|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-1464 |
0e+00 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 2894.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1 MKKDQRQPRDNSNSSNNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPSSHRKLLGVSFVCATISGGTLPFFV 80
Cdd:PTZ00265 1 MKKDQRQKKDNNSGGGNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDL 160
Cdd:PTZ00265 81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
Cdd:PTZ00265 161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 241 EALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
Cdd:PTZ00265 321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNI 480
Cdd:PTZ00265 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 481 KYSLYSLKDLEALSEESNEDGFSSQSDSNSRNSCRAKCAGDLNDMIQTTDSTELIQVRKNYETIEDSEVVSVSKKVLIHD 560
Cdd:PTZ00265 481 KYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLIHD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PTZ00265 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 641 STIRYANTIFVLSNRENGSTVDVDVLGEDPTKDSNEKNEKHDKQEKGGKNSSANQKIGNAGSYIIEQGTHDALMKNKNGI 720
Cdd:PTZ00265 641 STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSYIIEQGTHDALMKNKNGI 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 721 YYTMINNQKVSSKSSSNNDNDKDSDMKSSIYKDSERGYDPDEANGNAK--NESASAKKSEKMSDAKASNTNAGGRLAFLR 798
Cdd:PTZ00265 721 YYTMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKheNESASNKKSCKMSDENASENNAGGKLPFLR 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 799 NLFKRKPKAPNNLRVVYREIFSYKKDIAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAMF 878
Cdd:PTZ00265 801 NLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMF 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 879 ISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQDSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVST 958
Cdd:PTZ00265 881 ISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSM 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 959 VMSFYFCPIVAAVLTGTYFIFMRVFAIRARIAANKDVEKKRVNQPGTAFVYNSDDEIFKDPSFLIQEAFYNMNTVIIYGL 1038
Cdd:PTZ00265 961 VMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGL 1040
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1039 EDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLM 1118
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1119 SLKGDSENAKLSFERYYPLITRKSLIDVRDNGGIKIKNSNDIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIV 1198
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1199 GETGSGKSTVMSLLMRFYDLKNDHHIVFKNEQTGESSKEQMQQGDEEQNVGMKNANEFSSSKEGADGQSSTLFKNSGKIL 1278
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVFKNSGKIL 1280
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1279 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLS 1358
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLS 1360
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1359 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSF 1438
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSF 1440
|
1450 1460
....*....|....*....|....*.
gi 156095386 1439 VQAQGTHEELLSVQDGVYKKYVKLAK 1464
Cdd:PTZ00265 1441 VQAHGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
811-1462 |
4.93e-133 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 423.42 E-value: 4.93e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 811 LRVVYREIFSYKKDIAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEAnSNKYSLYILVIAIAMFISETLKNYYNNV 890
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA-LLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 891 IGEKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP---I 967
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWrlaL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 968 VAAVLTGTYFIFMRVFAIRARIAANKdvekkrvnqpgtafVYNSDDEIfkdpSFLIQEAFYNMNTVIIYGLEDYFCTLIE 1047
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRR--------------VQEALAEL----NGRLQESLSGIRVVKAFGREERELERFR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1048 KAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMksLFTFLFTGSYA--GKLMSLKGDSE 1125
Cdd:COG1132 228 EANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLV--AFILYLLRLFGplRQLANVLNQLQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1126 NAKLSFERYYPLITRKSLIDVRDNGgikiKNSNDIKGKIEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGK 1205
Cdd:COG1132 306 RALASAERIFELLDEPPEIPDPPGA----VPLPPVRGEIEFENVSFSY--PGDRPVLKDISLTIPPGETVALVGPSGSGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1206 STVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDIC 1285
Cdd:COG1132 380 STLVNLLLRFYDP------------------------------------------------------TSGRILIDGVDIR 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1286 DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRI 1365
Cdd:COG1132 406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1366 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAQGTH 1445
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLDD----GR-IVEQGTH 558
|
650
....*....|....*..
gi 156095386 1446 EELLSvQDGVYKKYVKL 1462
Cdd:COG1132 559 EELLA-RGGLYARLYRL 574
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
58-728 |
1.01e-125 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 403.39 E-value: 1.01e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 58 HRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDIIFS---LVLIGIFQFILSFISSFCMDVVTTKILKTLKI 134
Cdd:COG1132 19 YRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLlllLLGLALLRALLSYLQRYLLARLAQRVVADLRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 135 EFLKSVFYQDGQFHDNNP-G---SKLTSDLDfyleQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI 210
Cdd:COG1132 99 DLFEHLLRLPLSFFDRRRtGdllSRLTNDVD----AVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFN-LSEKLYsKYTLKANLMESLHIGMING 289
Cdd:COG1132 175 LLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFReANEELR-RANLRAARLSALFFPLMEL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 290 FILASYAFGFWYGTRIIIS-DLSnqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRKPLV 368
Cdd:COG1132 254 LGNLGLALVLLVGGLLVLSgSLT---------VGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 369 ENNQDGKKLKDIK-KIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDs 447
Cdd:COG1132 325 PDPPGAVPLPPVRgEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 448 HNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcaGDLNdmiq 527
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRY-------------------------------------GRPD---- 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 528 ttdsteliqvrknyetIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEAT 607
Cdd:COG1132 441 ----------------ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 608 SSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrengstvdvdvlgedptkdsneknekhdkqeKG 687
Cdd:COG1132 505 SALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRNADRILVL---------------------------------DD 549
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 156095386 688 GKnssanqkignagsyIIEQGTHDALMKnKNGIYYTMINNQ 728
Cdd:COG1132 550 GR--------------IVEQGTHEELLA-RGGLYARLYRLQ 575
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1164-1463 |
6.06e-112 |
|
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: 352.61 E-value: 6.06e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:cd03249 56 -----------------------------TSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:cd03249 107 EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA- 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAQGTHEELLSvQDGVYKKYVKLA 1463
Cdd:cd03249 186 -MKGRTTIVIAHRLSTIRNADLIAVLQN-----GQVVEQGTHDELMA-QKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
383-728 |
1.55e-108 |
|
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: 343.37 E-value: 1.55e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKI 462
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG-VDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNSIKNNIKYSlyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrKNYE 542
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYG-------------------------------------------------------KPDA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 TieDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03249 105 T--DEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 623 NNLKgnENRITIIIAHRLSTIRYANTIFVLSNrengstvdvdvlgedptkdsneknekhdkqekggknssanqkignagS 702
Cdd:cd03249 183 DRAM--KGRTTIVIAHRLSTIRNADLIAVLQN-----------------------------------------------G 213
|
330 340
....*....|....*....|....*.
gi 156095386 703 YIIEQGTHDALMKNKnGIYYTMINNQ 728
Cdd:cd03249 214 QVVEQGTHDELMAQK-GVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
801-1461 |
1.63e-106 |
|
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: 355.30 E-value: 1.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 801 FKRKPKAPNNLRVVYREIFSYKKDIAIIALSIMVAGglypLFALLYAKYVGTLFDFAnlEANSNKYSLYILVIAIAM--- 877
Cdd:COG2274 134 FDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLIN----LLALATPLFTQVVIDRV--LPNQDLSTLWVLAIGLLLall 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 878 --FISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQDShaPGLLSAHInRDVH----LLKTGLVNNIVIFThFI 951
Cdd:COG2274 208 feGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRS--VGDLASRF-RDVEsireFLTGSLLTALLDLL-FV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 952 VLFLVstVMSFY-----FCPIVAAVLtgtYFIFMRVFAIRARIAANKDVEKKRVNQpgtafvynsddeifkdpSFLIqEA 1026
Cdd:COG2274 284 LIFLI--VLFFYspplaLVVLLLIPL---YVLLGLLFQPRLRRLSREESEASAKRQ-----------------SLLV-ET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1027 FYNMNTVIIYGLEDYFCTLIEKAI-DYSNKGQKRKTLINSMLWgFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMK-SL 1104
Cdd:COG2274 341 LRGIETIKALGAESRFRRRWENLLaKYLNARFKLRRLSNLLST-LSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAfNI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1105 FTFLFTGSyAGKLMSLKGDSENAKLSFERYYPLITRKslidVRDNGGIKIKNSNDIKGKIEIMDVNFRYlSRPNVPIYKD 1184
Cdd:COG2274 420 LSGRFLAP-VAQLIGLLQRFQDAKIALERLDDILDLP----PEREEGRSKLSLPRLKGDIELENVSFRY-PGDSPPVLDN 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1185 LTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegad 1264
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP---------------------------------------------- 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1265 gqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPN 1344
Cdd:COG2274 528 --------TSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPM 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1345 QYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSD 1424
Cdd:COG2274 600 GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLAD 677
|
650 660 670
....*....|....*....|....*....|....*..
gi 156095386 1425 KIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYKKYVK 1461
Cdd:COG2274 678 RIIVLDK----GRIVE-DGTHEELLA-RKGLYAELVQ 708
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
58-728 |
2.85e-92 |
|
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: 315.23 E-value: 2.85e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 58 HRKLLGVSFVCATISGG---TLPFFVSVF---GVIMKNMNLgenVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKT 131
Cdd:COG2274 154 YRRLLLQVLLASLLINLlalATPLFTQVVidrVLPNQDLST---LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLR 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 132 LKIEFLKSVFYQDGQFHDNNPGSKLTSDLdFYLEQVNAGIGTKFITIFTyASAFLGLYIWSLFK-NARLTLCITCVFPLI 210
Cdd:COG2274 231 LSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALL-DLLFVLIFLIVLFFySPPLALVVLLLIPLY 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFnlsEKLYSKYtLKANlMESLHIGMINGF 290
Cdd:COG2274 309 VLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRW---ENLLAKY-LNAR-FKLRRLSNLLST 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 291 I-----LASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVI--SILLGVLISmFMLTIILpNITEYMKSLEATNNLYEIIN 363
Cdd:COG2274 384 LsgllqQLATVALLWLGAYLVI--------DGQLTLGQLIafNILSGRFLA-PVAQLIG-LLQRFQDAKIALERLDDILD 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 364 RKPLVENNQDGKKLKDIK-KIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDV 442
Cdd:COG2274 454 LPPEREEGRSKLSLPRLKgDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 443 IINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakCAGDl 522
Cdd:COG2274 533 LIDG-IDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI-------------------------------------TLGD- 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 523 ndmiqttdsteliqvrknyETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILI 602
Cdd:COG2274 574 -------------------PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILI 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 603 LDEATSSLDNKSEYLVQKTINNLKGneNRITIIIAHRLSTIRYANTIFVLSNrengstvdvdvlgedptkdsneknekhd 682
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDK---------------------------- 684
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 156095386 683 kqekgGKnssanqkignagsyIIEQGTHDALMKnKNGIYYTMINNQ 728
Cdd:COG2274 685 -----GR--------------IVEDGTHEELLA-RKGLYAELVQQQ 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
826-1462 |
5.61e-83 |
|
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: 284.29 E-value: 5.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 826 AIIALSIMVAGGLyplfALLYAkyVGTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLR 902
Cdd:TIGR02204 23 ALVALLITAAATL----SLPYA--VRLMIDHGFSKDSSgllNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 903 LFENIMYQEISFFDQDShaPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAA-VLTGTYFIF-- 979
Cdd:TIGR02204 97 VFAHLISLSPSFFDKNR--SGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSlVLLAVPLVLlp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 980 MRVFAIRARIAAnkdvekkRVNQpgtafvynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDY----FCTLIEKAIDYSNK 1055
Cdd:TIGR02204 175 ILLFGRRVRKLS-------RESQ-----------DRIADAGSYAGETLGAIRTVQAFGHEDAersrFGGAVEKAYEAARQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1056 GQKRKTLINSMLWGFSQSAQFFInsfaYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFERYY 1135
Cdd:TIGR02204 237 RIRTRALLTAIVIVLVFGAIVGV----LWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1136 PLITRKSLIDVRDNggiKIKNSNDIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRF 1215
Cdd:TIGR02204 313 ELLQAEPDIKAPAH---PKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1216 YDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNL 1295
Cdd:TIGR02204 390 YD------------------------------------------------------PQSGRILLDGVDLRQLDPAELRAR 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1296 FSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREP 1375
Cdd:TIGR02204 416 MALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDA 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1376 KILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELLSvQDGV 1455
Cdd:TIGR02204 496 PILLLDEATSALDAESEQLVQQALETL--MKGRTTLIIAHRLATVLKADRIVVMDQ----GRIV-AQGTHAELIA-KGGL 567
|
....*..
gi 156095386 1456 YKKYVKL 1462
Cdd:TIGR02204 568 YARLARL 574
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1164-1459 |
1.71e-81 |
|
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: 267.56 E-value: 1.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:cd03251 55 -----------------------------DSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGRPGATR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdik 1403
Cdd:cd03251 106 EEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAAL---- 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1404 DK--ADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYKKY 1459
Cdd:cd03251 182 ERlmKNRTTFVIAHRLSTIENADRIVVLED----GKIVE-RGTHEELLA-QGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
57-727 |
3.51e-78 |
|
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: 270.43 E-value: 3.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 57 SHRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDIIF-SLVLIGIF--QFILSFISSFCMDVVTTKILKTLK 133
Cdd:TIGR02203 11 PYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWvPLVVIGLAvlRGICSFVSTYLLSWVSNKVVRDIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 134 IEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC 213
Cdd:TIGR02203 91 VRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSIL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 214 GVICNKKVK-INKKTSLLyNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINgfIL 292
Cdd:TIGR02203 171 MRRVSKRLRrISKEIQNS-MGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQ--LI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 293 ASYAFGFwygtriIISDLSNQQPNNDFHGGSVISILlgvlisMFMLTIILP-----NITEYMKS-LEATNNLYEIINRKP 366
Cdd:TIGR02203 248 ASLALAV------VLFIALFQAQAGSLTAGDFTAFI------TAMIALIRPlksltNVNAPMQRgLAAAESLFTLLDSPP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 367 LVennQDGKKLKD--IKKIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVII 444
Cdd:TIGR02203 316 EK---DTGTRAIEraRGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 445 nDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcaGDLnd 524
Cdd:TIGR02203 392 -DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAY-------------------------------------GRT-- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 525 miqttdsteliqvrknyETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILD 604
Cdd:TIGR02203 432 -----------------EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 605 EATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNrengstvdvdvlgedptkdsneknekhdkq 684
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTIEKADRIVVMDD------------------------------ 542
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 156095386 685 ekgGKnssanqkignagsyIIEQGTHDALMkNKNGiYYTMINN 727
Cdd:TIGR02203 543 ---GR--------------IVERGTHNELL-ARNG-LYAQLHN 566
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1162-1449 |
8.30e-77 |
|
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: 254.07 E-value: 8.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqq 1241
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENA 1321
Cdd:cd03254 55 ------------------------------PQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:cd03254 105 TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 156095386 1402 IKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELL 1449
Cdd:cd03254 185 LMK--GRTSIIIAHRLSTIKNADKILVLDD----GKIIE-EGTHDELL 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1164-1458 |
1.20e-76 |
|
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: 253.69 E-value: 1.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:cd03253 54 -----------------------------SSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRPDATD 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:cd03253 105 EEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV- 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYKK 1458
Cdd:cd03253 184 -SKGRTTIVIAHRLSTIVNADKIIVLKD----GRIVE-RGTHEELLA-KGGLYAE 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
383-724 |
3.60e-75 |
|
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: 249.46 E-value: 3.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DGHDVRDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNSIKNNIKYSlyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqTTDSTEliqvrknye 542
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYG--------------------------------------------RPGATR--------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiedSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03251 106 ----EEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAAL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 623 NNLKgnENRITIIIAHRLSTIRYANTIFVLsnrengstvdvdvlgedptkdsneknekhdkqEKGGknssanqkignags 702
Cdd:cd03251 182 ERLM--KNRTTFVIAHRLSTIENADRIVVL--------------------------------EDGK-------------- 213
|
330 340
....*....|....*....|..
gi 156095386 703 yIIEQGTHDALMKnKNGIYYTM 724
Cdd:cd03251 214 -IVERGTHEELLA-QGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1162-1456 |
6.75e-75 |
|
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: 261.68 E-value: 6.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqq 1241
Cdd:COG5265 356 GEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV----------------------- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENA 1321
Cdd:COG5265 411 -------------------------------TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:COG5265 460 SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE 539
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1402 IkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVY 1456
Cdd:COG5265 540 V--ARGRTTLVIAHRLSTIVDADEILVLEA----GRIVE-RGTHAELLA-QGGLY 586
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
100-652 |
3.91e-74 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 262.74 E-value: 3.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 100 IFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQV--NAGIGT 173
Cdd:TIGR00958 204 IFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTgeltSRLSSDTQTMSRSLslNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 174 KFITIFtyasafLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKV-KINKKT--SLLYNNNtmsIIEEALVGIRTVV 250
Cdd:TIGR00958 284 RNLVML------LGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYqLLSEELqeAVAKANQ---VAEEALSGMRTVR 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 251 SYCGENTILKKFN--LSEKL---------YSKYTLkanLMESLHIGMINGfILasyafgfWYGTRIIISdlsnqqpnNDF 319
Cdd:TIGR00958 355 SFAAEEGEASRFKeaLEETLqlnkrkalaYAGYLW---TTSVLGMLIQVL-VL-------YYGGQLVLT--------GKV 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 320 HGGSVISILL---------GVLISMFmltiilpniTEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRF 390
Cdd:TIGR00958 416 SSGNLVSFLLyqeqlgeavRVLSYVY---------SGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSF 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 391 HYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPL 470
Cdd:TIGR00958 487 SYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPLVQYDHHYLHRQVALVGQEPV 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 471 LFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrNSCrakcagdlndmiqttdsteliqvrknyetiEDSEVV 550
Cdd:TIGR00958 566 LFSGSVRENIAYGL---------------------------TDT------------------------------PDEEIM 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 551 SVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQktinNLKGNEN 630
Cdd:TIGR00958 589 AAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ----ESRSRAS 664
|
570 580
....*....|....*....|..
gi 156095386 631 RITIIIAHRLSTIRYANTIFVL 652
Cdd:TIGR00958 665 RTVLLIAHRLSTVERADQILVL 686
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
383-728 |
2.61e-72 |
|
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: 241.37 E-value: 2.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:cd03253 1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI-DGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcaGDLNdmiqttdsteliqvrknye 542
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRY-------------------------------------GRPD------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03253 102 -ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAAL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 623 NNLKgnENRITIIIAHRLSTIRYANTIFVLSNrengstvdvdvlgedptkdsneknekhdkqekgGKnssanqkignags 702
Cdd:cd03253 181 RDVS--KGRTTIVIAHRLSTIVNADKIIVLKD---------------------------------GR------------- 212
|
330 340
....*....|....*....|....*.
