18567 196 fgrEAEREARW---LNLLVDAINADIRLQRLQILFsAANGLLFGLENILVIYLGALLVLDGEF 255
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
550-586 |
1.77e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 1.77e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2024474312 550 AQMSGGQKQRIAIARALVRNPKILLLDEATSALDTES 586
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1069-1251 |
1.90e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIeVEKGQTLALVGSSGCGKSTVVQLLerfydplSGEvlldgrntktlniqwLRAQIGIVSQEPilfdcTIAENI 1148
Cdd:PRK13409 89 KLYGLPI-PKEGKVTGILGPNGIGKTTAVKIL-------SGE---------------LIPNLGDYEEEP-----SWDEVL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1149 AY------GDNSREVSHEEIVSAAKAanihSFIESLPKKYNTRVGD-------KGA-------------------QLSGG 1196
Cdd:PRK13409 141 KRfrgtelQNYFKKLYNGEIKVVHKP----QYVDLIPKVFKGKVREllkkvdeRGKldevverlglenildrdisELSGG 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALDtesekiVQEALDKAR------EGRTCIVIAHRL 1251
Cdd:PRK13409 217 ELQRVAIAAALLRDADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDL 271
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
427-659 |
1.93e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGQDLKSLNVRYLREIigvVNQEpvlFATTIA 506
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDE---WQRNNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 507 ENIRYGREDV---TMEEIERATKEANAydfIMKLPKKF--ETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSA 581
Cdd:PRK10938 89 DMLSPGEDDTgrtTAEIIQDEVKDPAR---CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 582 LDTESESVVQAALDKI-RKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQKGVYY-----KLVNMQASET 654
Cdd:PRK10938 166 LDVASRQQLAELLASLhQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQALVAQlahseQLEGVQLPEP 245
|
....*
gi 2024474312 655 EDQLQ 659
Cdd:PRK10938 246 DEPSA 250
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
768-986 |
2.67e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 47.49 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 768 TNSTYALLFLGFGLISFVTFFLQGF-------TFGKAGEILTMRLrsmaFRAILRQEISWFDepKNSTGELITRLaNDAS 840
Cdd:cd18588 37 SLSTLDVLAIGLLVVALFEAVLSGLrtylfshTTNRIDAELGARL----FRHLLRLPLSYFE--SRQVGDTVARV-RELE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 841 QVKG-ATGSRLALVAqNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLaghakkdKKELETLGKVAS---- 915
Cdd:cd18588 110 SIRQfLTGSALTLVL-DLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPIL-------RRRLEEKFQRGAenqs 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 916 ---EAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18588 182 flvETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGEL 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
551-620 |
2.79e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 2.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 551 QMSGGQKQRIAIARALVRNPKILLLDEATSALD-TESESVVQAALDKIRKGRTILVIAHRLSTVrnaDLIA 620
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAIL---DYLA 279
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
428-637 |
2.91e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 428 IKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLI------------QRFydpkegtiTIDGQDLKSLNVRYLREIIG--- 492
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtaDRM--------RFDDIDLLRLSPRERRKLVGhnv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 493 -VVNQEPvlfATTIAENIRYGREdvTMEEIERAT-----------KEANAYDFIMKLP-KKFETVVGERGAQMSGGQKQR 559
Cdd:PRK15093 92 sMIFQEP---QSCLDPSERVGRQ--LMQNIPGWTykgrwwqrfgwRKRRAIELLHRVGiKDHKDAMRSFPYELTEGECQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 560 IAIARALVRNPKILLLDEATSALDTESESVVQAALDKIRK--GRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDEL 636
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKEL 246
|
.
gi 2024474312 637 M 637
Cdd:PRK15093 247 V 247
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
437-620 |
2.99e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 437 KVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDgqdlksLNVRYLREIIGVVNQEPV--LFATTIAENIrygre 514
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKISYKPQYISPDYDGTVeeFLRSANTDDF----- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 515 DVTMEEIERATKeanaydfiMKLPKKFETVVGErgaqMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAAL 594
Cdd:COG1245 431 GSSYYKTEIIKP--------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180
....*....|....*....|....*...