gi 156095386 703 yIIEQGTHDALMkNKNGIYYTMINNQ 728
Cdd:cd03253 213 -IVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
331-728 |
2.91e-72 |
|
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: 253.97 E-value: 2.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 331 VLISMFMLTIILP-NI--TEY--MK-SLEATNNLYEIINRKPLVENNQDGKKLK-DIKKIQFKNVRFHYDTRKdvEIYKD 403
Cdd:COG5265 299 VLVNAYLIQLYIPlNFlgFVYreIRqALADMERMFDLLDQPPEVADAPDAPPLVvGGGEVRFENVSFGYDPER--PILKG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI-DGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 484 lyslkDLEAlSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsEVVSVSKKVLIHDFVS 563
Cdd:COG5265 456 -----RPDA-SEE---------------------------------------------------EVEAAARAAQIHDFIE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTI 643
Cdd:COG5265 479 SLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA--RGRTTLVIAHRLSTI 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 644 RYANTIFVLsnrengstvdvdvlgedptkdsneknekhdkqEKGgknssanqkignagsYIIEQGTHDALMKnKNGIYYT 723
Cdd:COG5265 557 VDADEILVL--------------------------------EAG---------------RIVERGTHAELLA-QGGLYAQ 588
|
....*
gi 156095386 724 MINNQ 728
Cdd:COG5265 589 MWARQ 593
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
838-1460 |
7.25e-71 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 253.11 E-value: 7.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 838 LYPLFALLYAKYVGTLFD--FANLEANSNKYSLYIL-VIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISF 914
Cdd:TIGR00958 172 LSSLGEMFIPFYTGRVIDtlGGDKGPPALASAIFFMcLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 915 FDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLtgtyFIFMR-VFAIRARIAANK 993
Cdd:TIGR00958 252 FDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT----LINLPlVFLAEKVFGKRY 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 994 DVEKKRVnQPGTAfvyNSDDeifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQS 1073
Cdd:TIGR00958 326 QLLSEEL-QEAVA---KANQ--------VAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSV 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1074 AQFFINSFAYWFGSFLIRRGTIQVDDfmksLFTFLF----TGSYAGKLMSLKGDSENAKLSFERYYPLITRKSLIDvrDN 1149
Cdd:TIGR00958 394 LGMLIQVLVLYYGGQLVLTGKVSSGN----LVSFLLyqeqLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP--LT 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1150 GGIKIKNsndIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkne 1229
Cdd:TIGR00958 468 GTLAPLN---LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ------------ 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1230 qtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMS 1309
Cdd:TIGR00958 533 ------------------------------------------PTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGS 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1310 IYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1390 NSEKLIEktivDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaQGTHEELLSvQDGVYKKYV 1460
Cdd:TIGR00958 651 ECEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVL----KKGSVVE-MGTHKQLME-DQGCYKHLV 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1164-1450 |
2.06e-70 |
|
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: 247.36 E-value: 2.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4988 337 IELEDVSFSYPGGRPAL--DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP------------------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:COG4988 390 -----------------------------YSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASD 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:COG4988 441 EELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL- 519
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLS 1450
Cdd:COG4988 520 -AKGRTVILITHRLALLAQADRILVLDD----GRIVE-QGTHEELLA 560
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
825-1458 |
1.21e-68 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 243.00 E-value: 1.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLYpLFALLYAkyvgtLFD--FANleANSNKYSLYILVIAIAMF---ISETLKNYYNNVIGEKVEKTM 899
Cdd:PRK11176 29 VAGVALILNAASDTF-MLSLLKP-----LLDdgFGK--ADRSVLKWMPLVVIGLMIlrgITSFISSYCISWVSGKVVMTM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 900 KLRLFENIMYQEISFFDQDShaPGLLSAHINRD---VHLLKTGLVNNIV-----IFTHFIVLFLVSTVMS---FYFCPIV 968
Cdd:PRK11176 101 RRRLFGHMMGMPVSFFDKQS--TGTLLSRITYDseqVASSSSGALITVVregasIIGLFIMMFYYSWQLSlilIVIAPIV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 969 AavltgtyfIFMRVFAIRARiaankDVEKKRVNQPGTafVYNSDDEIFKdpsfliqeafyNMNTVIIYGLEDyfctLIEK 1048
Cdd:PRK11176 179 S--------IAIRVVSKRFR-----NISKNMQNTMGQ--VTTSAEQMLK-----------GHKEVLIFGGQE----VETK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1049 AIDY-SN--KGQKRKTLINSmlwGFSQSAQFFINSFAYWFGSFLIrrgtiQVDDFMKSL----FTFLFTGSYAgkLMS-L 1120
Cdd:PRK11176 229 RFDKvSNrmRQQGMKMVSAS---SISDPIIQLIASLALAFVLYAA-----SFPSVMDTLtagtITVVFSSMIA--LMRpL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1121 KGDSeNAKLSFER-YYPLITRKSLIDV---RDNGGIKIKNSndiKGKIEIMDVNFRYLSRpNVPIYKDLTFSCESKKTTA 1196
Cdd:PRK11176 299 KSLT-NVNAQFQRgMAACQTLFAILDLeqeKDEGKRVIERA---KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1197 IVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfkNSGK 1276
Cdd:PRK11176 374 LVGRSGSGKSTIANLLTRFYDI------------------------------------------------------DEGE 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1277 ILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENA-TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGK 1355
Cdd:PRK11176 400 ILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGV 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrt 1435
Cdd:PRK11176 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVED---- 553
|
650 660
....*....|....*....|...
gi 156095386 1436 GSFVQaQGTHEELLSvQDGVYKK 1458
Cdd:PRK11176 554 GEIVE-RGTHAELLA-QNGVYAQ 574
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
382-654 |
1.51e-67 |
|
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: 227.49 E-value: 1.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03254 2 EIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI-DGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkNY 541
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRL---------------------------------------------------------GR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 ETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03254 102 PNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEA 181
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 622 INNLkgNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03254 182 LEKL--MKGRTSIIIAHRLSTIKNADKILVLDD 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
383-654 |
1.11e-64 |
|
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: 216.87 E-value: 1.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKI 462
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG-VDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI-------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03228 97 -------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL 139
|
250 260 270
....*....|....*....|....*....|..
gi 156095386 623 NNLKGneNRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03228 140 RALAK--GKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1164-1462 |
8.49e-63 |
|
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: 225.42 E-value: 8.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4987 334 LELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP------------------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:COG4987 388 -----------------------------QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:COG4987 439 EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA- 517
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELLSvQDGVYKKYVKL 1462
Cdd:COG4987 518 -LAGRTVLLITHRLAGLERMDRILVLED----GRIV-EQGTHEELLA-QNGRYRQLYQR 569
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
349-654 |
8.88e-63 |
|
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: 225.02 E-value: 8.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 349 MKSLEATNNLYEIINR-KPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTI 427
Cdd:COG4988 302 ANGIAAAEKIFALLDApEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 428 LKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsd 507
Cdd:COG4988 380 LNLLLGFLPPYSGSILING-VDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL--------------------------- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 508 snsrnscrakcagdlndMIQTTDSTeliqvrknyetieDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQR 587
Cdd:COG4988 432 -----------------RLGRPDAS-------------DEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQR 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 588 ISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQADRILVLDD 546
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
99-662 |
3.36e-62 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 224.13 E-value: 3.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 99 IIFSLVLIG--IFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFI 176
Cdd:PRK11176 65 KWMPLVVIGlmILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 177 TIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI-YICGVICNKKVKINKKTsllynNNTM----SIIEEALVGIRTVVS 251
Cdd:PRK11176 145 TVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVsIAIRVVSKRFRNISKNM-----QNTMgqvtTSAEQMLKGHKEVLI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 252 YCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINgfILASYAFGF-WYGTRI--IISDLSnqqpnndfhGGSvISIl 328
Cdd:PRK11176 220 FGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQ--LIASLALAFvLYAASFpsVMDTLT---------AGT-ITV- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 329 lgVLISMFMLTIILPNIT----EYMKSLEATNNLYEIINRKPlvENNQDGKKLKDIK-KIQFKNVRFHYDTrKDVEIYKD 403
Cdd:PRK11176 287 --VFSSMIALMRPLKSLTnvnaQFQRGMAACQTLFAILDLEQ--EKDEGKRVIERAKgDIEFRNVTFTYPG-KEVPALRN 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 484 ---LYSLKDLEalseesnedgfssqsdsnsrNSCRAKCAgdlndMiqttdsteliqvrknyetiedsevvsvskkvlihD 560
Cdd:PRK11176 441 rteQYSREQIE--------------------EAARMAYA-----M----------------------------------D 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRL 640
Cdd:PRK11176 462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRL 539
|
570 580
....*....|....*....|..
gi 156095386 641 STIRYANTIFVLsnrENGSTVD 662
Cdd:PRK11176 540 STIEKADEILVV---EDGEIVE 558
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
147-662 |
5.83e-62 |
|
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: 223.04 E-value: 5.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 147 FHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKK 226
Cdd:TIGR02204 108 FFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 227 TSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLS-EKLYsKYTLKANLMESLHIGMINGFILASYAFGFWYGTRI 305
Cdd:TIGR02204 188 ESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAvEKAY-EAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHD 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 306 IISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRKPLVENNQDGKKL--KDIKKI 383
Cdd:TIGR02204 267 VIA--------GKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLpvPLRGEI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 384 QFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIG 463
Cdd:TIGR02204 339 EFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILL-DGVDLRQLDPAELRARMA 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 464 VVSQDPLLFSNSIKNNIKYslyslkdlealseesnedGFSSQSDSNSRNSCRAKCAgdlndmiqttdsteliqvrknyet 543
Cdd:TIGR02204 418 LVPQDPVLFAASVMENIRY------------------GRPDATDEEVEAAARAAHA------------------------ 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 544 iedsevvsvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
Cdd:TIGR02204 456 ---------------HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALE 520
|
490 500 510
....*....|....*....|....*....|....*....
gi 156095386 624 NLKgnENRITIIIAHRLSTIRYANTIFVLsnrENGSTVD 662
Cdd:TIGR02204 521 TLM--KGRTTLIIAHRLATVLKADRIVVM---DQGRIVA 554
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
825-1144 |
1.38e-61 |
|
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: 213.85 E-value: 1.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLYPLFALLYAKYVGTLF--DFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLR 902
Cdd:cd18578 11 LLLGLIGAIIAGAVFPVFAILFSKLISVFSlpDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 903 LFENIMYQEISFFDQDSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGTYFIFMRV 982
Cdd:cd18578 91 AFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 983 FAIRARIAANKDVEKKRVNQPGTAFVYnsddeifkdpsfliqEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTL 1062
Cdd:cd18578 171 GYLRMRLLSGFEEKNKKAYEESSKIAS---------------EAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1063 INSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFERYYPLITRKS 1142
Cdd:cd18578 236 ISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
|
..
gi 156095386 1143 LI 1144
Cdd:cd18578 316 EI 317
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1164-1431 |
2.06e-61 |
|
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: 207.24 E-value: 2.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIkfgkenatr 1323
Cdd:cd03228 55 -----------------------------TSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI--------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 edvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03228 97 ---------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALA 143
|
250 260
....*....|....*....|....*...
gi 156095386 1404 DkaDKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03228 144 K--GKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
815-1456 |
8.97e-61 |
|
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: 219.59 E-value: 8.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 815 YREIFSYKKDIAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEANSNK---YSLYILVIAIAMFISETLKNYYNNVI 891
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVlwwVPLVVIGLAVLRGICSFVSTYLLSWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 892 GEKVEKTMKLRLFENIMYQEISFFDQDSHAPGLL--------SAHINRDVhlLKTGLVNNIVIFTHFIVLFLvstvMSFY 963
Cdd:TIGR02203 82 SNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSritfdseqVASAATDA--FIVLVRETLTVIGLFIVLLY----YSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 964 FCPIVAAVLTGTYFIfMRVFAIRARiaankDVEKKRVNQPGTAfvynsddeifkdpSFLIQEAFYNMNTVIIYGLEDY-- 1041
Cdd:TIGR02203 156 LTLIVVVMLPVLSIL-MRRVSKRLR-----RISKEIQNSMGQV-------------TTVAEETLQGYRVVKLFGGQAYet 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1042 --FctlieKAIDYSNKG-QKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLM 1118
Cdd:TIGR02203 217 rrF-----DAVSNRNRRlAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1119 SLKGDSENAKLSFERYYPLITRKsliDVRDNGGIKIKNsndIKGKIEIMDVNFRYLSRpNVPIYKDLTFSCESKKTTAIV 1198
Cdd:TIGR02203 292 NVNAPMQRGLAAAESLFTLLDSP---PEKDTGTRAIER---ARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1199 GETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKNSGKIL 1278
Cdd:TIGR02203 365 GRSGSGKSTLVNLIPRFYE------------------------------------------------------PDSGQIL 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1279 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK-ENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSL 1357
Cdd:TIGR02203 391 LDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLL 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1358 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGS 1437
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDD----GR 544
|
650
....*....|....*....
gi 156095386 1438 FVQaQGTHEELLSvQDGVY 1456
Cdd:TIGR02203 545 IVE-RGTHNELLA-RNGLY 561
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1145-1449 |
2.01e-59 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 215.98 E-value: 2.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1145 DVRDNGGIKikNSNDIKGKIEIMDVNFRYL-SRPNVpiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKndhh 1223
Cdd:PRK13657 318 DVRDPPGAI--DLGRVKGAVEFDDVSFSYDnSRQGV---EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ---- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1224 ivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEP 1303
Cdd:PRK13657 389 --------------------------------------------------SGRILIDGTDIRTVTRASLRRNIAVVFQDA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1304 MLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEA 1383
Cdd:PRK13657 419 GLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1384 TSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAqGTHEELL 1449
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDN----GRVVES-GSFDELV 557
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
62-358 |
2.49e-59 |
|
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: 206.56 E-value: 2.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 62 LGVSFVCATISGGTLPFFVSVFGVIMKNMN-----------LGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILK 130
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgesspdeFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 131 TLKIEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI 210
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGF 290
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 291 ILASYAFGFWYGTRIIISDLSNqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNL 358
Cdd:cd18577 241 IFAMYALAFWYGSRLVRDGEIS--------PGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1159-1428 |
5.78e-59 |
|
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: 202.70 E-value: 5.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1159 DIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneqtgesskeQ 1238
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFY---------------------Q 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1239 MQQGdeeqnvgmknanefssskegadgqsstlfknsgKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK 1318
Cdd:cd03248 66 PQGG---------------------------------QVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:cd03248 113 QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQA 192
|
250 260 270
....*....|....*....|....*....|
gi 156095386 1399 IVDikDKADKTIITIAHRIASIKRSDKIVV 1428
Cdd:cd03248 193 LYD--WPERRTVLVIAHRLSTVERADQILV 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
382-652 |
1.13e-57 |
|
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: 198.85 E-value: 1.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL-DGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGL--------------------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 ETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03248 113 QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQA 192
|
250 260 270
....*....|....*....|....*....|.
gi 156095386 622 INNlkGNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:cd03248 193 LYD--WPERRTVLVIAHRLSTVERADQILVL 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
358-662 |
2.87e-55 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 203.65 E-value: 2.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 358 LYEIINRKPLVENNQDGKKLKDIK-KIQFKNVRFHYD-TRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
Cdd:PRK13657 309 FFEVEDAVPDVRDPPGAIDLGRVKgAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 436 DPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdlealseesnedgfssqsdsnsrnscr 515
Cdd:PRK13657 386 DPQSGRILI-DGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR---------------------------------- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 516 akcagdlndmIQTTDSTeliqvrknyetieDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAII 595
Cdd:PRK13657 431 ----------VGRPDAT-------------DEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL 487
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 596 RNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrENGSTVD 662
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRNADRILVF---DNGRVVE 549
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
383-728 |
7.48e-55 |
|
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: 191.16 E-value: 7.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYdtRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSNSIKNNIkyslySLKDlEALSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNI-----ALAD-PGMSME--------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etiedsEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03252 107 ------RVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 622 INNLkgNENRITIIIAHRLSTIRYANTIFVLsnrengstvdvdvlgedptkdsneknekhdkqEKGGknssanqkignag 701
Cdd:cd03252 181 MHDI--CAGRTVIIIAHRLSTVKNADRIIVM--------------------------------EKGR------------- 213
|
330 340
....*....|....*....|....*..
gi 156095386 702 syIIEQGTHDALMKnKNGIYYTMINNQ 728
Cdd:cd03252 214 --IVEQGSHDELLA-ENGLYAYLYQLQ 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1162-1431 |
7.39e-54 |
|
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: 187.70 E-value: 7.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmq 1240
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKe 1319
Cdd:cd03244 57 --------------------------------SSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDpFGE- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 nATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTi 1399
Cdd:cd03244 104 -YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT- 181
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 1400 vdIKDK-ADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03244 182 --IREAfKDCTVLTIAHRLDTIIDSDRILVLDK 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1164-1462 |
1.45e-53 |
|
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: 187.69 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstlFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENAT 1322
Cdd:cd03252 53 ----------------------------VPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:cd03252 105 MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1403 kdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYKKYVKL 1462
Cdd:cd03252 185 --CAGRTVIIIAHRLSTVKNADRIIVMEK----GRIVE-QGSHDELLA-ENGLYAYLYQL 236
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
815-1458 |
1.36e-52 |
|
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: 198.04 E-value: 1.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 815 YREIFSykkDIAIIALSIMVAGGLYPLF------ALLYAKYVGTLfdfanleansNKYSLYILVIAIAMFISETLKNYYN 888
Cdd:TIGR01846 137 YRKQFR---EVLLISLALQLFALVTPLLfqvvidKVLVHRGLSTL----------SVLALAMLAVAIFEPALGGLRTYLF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 889 NVIGEKVEKTMKLRLFENIMYQEISFFDqdSHAPGLLSAHInRDVHLLK---TGLVNNIVIFTHFIVLFLvsTVMSFYFC 965
Cdd:TIGR01846 204 AHLTSRIDVELGARLYRHLLGLPLGYFE--SRRVGDTVARV-RELEQIRnflTGSALTVVLDLLFVVVFL--AVMFFYSP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 966 PIVAAVLTGTYFIFMRVFAIRARIaankdveKKRVNQpgtAFVYNSDDEifkdpSFLIqEAFYNMNTVIIYGLEDYFCTL 1045
Cdd:TIGR01846 279 TLTGVVIGSLVCYALLSVFVGPIL-------RKRVED---KFERSAAAT-----SFLV-ESVTGIETIKATATEPQFQNR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1046 IEKAI-DYSNKGQKrktLINSMLWGfSQSAQFfIN--SFA--YWFGSFLIRRGTIQVDdfmkSLFTF-LFTGSYAG---K 1116
Cdd:TIGR01846 343 WDRQLaAYVAASFR---VTNLGNIA-GQAIEL-IQklTFAilLWFGAHLVIGGALSPG----QLVAFnMLAGRVTQpvlR 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1117 LMSLKGDSENAKLSFERyyplitrksLIDV----RDNGGIKIKNSNDIKGKIEIMDVNFRYlsRPNVP-IYKDLTFSCES 1191
Cdd:TIGR01846 414 LAQLWQDFQQTGIALER---------LGDIlnspTEPRSAGLAALPELRGAITFENIRFRY--APDSPeVLSNLNLDIKP 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1192 KKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlf 1271
Cdd:TIGR01846 483 GEFIGIVGPSGSGKSTLTKLLQRLYTPQH--------------------------------------------------- 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1272 knsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVG 1351
Cdd:TIGR01846 512 ---GQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVG 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1352 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:TIGR01846 589 EKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREI--CRGRTVIIIAHRLSTVRACDRIIVLEK 666
|
650 660
....*....|....*....|....*..
gi 156095386 1432 pdrtGSFVQaQGTHEELLSvQDGVYKK 1458
Cdd:TIGR01846 667 ----GQIAE-SGRHEELLA-LQGLYAR 687
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
321-724 |
1.34e-51 |
|
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: 192.29 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 321 GGSVISILL------------GVLISMFMLTII--------LPN-ITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKD 379
Cdd:COG4987 251 GLAVVAVLWlaaplvaagalsGPLLALLVLAALalfealapLPAaAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 380 IKKIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWR 459
Cdd:COG4987 331 GPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG-VDLRDLDEDDLR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQDPLLFSNSIKNNIKyslysLKDLEAlseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrk 539
Cdd:COG4987 409 RRIAVVPQRPHLFDTTLRENLR-----LARPDA----------------------------------------------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyetiEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG4987 437 -----TDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 620 KTInnLKGNENRITIIIAHRLSTIRYANTIFVLsnrENGStvdvdvlgedptkdsneknekhdkqekggknssanqkign 699
Cdd:COG4987 512 ADL--LEALAGRTVLLITHRLAGLERMDRILVL---EDGR---------------------------------------- 546
|
410 420
....*....|....*....|....*
gi 156095386 700 agsyIIEQGTHDALMKnKNGIYYTM 724
Cdd:COG4987 547 ----IVEQGTHEELLA-QNGRYRQL 566
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
153-652 |
1.53e-50 |
|
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: 191.88 E-value: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 153 GSKLTSDLDFYLEQVNAGIgtkfitIFTYASAFLGLYIWSLfknarltlciTCVFPLIYICGVICNKKVKINKKTSllyn 232
Cdd:TIGR01846 254 GSALTVVLDLLFVVVFLAV------MFFYSPTLTGVVIGSL----------VCYALLSVFVGPILRKRVEDKFERS---- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 233 NNTMSIIEEALVGIRTVVSYCGENTILKKFN--LSEKLYSKYTL-KANLMESLHIGMINGFilaSYAFGFWYGTRIIIsd 309
Cdd:TIGR01846 314 AAATSFLVESVTGIETIKATATEPQFQNRWDrqLAAYVAASFRVtNLGNIAGQAIELIQKL---TFAILLWFGAHLVI-- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 310 lsnqqpnndfhGGSvISILLGVLISMFMLTIILPNI------TEYMKSLEATNNLYEIINRKplVENNQDGK-KLKDIK- 381
Cdd:TIGR01846 389 -----------GGA-LSPGQLVAFNMLAGRVTQPVLrlaqlwQDFQQTGIALERLGDILNSP--TEPRSAGLaALPELRg 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:TIGR01846 455 AITFENIRFRYA-PDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLV-DGVDLAIADPAWLRRQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfsSQSDSNsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:TIGR01846 533 MGVVLQENVLFSRSIRDNI-----------------------ALCNPG-------------------------------- 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:TIGR01846 558 --APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRN 635
|
490 500 510
....*....|....*....|....*....|.
gi 156095386 622 INNLkgNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:TIGR01846 636 MREI--CRGRTVIIIAHRLSTVRACDRIIVL 664
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
62-309 |
1.45e-48 |
|
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: 174.75 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 62 LGVSFVCATISGGTLPFFVSVFGVIMKNM---NLGENVNDIIFSLVLI--GIFQFILSFISSFCMDVVTTKILKTLKIEF 136
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLlpdGDPETQALNVYSLALLllGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 137 LKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVI 216
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 217 CNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYA 296
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250
....*....|...
gi 156095386 297 FGFWYGTRIIISD 309
Cdd:pfam00664 241 LALWFGAYLVISG 253
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1162-1431 |
3.87e-48 |
|
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: 171.23 E-value: 3.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsrPNVPI--YKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqm 1239
Cdd:cd03245 1 GRIEFRNVSFSY---PNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK---------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 qqgdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1319
Cdd:cd03245 56 --------------------------------PTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGAP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE-KLIEKt 1398
Cdd:cd03245 104 LADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEeRLKER- 182
|
250 260 270
....*....|....*....|....*....|....
gi 156095386 1399 ivdIKD-KADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03245 183 ---LRQlLGDKTLIIITHRPSLLDLVDRIIVMDS 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1038-1458 |
1.34e-44 |
|
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: 173.77 E-value: 1.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1038 LEDYFCTLIEKAIDYSnKGQKRKTLINSMLwgfsqsaQFFINSFAYWFGSFLIRRGTIQVDdfmkSLFTFLFTGSY---- 1113
Cdd:TIGR01193 360 IDSEFGDYLNKSFKYQ-KADQGQQAIKAVT-------KLILNVVILWTGAYLVMRGKLTLG----QLITFNALLSYfltp 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1114 AGKLMSLKGDSENAKLSFERyyplITRKSLIDVRDNGGIKIKNSNDIKGKIEIMDVNFRYlsRPNVPIYKDLTFSCESKK 1193
Cdd:TIGR01193 428 LENIINLQPKLQAARVANNR----LNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSY--GYGSNILSDISLTIKMNS 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1194 TTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKN 1273
Cdd:TIGR01193 502 KTTIVGMSGSGKSTLAKLLVGFFQ------------------------------------------------------AR 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KENATREDVKRACKFAAIDEFIESLPNQYDTNVGP 1352
Cdd:TIGR01193 528 SGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSE 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkaDKTIITIAHRIASIKRSDKIVVFNNp 1432
Cdd:TIGR01193 608 EGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVAKQSDKIIVLDH- 683
|
410 420
....*....|....*....|....*.
gi 156095386 1433 drtGSFVQaQGTHEELLSvQDGVYKK 1458
Cdd:TIGR01193 684 ---GKIIE-QGSHDELLD-RNGFYAS 704
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
825-1110 |
4.91e-44 |
|
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: 161.66 E-value: 4.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEAN-SNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRL 903
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 904 FENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGTYFIFMRVF 983
Cdd:pfam00664 81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 984 AIRARIAAN-KDVEKKRVNQPGTafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTL 1062
Cdd:pfam00664 159 AVFAKILRKlSRKEQKAVAKASS----------------VAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 156095386 1063 INSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDF--MKSLFTFLFT 1110
Cdd:pfam00664 223 ANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLvaFLSLFAQLFG 272
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
58-366 |
9.30e-44 |
|
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: 162.24 E-value: 9.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 58 HRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLG------ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKT 131
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPdddelrSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 132 LKIEFLKSVFYQDGQFHD---NNPGSkLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFP 208
Cdd:cd18578 87 LRKLAFRAILRQDIAWFDdpeNSTGA-LTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 209 LIYICGVIcnkKVKINKKTSLLYNN---NTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIG 285
Cdd:cd18578 166 LLLLAGYL---RMRLLSGFEEKNKKayeESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 286 MINGFILASYAFGFWYGTRIIISDLSNQQpnndfhggSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRK 365
Cdd:cd18578 243 LSQSLTFFAYALAFWYGGRLVANGEYTFE--------QFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRK 314
|
.
gi 156095386 366 P 366
Cdd:cd18578 315 P 315
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
349-652 |
1.10e-43 |
|
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: 167.85 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 349 MKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 429 KLIERLYDPTEGDVIINDShNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKyslysLKDLEAlseesnedgfssqsds 508
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGV-PLADADADSWRDQIAWVPQHPFLFAGTIAENIR-----LARPDA---------------- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 509 nsrnscrakcagdlndmiqttdsteliqvrknyetiEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRI 588
Cdd:TIGR02857 424 ------------------------------------SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRL 467
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 589 SIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
382-654 |
3.79e-43 |
|
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: 156.88 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRS 460
Cdd:cd03244 2 DIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI-DGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesneDGFSSQSDSnsrnscrakcagdlndmiqttdsteliqvrkn 540
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL-------------------DPFGEYSDE-------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 yetiedsEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03244 108 -------ELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQK 180
|
250 260 270
....*....|....*....|....*....|....*
gi 156095386 621 TI-NNLKgneNRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03244 181 TIrEAFK---DCTVLTIAHRLDTIIDSDRILVLDK 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1164-1428 |
4.69e-43 |
|
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: 165.92 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-------------------------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:TIGR02857 374 ----------------------------PTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASD 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:TIGR02857 426 AEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA 505
|
250 260
....*....|....*....|....*
gi 156095386 1404 DkaDKTIITIAHRIASIKRSDKIVV 1428
Cdd:TIGR02857 506 Q--GRTVLLVTHRLALAALADRIVV 528
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
382-652 |
9.30e-43 |
|
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: 155.83 E-value: 9.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL-DGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSNSIKNNIkyslySLKDLEAlseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNI-----TLGAPLA------------------------------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etiEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03245 106 ---DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER 182
|
250 260 270
....*....|....*....|....*....|.
gi 156095386 622 INNLKGneNRITIIIAHRLSTIRYANTIFVL 652
Cdd:cd03245 183 LRQLLG--DKTLIIITHRPSLLDLVDRIIVM 211
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
382-661 |
5.44e-41 |
|
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: 162.81 E-value: 5.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:TIGR03796 477 YVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILF-DGIPREEIPREVLANS 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSNSIKNNIkyslySLKDlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:TIGR03796 555 VAMVDQDIFLFEGTVRDNL-----TLWD---------------------------------------------------- 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 ETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVqkt 621
Cdd:TIGR03796 578 PTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII--- 654
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156095386 622 INNLKgneNR--ITIIIAHRLSTIRYANTIFVLsnrENGSTV 661
Cdd:TIGR03796 655 DDNLR---RRgcTCIIVAHRLSTIRDCDEIIVL---ERGKVV 690
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1130-1462 |
7.04e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 160.38 E-value: 7.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1130 SFERYYPLITRKSLIDVRDNGGIKIKnsndiKGKIEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVM 1209
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD-----QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1210 SLLMRFYDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNL 1289
Cdd:PRK11160 384 QLLTRAWD------------------------------------------------------PQQGEILLNGQPIADYSE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1290 KDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESlPNQYDTNVGPYGKSLSGGQKQRIAIAR 1369
Cdd:PRK11160 410 AALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIAR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1370 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELL 1449
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLTGLEQFDRICVMDN----GQII-EQGTHQELL 561
|
330
....*....|...
gi 156095386 1450 SVQDGVYKKYVKL 1462
Cdd:PRK11160 562 AQQGRYYQLKQRL 574
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1083-1461 |
9.34e-41 |
|
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: 161.66 E-value: 9.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1083 YWFGSFLIRRGTIQVDDFMKslFTFLFtGSYAGKLMSLKG---DSENAKLSFERYYPLItrKSLIDVRDNGgikiKNSND 1159
Cdd:TIGR03797 377 FAAAISLLGGAGLSLGSFLA--FNTAF-GSFSGAVTQLSNtliSILAVIPLWERAKPIL--EALPEVDEAK----TDPGK 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1160 IKGKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknEQTGesskeq 1238
Cdd:TIGR03797 448 LSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGF-------------ETPE------ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1239 mqqgdeeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGK 1318
Cdd:TIGR03797 507 -----------------------------------SGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GG 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:TIGR03797 551 APLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSES 630
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1399 IvdikDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSVqDGVYKKYVK 1461
Cdd:TIGR03797 631 L----ERLKVTRIVIAHRLSTIRNADRIYVLDA----GRVVQ-QGTYDELMAR-EGLFAQLAR 683
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1185-1457 |
9.60e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 160.01 E-value: 9.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1185 LTFSCESKKTTAIVGETGSGKSTVMSLLMRF--Ydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskeg 1262
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---------------------------------------------- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESL 1342
Cdd:PRK11174 403 -----------QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLL 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKR 1422
Cdd:PRK11174 472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLEDLAQ 549
|
250 260 270
....*....|....*....|....*....|....*
gi 156095386 1423 SDKIVVFNNpdrtGSFVQaQGTHEElLSVQDGVYK 1457
Cdd:PRK11174 550 WDQIWVMQD----GQIVQ-QGDYAE-LSQAGGLFA 578
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1161-1450 |
2.13e-40 |
|
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: 158.76 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1161 KGKIEIMDVNFRYlsrP--NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeq 1238
Cdd:COG4618 328 KGRLSVENLTVVP---PgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL-------------------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1239 mqqgdeeqnVGMknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI-KFG 1317
Cdd:COG4618 379 ---------VGV-------------------WPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 keNATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:COG4618 431 --DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA 508
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1398 TIVDIKdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:COG4618 509 AIRALK-ARGATVVVITHRPSLLAAVDKLLVLRD----GR-VQAFGPRDEVLA 555
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1166-1457 |
4.74e-40 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 157.95 E-value: 4.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1166 IMDVNFRYLSRP--NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK10789 313 ELDVNIRQFTYPqtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV------------------------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:PRK10789 368 -----------------------------SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:PRK10789 419 QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG 498
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1404 DKadKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYK 1457
Cdd:PRK10789 499 EG--RTVIISAHRLSALTEASEILVMQH----GHIAQ-RGNHDQLAQ-QSGWYR 544
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
321-652 |
1.14e-39 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 156.80 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 321 GGS--VI--SILLGVLIS--MFMLTIILP--------NITEymKSLEATNNLYEIINRKPLVEnnqDGKK-LKDIKKIQF 385
Cdd:PRK10789 241 GGSwmVVngSLTLGQLTSfvMYLGLMIWPmlalawmfNIVE--RGSAAYSRIRAMLAEAPVVK---DGSEpVPEGRGELD 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 386 KNVR-FHYDTrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGV 464
Cdd:PRK10789 316 VNIRqFTYPQ-TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD-IPLTKLQLDSWRSRLAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 465 VSQDPLLFSNSIKNNIkyslyslkdleALSEesnedgfssqsdsnsrnscrakcagdlndmiqtTDSTEliqvrknyETI 544
Cdd:PRK10789 394 VSQTPFLFSDTVANNI-----------ALGR---------------------------------PDATQ--------QEI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 545 EDsevvsVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYlvqKTINN 624
Cdd:PRK10789 422 EH-----VARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH---QILHN 493
|
330 340
....*....|....*....|....*....
gi 156095386 625 LKG-NENRITIIIAHRLSTIRYANTIFVL 652
Cdd:PRK10789 494 LRQwGEGRTVIISAHRLSALTEASEILVM 522
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1162-1459 |
1.78e-38 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 153.34 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqq 1241
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL----------------------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKeNA 1321
Cdd:PRK10790 394 -------------------------------TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PRK10790 442 SEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1402 IKDKAdkTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSVQDGVYKKY 1459
Cdd:PRK10790 522 VREHT--TLVVIAHRLSTIVEADTILVLHR----GQAVE-QGTHQQLLAAQGRYWQMY 572
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
383-652 |
1.80e-38 |
|
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: 143.80 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWR 459
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQDPllfsnsiknnikyslyslkdlealseesnedgFSSqsdsnsrnscrakcagdLN------DMIqttdsTE 533
Cdd:cd03257 82 KEIQMVFQDP--------------------------------MSS-----------------LNprmtigEQI-----AE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 534 LIQVRKNYETIEDSEVVSVSKKVLIHDfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03257 108 PLRIHGKLSKKEARKEAVLLLLVGVGL-PEEVLNRY-------PHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 156095386 614 SEYLVQKTINNLKgNENRITII-IAHRLSTIRY-ANTIFVL 652
Cdd:cd03257 180 VQAQILDLLKKLQ-EELGLTLLfITHDLGVVAKiADRVAVM 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1164-1431 |
4.90e-38 |
|
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: 142.70 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG---------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlFKNSGKILLDGVDIC--DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG---- 1317
Cdd:cd03260 56 ---------------------------APDEGEVLLDGKDIYdlDVDVLELRRRVGMVFQKPNPFPGSIYDNVAYGlrlh 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 ---KENATREDVKRACKFAAI-DEFIESLpnqydtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:cd03260 109 gikLKEELDERVEEALRKAALwDEVKDRL----------HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTA 178
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 1394 LIEKTIVDIKDkaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03260 179 KIEELIAELKK--EYTIVIVTHNMQQAARvADRTAFLLN 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
401-608 |
4.67e-37 |
|
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: 137.01 E-value: 4.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSN-SIKNN 479
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG-QDLTDDERKSLRKEIGYVFQDPQLFPRlTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 IKYSLYslkdLEALSeesnedgfssqsdsnsrnscrakcagdlndmiQTTDSTELIQVRKNYetiedsevvsvskkvlih 559
Cdd:pfam00005 80 LRLGLL----LKGLS--------------------------------KREKDARAEEALEKL------------------ 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 156095386 560 dfvsALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
Cdd:pfam00005 106 ----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1162-1428 |
3.87e-36 |
|
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: 136.39 E-value: 3.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfkneqtgesskeqmq 1240
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEE-------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI-KFGKE 1319
Cdd:cd03369 63 ----------------------------------GKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEY 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 naTREDVKRACKfaaidefieslpnqydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:cd03369 109 --SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
250 260
....*....|....*....|....*....
gi 156095386 1400 VdiKDKADKTIITIAHRIASIKRSDKIVV 1428
Cdd:cd03369 169 R--EEFTNSTILTIAHRLRTIIDYDKILV 195
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1164-1450 |
4.05e-36 |
|
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: 137.08 E-value: 4.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1122 1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENA 1321
Cdd:COG1122 55 ------------------------------SGEVLVDGKDITKKNLRELRRKVGLVFQNPddQLFAPTVEEDVAFGPENL 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 --TREDVKRACKfAAIDEF-IESLPNQYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG1122 105 glPREEIRERVE-EALELVgLEHLADRP-----PH--ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLEL 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1399 IVDIKdKADKTIITIAHRIASI-KRSDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:COG1122 177 LKRLN-KEGKTVIIVTHDLDLVaELADRVIVLDD----GR-IVADGTPREVFS 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
383-654 |
4.17e-36 |
|
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: 137.08 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKI 462
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG-KDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPL--LFSNSIKNNIKYSLYSLKdleaLSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkn 540
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFGPENLG----LPRE-------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 yetiedsEVVSVSKKVLihDFV--SALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:COG1122 110 -------EIRERVEEAL--ELVglEHLADR-------PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRREL 173
|
250 260 270
....*....|....*....|....*....|....*...