gi 2024474312 595 DKI--RKGRTILVIAHRLSTVrnaDLIA 620
Cdd:COG1245 499 RRFaeNRGKTAMVVDHDIYLI---DYIS 523
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
225-362 |
3.14e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 47.58 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 225 FIVGFTKGWKLTLVILALSPVLgfssALWAKIISTFTNKELtayaKAGAVAE--------EVLAAVRTVVAFGGQRKETE 296
Cdd:cd18566 133 LGLIWYLGGKLVLVPLVLLGLF----VLVAILLGPILRRAL----KERSRADerrqnfliETLTGIHTIKAMAMEPQMLR 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 297 RYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVftVFFSILVG 362
Cdd:cd18566 205 RYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGAL--IACTMLSG 268
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
518-645 |
3.60e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 518 MEEIERATKEANAYDFIMKLPKKFETVVgERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKI 597
Cdd:PLN03073 312 LELIDAYTAEARAASILAGLSFTPEMQV-KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW 390
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2024474312 598 RKgrTILVIAHrlstVRNadliaaFENGVITEQgTHdeLMEQKGVYYK 645
Cdd:PLN03073 391 PK--TFIVVSH----ARE------FLNTVVTDI-LH--LHGQKLVTYK 423
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
552-623 |
3.86e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 3.86e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 552 MSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALDKI--RKGRTILVIAHRLSTVRN-ADLIAAFE 623
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
423-640 |
4.45e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 423 PARPDIKILKG------LNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITIDGqdlKSLNVRYLREII--GVV 494
Cdd:PRK11288 255 EVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIraGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 495 ------NQEPVLFATTIAENIRYG--REDVTMEEIERATKEA-NAYDFIMKLPKKF---ETVVGergaQMSGGQKQRIAI 562
Cdd:PRK11288 332 lcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 563 ARALVRNPKILLLDEATSALDTESESVVQAALDKI-RKGRTILVIAHRLSTVRN-ADLIAAFENGVITEQGTHDELMEQK 640
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQATERQ 487
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
225-365 |
4.97e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 46.72 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 225 FIVGFTKGWKLTLVILALSPVLGFSSALWAKIISTFTNKELTAYAKAGAVAEEVLAAVRTVVAFGGQRKETERYQKNLED 304
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 305 AKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGKVftVFFSILVGAFS 365
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQL--IAFNMLAGQVS 271
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
146-364 |
5.29e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 46.70 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 146 VLFAAYIQVSFWtlaagrqiKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKInegiGEKIA-MFFQAV-ATFFT 223
Cdd:cd18540 63 IRLAGKIEMGVS--------YDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRL----GEIISwGLVDLVwGITYM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 224 GFIVG--FTKGWKLTLVILALSPVLGFSSALWAKIISTF------TNKELT-AYakagavaEEVLAAVRTVVAFGGQRKE 294
Cdd:cd18540 131 IGILIvmLILNWKLALIVLAVVPVLAVVSIYFQKKILKAyrkvrkINSRITgAF-------NEGITGAKTTKTLVREEKN 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 295 TERYQKNLEDAKRMGIQKAISANISMGVSFFLIYGSYALAFWYGTILVLSEDYTIGkVFTVFFSILVGAF 364
Cdd:cd18540 204 LREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIG-TLVAFISYATQFF 272
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1062-1247 |
5.35e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1062 PTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKS-TVVQLLERFYDP-LSGEVLLDGRNTKTLNI-QWLRAQIGIVSQEP- 1137
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVsDAIDAGLAYVTEDRk 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1138 ----ILFDcTIAENIAYGdNSREVS-------HEEIVSAakaanihsfiESLPKKYNTR---VGDKGAQLSGGQKQRIAI 1203
Cdd:NF040905 348 gyglNLID-DIKRNITLA-NLGKVSrrgvideNEEIKVA----------EEYRKKMNIKtpsVFQKVGNLSGGNQQKVVL 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2024474312 1204 ARALIRQPRILLLDEATSALDT----ESEKIVQEAldkAREGRTCIVI 1247