gi 156095386 619 QKTINNLkgNENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:COG1122 174 LELLKRL--NKEGKTVIIVtHDLDLVaELADRVIVLDD 209
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
206-1460 |
4.86e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 149.74 E-value: 4.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 206 VFPLIYICGVICNKKVKINKKtSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIG 285
Cdd:PLN03232 450 LFLLIPLQTLIVRKMRKLTKE-GLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSF 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 286 MINGFILASYAFGFwyGTRIIIS-DLSnqqPNNDFHGGSVISILLGVLismFMLTIILPNITEYMKSLEATNNLY----E 360
Cdd:PLN03232 529 ILNSIPVVVTLVSF--GVFVLLGgDLT---PARAFTSLSLFAVLRSPL---NMLPNLLSQVVNANVSLQRIEELLlseeR 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 361 IINRKPLVEnnqdgkklKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILK-LIERLYDPTE 439
Cdd:PLN03232 601 ILAQNPPLQ--------PGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAET 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 440 GDVIIndshnlkdvnlkwwRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealseesnedgfssqSDSNSRNSCRAkca 519
Cdd:PLN03232 673 SSVVI--------------RGSVAYVPQVSWIFNATVRENILFG----------------------SDFESERYWRA--- 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 520 gdlndmiqtTDSTeliqvrknyetiedsevvsvskkVLIHDfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
Cdd:PLN03232 714 ---------IDVT-----------------------ALQHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 600 ILILDEATSSLDNKSEYLVQKTI--NNLKGnenRITIIIAHRLSTIRYANTIFVLSN---RENGSTVDVDVLGEdPTKDS 674
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFDSCmkDELKG---KTRVLVTNQLHFLPLMDRIILVSEgmiKEEGTFAELSKSGS-LFKKL 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 675 NEKNEKHDKQEKGGKNSSANQKIGNAGSYIIEQGTHDALMKNKNGiyytminnqkvssksssnndndkdsdmKSSIYKDS 754
Cdd:PLN03232 837 MENAGKMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKRG---------------------------RSVLVKQE 889
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 755 ERgydpdeangnaknesasakksekmsdakasntnAGGRLAFlrNLFKRKPKAPNNLRVVYREIFSYKkdiaiialsimv 834
Cdd:PLN03232 890 ER---------------------------------ETGIISW--NVLMRYNKAVGGLWVVMILLVCYL------------ 922
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 835 aggLYPLFALLYAKYVGTLFDFANLEANSNKYslYILVIAIAMF--ISETLKNYYNnVIGEKVEKTMKLR--LFENIMYQ 910
Cdd:PLN03232 923 ---TTEVLRVSSSTWLSIWTDQSTPKSYSPGF--YIVVYALLGFgqVAVTFTNSFW-LISSSLHAAKRLHdaMLNSILRA 996
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 911 EISFFDqdSHAPGLLSAHINRDVHLLKTGLVNNIVIFTH--------FIVLFLVSTVMSFYFCPIVAaVLTGTYFIFMrv 982
Cdd:PLN03232 997 PMLFFH--TNPTGRVINRFSKDIGDIDRNVANLMNMFMNqlwqllstFALIGTVSTISLWAIMPLLI-LFYAAYLYYQ-- 1071
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 983 fairariaaNKDVEKKRVnqpgtafvynsdDEIFKDPSF-LIQEAFYNMNTVIIYGLEDYFCTLIEKAID---------- 1051
Cdd:PLN03232 1072 ---------STSREVRRL------------DSVTRSPIYaQFGEALNGLSSIRAYKAYDRMAKINGKSMDnnirftlant 1130
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1052 YSNK--GQKRKTLINSMLWgfsqsaqfFINSFAywfgsfLIRRGTIQVDDFMKSLFTFLFtgSYAGKLMSL-------KG 1122
Cdd:PLN03232 1131 SSNRwlTIRLETLGGVMIW--------LTATFA------VLRNGNAENQAGFASTMGLLL--SYTLNITTLlsgvlrqAS 1194
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1123 DSENAKLSFERYyplitrKSLIDVRDNGGIKIKNSNDI-----KGKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTA 1196
Cdd:PLN03232 1195 KAENSLNSVERV------GNYIDLPSEATAIIENNRPVsgwpsRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVG 1266
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1197 IVGETGSGKSTVMSLLMRFYDLKNdhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfknsGK 1276
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEK------------------------------------------------------GR 1292
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1277 ILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKENATreDVKRACKFAAIDEFIESLPNQYDTNVGPYGK 1355
Cdd:PLN03232 1293 IMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDpFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGE 1370
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikDKADKTIITIAHRIASIKRSDKIVVFNNPDrt 1435
Cdd:PLN03232 1371 NFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDCDKILVLSSGQ-- 1446
|
1290 1300
....*....|....*....|....*
gi 156095386 1436 gsfVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PLN03232 1447 ---VLEYDSPQELLSRDTSAFFRMV 1468
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
383-656 |
1.12e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.94 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNLKDVNLKWWRSKI 462
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK-PLSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNSIKNNIKYSlYSLKDLealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvRKNYE 542
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFP-FQLRER-----------------------------------------------KFDRE 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 TIEDsevvsvskkvLIHDFvsALPDKYetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:COG4619 109 RALE----------LLERL--GLPPDI---LDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELL 173
|
250 260 270
....*....|....*....|....*....|....*
gi 156095386 623 NNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRE 656
Cdd:COG4619 174 REYLAEEGRAVLWVSHDPEQIeRVADRVLTLEAGR 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
383-663 |
1.48e-35 |
|
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: 143.12 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRK--DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWW 458
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 459 RSKIGVVSQDPL--LF-SNSIKNNIKYSLYSLKDLealseesnedgfssqsdsnSRNSCRAKCAgdlndmiqttdstELI 535
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIAEPLRLHGLL-------------------SRAERRERVA-------------ELL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 536 -QVRknyetiedsevvsvskkvLIHDFVSALPdkYEtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDnks 614
Cdd:COG1123 389 eRVG------------------LPPDLADRYP--HE---------LSGGQRQRVAIARALALEPKLLILDEPTSALD--- 436
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 615 eYLVQKTI-NNLKG--NENRITII-IAHRLSTIRY-ANTIFVLSN-R--ENGSTVDV 663
Cdd:COG1123 437 -VSVQAQIlNLLRDlqRELGLTYLfISHDLAVVRYiADRVAVMYDgRivEDGPTEEV 492
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
100-727 |
4.21e-35 |
|
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: 144.50 E-value: 4.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 100 IFSLVLIG--IFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAgIGTKFIT 177
Cdd:TIGR01193 197 IISIGLIIayIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDA-LASTILS 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 178 IFTYASAFLGLYIWSLFKNARLTLCITCVFPlIYICGVICNKKV--KINKKTslLYNNNTM-SIIEEALVGIRTVVSYCG 254
Cdd:TIGR01193 276 LFLDMWILVIVGLFLVRQNMLLFLLSLLSIP-VYAVIIILFKRTfnKLNHDA--MQANAVLnSSIIEDLNGIETIKSLTS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 255 ENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISilLGVLIS 334
Cdd:TIGR01193 353 EAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMR--------GKLTLGQLIT--FNALLS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 335 MFmlTIILPNITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKK-----IQFKNVRFHYDTRKdvEIYKDLNFTLT 409
Cdd:TIGR01193 423 YF--LTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNnlngdIVINDVSYSYGYGS--NILSDISLTIK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 410 EGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkd 489
Cdd:TIGR01193 499 MNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN-GFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL--------- 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 490 lealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteLIQVRKNYETIEDSEVVSVSKkvlIHDFVSALPDKY 569
Cdd:TIGR01193 569 --------------------------------------------LLGAKENVSQDEIWAACEIAE---IKDDIENMPLGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKGNENRITIIIAHRLSTIRYANTI 649
Cdd:TIGR01193 602 QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLLNLQDKTIIFVAHRLSVAKQSDKI 678
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 650 FVLSNrengstvdvdvlgedptkdsneknekhdkqekgGKnssanqkignagsyIIEQGTHDALMkNKNGIYYTMINN 727
Cdd:TIGR01193 679 IVLDH---------------------------------GK--------------IIEQGSHDELL-DRNGFYASLIHN 708
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
382-654 |
4.66e-35 |
|
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: 144.33 E-value: 4.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYdtRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdVIINDSHNLKDVNLKWWRS 460
Cdd:TIGR03797 451 AIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESG-SVFYDGQDLAGLDVQAVRR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSNSIKNNIKYS-LYSLKD-LEALSeesnedgfssqsdsnsrnscRAKCAGDLNDMiqttdsteliqvr 538
Cdd:TIGR03797 528 QLGVVLQNGRLMSGSIFENIAGGaPLTLDEaWEAAR--------------------MAGLAEDIRAM------------- 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 539 knyetiedsevvsvskkvlihdfvsalPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:TIGR03797 575 ---------------------------PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIV 627
|
250 260 270
....*....|....*....|....*....|....*.
gi 156095386 619 QKTINNLKGNEnritIIIAHRLSTIRYANTIFVLSN 654
Cdd:TIGR03797 628 SESLERLKVTR----IVIAHRLSTIRNADRIYVLDA 659
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1177-1450 |
4.89e-35 |
|
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: 142.10 E-value: 4.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1177 PNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnVGMknanef 1256
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI-----------------------------------VGI------ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1257 ssskegadgQSSTlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI-KFGkENATREDVKRACKFAAI 1335
Cdd:TIGR01842 368 ---------WPPT----SGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFG-ENADPEKIIEAAKLAGV 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1336 DEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAH 1415
Cdd:TIGR01842 434 HELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITH 512
|
250 260 270
....*....|....*....|....*....|....*
gi 156095386 1416 RIASIKRSDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:TIGR01842 513 RPSLLGCVDKILVLQD----GR-IARFGERDEVLA 542
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
825-1118 |
5.24e-35 |
|
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: 136.07 E-value: 5.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEANS-------NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEK 897
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPdeflddvNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 898 TMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGTY- 976
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 977 --FIFMRVFAIRARIAANKdvEKKRVNQPGTafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSN 1054
Cdd:cd18577 159 liAIVGGIMGKLLSKYTKK--EQEAYAKAGS----------------IAEEALSSIRTVKAFGGEEKEIKRYSKALEKAR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1055 KGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLM 1118
Cdd:cd18577 221 KAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIA 284
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1164-1431 |
1.12e-34 |
|
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: 130.80 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnVGMknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIkfgkenatr 1323
Cdd:cd03246 49 ----LGL-------------------LRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENI--------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 edvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03246 97 ---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK 143
|
250 260
....*....|....*....|....*...
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03246 144 -AAGATRIVIAHRPETLASADRILVLED 170
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1165-1431 |
1.17e-34 |
|
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: 132.21 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgde 1244
Cdd:cd03225 1 ELKNLSFSY-PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL----------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENA- 1321
Cdd:cd03225 51 -------------------------LGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEEEVAFGLENLg 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 -TREDVKRACKFAAIDEFIESLPNQYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03225 106 lPEEEIEERVEEALELVGLEGLRDRS-----PF--TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK 178
|
250 260 270
....*....|....*....|....*....|..
gi 156095386 1401 DIKDKaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03225 179 KLKAE-GKTIIIVTHDLDLLLElADRVIVLED 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1164-1428 |
8.02e-34 |
|
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: 130.32 E-value: 8.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEPML-FN--MSIYENIKF 1316
Cdd:cd03257 55 ---------------------------LKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMSsLNprMTIGEQIAE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 GKENATREDVKRACKFAAI---------DEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:cd03257 108 PLRIHGKLSKKEARKEAVLlllvgvglpEEVLNRYPHE-----------LSGGQRQRVAIARALALNPKLLIADEPTSAL 176
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156095386 1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03257 177 DVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAV 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
384-654 |
2.58e-33 |
|
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: 128.35 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 384 QFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNLKDVNLKWWRSKIG 463
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-DLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 464 VVSQDP--LLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsRNSCRAKcagdlndmiqttdstELIQVRkny 541
Cdd:cd03225 79 LVFQNPddQFFGPTVEEEVAFGL--------------------------ENLGLPE---------------EEIEER--- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etiedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03225 115 -------VEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEL 176
|
250 260 270
....*....|....*....|....*....|....*
gi 156095386 622 INNLKgnENRITIIIA-HRLSTIR-YANTIFVLSN 654
Cdd:cd03225 177 LKKLK--AEGKTIIIVtHDLDLLLeLADRVIVLED 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1164-1431 |
2.72e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG----KE 1319
Cdd:COG4619 53 -----------------------------TSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLPFPfqlrER 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATREDVKRAckFAAIDefiesLPNQY-DTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG4619 104 KFDRERALEL--LERLG-----LPPDIlDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEEL 172
|
250 260 270
....*....|....*....|....*....|....
gi 156095386 1399 IVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4619 173 LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEA 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
383-637 |
6.52e-33 |
|
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: 127.68 E-value: 6.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDVIINDSH-NLKDVNLK 456
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 457 WWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdleALSEESNEDGFssqsdsnsrnscrakcagdlndmiqttdsteliq 536
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGL-------RLHGIKLKEEL---------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 537 vrknyetieDSEVVSVSKKVLIHDFVSalpDKyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:cd03260 117 ---------DERVEEALRKAALWDEVK---DR------LHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTA 178
|
250 260
....*....|....*....|.
gi 156095386 617 LVQKTINNLKgneNRITIIIA 637
Cdd:cd03260 179 KIEELIAELK---KEYTIVIV 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1164-1431 |
1.06e-32 |
|
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: 126.43 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPIY--KDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtGEsskeqmqq 1241
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALL------------------GE-------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstLFKNSGKILLDGVdicdynlkdlrnlFSIVSQEPMLFNMSIYENIKFGKE-N 1320
Cdd:cd03250 55 ----------------------------LEKLSGSVSVPGS-------------IAYVSQEPWIQNGTIRENILFGKPfD 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 ATR-EDVKRACkfaAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKT 1398
Cdd:cd03250 94 EERyEKVIKAC---ALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENC 170
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 1399 IVDIKdKADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03250 171 ILGLL-LNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
402-654 |
2.41e-32 |
|
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: 134.11 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDvnlkWWRSK----IGVVSQDPLLFSNSIK 477
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL-DGADLSQ----WDREElgrhIGYLPQDVELFDGTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 478 NNIkyslyslkdlealseesnedgfssqsdsnsrnsCRakcagdlndmiqttdsteliqvrknYETIEDSEVVSVSKKVL 557
Cdd:COG4618 424 ENI---------------------------------AR-------------------------FGDADPEKVVAAAKLAG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 558 IHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIA 637
Cdd:COG4618 446 VHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVIT 524
|
250
....*....|....*..
gi 156095386 638 HRLSTIRYANTIFVLSN 654
Cdd:COG4618 525 HRPSLLAAVDKLLVLRD 541
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
337-1463 |
2.45e-32 |
|
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: 137.77 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 337 MLTIILPNITEYMKSLEatnNLYEIINRKPLVENNQDGKKLKD--IKKIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTY 414
Cdd:TIGR00957 592 ILPMVISSIVQASVSLK---RLRIFLSHEELEPDSIERRTIKPgeGNSITVHNATFTW-ARDLPPTLNGITFSIPEGALV 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 415 AFVGESGCGKSTILKLIERLYDPTEGDVIINDShnlkdvnlkwwrskIGVVSQDPLLFSNSIKNNIKyslyslkdleals 494
Cdd:TIGR00957 668 AVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWIQNDSLRENIL------------- 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 495 eesnedgFSSQSDSNSRNSCRAKCAgdlndmiqttdsteliqvrknyeTIEDSEVvsvskkvlihdfvsaLPDKYETLVG 574
Cdd:TIGR00957 721 -------FGKALNEKYYQQVLEACA-----------------------LLPDLEI---------------LPSGDRTEIG 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLS 653
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMS 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 654 nrengstvdvdvlgedptkdsneknekhdkqekGGKnssanqkignagsyIIEQGTHDALMKnKNGIYYTMInnqkvssk 733
Cdd:TIGR00957 836 ---------------------------------GGK--------------ISEMGSYQELLQ-RDGAFAEFL-------- 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 734 sssnndndkdsdmkssiykdseRGYDPDEANGNAKN-----ESASAKKSEKMSDAKASNTNAGGRlaFLRNL-------- 800
Cdd:TIGR00957 860 ----------------------RTYAPDEQQGHLEDswtalVSGEGKEAKLIENGMLVTDVVGKQ--LQRQLsasssdsg 915
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 801 -FKRKPKAPNNLRVV------YREIFSYKKDIAIIALSI----MVAGGLYPLFA--LLY---------AKYVGTLFD--- 855
Cdd:TIGR00957 916 dQSRHHGSSAELQKAeakeetWKLMEADKAQTGQVELSVywdyMKAIGLFITFLsiFLFvcnhvsalaSNYWLSLWTddp 995
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 856 FAN-LEANSN-KYSLY--------ILVIAIAMFISetlknyynnVIGEKVEKTMKLRLFENIMYQEISFFDQDShaPGLL 925
Cdd:TIGR00957 996 MVNgTQNNTSlRLSVYgalgilqgFAVFGYSMAVS---------IGGIQASRVLHQDLLHNKLRSPMSFFERTP--SGNL 1064
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 926 SAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAV---LTGTYFIFMRVFAIRARiaankdvEKKRVNQ 1002
Cdd:TIGR00957 1065 VNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIippLGLLYFFVQRFYVASSR-------QLKRLES 1137
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1003 PGTAFVYNSddeifkdpsflIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTLINSMLwgfSQSAQFFINS-- 1080
Cdd:TIGR00957 1138 VSRSPVYSH-----------FNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWL---AVRLECVGNCiv 1203
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1081 -FAYWFGsfLIRRGTIQVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFERY--YPLITRKSLIDVRdngGIKIKNS 1157
Cdd:TIGR00957 1204 lFAALFA--VISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLkeYSETEKEAPWQIQ---ETAPPSG 1278
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1158 NDIKGKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtGESSK 1236
Cdd:TIGR00957 1279 WPPRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRI----------------NESAE 1340
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1237 eqmqqgdeeqnvgmknanefssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK- 1315
Cdd:TIGR00957 1341 --------------------------------------GEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDp 1382
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 FGKenATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:TIGR00957 1383 FSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1396 EKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAQGTHEELLSvQDGVYKKYVKLA 1463
Cdd:TIGR00957 1461 QSTIRTQFE--DCTVLTIAHRLNTIMDYTRVIVLDKGE-----VAEFGAPSNLLQ-QRGIFYSMAKDA 1520
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1164-1416 |
4.24e-32 |
|
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: 132.87 E-value: 4.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:TIGR02868 335 LELRDLSAGY--PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-------------------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:TIGR02868 387 ----------------------------PLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:TIGR02868 439 EELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
|
250
....*....|...
gi 156095386 1404 DKadKTIITIAHR 1416
Cdd:TIGR02868 519 SG--RTVVLITHH 529
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1182-1385 |
5.31e-32 |
|
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: 122.37 E-value: 5.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1182 YKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneqtgesskeqmqQGDEeqnvgmknanefssske 1261
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL------------------------SPTE----------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1262 gadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKFGKENATREDVKRACKFAAIDEFIe 1340
Cdd:pfam00005 40 -------------GTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENLRLGLLLKGLSKREKDARAEEALEKL- 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 156095386 1341 SLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1385
Cdd:pfam00005 106 GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
404-654 |
1.03e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 132.66 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 404 LNFTLTEGKTYAFVGESGCGKSTILKLIerL-YDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIky 482
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNAL--LgFLPYQGSLKING-IELRELDPESWRKHLSWVGQNPQLPHGTLRDNV-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 483 slyslkdleALSEESnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetIEDSEVVSVSKKVLIHDFV 562
Cdd:PRK11174 444 ---------LLGNPD----------------------------------------------ASDEQLQQALENAWVSEFL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 563 SALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLST 642
Cdd:PRK11174 469 PLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLED 546
|
250
....*....|..
gi 156095386 643 IRYANTIFVLSN 654
Cdd:PRK11174 547 LAQWDQIWVMQD 558
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
383-654 |
1.70e-31 |
|
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: 121.94 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-DGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
250 260 270
....*....|....*....|....*....|..
gi 156095386 623 NNLKGnENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03246 140 AALKA-AGATRIVIAHRPETLASADRILVLED 170
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1164-1431 |
1.79e-31 |
|
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: 122.04 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRpNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfyDLKndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLK------------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNlKDLRNLFSIVSQEPMLFNMSIYENIkfgkenatr 1323
Cdd:cd03247 54 ----------------------------PQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL--------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 edvkrackfaaidefieslpnqydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03247 96 ------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL 145
|
250 260
....*....|....*....|....*...