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
190-364 |
6.33e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 46.40 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 190 CELNTRIVDDI-SKINEGigEKIAMFF--QAVATF---FTGFIVG---FTKGWKLTLVILALSPVLGFSSALWAKIISTF 260
Cdd:cd18568 91 SFFASRKVGDIiTRFQEN--QKIRRFLtrSALTTIldlLMVFIYLglmFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRN 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 261 TNKELTAYAKAGAVAEEVLAAVRTVVAFGGQR----KETERYQKNLEdaKRMGIQKaISANISMGVSFFLIYGSYALaFW 336
Cdd:cd18568 169 SREIFQANAEQQSFLVEALTGIATIKALAAERpirwRWENKFAKALN--TRFRGQK-LSIVLQLISSLINHLGTIAV-LW 244
|
170 180 190
....*....|....*....|....*....|
gi 2024474312 337 YGTILVLSEDYTIGKV--FTVFFSILVGAF 364
Cdd:cd18568 245 YGAYLVISGQLTIGQLvaFNMLFGSVINPL 274
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1070-1280 |
7.82e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1070 LQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLDGRNTKTLNIQWLRAQIGIVsqEPILFDCtiaenIA 1149
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGI--ENIEFKM-----LC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1150 YGDNSREVSH--EEIVsaaKAANIHSFIESLPKKYntrvgdkgaqlSGGQKQRIAIARALIRQPRILLLDEATSALDtes 1227
Cdd:PRK13546 113 MGFKRKEIKAmtPKII---EFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD--- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1228 EKIVQEALDKARE----GRTCIVIAHRLSTIQN-ADKIAVIQNGKVIEQGTHQQLLAE 1280
Cdd:PRK13546 176 QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1192-1249 |
8.43e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 8.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1192 QLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKARegRTCIVIAH 1249
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1193-1264 |
1.15e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.49 E-value: 1.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1193 LSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVIQ 1264
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1069-1268 |
1.48e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1069 VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLdGRNTK-----TLNIQWLRAqigivSQEPILFDCT 1143
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKlgyfaQHQLEFLRA-----DESPLQHLAR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1144 IAEniaygdnsREVSHEeivsaakaanIHSFIESLPKKyNTRVGDKGAQLSGGQKQRIAIARALIRQPRILLLDEATSAL 1223
Cdd:PRK10636 401 LAP--------QELEQK----------LRDYLGGFGFQ-GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024474312 1224 DTESEKIVQEALDKArEGrTCIVIAHRLSTIQN-ADKIAVIQNGKV 1268
Cdd:PRK10636 462 DLDMRQALTEALIDF-EG-ALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1052-1252 |
1.50e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1052 ITFKDVAFKYPTRPEVK----------VLQGLNIEVEKGQTLALVGSSGCGKSTVVQLL--ERFYDPLSGEVLLDGRNTK 1119
Cdd:PLN03140 868 MSFDDVNYFVDMPAEMKeqgvtedrlqLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKK 947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1120 tlniQWLRAQI-GIVSQEPILF-DCTIAENIAYGDNSR---EVSHEE-------IVSAAKAANIHSFIESLPkkyntrvG 1187
Cdd:PLN03140 948 ----QETFARIsGYCEQNDIHSpQVTVRESLIYSAFLRlpkEVSKEEkmmfvdeVMELVELDNLKDAIVGLP-------G 1016
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1188 DKGaqLSGGQKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEAL-DKAREGRTCIVIAHRLS 1252
Cdd:PLN03140 1017 VTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1047-1272 |
1.51e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 44.18 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1047 MFGGNITFkdvaFKYPTRPEVKVLQGLNIEVEKGQTLALVGSSGCGKST----VVQLLERFYDPlSGEVLLDGRNTKTLN 1122
Cdd:cd03233 4 LSWRNISF----TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1123 IQWlRAQIGIVSQEpilfDCTIAEniaygdnsreVSHEEIVSAAKAANIHSFIeslpkkyntrvgdKGaqLSGGQKQRIA 1202
Cdd:cd03233 79 EKY-PGEIIYVSEE----DVHFPT----------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 1203 IARALIRQPRILLLDEATSALDTESE----KIVQEALDKarEGRTCIVIAHRLS-TIQNA-DKIAVIQNGKVIEQG 1272
Cdd:cd03233 129 IAEALVSRASVLCWDNSTRGLDSSTAleilKCIRTMADV--LKTTTFVSLYQASdEIYDLfDKVLVLYEGRQIYYG 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
552-617 |
1.76e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 552 MSGGQkQRIA-IARALVRNPKILLLDEATSALDTESESVVQAALDK-IRKGRTILV------------IAHRLSTVRNAD 617
Cdd:PRK10938 402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFVPDGD 480
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
864-986 |
1.87e-04 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 45.12 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 864 IVLSLIyGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKKELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQV 943
Cdd:cd18587 133 AVIALI-GGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAA 211
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2024474312 944 SYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGHM 986
Cdd:cd18587 212 LARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGEL 254
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
552-643 |
2.39e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 552 MSGGQKQRIAIARALVRNPKILLLDEATSALDTESE-SVVQAALDKIRKGRTILVIAHRLSTVRN-ADLIAAFENG---- 625
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGlvag 471
|
90
....*....|....*....
gi 2024474312 626 -VITEQGTHDELMEQKGVY 643
Cdd:PRK10982 472 iVDTKTTTQNEILRLASLH 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
532-583 |
2.87e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 2.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024474312 532 DFIM----KLPKKfETVVGErgaqMSGGQKQRIAIARALVRNPKILLLDEATSALD 583
Cdd:PRK10762 377 DFIRlfniKTPSM-EQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
448-619 |
3.66e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 448 GGSGCGKSTTVQLIQRFYDPKEGTITIdgqdlKSLNVrylreiigvvNQEPVLFATTIAENIRYGREdvtMEEIERATKE 527
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNI----------NNIAKPYCTYIGHNLGLKLE---MTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 528 ANAYDFIMKLPK-----KFETVVGERGAQMSGGQKQRIAIARALVRNPKILLLDEATSALDTESESVVQAALD-KIRKGR 601
Cdd:PRK13541 95 SEIYNSAETLYAaihyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGG 174
|
170
....*....|....*...
gi 2024474312 602 TILVIAHRLSTVRNADLI 619
Cdd:PRK13541 175 IVLLSSHLESSIKSAQIL 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1063-1281 |
5.64e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1063 TRPEVKVLQGLNIEVEKGQTLALVGSSGCGKStvvQLLERFY--DPL-SGEVLLDGRNTKTLN-IQWLRAQIGIVSQ--- 1135
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRaGGEIRLNGKDISPRSpLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1136 EPILF-DCTIAENIA---------YGDNSREVSHEEIVSAAKAANihsfiESLPKKYNTrVGDKGAQLSGGQKQRIAIAR 1205
Cdd:PRK09700 349 DNGFFpNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 1206 ALIRQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQNA-DKIAVIQNGKVIEQGTHQQLLAEK 1281
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
427-718 |
7.86e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 427 DIKILKGLNLKVNCGQTVALVGGSGCGKSTTVQLIQRFYDPKEGTITI-DGQDLKSL---NVRYLReiigvVNQEPVLFA 502
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFaqhQLEFLR-----ADESPLQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 503 TTIAEnirygredvtmEEIERATKeanayDFIMKLPKKFETVVgERGAQMSGGQKQRIAIARALVRNPKILLLDEATSAL 582
Cdd:PRK10636 399 ARLAP-----------QELEQKLR-----DYLGGFGFQGDKVT-EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 583 DTESESVVQAALdkIRKGRTILVIAHRLSTVRNA--DLIAAFENGVITEQGTHDELMEQkgvyykLVNMQASET-EDQLQ 659
Cdd:PRK10636 462 DLDMRQALTEAL--IDFEGALVVVSHDRHLLRSTtdDLYLVHDGKVEPFDGDLEDYQQW------LSDVQKQENqTDEAP 533
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 660 EEGNASSVSEEalngsvlTGQKR---------QSTRKSIKRVRIQNDELDVKADQLDKNMPPSSFFKI 718
Cdd:PRK10636 534 KENNANSAQAR-------KDQKRreaelrtqtQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQ 594
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
552-619 |
1.12e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 552 MSGGQKQRIAIARAL---VRNPKILLLDEATSALDTES-ESVVQAALDKIRKGRTILVIAHRLSTVRNADLI 619
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1193-1284 |
1.12e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1193 LSGGQKQRIAIARALIRQP--RIL-LLDEATSALDTES----EKIVQEALDKareGRTCIVIAHRLSTIQNADKIavI-- 1263
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTADWI--Idl 905
|
90 100
....*....|....*....|....*..