gi 156095386 1404 DkaDKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03247 146 K--DKTLIWITHHLTGIEHMDKILFLEN 171
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
320-640 |
5.83e-31 |
|
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: 129.40 E-value: 5.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 320 HGGSVISILLGVLISMFMLTIILPN----ITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTr 395
Cdd:TIGR02868 268 LAPVTLAVLVLLPLAAFEAFAALPAaaqqLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPG- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 396 kDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnLKDVNLKWWRSKIGVVSQDPLLFSNS 475
Cdd:TIGR02868 347 -APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP-VSSLDQDEVRRRVSVCAQDAHLFDTT 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 476 IKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndMIQTTDSTeliqvrknyetieDSEVVSVSKK 555
Cdd:TIGR02868 425 VRENL--------------------------------------------RLARPDAT-------------DEELWAALER 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 556 VLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITII 635
Cdd:TIGR02868 448 VGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVL 525
|
....*
gi 156095386 636 IAHRL 640
Cdd:TIGR02868 526 ITHHL 530
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1164-1450 |
9.47e-31 |
|
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: 122.92 E-value: 9.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPN--VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqq 1241
Cdd:TIGR04520 1 IEVENVSFSY---PEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLL----------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegaDGQsstLFKNSGKILLDGVDICD-YNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGK 1318
Cdd:TIGR04520 49 ----------------------NGL---LLPTSGKVTVDGLDTLDeENLWEIRKKVGMVFQNPdnQFVGATVEDDVAFGL 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ENA------TREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:TIGR04520 104 ENLgvpreeMRKRVDEALKLVGMEDFRDREPHL-----------LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGR 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1393 KLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:TIGR04520 173 KEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNK----GK-IVAEGTPREIFS 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1155-1431 |
1.11e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.45 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1155 KNSNDIKGKIEIMDVNFRYLSRPNVpiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneqtges 1234
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQAL---KDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARV---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1235 skeqmqqgdeeqnvgmknanefssskegadgqsstlfknSGKILLDGVDI--CDYNLKDLRNLFSIVSQEPMLFNMSIYE 1312
Cdd:COG1117 70 ---------------------------------------EGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYD 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1313 NIKFG-KENATR------EDVKRACKFAAI-DEFIESLpnqyDTNvgpyGKSLSGGQKQRIAIARALLREPKILLLDEAT 1384
Cdd:COG1117 111 NVAYGlRLHGIKskseldEIVEESLRKAALwDEVKDRL----KKS----ALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 156095386 1385 SSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG1117 183 SALDPISTAKIEELILELKK--DYTIVIVTHNMQQAARvSDYTAFFYL 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
383-654 |
3.03e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.55 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDvNLKWWRSKI 462
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG-EDVAR-DPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSN-SIKNNIKY--SLYSLKDLEAlseesnedgfssqsdsnsrnscRAKCAgdlndmiqttdstELIqvrk 539
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFfaRLYGLPRKEA----------------------RERID-------------ELL---- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyetiedsevvsvskkvlihDFVSaLPDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG1131 117 --------------------ELFG-LTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELW 171
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 620 KTINNLKgnENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:COG1131 172 ELLRELA--AEGKTVLLStHYLEEAeRLCDRVAIIDK 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1164-1450 |
3.11e-30 |
|
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: 126.94 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN--VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqq 1241
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP----------------------- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNL---FSIVSQEPML-FN--MSIYENIK 1315
Cdd:COG1123 318 -------------------------------TSGSILFDGKDLTKLSRRSLRELrrrVQMVFQDPYSsLNprMTVGDIIA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 FG-------KENATREDVKRACKFAAID-EFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:COG1123 367 EPlrlhgllSRAERRERVAELLERVGLPpDLADRYPHE-----------LSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:COG1123 436 DVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYD----GRIV-EDGPTEEVFA 494
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1164-1432 |
3.15e-30 |
|
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: 118.44 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYN--LKDLRNLFSIVSQEPMLF-NMSIYENIKFGken 1320
Cdd:cd03229 50 EE--------------------------PDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFpHLTVLENIALG--- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 atredvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03229 101 ------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 1401 DIKDKADKTIITIAHRIASIKR-SDKIVVFNNP 1432
Cdd:cd03229 145 SLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1162-1461 |
4.01e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 130.63 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfkneqtgesskeqmq 1240
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE--------------------- 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKE 1319
Cdd:PLN03130 1293 ---------------------------------RGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDpFNEH 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATreDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PLN03130 1340 NDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTI 1417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1400 VDikDKADKTIITIAHRIASIKRSDKIVVFNnpdrTGSfVQAQGTHEELLSVQDGVYKKYVK 1461
Cdd:PLN03130 1418 RE--EFKSCTMLIIAHRLNTIIDCDRILVLD----AGR-VVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1164-1453 |
4.23e-30 |
|
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: 119.91 E-value: 4.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRfydlkndhHIVfkneqtgesskeqmqqgd 1243
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKST----LLR--------LIV------------------ 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadGQsstLFKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEPMLFN-MSIYENIKFG-- 1317
Cdd:cd03261 48 ---------------------GL---LRPDSGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSGALFDsLTVFENVAFPlr 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -----KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:cd03261 104 ehtrlSEEEIREIVLEKLEAVGLRGAEDLYPAE-----------LSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1393 KLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtgSFVQAQGTHEELLSVQD 1453
Cdd:cd03261 173 GVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYD-----GKIVAEGTPEELRASDD 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
383-655 |
4.52e-30 |
|
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: 119.91 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSN-SIKNNIKYSLYslkDLEALSEEsnedgfssqsdsnsrnscrakcagdlndMIqttdsTELIQvrk 539
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLR---EHTRLSEE----------------------------EI-----REIVL--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyETIEdsevvsvskKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:cd03261 119 --EKLE---------AVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVID 176
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 620 KTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNR 655
Cdd:cd03261 177 DLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1164-1450 |
4.85e-30 |
|
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: 126.56 E-value: 4.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneQTGESSkeqmqqgd 1243
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP------------HGGRIS-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPM--LFNMSIYENIKFGKEN- 1320
Cdd:COG1123 64 -------------------------------GEVLLDGRDLLELSEALRGRRIGMVFQDPMtqLNPVTVGDQIAEALENl 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 -----ATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:COG1123 113 glsraEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEI 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1396 EKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:COG1123 182 LDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDD----GRIV-EDGPPEEILA 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1164-1449 |
5.25e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.87 E-value: 5.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK13632 8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKIL------------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsSTLFK-NSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN 1320
Cdd:PRK13632 56 ------------------------TGLLKpQSGEIKIDGITISKENLKEIRKKIGIIFQNPdnQFIGATVEDDIAFGLEN 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 A--TREDVKRACKFAA----IDEFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1394
Cdd:PRK13632 112 KkvPPKKMKDIIDDLAkkvgMEDYLDKEP-----------QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1395 IEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELL 1449
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSE----GKLI-AQGKPKEIL 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
383-654 |
5.41e-30 |
|
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: 117.67 E-value: 5.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNLKWWRSK 461
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGeDLTDLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkn 540
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENI------------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 yetiedsevvsvskkvlihdfvsALPdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03229 98 -----------------------ALG-------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRA 141
|
250 260 270
....*....|....*....|....*....|....*
gi 156095386 621 TINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:cd03229 142 LLKSLQAQLGITVVLVTHDLDeAARLADRVVVLRD 176
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1164-1453 |
7.15e-30 |
|
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: 119.31 E-value: 7.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRfydlkndhHIVfkneqtgesskeqmqqgd 1243
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSV----LLK--------LII------------------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadGQsstLFKNSGKILLDGVDICDYNLKDLRNL---FSIVSQEPMLF-NMSIYENIKFG-- 1317
Cdd:COG1127 53 ---------------------GL---LRPDSGEILVDGQDITGLSEKELYELrrrIGMLFQGGALFdSLTVFENVAFPlr 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -----KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:COG1127 109 ehtdlSEAEIRELVLEKLELVGLPGAADKMPSE-----------LSGGMRKRVALARALALDPEILLYDEPTAGLDPITS 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1393 KLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLSVQD 1453
Cdd:COG1127 178 AVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLAD----GK-IIAEGTPEELLASDD 234
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1162-1464 |
7.70e-30 |
|
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: 120.01 E-value: 7.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhiVFKneqtgesskeqmqq 1241
Cdd:cd03288 18 GEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD-------IFD-------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGKENA 1321
Cdd:cd03288 76 ---------------------------------GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD-PECKC 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvd 1401
Cdd:cd03288 122 TDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV-- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1402 IKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAQgTHEELLSVQDGVYKKYVKLAK 1464
Cdd:cd03288 200 MTAFADRTVVTIAHRVSTILDADLVLVLSR----GILVECD-TPENLLAQEDGVFASLVRTDK 257
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
383-654 |
3.30e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 117.07 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS--HNLKDVNL-KWW 458
Cdd:COG1136 5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdiSSLSERELaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 459 RSKIGVVSQDPLLFSN-SIKNNIKYSLYslkdlealseesnedgFSSQSDSNSRNscRAKcagdlndmiqttdstELIqv 537
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLL----------------LAGVSRKERRE--RAR---------------ELL-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 538 rknyetiedsevvsvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG1136 130 ----------------ERVGLGDRLDHRP-----------SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEE 182
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 618 VQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:COG1136 183 VLELLRELNRELGTTIVMVTHDPELAARADRVIRLRD 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
400-654 |
3.74e-29 |
|
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: 124.38 E-value: 3.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNN 479
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL-DGADLKQWDRETFGKHIGYLPQDVELFPGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 IkyslyslkdlealseesnedgfssqsdsnsrnsCRAKcagdlndmiqttdsteliqvrknyETIEDSEVVSVSKKVLIH 559
Cdd:TIGR01842 412 I---------------------------------ARFG------------------------ENADPEKIIEAAKLAGVH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHR 639
Cdd:TIGR01842 435 ELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHR 513
|
250
....*....|....*
gi 156095386 640 LSTIRYANTIFVLSN 654
Cdd:TIGR01842 514 PSLLGCVDKILVLQD 528
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
384-654 |
5.22e-29 |
|
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: 114.26 E-value: 5.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 384 QFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIG 463
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-KDIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 464 VVSQdpllfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyet 543
Cdd:cd00267 77 YVPQ---------------------------------------------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 544 iedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
Cdd:cd00267 81 ------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
250 260 270
....*....|....*....|....*....|..
gi 156095386 624 NLKgNENRITIIIAHRLSTI-RYANTIFVLSN 654
Cdd:cd00267 125 ELA-EEGRTVIIVTHDPELAeLAADRVIVLKD 155
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
383-643 |
6.95e-29 |
|
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: 116.88 E-value: 6.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNlkWWRSKI 462
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSN-SIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcAGDLNDMiqttdsteliQVRKNY 541
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRY------------------------------------FAELYGL----------FDEELK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 ETIEDsevvsvskkvLIHDFvsALPDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:COG4555 111 KRIEE----------LIELL--GLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREI 174
|
250 260
....*....|....*....|..
gi 156095386 622 INNLKgNENRITIIIAHRLSTI 643
Cdd:COG4555 175 LRALK-KEGKTVLFSSHIMQEV 195
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1164-1427 |
7.40e-29 |
|
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: 115.66 E-value: 7.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNIL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsSTLFK-NSGKILLDGVDICDYNLKDLRNL----FSIVSQEPMLF-NMSIYENIKF 1316
Cdd:cd03255 51 -------------------------GGLDRpTSGEVRVDGTDISKLSEKELAAFrrrhIGFVFQSFNLLpDLTALENVEL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 -----GKENATRED-VKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:cd03255 106 plllaGVPKKERRErAEELLERVGLGDRLNHYPSE-----------LSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 1391 SEKLIEKTIVDIKDKADKTIITIAH--RIASikRSDKIV 1427
Cdd:cd03255 175 TGKEVMELLRELNKEAGTTIVVVTHdpELAE--YADRII 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
383-656 |
7.63e-29 |
|
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: 116.62 E-value: 7.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgqDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLKDleaLSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrk 539
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPLREHTD---LSEA------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyetiedsevvsvskkvLIHDFVSalpDKYEtLVG-SNA-----SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG1127 117 -----------------EIRELVL---EKLE-LVGlPGAadkmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPI 175
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 156095386 614 SEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNRE 656
Cdd:COG1127 176 TSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGK 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1164-1464 |
8.18e-29 |
|
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: 116.50 E-value: 8.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL---------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFsIVSQEPMLF-NMSIYENIKFgkeNAT 1322
Cdd:COG4555 51 --------------------------LKPDSGSILIDGEDVRKEPREARRQIG-VLPDERGLYdRLTVRENIRY---FAE 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REDVKRACKFAAIDEFIES--LPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:COG4555 101 LYGLFDEELKKRIEELIELlgLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILR 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1401 DIKDKaDKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLS--VQDGVYKKYVKLAK 1464
Cdd:COG4555 177 ALKKE-GKTVLFSSHIMQEVEAlCDRVVILHK----GK-VVAQGSLDELREeiGEENLEDAFVALIG 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
360-725 |
1.37e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 123.01 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 360 EIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
Cdd:PRK11160 316 EITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 440 GDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrAKca 519
Cdd:PRK11160 395 GEILLNG-QPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL---------------------------------AA-- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 520 gdlndmiqttdsteliqvrknyETIEDSEVVSVSKKVLIHDFVSAlPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
Cdd:PRK11160 439 ----------------------PNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 600 ILILDEATSSLDNKSEylvQKTINNL-KGNENRITIIIAHRLSTIRYANTIFVLsnrENGStvdvdvlgedptkdsnekn 678
Cdd:PRK11160 496 LLLLDEPTEGLDAETE---RQILELLaEHAQNKTVLMITHRLTGLEQFDRICVM---DNGQ------------------- 550
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 156095386 679 ekhdkqekggknssanqkignagsyIIEQGTHDALMKNKNGiYYTMI 725
Cdd:PRK11160 551 -------------------------IIEQGTHQELLAQQGR-YYQLK 571
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1164-1440 |
1.88e-28 |
|
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: 114.54 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskEQMqqgd 1243
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL---------------------ERP---- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG----- 1317
Cdd:cd03259 53 -----------------------------DSGEILIDGRDVTGVPPER-RNI-GMVFQDYALFpHLTVAENIAFGlklrg 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03259 102 vPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELR 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 156095386 1397 KTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQ 1440
Cdd:cd03259 171 EELKELQRELGITTIYVTHDQEEALAlADRIAVMNE----GRIVQ 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
382-730 |
2.81e-28 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 122.13 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:PRK10790 340 RIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL-DGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSNSIKNNIkyslyslkdleALSEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKNY 541
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANV-----------TLGRDISEE-----------------------------------QVWQAL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 ETIEdsevvsvskkvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:PRK10790 451 ETVQ------------LAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 622 INNLKgnENRITIIIAHRLSTIRYANTIFVLsnrengstvdvdvlgedptkdsneknekHDKQekggknssanqkignag 701
Cdd:PRK10790 519 LAAVR--EHTTLVVIAHRLSTIVEADTILVL----------------------------HRGQ----------------- 551
|
330 340
....*....|....*....|....*....
gi 156095386 702 syIIEQGTHDALMKnKNGIYYTMINNQKV 730
Cdd:PRK10790 552 --AVEQGTHQQLLA-AQGRYWQMYQLQLA 577
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
383-661 |
3.89e-28 |
|
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: 114.52 E-value: 3.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSK 461
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG-RPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLfsnSIknNIKYSLYslkdlEALSEEsnedgfssqsdsnsrnscrAKCAGDLNDmiqttdsteliqvrkny 541
Cdd:COG1124 81 VQMVFQDPYA---SL--HPRHTVD-----RILAEP-------------------LRIHGLPDR----------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etieDSEVVSVSKKV-LIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseYLVQK 620
Cdd:COG1124 115 ----EERIAELLEQVgLPPSFLDRYP-----------HQLSGGQRQRVAIARALILEPELLLLDEPTSALD----VSVQA 175
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 156095386 621 TINNL----KGNENRITIIIAHRLSTIRY-ANTIFVLsnrENGSTV 661
Cdd:COG1124 176 EILNLlkdlREERGLTYLFVSHDLAVVAHlCDRVAVM---QNGRIV 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
383-656 |
4.59e-28 |
|
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: 113.35 E-value: 4.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNL-KWW 458
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtDISKLSEKELaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 459 RSKIGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEALSEEsnedgfssqsdsnsrnscRAKcagdlndmiqttdstELIqv 537
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRE------------------RAE---------------ELL-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 538 rknyetiedsevvsvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:cd03255 126 ----------------ERVGLGDRLNHYP-----------SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKE 178
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 618 VQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
Cdd:cd03255 179 VMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1164-1429 |
5.54e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.60 E-value: 5.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL------------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsSTLFK-NSGKILLDGVDICDYNLKDL----RNLFSIVSQEPMLF-NMSIYENIKF 1316
Cdd:COG1136 55 -------------------------GGLDRpTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFFNLLpELTALENVAL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 G------KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:COG1136 110 PlllagvSRKERRERARELLERVGLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLILADEPTGNLDSK 178
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 156095386 1391 SEKLIEKTIVDIKDKADKTIITIAH--RIASikRSDKIVVF 1429
Cdd:COG1136 179 TGEEVLELLRELNRELGTTIVMVTHdpELAA--RADRVIRL 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
383-668 |
6.69e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.22 E-value: 6.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:COG2884 2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqDLSRLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQD-PLLFSNSIKNNIKYSLyslkdlEALSEESNEdgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRk 539
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALPL------RVTGKSRKE-----------------------------------IRRR- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyetiedseVVSVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDnksEYLVQ 619
Cdd:COG2884 118 ---------VREVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIARALVNRPELLLADEPTGNLD---PETSW 174
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 156095386 620 KTINNLKG-NENRITIIIA-HRLSTI-RYANTIFVLsnrENGSTVDVDVLGE 668
Cdd:COG2884 175 EIMELLEEiNRRGTTVLIAtHDLELVdRMPKRVLEL---EDGRLVRDEARGV 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1274-1450 |
1.03e-27 |
|
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: 113.20 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFAAIDEF--IESLPNQYDtnv 1350
Cdd:cd03299 53 SGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMlgIDHLLNRKP--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1351 gpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIEKtIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03299 128 ----ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLREE-LKKIRKEFGVTVLHVTHDFEEAWAlADKVAI 202
|
170 180
....*....|....*....|..
gi 156095386 1429 FNNpdrtGSFVQAqGTHEELLS 1450
Cdd:cd03299 203 MLN----GKLIQV-GKPEEVFK 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
382-653 |
1.25e-27 |
|
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: 111.74 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYdtRKDV-EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRS 460
Cdd:cd03369 6 EIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesneDGFSSQSDsnsrnscrakcagdlndmiqttdsteliqvRKN 540
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL-------------------DPFDEYSD------------------------------EEI 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 YETIEDSEVvsvskkvlihdfvsalpdkyetlvGSNaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03369 114 YGALRVSEG------------------------GLN---LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 621 TINNLKGNENriTIIIAHRLSTIRYANTIFVLS 653
Cdd:cd03369 167 TIREEFTNST--ILTIAHRLRTIIDYDKILVMD 197
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
383-661 |
2.47e-27 |
|
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: 110.10 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKwwRSKI 462
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL--SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL-------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03247 96 ----------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 623 nnLKGNENRITIIIAHRLSTIRYANTIFVLsnrENGSTV 661
Cdd:cd03247 142 --FEVLKDKTLIWITHHLTGIEHMDKILFL---ENGKII 175
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
386-654 |
3.42e-27 |
|
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: 109.83 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 386 KNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVV 465
Cdd:cd03214 3 ENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-KDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 466 SQdpllfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndMIQTTDSTELIQvrKNYETie 545
Cdd:cd03214 79 PQ---------------------------------------------------------ALELLGLAHLAD--RPFNE-- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 546 dsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:cd03214 98 ----------------------------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRL 143
|
250 260 270
....*....|....*....|....*....|
gi 156095386 626 KGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:cd03214 144 ARERGKTVVMVLHDLNlAARYADRVILLKD 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1164-1450 |
3.93e-27 |
|
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: 112.06 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1120 2 LEAENLSVGY---GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL--LKPS---------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGK---- 1318
Cdd:COG1120 55 ------------------------------SGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRELVALGRyphl 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ---ENATREDVKRAckFAAIDEF-IESLPNQydtnvgPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEK 1393
Cdd:COG1120 105 glfGRPSAEDREAV--EEALERTgLEHLADR------PVD-ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLE 175
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1394 LIEkTIVDIKDKADKTII------TIAHRIAsikrsDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:COG1120 176 VLE-LLRRLARERGRTVVmvlhdlNLAARYA-----DRLVLLKD----GR-IVAQGPPEEVLT 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
383-663 |
4.25e-27 |
|
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: 111.13 E-value: 4.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHY-DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWR 459
Cdd:cd03258 2 IELKNVSKVFgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnEDGFSSQSDSNSRnscrakcagdlndmiqttdSTELIqvr 538
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPL--------------EIAGVPKAEIEER-------------------VLELL--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 539 knyetiedsEVVSVSKKVlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS---- 614
Cdd:cd03258 126 ---------ELVGLEDKA----------DAY-------PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsi 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 615 -EYLvqKTINnlkgNENRITI-IIAHRLSTIR-YANTIFVLSNR---ENGSTVDV 663
Cdd:cd03258 180 lALL--RDIN----RELGLTIvLITHEMEVVKrICDRVAVMEKGevvEEGTVEEV 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1165-1431 |
5.99e-27 |
|
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: 108.10 E-value: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgde 1244
Cdd:cd00267 1 EIENLSFRY---GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL----------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQepmlfnmsiyenikfgkenatre 1324
Cdd:cd00267 49 -------------------------LKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1325 dvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:cd00267 81 --------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE 128
|
250 260
....*....|....*....|....*...