gi 2024474312 1264 ------QNGKVIEQGTHQQLLAEKGFY 1284
Cdd:PRK00349 906 gpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
551-620 |
1.23e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024474312 551 QMSGGQKQRIAIARAL----VRNPKILLLDEATSALDTESesvVQAALDKIR----KGRTILVIAHRLSTVRNADLIA 620
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRD---GQALAEAILehlvKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
826-986 |
1.57e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 42.02 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 826 NSTGELITRLANDASQVKGATGSRLALVAQNIANLGTGIVLSLIYGWQLTLLLLAIVPIIAITGMIQMKMLAGHAKKDKK 905
Cdd:cd18554 100 NRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 906 ELETLGKVASEAIENIRTVVALTQERKFEYMYGQNLQVSYRNSIKKAHIFGFTFAFTQAIMYFTYAGCFRFGAYLVKNGH 985
Cdd:cd18554 180 ALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGN 259
|
.
gi 2024474312 986 M 986
Cdd:cd18554 260 L 260
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1191-1282 |
1.71e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1191 AQLSGGQKQRIAIARALIRQPRILLLDEATSALDTES-----EKIvqEALDKAREGRTCIViahrlST--IQNA---DKI 1260
Cdd:NF033858 135 GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSrrqfwELI--DRIRAERPGMSVLV-----ATayMEEAerfDWL 207
|
90 100
....*....|....*....|..
gi 2024474312 1261 AVIQNGKVIEQGTHQQLLAEKG 1282
Cdd:NF033858 208 VAMDAGRVLATGTPAELLARTG 229
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
135-248 |
1.79e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 41.72 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 135 YAYYYSGIGAGVLFAAYIQVSFWTLAAGRQIKRIRQEFFHAVMRQEIGWFDVNDVCELNTRIVDDISKINEGIGEKIAMF 214
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDF 120
|
90 100 110
....*....|....*....|....*....|....
gi 2024474312 215 FQAVATFFTGFIVGFTKGWKLTLVILALSPVLGF 248
Cdd:cd18580 121 LQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYL 154
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1193-1284 |
1.88e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1193 LSGGQKQRIAIARALIR--QPRIL-LLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIavI----- 1263
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWI--Idlgpe 904
|
90 100
....*....|....*....|....
gi 2024474312 1264 ---QNGKVIEQGTHQQLLAEKGFY 1284
Cdd:COG0178 905 ggdGGGEIVAEGTPEEVAKVKASY 928
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1192-1260 |
2.01e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 2.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024474312 1192 QLSGGQKQRIAIAraLI-----RQPR-ILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKI 1260
Cdd:pfam02463 1077 LLSGGEKTLVALA--LIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKL 1149
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1193-1272 |
3.23e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.70 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1193 LSGGQKQRIAIARALIRQPR--ILLLDEATSAL-DTESEKIVqEALDKARE-GRTCIVIAHRLSTIQNADKI------AV 1262
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhPRDNDRLI-ETLKRLRDlGNTVLVVEHDEDTIRAADHVidigpgAG 216
|
90
....*....|
gi 2024474312 1263 IQNGKVIEQG 1272
Cdd:cd03270 217 VHGGEIVAQG 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1186-1281 |
3.43e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1186 VGDKGAQLSGGQKQRIAIARALI---RQPRILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQNADKIA 1261
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
90 100
....*....|....*....|....*.
gi 2024474312 1262 VI------QNGKVIEQGTHQQLLAEK 1281
Cdd:PRK00635 1773 EMgpgsgkTGGKILFSGPPKDISASK 1798
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
510-619 |
4.07e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 510 RYGRE---------------DVTMEEieratkeanAYDFIMKLPK---KFETVV---------GERGAQMSGGQKQRIAI 562
Cdd:PRK00349 771 RYNREtlevkykgkniadvlDMTVEE---------ALEFFEAIPKiarKLQTLVdvglgyiklGQPATTLSGGEAQRVKL 841
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024474312 563 ARALVRNP--KIL-LLDEATSALDTESES----VVQAALDKirkGRTILVIAHRLSTVRNADLI 619
Cdd:PRK00349 842 AKELSKRStgKTLyILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLDVIKTADWI 902
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
730-969 |
4.95e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 40.69 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 730 VVGTLCAIING--ALQPIFsvmISDVIGMFVEKGKAAIRETnstYaLLFLGFGLISFV-TFFLQGFTFGKagEILTMRLR 806
Cdd:cd18594 1 LLGILLFLEESlkIVQPLL---LGRLVAYFVPDSTVTKTEA---Y-LYALGLSLCAFLrVLLHHPYFFGL--HRYGMQLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 807 ----SMAFRAILRQEISWFDepKNSTGELITRLANDASQVKGATGSRLALVaqnIANLGTGIVLSLIygWQ--------- 873
Cdd:cd18594 72 ialsSLIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLW---IAPLQVIVLTGLL--WReigpsslag 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 874 LTLLLLaIVPIIAITGMIQMKMLAGHAKKDKKELetlgKVASEAIENIRTVVALTQERKFEYMYgQNLQVSYRNSIKKAH 953
Cdd:cd18594 145 LGVLLL-LLPLQAYLGKLFAKYRRKTAGLTDERV----KIMNEIISGMRVIKMYTWEESFAKLI-ENIRKKELKLIRKAA 218
|
250 260
....*....|....*....|
gi 2024474312 954 IFGFT----FAFTQAIMYFT 969
Cdd:cd18594 219 YIRAFnmafFFFSPTLVSFA 238
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1046-1236 |
5.24e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1046 KMFGGNITFKDVAFKYPtrpevkvlqglnieveKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLdGrntKTlniqw 1125
Cdd:PRK11819 332 KSFGDRLLIDDLSFSLP----------------PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G---ET----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1126 lrAQIGIVSQ--EPILFDCTIAENIAYGDNSREVSHEEIVSAAkaanihsfieslpkkYNTRVGDKGA-------QLSGG 1196
Cdd:PRK11819 387 --VKLAYVDQsrDALDPNKTVWEEISGGLDIIKVGNREIPSRA---------------YVGRFNFKGGdqqkkvgVLSGG 449
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2024474312 1197 QKQRIAIARALIRQPRILLLDEATSALDTESEKIVQEALD 1236
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
552-619 |
6.09e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.93 E-value: 6.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024474312 552 MSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESESVVQAALDKIR-KGRTILVIAHRLSTVRNADLI 619
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHV 208
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
1191-1227 |
6.92e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.21 E-value: 6.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2024474312 1191 AQLSGGQKQR---IAIARALIRQ----------PRILLLDEATSALDTES 1227
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAAQygsaegrppaPRLVFLDEAFAKLDEEN 80
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
552-619 |
9.24e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 9.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024474312 552 MSGGQKQRIAIARALVR--NPKIL-LLDEATSALDTESESVVQAALDKIR-KGRTILVIAHRLSTVRNADLI 619
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVdKGNTVVVIEHNLDVIKTADWI 898
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1077-1120 |
9.69e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.92 E-value: 9.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2024474312 1077 VEKGQTLALVGSSGCGKSTVVQLLERFYDPLSGEVLLD---GRNTKT 1120
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVREDdskGRHTTT 238
|
|
| |