gi 156095386 1405 KaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd00267 129 E-GRTVIIVTHDPELAELaADRVIVLKD 155
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
382-636 |
6.49e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.28 E-value: 6.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD--P---TEGDVIINDsHNL--KDVN 454
Cdd:COG1117 11 KIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDG-EDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 455 LKWWRSKIGVVSQDPLLFSNSIKNNIKYSL-----YSLKDLEALSEESnedgfssqsdsnsrnscrakcagdlndmiqtt 529
Cdd:COG1117 87 VVELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiKSKSELDEIVEES-------------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 530 dsteLIQVrknyetiedsevvsvskkvlihdfvsALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSS 609
Cdd:COG1117 135 ----LRKA--------------------------ALWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSA 184
|
250 260
....*....|....*....|....*..
gi 156095386 610 LDNKSEYLVQKTINNLKgneNRITIII 636
Cdd:COG1117 185 LDPISTAKIEELILELK---KDYTIVI 208
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
383-654 |
8.04e-27 |
|
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: 111.37 E-value: 8.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKI 462
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPllfSNSIKNNIkyslyslkdLEalseesnED-GFssqsdsnsrnscrakcaGDLNDMIqttdSTELIQVRkny 541
Cdd:TIGR04520 80 GMVFQNP---DNQFVGAT---------VE-------DDvAF-----------------GLENLGV----PREEMRKR--- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etiedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:TIGR04520 117 -------VDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLET 178
|
250 260 270
....*....|....*....|....*....|....
gi 156095386 622 INNLKgNENRITII-IAHRLSTIRYANTIFVLSN 654
Cdd:TIGR04520 179 IRKLN-KEEGITVIsITHDMEEAVLADRVIVMNK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1164-1450 |
1.46e-26 |
|
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: 110.28 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRP-NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqg 1242
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL--ERPW--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FN------MSIYENIK 1315
Cdd:COG1124 59 -------------------------------SGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAsLHprhtvdRILAEPLR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 FGKENATREDVKRACKFAAID-EFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1394
Cdd:COG1124 108 IHGLPDREERIAELLEQVGLPpSFLDRYPHQ-----------LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAE 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1395 IEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:COG1124 177 ILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQN----GRIV-EELTVADLLA 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1164-1450 |
2.19e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.38 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL---------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDyNLKDLRNLFSIVSQEPMLF-NMSIYENIKF-----G 1317
Cdd:COG1131 50 --------------------------LRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYpDLTVRENLRFfarlyG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KENATREdvkrackfAAIDEFIE--SLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:COG1131 103 LPRKEAR--------ERIDELLElfGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARREL 170
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1396 EKTIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:COG1131 171 WELLRELAAE-GKTVLLSTHYLEEAERlCDRVAIIDK----GRIV-ADGTPDELKA 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
383-655 |
2.31e-26 |
|
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: 108.71 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLKwwRSK 461
Cdd:cd03293 1 LEVRNVSKTYGGGGGaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGP--GPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFS-NSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmIQTTDSTEliqvrkn 540
Cdd:cd03293 75 RGYVFQQDALLPwLTVLDNVALGL--------------------------------ELQG-----VPKAEARE------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 yetiedsEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03293 111 -------RAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQE 172
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 621 TINNLKgNENRITII-IAHRLS-TIRYANTIFVLSNR 655
Cdd:cd03293 173 ELLDIW-RETGKTVLlVTHDIDeAVFLADRVVVLSAR 208
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
383-659 |
3.64e-26 |
|
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: 107.56 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEIY--KDLNFTLTEGKTYAFVGESGCGKSTILKLI--ErlYDPTEGDVIINDShnlkdvnlkww 458
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 459 rskIGVVSQDPLLFSNSIKNNIKyslyslkdlealseesnedgFSSQSDSnsrnscrakcagdlndmiqttdsteliqvr 538
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENIL--------------------FGKPFDE------------------------------ 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 539 KNYEtiedsEVVSVSkkVLIHDFvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYL 617
Cdd:cd03250 95 ERYE-----KVIKAC--ALEPDL-EILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHI 166
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156095386 618 VQKTINNLkGNENRITIIIAHRLSTIRYANTIFVLsnrENGS 659
Cdd:cd03250 167 FENCILGL-LLNNKTRILVTHQLQLLPHADQIVVL---DNGR 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
383-654 |
4.20e-26 |
|
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: 108.98 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKI 462
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLL-FSnsiknnikyslYSLKDL---------EALSEESNEDgfssqsdsnsrnscRAKCAgdlnDMIQTTDST 532
Cdd:COG1120 78 AYVPQEPPApFG-----------LTVRELvalgryphlGLFGRPSAED--------------REAVE----EALERTGLE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 533 ELIQvrKNYETiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:COG1120 129 HLAD--RPVDE------------------------------------LSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 156095386 613 KSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNlAARYADRLVLLKD 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
403-645 |
4.27e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.98 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRSKIGVVSQDPllfsnsiknni 480
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqDITGLSGRELRPLRRRMQMVFQDP----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 481 kYSlySLkdlealseesnedgfssqsdsNSRnscrakcagdlndMiqttdsteliqvrknyeTIEDsevvSVSKKVLIHD 560
Cdd:COG4608 105 -YA--SL---------------------NPR-------------M-----------------TVGD----IIAEPLRIHG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 561 FVSA--LPDKYETL---VGSNAS-------KLSGGQKQRISIARAIIRNPKILILDEATSSLDnKSeylVQKTINNLKG- 627
Cdd:COG4608 127 LASKaeRRERVAELlelVGLRPEhadryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQAQVLNLLEd 202
|
250 260
....*....|....*....|.
gi 156095386 628 --NENRIT-IIIAHRLSTIRY 645
Cdd:COG4608 203 lqDELGLTyLFISHDLSVVRH 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1164-1432 |
4.60e-26 |
|
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: 107.94 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRY-LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03293 1 LEVRNVSKTYgGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRII------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknAnefssskeGADGQSStlfknsGKILLDGVDICDYNLKdlrnlFSIVSQEPMLFN-MSIYENIKFGKENA 1321
Cdd:cd03293 51 ----------A--------GLERPTS------GEVLVDGEPVTGPGPD-----RGYVFQQDALLPwLTVLDNVALGLELQ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 ------TREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:cd03293 102 gvpkaeARERAEELLELVGLSGFENAYPHQ-----------LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQL 170
|
250 260 270
....*....|....*....|....*....|....*...
gi 156095386 1396 EKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFNNP 1432
Cdd:cd03293 171 QEELLDIWRETGKTVLLVTHDIDeAVFLADRVVVLSAR 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
383-654 |
6.09e-26 |
|
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: 105.94 E-value: 6.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDvNLKWWRSKI 462
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG-KDIKK-EPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03230 76 GYLPEEPSLYEN-------------------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiedsevVSVskkvlihdfvsalpdkYETLvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03230 88 -------LTV----------------RENL------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELL 138
|
250 260 270
....*....|....*....|....*....|....
gi 156095386 623 NNLKgnENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:cd03230 139 RELK--KEGKTILLSsHILEEAeRLCDRVAILNN 170
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
383-654 |
1.11e-25 |
|
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: 106.45 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSK 461
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVtGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEAlseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKN 540
Cdd:cd03259 74 IGMVFQDYALFPHlTVAENIAFGLKLRGVPKA-------------------------------------------EIRAR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 yetiedseVVSVSKKVLIHDFVSALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03259 111 --------VRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE 171
|
250 260 270
....*....|....*....|....*....|....*
gi 156095386 621 TINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:cd03259 172 ELKELQRELGITTIYVTHDQEeALALADRIAVMNE 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1164-1448 |
1.35e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 110.19 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDIcdynlKDL----RNlFSIVSQEPMLF-NMSIYENIKFG- 1317
Cdd:COG3842 58 -----------------------------DSGRILLDGRDV-----TGLppekRN-VGMVFQDYALFpHLTVAENVAFGl 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -----KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnse 1392
Cdd:COG3842 103 rmrgvPKAEIRARVAELLELVGLEGLADRYPHQ-----------LSGGQQQRVALARALAPEPRVLLLDEPLSALDA--- 168
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1393 KLIEKTIVDIKD---KADKTIITIAH------RIasikrSDKIVVFNNpdrtGSFVQaQGTHEEL 1448
Cdd:COG3842 169 KLREEMREELRRlqrELGITFIYVTHdqeealAL-----ADRIAVMND----GRIEQ-VGTPEEI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1165-1431 |
1.97e-25 |
|
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: 104.82 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgde 1244
Cdd:cd03214 1 EVENLSVGY---GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL--LKPS----------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQepmlfnmsiyenikfgkenatre 1324
Cdd:cd03214 53 -----------------------------SGEILLDGKDLASLSPKELARKIAYVPQ----------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1325 dvkrACKFAAIDEFIESlpnQYDTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:cd03214 81 ----ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLAR 145
|
250 260
....*....|....*....|....*...
gi 156095386 1405 KADKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03214 146 ERGKTVVMVLHDLNLAARyADRVILLKD 173
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
64-361 |
3.00e-25 |
|
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: 108.13 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 64 VSFVCATISGGTLPFFVSVFG--------VIMKNMN---------------LGENVNDIIFSLVLIGIFQFILSFISSFC 120
Cdd:cd18558 3 VGILCAIIHGGLLPAFMVIFGdmtdsftnGGMTNITgnssglnssagpfekLEEEMTLYAYYYLIIGAIVLITAYIQGSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 121 MDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLT 200
Cdd:cd18558 83 WGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 201 LCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLME 280
Cdd:cd18558 163 LVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 281 SLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKsleATNNLYE 360
Cdd:cd18558 243 NISMGAAFLLIYASYALAFWYGTYLVTQ--------QEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFAN---ARGAAYH 311
|
.
gi 156095386 361 I 361
Cdd:cd18558 312 I 312
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
383-663 |
4.21e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 108.24 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWR 459
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQDP-LLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmiqttdsteliqVR 538
Cdd:COG1135 82 RKIGMIFQHFnLLSSRTVAENVALPL--------------------------------EIAG----------------VP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 539 KnyETIEdsevvsvsKKV--LIhDFVSaLPDKyetlvgSNA--SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:COG1135 114 K--AEIR--------KRVaeLL-ELVG-LSDK------ADAypSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 615 -----EYLvqKTINnlkgNENRITI-IIAHRLSTIRY-ANTIFVLSN-R--ENGSTVDV 663
Cdd:COG1135 176 trsilDLL--KDIN----RELGLTIvLITHEMDVVRRiCDRVAVLENgRivEQGPVLDV 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
391-654 |
4.49e-25 |
|
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: 104.65 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 391 HYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLKWWRSKIGVVSQDP- 469
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRKSIGYVMQDVd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 470 -LLFSNSIKNNIkysLYSLKDLEAlseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkNYETIEDse 548
Cdd:cd03226 82 yQLFTDSVREEL---LLGLKELDA-----------------------------------------------GNEQAET-- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 549 vvsVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGn 628
Cdd:cd03226 110 ---VLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA- 174
|
250 260
....*....|....*....|....*..
gi 156095386 629 ENRITIIIAHRLSTI-RYANTIFVLSN 654
Cdd:cd03226 175 QGKAVIVITHDYEFLaKVCDRVLLLAN 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
383-663 |
7.16e-25 |
|
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: 110.76 E-value: 7.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT---EGDVIINDsHNLKDVNLKWWR 459
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDG-RDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQDPL--LFSNSIKNNIkyslyslkdLEALseesnedgfssqsdsnsRNSCRAKcagdlndmiqttdstELIQV 537
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQI---------AEAL-----------------ENLGLSR---------------AEARA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 538 RknyetiedseVVSVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG1123 122 R----------VLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAE 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 156095386 618 VQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLSN---RENGSTVDV 663
Cdd:COG1123 181 ILDLLRELQRERGTTVLLITHDLGVVaEIADRVVVMDDgriVEDGPPEEI 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
382-655 |
7.42e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.56 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLKwwRS 460
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGP--GP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFS-NSIKNNIkysLYSLKDLEALSEESNEdgfssqsdsnsrnscRAkcagdlndmiqttdsTELIqvrk 539
Cdd:COG1116 81 DRGVVFQEPALLPwLTVLDNV---ALGLELRGVPKAERRE---------------RA---------------RELL---- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyetiedsevvsvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG1116 124 --------------ELVGLAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQ 178
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156095386 620 KTINNLKGNENRITIIIAH------RLstiryANTIFVLSNR 655
Cdd:COG1116 179 DELLRLWQETGKTVLFVTHdvdeavFL-----ADRVVVLSAR 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
383-654 |
1.46e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.07 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:PRK13632 8 IKVENVSFSYPNSENNAL-KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-DGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDP--LLFSNSIKNNIKYSLyslkdlealsEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliqvRKN 540
Cdd:PRK13632 86 GIIFQNPdnQFIGATVEDDIAFGL----------ENKKVP-------------------------------------PKK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 YETIedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13632 119 MKDI----IDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK 183
|
250 260 270
....*....|....*....|....*....|....
gi 156095386 621 TINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:PRK13632 184 IMVDLRKTRKKTLISITHDMDEAILADKVIVFSE 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1184-1428 |
1.53e-24 |
|
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: 106.29 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfKNEQTgesskeqmqqgdeeqnvgmknanefssskega 1263
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLP---------PPGIT-------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 dgqsstlfknSGKILLDGVDICDYNLKDLRNL----FSIVSQEPML-FN--MSIYENI-------KFGKENATREDVK-- 1327
Cdd:COG0444 62 ----------SGEILFDGEDLLKLSEKELRKIrgreIQMIFQDPMTsLNpvMTVGDQIaeplrihGGLSKAEARERAIel 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1328 -RACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1406
Cdd:COG0444 132 lERVGLPDPERRLDRYPHE-----------LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQREL 200
|
250 260
....*....|....*....|...
gi 156095386 1407 DKTIITIAHRIASIKR-SDKIVV 1428
Cdd:COG0444 201 GLAILFITHDLGVVAEiADRVAV 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1164-1449 |
2.40e-24 |
|
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: 103.53 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEQTgesskeqmqqgd 1243
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI------------EPT------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFgkeNAT 1322
Cdd:cd03295 55 ------------------------------SGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFpHMTVEENIAL---VPK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REDVKRACKFAAIDEFIESL---PNQYdtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:cd03295 102 LLKWPKEKIRERADELLALVgldPAEF---ADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEF 178
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1400 VDIKDKADKTIITIAHRI-ASIKRSDKIVVFNNpdrtGSFVQaQGTHEELL 1449
Cdd:cd03295 179 KRLQQELGKTIVFVTHDIdEAFRLADRIAIMKN----GEIVQ-VGTPDEIL 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
383-613 |
2.53e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 106.31 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LKWWRSK 461
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTdLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmiqttdsteliqVRKn 540
Cdd:COG3839 77 IAMVFQSYALYPHmTVYENIAFPL--------------------------------KLRK----------------VPK- 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 541 yETIeDSEVVSVSKKVLIHDFVsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG3839 108 -AEI-DRRVREAAELLGLEDLL----DRK-------PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
383-613 |
2.91e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 105.95 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSK 461
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVtGLPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLySLKDLEAlsEEsnedgfssqsdsnsrnscRAKCAGDLNDMIQttdsteliqvrkn 540
Cdd:COG3842 79 VGMVFQDYALFPHlTVAENVAFGL-RMRGVPK--AE------------------IRARVAELLELVG------------- 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 541 yetiedsevvsvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG3842 125 ---------------------LEGLADRY-------PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAK 169
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1273-1448 |
3.07e-24 |
|
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: 103.09 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDIcdYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG------KENATREDVKRACKFAAIDEFIESLPNQ 1345
Cdd:cd03300 53 TSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1346 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK---TIITIAH-RIASIK 1421
Cdd:cd03300 131 -----------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDL---KLRKDMQLELKRLQKElgiTFVFVTHdQEEALT 196
|
170 180
....*....|....*....|....*..
gi 156095386 1422 RSDKIVVFNNpdrtGSFVQAqGTHEEL 1448
Cdd:cd03300 197 MSDRIAVMNK----GKIQQI-GTPEEI 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1164-1450 |
3.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.04 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegaDGqssTLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENA 1321
Cdd:PRK13650 54 --------------------DG---LLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDDVAFGLENK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 ------TREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK13650 111 gipheeMKERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1396 EKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAQGTHEELLS 1450
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQ-----VESTSTPRELFS 229
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1164-1450 |
8.18e-24 |
|
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: 101.89 E-value: 8.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmkNANEFSSSkegadgqsstlfknsGKILLDGVDICDYNLKDLRNL---FSIVSQEPMLFN-MSIYENIKFGK 1318
Cdd:cd03258 52 ---------NGLERPTS---------------GSVLVDGTDLTLLSGKELRKArrrIGMIFQHFNLLSsRTVFENVALPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ENATREDVKRACKfaaIDEFIEsLPNQYDtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:cd03258 108 EIAGVPKAEIEER---VLELLE-LVGLED-KADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILAL 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1399 IVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQaQGTHEELLS 1450
Cdd:cd03258 183 LRDINRELGLTIVLITHEMEVVKRiCDRVAVMEK----GEVVE-EGTVEEVFA 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1165-1431 |
1.15e-23 |
|
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: 100.69 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgde 1244
Cdd:cd03235 1 EVEDLTVSY---GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvgmknanefssskegadGQsstLFKNSGKILLDGvdicdYNLKDLRNLFSIVSQEPML---FNMSIYENIKFGKEN- 1320
Cdd:cd03235 47 --------------------GL---LKPTSGSIRVFG-----KPLEKERKRIGYVPQRRSIdrdFPISVRDVVLMGLYGh 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 ---------ATREDVKRACKFAAIDEFIeslpnqyDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:cd03235 99 kglfrrlskADKAKVDEALERVGLSELA-------DRQIG----ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 156095386 1392 EKLIEKTIVDIKDKaDKTIITIAHRI-ASIKRSDKIVVFNN 1431
Cdd:cd03235 168 QEDIYELLRELRRE-GMTILVVTHDLgLVLEYFDRVLLLNR 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
383-652 |
1.29e-23 |
|
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: 103.59 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDVIIN--DSHNLKDVNLK 456
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgeDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 457 WWRSK-IGVVSQDPllfsnsiknnikyslyslkdlealseesnedgFSSqsdsnsrnscrakcagdLN------DMIqtt 529
Cdd:COG0444 82 KIRGReIQMIFQDP--------------------------------MTS-----------------LNpvmtvgDQI--- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 530 dsTELIQVRKNYETIE-DSEVVSVSKKVLIHDFVSALpDKY--EtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEA 606
Cdd:COG0444 110 --AEPLRIHGGLSKAEaRERAIELLERVGLPDPERRL-DRYphE---------LSGGMRQRVMIARALALEPKLLIADEP 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 156095386 607 TSSLDnkseYLVQKTI----NNLKgNENRITII-IAHRLSTIRY-ANTIFVL 652
Cdd:COG0444 178 TTALD----VTIQAQIlnllKDLQ-RELGLAILfITHDLGVVAEiADRVAVM 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1164-1431 |
1.35e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1118 3 IEVRNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnVGMknanefssskEGADgqsstlfknSGKILLDGVDIcDYNL--KDlRNL-FsiVSQEPMLF-NMSIYENIKFG-- 1317
Cdd:COG1118 49 ----AGL----------ETPD---------SGRIVLNGRDL-FTNLppRE-RRVgF--VFQHYALFpHMTVAENIAFGlr 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 ----KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:COG1118 102 vrppSKAEIRARVEELLELVQLEGLADRYPSQ-----------LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 156095386 1394 LIEKTIVDIKDKADKTIITIAH------RIAsikrsDKIVVFNN 1431
Cdd:COG1118 171 ELRRWLRRLHDELGGTTVFVTHdqeealELA-----DRVVVMNQ 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
383-664 |
1.59e-23 |
|
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: 101.11 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS--HNLKDVNLKWWRS 460
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdiNKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSNS--IKNnikyslyslkdleALSeesnedgfssqsdsnsrnscrakcaGDLNDMiqttdstELIQVR 538
Cdd:cd03256 79 QIGMIFQQFNLIERLsvLEN-------------VLS-------------------------GRLGRR-------STWRSL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 539 KNYETIEDSEV-VSVSKKVLIHDFVSAlpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:cd03256 114 FGLFPKEEKQRaLAALERVGLLDKAYQ-----------RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 156095386 618 VQKTINNLKGNENRITIIIAHRLSTIR-YANTIFVLSNRE---NGSTVDVD 664
Cdd:cd03256 183 VMDLLKRINREEGITVIVSLHQVDLAReYADRIVGLKDGRivfDGPPAELT 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1164-1431 |
2.66e-23 |
|
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: 98.24 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL--LKPD---------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDyNLKDLRNLFSIVSQEPMLF-NMSIYENIKfgkenat 1322
Cdd:cd03230 54 ------------------------------SGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYeNLTVRENLK------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 redvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:cd03230 96 ----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL 141
|
250 260 270
....*....|....*....|....*....|
gi 156095386 1403 KDKaDKTIITIAHRIASI-KRSDKIVVFNN 1431
Cdd:cd03230 142 KKE-GKTILLSSHILEEAeRLCDRVAILNN 170
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1163-1450 |
3.68e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 101.25 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRY--LSRPNVpiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmq 1240
Cdd:PRK13635 5 IIRVEHISFRYpdAATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLL---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegaDGqssTLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGK 1318
Cdd:PRK13635 54 -----------------------NG---LLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdnQFVGATVQDDVAFGL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 EN--ATRED----VKRACKFAAIDEFIESLPNqydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:PRK13635 108 ENigVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1393 KLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAQGTHEELLS 1450
Cdd:PRK13635 177 REVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGE-----ILEEGTPEEIFK 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1164-1431 |
7.11e-23 |
|
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: 98.48 E-value: 7.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRfydlkndhhivfkneqtgesskeqMQQGD 1243
Cdd:cd03301 1 VELENVTKRF---GNVTALDDLNLDIADGEFVVLLGPSGCGKTT----TLR------------------------MIAGL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG----- 1317
Cdd:cd03301 50 EE--------------------------PTSGRIYIGGRDVTDLPPKD-RDI-AMVFQNYALYpHMTVYDNIAFGlklrk 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIE 1396
Cdd:cd03301 102 vPKDEIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA---KLRV 167
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 1397 KT---IVDIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1431
Cdd:cd03301 168 QMraeLKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMND 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
383-611 |
7.73e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.91 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH-NLKDVNLKWWRSK 461
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDlTDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIkyslyslkdLEALseesnedgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRKn 540
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENV---------TLAP-----------------------------------------IKVKK- 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 541 yetIEDSEVVSVSKKVL----IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG1126 108 ---MSKAEAEERAMELLervgLADKADAYP-----------AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1163-1434 |
1.03e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 99.39 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqq 1241
Cdd:COG1116 7 ALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskeGADGQSStlfknsGKILLDGVDIcdynlKDLRNLFSIVSQEPMLFN-MSIYENIKFGKEN 1320
Cdd:COG1116 59 --------------------GLEKPTS------GEVLVDGKPV-----TGPGPDRGVVFQEPALLPwLTVLDNVALGLEL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 A---TREDVKRACKFAAI---DEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1394
Cdd:COG1116 108 RgvpKAERRERARELLELvglAGFEDAYPHQ-----------LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER 176
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156095386 1395 IEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVF-NNPDR 1434
Cdd:COG1116 177 LQDELLRLWQETGKTVLFVTHDVDeAVFLADRVVVLsARPGR 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1164-1450 |
1.14e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1121 7 IELENLTVSY---GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGL--LPPT---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDIcdynlKDLRNLFSIVSQE-------PM----LFNMSIYE 1312
Cdd:COG1121 60 ------------------------------SGTVRLFGKPP-----RRARRRIGYVPQRaevdwdfPItvrdVVLMGRYG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1313 NIKFGKeNATREDVKRAckFAAIDEF-IESLPNQydtnvgPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:COG1121 105 RRGLFR-RPSRADREAV--DEALERVgLEDLADR------PIG-ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1392 EKLIEKTIVDIKdKADKTIITIAHRIASIKR-SDKIVVFNnpdRTgsfVQAQGTHEELLS 1450
Cdd:COG1121 175 EEALYELLRELR-REGKTILVVTHDLGAVREyFDRVLLLN---RG---LVAHGPPEEVLT 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
398-652 |
1.37e-22 |
|
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: 97.75 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 398 VEIYKDL-NFTL-----TEGKTYAFVGESGCGKSTILKLIERLYDPTEG-----DVIINDSHnlKDVNLKWWRSKIGVVS 466
Cdd:cd03297 4 VDIEKRLpDFTLkidfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlnGTVLFDSR--KKINLPPQQRKIGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 467 QDPLLFSN-SIKNNIKYSLYSLKDLEalseesnedgfssqsdsnsrnscrakcagdlnDMIQTTDSTELIQVrknyetie 545
Cdd:cd03297 82 QQYALFPHlNVRENLAFGLKRKRNRE--------------------------------DRISVDELLDLLGL-------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 546 dsevvsvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:cd03297 122 ------------------------DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
250 260
....*....|....*....|....*...
gi 156095386 626 KGNENRITIIIAHRLSTIRY-ANTIFVL 652
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYlADRIVVM 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
383-611 |
1.47e-22 |
|
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: 97.60 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNLKWWRSK 461
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlKLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSlyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteLIQVRKn 540
Cdd:cd03262 78 VGMVFQQFNLFPHlTVLENITLA--------------------------------------------------PIKVKG- 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 541 yetIEDSEVVSVS----KKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:cd03262 107 ---MSKAEAEERAlellEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
383-638 |
1.47e-22 |
|
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: 97.33 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LKWWRSK 461
Cdd:cd03301 1 VELENVTKRFGNVTAL---DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG----RDVTdLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKN 540
Cdd:cd03301 74 IAMVFQNYALYPHmTVYDNIAFGL---------------------------------------------------KLRKV 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 YETIEDSEVVSVSKKVLIhdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03301 103 PKDEIDERVREVAELLQI----EHLLDRK-------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRA 171
|
250
....*....|....*...
gi 156095386 621 TINNLKGNENRITIIIAH 638
Cdd:cd03301 172 ELKRLQQRLGTTTIYVTH 189
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1274-1449 |
1.49e-22 |
|
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: 99.26 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNL----FSIVSQEPMLF-NMSIYENIKFGKE------NATREDVKRACKFAAIDEFIESL 1342
Cdd:cd03294 78 SGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENVAFGLEvqgvprAEREERAAEALELVGLEGWEHKY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIK 1421
Cdd:cd03294 158 PDE-----------LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDeALR 226
|
170 180
....*....|....*....|....*...
gi 156095386 1422 RSDKIVVFnnpdRTGSFVQAqGTHEELL 1449
Cdd:cd03294 227 LGDRIAIM----KDGRLVQV-GTPEEIL 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1164-1450 |
1.54e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.49 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLIN------------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvGMKNANEFSSSKegadgqsstlfknsgkILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN- 1320
Cdd:PRK13640 55 -----GLLLPDDNPNSK----------------ITVDGITLTAKTVWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENr 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 -ATREDVKRACKFAAID----EFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK13640 114 aVPRPEMIKIVRDVLADvgmlDYIDSEP-----------ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1396 EKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:PRK13640 183 LKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDD----GKLL-AQGSPVEIFS 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
384-655 |
1.88e-22 |
|
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: 97.22 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 384 QFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDvnlkwwRSKIG 463
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 464 VVSQdpllfsnsiknnikySLYSLKDLEALSEESNEDGFSSQSDSNSRNSCRAKCAGDlnDMIQTTDSTELIQvrknyet 543
Cdd:cd03235 72 YVPQ---------------RRSIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVD--EALERVGLSELAD------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 544 iedsevvsvskkvlihdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
Cdd:cd03235 128 -------------------------------RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR 176
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 624 NLKGnENRITIIIAHRLSTI-RYANTIFVLSNR 655
Cdd:cd03235 177 ELRR-EGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1183-1439 |
3.31e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.54 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneqTGEsskeqmqqgdeeqnVGMKNANEFSSSKeg 1262
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTI------TGS--------------IVYNGHNIYSPRT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstlfknsgkillDGVDicdynlkdLRNLFSIVSQEPMLFNMSIYENIKFG------KENAT-REDVKRACKFAAI 1335
Cdd:PRK14239 80 -----------------DTVD--------LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVlDEAVEKSLKGASI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1336 -DEFIESLpnqYDTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIA 1414
Cdd:PRK14239 135 wDEVKDRL---HDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVT 204
|
250 260
....*....|....*....|....*
gi 156095386 1415 HriaSIKRSDKIvvfnnPDRTGSFV 1439
Cdd:PRK14239 205 R---SMQQASRI-----SDRTGFFL 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1162-1448 |
4.70e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.38 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRfydlkndhhivfkneqtgesskeqMQQ 1241
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLR------------------------MIA 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 GDEEQNvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFGKEN 1320
Cdd:COG3839 51 GLEDPT--------------------------SGEILIGGRDVTDLPPKD-RNI-AMVFQSYALYpHMTVYENIAFPLKL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 A--TREDVKRACKFAA----IDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKL 1394
Cdd:COG3839 103 RkvPKAEIDRRVREAAellgLEDLLDRKPKQ-----------LSGGQRQRVALGRALVREPKVFLLDEPLSNLDA---KL 168
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1395 IEKTIVDIKD---KADKTII----------TIAhriasikrsDKIVVFNNpdrtGSFVQaQGTHEEL 1448
Cdd:COG3839 169 RVEMRAEIKRlhrRLGTTTIyvthdqveamTLA---------DRIAVMND----GRIQQ-VGTPEEL 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
383-655 |
9.70e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 95.93 E-value: 9.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDvnlkwwRSKI 462
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQdpllfsnsiknnikyslyslkdlealSEESNED--------------------GFSSQSDsnsrnscRAKCAgdl 522
Cdd:COG1121 78 GYVPQ--------------------------RAEVDWDfpitvrdvvlmgrygrrglfRRPSRAD-------REAVD--- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 523 nDMIQTTDSTELiqvrknyetiedsevvsvsKKVLIhdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILI 602
Cdd:COG1121 122 -EALERVGLEDL-------------------ADRPI-------------------GELSGGQQQRVLLARALAQDPDLLL 162
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 603 LDEATSSLDNKSEYLVQKTINNLkgNENRITIIIA-HRLSTIR-YANTIFVLSNR 655
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLREL--RREGKTILVVtHDLGAVReYFDRVLLLNRG 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1183-1439 |
1.04e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.48 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqTGesskeqMQQGDeeqnvgmknanefssskeg 1262
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKIL------------------SG------VYQPD------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstlfknSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFAAIDEFIE 1340
Cdd:COG1129 58 -----------SGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVpNLSVAENIFLGREPRRGGLIDWRAMRRRARELLA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 SL-----PnqyDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEkTIVDIKDKaDKTIITIA 1414
Cdd:COG1129 127 RLgldidP---DTPVG----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLFR-IIRRLKAQ-GVAIIYIS 197
|
250 260
....*....|....*....|....*.
gi 156095386 1415 HRIASIKR-SDKIVVFnnpdRTGSFV 1439
Cdd:COG1129 198 HRLDEVFEiADRVTVL----RDGRLV 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
386-663 |
1.07e-21 |
|
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: 100.91 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 386 KNVRFHYDTRK--------DVEIYKDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDVIINDS--HNLK 451
Cdd:COG4172 279 RDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQdlDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 452 DVNLKWWRSKIGVVSQDPllfsnsiknnikyslYSlkdleALS-----EESNEDGFSSQSDSNSRNSCRAKCAgdlndmi 526
Cdd:COG4172 354 RRALRPLRRRMQVVFQDP---------------FG-----SLSprmtvGQIIAEGLRVHGPGLSAAERRARVA------- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 527 qttdsteliqvrknyETIEDsevVSVSKKVL---IHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILIL 603
Cdd:COG4172 407 ---------------EALEE---VGLDPAARhryPHEF-------------------SGGQRQRIAIARALILEPKLLVL 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 604 DEATSSLDnKSeylVQKTINNLKGN---ENRIT-IIIAHRLSTIRY-ANTIFVLSN-R--ENGSTVDV 663
Cdd:COG4172 450 DEPTSALD-VS---VQAQILDLLRDlqrEHGLAyLFISHDLAVVRAlAHRVMVMKDgKvvEQGPTEQV 513
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1164-1431 |
1.29e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLsrPNVPIYK----DLTFSCESKKTTAIVGETGSGKSTVMsllmrfydlkndHHIvfkneqtgesskeqm 1239
Cdd:PRK13637 3 IKIENLTHIYM--EGTPFEKkaldNVNIEIEDGEFVGLIGHTGSGKSTLI------------QHL--------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 qqgdeeqnvgmknanefssskegadgqSSTLFKNSGKILLDGVDICD--YNLKDLRNLFSIVSQEP--MLFNMSIYENIK 1315
Cdd:PRK13637 54 ---------------------------NGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEETIEKDIA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 FGKENATRED------VKRACKFAAIDefieslpnqYDT--NVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:PRK13637 107 FGPINLGLSEeeienrVKRAMNIVGLD---------YEDykDKSPF--ELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 156095386 1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNN 1431
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNK 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
383-656 |
1.61e-21 |
|
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: 95.45 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHY-DTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNLKDVNLKWWRSK 461
Cdd:cd03295 1 IEFENVTKRYgGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKyslySLKDLEALSEESNEDgfssqsdsnsrnscRAKcagdlndmiqttdstELIQvrkn 540
Cdd:cd03295 77 IGYVIQQIGLFPHmTVEENIA----LVPKLLKWPKEKIRE--------------RAD---------------ELLA---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 yetiedsevvsvskkvLIHdfvsaLPDkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03295 120 ----------------LVG-----LDP--AEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQE 176
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 621 TINNLKGNENRITIIIAHRL-STIRYANTIFVLSNRE 656
Cdd:cd03295 177 EFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGE 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1156-1455 |
1.88e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.97 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1156 NSNDIkgkIEIMDVNFRYLSRPNVPIyKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgess 1235
Cdd:PRK13648 3 DKNSI---IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLM----------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1236 keqmqqgdeeqnVGMKNANEfssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEP-MLFNMSIYE-N 1313
Cdd:PRK13648 56 ------------IGIEKVKS-------------------GEIFYNNQAITDDNFEKLRKHIGIVFQNPdNQFVGSIVKyD 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1314 IKFGKENAT------REDVKRACKFAAIDEFIESLPNqydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:PRK13648 105 VAFGLENHAvpydemHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAQGTHEELLSVQDGV 1455
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGT-----VYKEGTPTEIFDHAEEL 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1162-1431 |
2.26e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 101.78 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmq 1240
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV---------------------- 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEn 1320
Cdd:PTZ00243 1363 --------------------------------CGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE- 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 ATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALL-REPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PTZ00243 1410 ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATV 1489
|
250 260 270
....*....|....*....|....*....|..
gi 156095386 1400 vdIKDKADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:PTZ00243 1490 --MSAFSAYTVITIAHRLHTVAQYDKIIVMDH 1519
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
383-660 |
2.56e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII-DGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPllfSNSIknnikyslyslkdLEALSEESNEDGFSSQsdsnsrnscrakcAGDLNDMIQTTDsteliqvrknye 542
Cdd:PRK13650 84 GMVFQNP---DNQF-------------VGATVEDDVAFGLENK-------------GIPHEEMKERVN------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiEDSEVVSVSkkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK13650 123 --EALELVGMQ------DFKEREP-----------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTI 183
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 623 NNLKgNENRITII-IAHRLSTIRYANTIFVLSNRENGST 660
Cdd:PRK13650 184 KGIR-DDYQMTVIsITHDLDEVALSDRVLVMKNGQVEST 221
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
826-1125 |
4.99e-21 |
|
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: 94.93 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 826 AIIALSIMVAGGL-YPLFALLYAKYVGTLFDFANLeansNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLF 904
Cdd:cd18557 1 GLLFLLISSAAQLlLPYLIGRLIDTIIKGGDLDVL----NELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 905 ENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGT---YFIFMR 981
Cdd:cd18557 77 SSLLRQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLViplLLIASK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 982 VFAIRARiAANKDVEKK--RVNQpgtafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDY----FCTLIEKAIDYSnk 1055
Cdd:cd18557 155 IYGRYIR-KLSKEVQDAlaKAGQ-------------------VAEESLSNIRTVRSFSAEEKeirrYSEALDRSYRLA-- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1056 gqKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDD---FMksLFTFLFTGSYAG------KLMSLKGDSE 1125
Cdd:cd18557 213 --RKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGEltsFI--LYTIMVASSVGGlssllaDIMKALGASE 287
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
383-637 |
5.43e-21 |
|
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: 92.86 E-value: 5.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqDVSDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrk 539
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFAL------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyetiedsEVVSVSKKvLIHDFVSA------LPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03292 104 --------EVTGVPPR-EIRKRVPAalelvgLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
250 260
....*....|....*....|....
gi 156095386 614 SEYLVQKTINnlKGNENRITIIIA 637
Cdd:cd03292 171 TTWEIMNLLK--KINKAGTTVVVA 192
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
100-653 |
5.85e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.44 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 100 IFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLtsdldfyLEQVNAGIGTKFITIF 179
Cdd:PLN03232 953 IVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRV-------INRFSKDIGDIDRNVA 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 180 TYASAFLGLyIWSLFKNARL-----TLCITCVFPLI---YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVS 251
Cdd:PLN03232 1026 NLMNMFMNQ-LWQLLSTFALigtvsTISLWAIMPLLilfYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRA 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 252 YcgentilKKFNLSEKLYSKYtlkanlmeslhigMING--FILASYAFGFWYGTRII------------ISDLSNQQPNN 317
Cdd:PLN03232 1105 Y-------KAYDRMAKINGKS-------------MDNNirFTLANTSSNRWLTIRLEtlggvmiwltatFAVLRNGNAEN 1164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 318 DFHGGSVISILLGVLISmfmLTIILPNITEY-------MKSLEATNNLYEIINRKP-LVENNQDGKKLKDIKKIQFKNVR 389
Cdd:PLN03232 1165 QAGFASTMGLLLSYTLN---ITTLLSGVLRQaskaensLNSVERVGNYIDLPSEATaIIENNRPVSGWPSRGSIKFEDVH 1241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 390 FHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQD 468
Cdd:PLN03232 1242 LRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD-CDVAKFGLTDLRRVLSIIPQS 1318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 469 PLLFSNSIKNNIkyslyslkdlealseesneDGFSSQSDSnsrnscrakcagDLndmiqttdsteliqvrknYETIEDSE 548
Cdd:PLN03232 1319 PVLFSGTVRFNI-------------------DPFSEHNDA------------DL------------------WEALERAH 1349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 549 vvsvskkvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkgN 628
Cdd:PLN03232 1350 ---------IKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR----E 1416
|
570 580
....*....|....*....|....*..
gi 156095386 629 ENR--ITIIIAHRLSTIRYANTIFVLS 653
Cdd:PLN03232 1417 EFKscTMLVIAHRLNTIIDCDKILVLS 1443
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1164-1460 |
6.17e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.33 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneqtgESSKEQMQQGD 1243
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRV--------EGRVEFFNQNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEQNVgmknanefssskegadgqsstlfknsgkilldgvdicdyNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KENAT 1322
Cdd:PRK14258 77 YERRV---------------------------------------NLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvKIVGW 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REDVKrackfaaIDEFIES------LPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:PRK14258 118 RPKLE-------IDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVE 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1397 KTIVDIKDKADKTIITIAHRIASIKRSDKIVVF--NNPDRTGSFVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PRK14258 191 SLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFfkGNENRIGQLVEFGLTKKIFNSPHDSRTREYV 256
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
62-309 |
9.29e-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: 94.41 E-value: 9.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 62 LGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDIIF-SLVLIGIF--QFILSFISSFCMDVVTTKILKTLKIEFLK 138
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLvPLAIIGLFllRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 139 SVFYQDGQFHDNNPG----SKLTSDldfyLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICG 214
Cdd:cd18552 81 KLLRLPLSFFDRNSSgdliSRITND----VNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 215 VICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINgfILAS 294
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME--LLGA 234
|
250
....*....|....*..
gi 156095386 295 YAFGF--WYGTRIIISD 309
Cdd:cd18552 235 IAIALvlWYGGYQVISG 251
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
383-636 |
1.17e-20 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 92.81 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDgqDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSNS--IKN----NIKY--------SLYSLKD----LEALSEesnedgfssqsdsnsrnscrakcagdl 522
Cdd:COG3638 81 RIGMIFQQFNLVPRLsvLTNvlagRLGRtstwrsllGLFPPEDreraLEALER--------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 523 ndmiqttdsteliqvrknyetiedsevVSVSKKVLIHdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILI 602
Cdd:COG3638 134 ---------------------------VGLADKAYQR-----------------ADQLSGGQQQRVAIARALVQEPKLIL 169
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 603 LDEATSSLDNKS-----EYLvqKTINnlkgNENRITIII 636
Cdd:COG3638 170 ADEPVASLDPKTarqvmDLL--RRIA----REDGITVVV 202
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
383-663 |
1.61e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.87 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDT-RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWR 459
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgqDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGDLNDMIQTTdSTELIqvr 538
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALPL--------------------------------ELAGTPKAEIKAR-VTELL--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 539 knyetiedsEVVSVSKKVlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylv 618
Cdd:PRK11153 126 ---------ELVGLSDKA----------DRY-------PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT---- 175
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 156095386 619 QKTINNLKGNENR---ITII-IAHRLSTI-RYANTIFVLSNR---ENGSTVDV 663
Cdd:PRK11153 176 TRSILELLKDINRelgLTIVlITHEMDVVkRICDRVAVIDAGrlvEQGTVSEV 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1165-1415 |
2.20e-20 |
|
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: 90.78 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgde 1244
Cdd:cd03226 1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvGMKNanefssskegadgqsstlfKNSGKILLDGVDICdynLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENAT 1322
Cdd:cd03226 48 ----GLIK-------------------ESSGSILLNGKPIK---AKERRKSIGYVMQDVdyQLFTDSVREELLLGLKELD 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 R--EDVKRACKFAAIDEFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03226 102 AgnEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIR 170
|
250
....*....|....*
gi 156095386 1401 DIKdKADKTIITIAH 1415
Cdd:cd03226 171 ELA-AQGKAVIVITH 184
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
64-355 |
2.42e-20 |
|
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: 93.01 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 64 VSFVCATISGGTLPFFVS-VFGVIMKNMNLgENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFY 142
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGrLIDTIIKGGDL-DVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 143 QDGQFHD-NNPG---SKLTSDLdfylEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICN 218
Cdd:cd18557 82 QEIAFFDkHKTGeltSRLSSDT----SVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 219 KKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFnlSEKLYSKYTL--KANLMESLHIGMINGFILASYA 296
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRY--SEALDRSYRLarKKALANALFQGITSLLIYLSLL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 297 FGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
Cdd:cd18557 236 LVLWYGGYLVLS--------GQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGAS 286
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
385-619 |
3.06e-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: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 385 FKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdshnlKDVnlkwwrsKIGV 464
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----KGL-------RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 465 VSQDPLLFSN-SIKNNIKYSLYSLKDLEALSEESNEDGFSSQSDSNSrnscrakcAGDLNDMIQTTDSTELiqvrknyet 543
Cdd:COG0488 66 LPQEPPLDDDlTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLER--------LAELQEEFEALGGWEA--------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 544 ieDSEVvsvsKKVLihdfvSAL---PDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-----E 615
Cdd:COG0488 129 --EARA----EEIL-----SGLgfpEEDLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleE 193
|
....
gi 156095386 616 YLVQ 619
Cdd:COG0488 194 FLKN 197
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1164-1388 |
3.72e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.97 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpiykdLTFSCESKK--TTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqq 1241
Cdd:COG3840 2 LRLDDLTYRYGDFP-------LRFDLTIAAgeRVAILGPSGAGKSTLLNLIAGF-------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNlKDLRnLFSIVSQEPMLFN-MSIYENIKFG--- 1317
Cdd:COG3840 49 ----------------------------LPPDSGRILWNGQDLTALP-PAER-PVSMLFQENNLFPhLTVAQNIGLGlrp 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1318 --KENAT-REDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:COG3840 99 glKLTAEqRAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1274-1432 |
5.99e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 92.83 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNL---FSIVSQEpmlFN-MS---IYENIKF-----GKENATREdvKRackfaaIDEFIE- 1340
Cdd:COG1135 59 SGSVLVDGVDLTALSERELRAArrkIGMIFQH---FNlLSsrtVAENVALpleiaGVPKAEIR--KR------VAELLEl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 --------SLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTI-- 1410
Cdd:COG1135 128 vglsdkadAYPSQ-----------LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIvl 196
|
170 180 190
....*....|....*....|....*....|....*..
gi 156095386 1411 IT--------IAHRIASIKRSdKIV-------VFNNP 1432
Cdd:COG1135 197 IThemdvvrrICDRVAVLENG-RIVeqgpvldVFANP 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
382-664 |
6.58e-20 |
|
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: 91.12 E-value: 6.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03288 19 EIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSNSIKNNIkyslyslkDLEAlseesnedgfssqsdsnsrnscraKCagdlndmiqtTDSTEliqvrknY 541
Cdd:cd03288 97 LSIILQDPILFSGSIRFNL--------DPEC------------------------KC----------TDDRL-------W 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 ETIEDSEvvsvskkvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03288 128 EALEIAQ---------LKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKV 198
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 156095386 622 InnLKGNENRITIIIAHRLSTIRYANTIFVLSnreNGSTVDVD 664
Cdd:cd03288 199 V--MTAFADRTVVTIAHRVSTILDADLVLVLS---RGILVECD 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1164-1429 |
6.81e-20 |
|
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: 89.86 E-value: 6.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFscESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03298 1 VRLDKIRFSY---GEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGF---------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG----- 1317
Cdd:cd03298 48 --------------------------ETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFaHLTVEQNVGLGlspgl 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KENAT-REDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03298 100 KLTAEdRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 1397 KTIVDIKDKADKTIITIAHRIASIKRSDKIVVF 1429
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVF 201
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-656 |
7.52e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 91.23 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 381 KKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN----DSHNLKDVnlk 456
Cdd:PRK13635 4 EIIRVEHISFRYPDAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlSEETVWDV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 457 wwRSKIGVVSQDPllfsnsikNNiKYSLYSLKDLEALSEESNedGFSSQsdsnsrnscrakcagdlnDMIQTTDSTeLIQ 536
Cdd:PRK13635 80 --RRQVGMVFQNP--------DN-QFVGATVQDDVAFGLENI--GVPRE------------------EMVERVDQA-LRQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 537 VRknyetiedsevvsvskkvlIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:PRK13635 128 VG-------------------MEDFLNREP-----------HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 156095386 617 LVQKTINNLKgNENRITII-IAHRLSTIRYANTIFVLSNRE 656
Cdd:PRK13635 178 EVLETVRQLK-EQKGITVLsITHDLDEAAQADRVIVMNKGE 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
351-653 |
7.79e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 96.73 E-value: 7.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 351 SLEATNNLYEIINRKPLV-ENNQDGKKLKDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
Cdd:PLN03130 1205 AVERVGTYIDLPSEAPLViENNRPPPGWPSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSML 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 429 KLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesneDGFSSQSDS 508
Cdd:PLN03130 1283 NALFRIVELERGRILI-DGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL-------------------DPFNEHNDA 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 509 NSRNSC-RAKcagdLNDMIqttdsteliqvRKNYETIeDSEVvsvskkvlihdfvsalpdkyeTLVGSNaskLSGGQKQR 587
Cdd:PLN03130 1343 DLWESLeRAH----LKDVI-----------RRNSLGL-DAEV---------------------SEAGEN---FSVGQRQL 1382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 588 ISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkgNENR--ITIIIAHRLSTIRYANTIFVLS 653
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR----EEFKscTMLIIAHRLNTIIDCDRILVLD 1446
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
383-653 |
1.10e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.39 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-EGEDISTLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKNye 542
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPW---------------------------------------------------QIRNQ-- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiedsevvSVSKKVLIHDFVS-ALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:PRK10247 111 --------QPDPAIFLDDLERfALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEI 179
|
250 260 270
....*....|....*....|....*....|..
gi 156095386 622 INNLKGNENRITIIIAHRLSTIRYANTIFVLS 653
Cdd:PRK10247 180 IHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
378-643 |
1.38e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.10 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 378 KDIKKIQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDV-IINDSHNLK 451
Cdd:PRK14258 3 KLIPAIKVNNLSFYYDTQKILE---GVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVeFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 452 DVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLkdlealseesnedgfssqsdsnsrnSCRAKCagDLNDMIQTtds 531
Cdd:PRK14258 80 RVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIV-------------------------GWRPKL--EIDDIVES--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 532 teliqvrknyeTIEDSEvvsvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK14258 130 -----------ALKDAD----------------LWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
250 260 270
....*....|....*....|....*....|..
gi 156095386 612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
Cdd:PRK14258 183 PIASMKVESLIQSLRLRSELTMVIVSHNLHQV 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1154-1437 |
1.49e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.23 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1154 IKNSNDIKGKIEIMDVNFRYLSRPNVpiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDhhivfkneqtge 1233
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAV---KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1234 sskeqmqqgdeeqnvgmknanefssskegadgqsstlFKNSGKILLDGVDICDYNLK--DLRNLFSIVSQEPMLFNMSIY 1311
Cdd:PRK14243 66 -------------------------------------FRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKSIY 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1312 ENIKFG-KENATRED----VKRACKFAAI-DEFIESLPNQydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATS 1385
Cdd:PRK14243 109 DNIAYGaRINGYKGDmdelVERSLRQAALwDEVKDKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1386 SLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKR-SDKIVVFN-NPDRTGS 1437
Cdd:PRK14243 181 ALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARvSDMTAFFNvELTEGGG 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
382-663 |
1.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYD--TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVNLK 456
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 457 WWRSKIGVVSQDP--LLFSNSIKNNIkysLYSLKDLEALSEESNEDGFssqsdsnsrnscrakcagDLndmiqttdsteL 534
Cdd:PRK13646 82 PVRKRIGMVFQFPesQLFEDTVEREI---IFGPKNFKMNLDEVKNYAH------------------RL-----------L 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 535 IQvrknyetiedsevVSVSKKVLihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK13646 130 MD-------------LGFSRDVM----------------SQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 156095386 615 EYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLsnrENGSTVDV 663
Cdd:PRK13646 181 KRQVMRLLKSLQTDENKTIILVSHDMNEVaRYADEVIVM---KEGSIVSQ 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1178-1427 |
1.77e-19 |
|
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: 89.16 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1178 NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefs 1257
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP--------------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1258 sskegadgqsstlfkNSGKILLDGVDICDYNLKDLRnlfSIVSQEPMLF-------NMSIYENIKFGKENA--------- 1321
Cdd:cd03256 54 ---------------TSGSVLIDGTDINKLKGKALR---QLRRQIGMIFqqfnlieRLSVLENVLSGRLGRrstwrslfg 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 --TREDVKRAckFAAIDEF-IESLPNQY-DTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:cd03256 116 lfPKEEKQRA--LAALERVgLLDKAYQRaDQ--------LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMD 185
|
250 260 270
....*....|....*....|....*....|.
gi 156095386 1398 TIVDIKDKADKTIITIAHRIASIKR-SDKIV 1427
Cdd:cd03256 186 LLKRINREEGITVIVSLHQVDLAREyADRIV 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
383-613 |
1.94e-19 |
|
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: 88.83 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSK 461
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDItNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLySLKDLealseesnedgfssqsdsnSRNSCRAKCAGDLnDMIQttdsteliqvrkn 540
Cdd:cd03300 74 VNTVFQNYALFPHlTVFENIAFGL-RLKKL-------------------PKAEIKERVAEAL-DLVQ------------- 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 541 yetiedsevvsvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03300 120 ---------------------LEGYANRK-------PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
383-613 |
2.05e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.36 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV--NLKWWRS 460
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG----RDLftNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLKdleaLSEESnedgfssqsdsnsrnscRAKCAGDLNDMIQttdsteliqvrk 539
Cdd:COG1118 76 RVGFVFQHYALFPHmTVAENIAFGLRVRP----PSKAE-----------------IRARVEELLELVQ------------ 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 540 nyetiedsevvsvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG1118 123 ----------------------LEGLADRY-------PSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1163-1460 |
2.16e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNfryLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneqtgesskeqmqqg 1242
Cdd:PRK14247 3 KIEIRDLK---VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARV------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPM-LFNMSIYENIKFG---- 1317
Cdd:PRK14247 62 -------------------------------SGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpIPNLSIFENVALGlkln 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 ----KENATREDVKRACKFAaidEFIESLPNQYDtnvGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:PRK14247 111 rlvkSKKELQERVRWALEKA---QLWDEVKDRLD---APAGK-LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTA 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1394 LIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNnpdRTGSFVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PRK14247 184 KIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFL---YKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1164-1415 |
5.55e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG2884 2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG----------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEQNvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNL---FSIVSQE-PMLFNMSIYENIKF--- 1316
Cdd:COG2884 51 EERP-------------------------TSGQVLVNGQDLSRLKRREIPYLrrrIGVVFQDfRLLPDRTVYENVALplr 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 --GKENAT-REDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSE 1392
Cdd:COG2884 106 vtGKSRKEiRRRVREVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIARALVNRPELLLADEPTGNLDpETSW 174
|
250 260 270
....*....|....*....|....*....|....*...
gi 156095386 1393 KLIE---------KTIV------DIKDKADKTIITIAH 1415
Cdd:COG2884 175 EIMElleeinrrgTTVLiathdlELVDRMPKRVLELED 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
383-652 |
6.51e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.27 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND----SHNLKDVnlkww 458
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitDDNFEKL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 459 RSKIGVVSQDPL-LFSNSIknnIKYSLyslkdleALSEEsnedgfssqsdsnsrnscrakcagdlNDMIQTTDSTEliqv 537
Cdd:PRK13648 82 RKHIGIVFQNPDnQFVGSI---VKYDV-------AFGLE--------------------------NHAVPYDEMHR---- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 538 rknyetiedsEVVSVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:PRK13648 122 ----------RVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
250 260 270
....*....|....*....|....*....|....*.
gi 156095386 618 VQKTINNLKGNENrITII-IAHRLSTIRYANTIFVL 652
Cdd:PRK13648 181 LLDLVRKVKSEHN-ITIIsITHDLSEAMEADHVIVM 215
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
389-611 |
1.03e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 87.59 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 389 RFHYDT----RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWwRSK-IG 463
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING-HKLEYGDYKY-RCKhIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 464 VVSQDPllfSNSIknNIKYSLYSLkdLEA-LSeesnedgfssqsdsnsrnscrakcagdLNdmiqtTDSTELIQVRKNYE 542
Cdd:COG4167 91 MIFQDP---NTSL--NPRLNIGQI--LEEpLR---------------------------LN-----TDLTAEEREERIFA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 543 TIEdsevvsvskkvlihdFVSALPDKYETlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4167 132 TLR---------------LVGLLPEHANF----YPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1273-1388 |
1.25e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 86.59 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICD--YNLKDLRNLFSIVSQEPMLF-NMSIYENI--------KFGKENATredvKRACKFAA---IDEF 1338
Cdd:COG1126 54 DSGTITVDGEDLTDskKDINKLRRKVGMVFQQFNLFpHLTVLENVtlapikvkKMSKAEAE----ERAMELLErvgLADK 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 IESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:COG1126 130 ADAYPAQ-----------LSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1273-1431 |
1.43e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG--------KENATRedVKRACKFAAIDEFIESLP 1343
Cdd:PRK09452 67 DSGRIMLDGQDITHVPAEN-RHV-NTVFQSYALFpHMTVFENVAFGlrmqktpaAEITPR--VMEALRMVQLEEFAQRKP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKR 1422
Cdd:PRK09452 143 HQ-----------LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTM 211
|
....*....
gi 156095386 1423 SDKIVVFNN 1431
Cdd:PRK09452 212 SDRIVVMRD 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1268-1429 |
1.58e-18 |
|
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: 85.81 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFKN--------SGKILLDGVDICDYNLK-DL---RNLFSIVSQEPMLF-NMSIYENIKFG-KENATREDVKRAckfa 1333
Cdd:cd03297 37 STLLRCiaglekpdGGTIVLNGTVLFDSRKKiNLppqQRKIGLVFQQYALFpHLNVRENLAFGlKRKRNREDRISV---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1334 aiDEFIESLpnQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1413
Cdd:cd03297 113 --DELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFV 188
|
170
....*....|....*..
gi 156095386 1414 AHRIASIKR-SDKIVVF 1429
Cdd:cd03297 189 THDLSEAEYlADRIVVM 205
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1174-1388 |
1.69e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.61 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1174 LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmkna 1253
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA---------------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1254 nefssskegadGQSSTLFKNSGKILLDGVDICDYNLkDLRNLfSIVSQEPMLF-NMSIYENIKFgkenATREDVKRACKF 1332
Cdd:COG4136 49 -----------GTLSPAFSASGEVLLNGRRLTALPA-EQRRI-GILFQDDLLFpHLSVGENLAF----ALPPTIGRAQRR 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1333 AAIDEFIES--LPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:COG4136 112 ARVEQALEEagLAGFADRDPA----TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
402-636 |
2.05e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.76 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD--PT---EGDVIINDsHNL--KDVNLKWWRSKIGVVSQDPLLFSN 474
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHG-KNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 475 SIKNNIKYSlyslkdlealseeSNEDGFSsqsdsnsrnscrakcaGDLNDMIQTTdsteLIQvrknyetiedsevvsvsk 554
Cdd:PRK14243 106 SIYDNIAYG-------------ARINGYK----------------GDMDELVERS----LRQ------------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 555 kvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRITI 634
Cdd:PRK14243 135 --------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK---EQYTI 203
|
..
gi 156095386 635 II 636
Cdd:PRK14243 204 II 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
402-652 |
2.32e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.03 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNL--KDVNLKWWRSKIGVVSQDP--LLFSNSIK 477
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGV-DItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 478 NNIKYSLYSLkdleALSEESNEDgfssqsdsnsrnscRAKCAGDLndmiqttdsteliqVRKNYETIEDSevvsvskkvl 557
Cdd:PRK13637 103 KDIAFGPINL----GLSEEEIEN--------------RVKRAMNI--------------VGLDYEDYKDK---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 558 ihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
Cdd:PRK13637 141 ------------------SPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVS 202
|
250
....*....|....*.
gi 156095386 638 HRLSTI-RYANTIFVL 652
Cdd:PRK13637 203 HSMEDVaKLADRIIVM 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1274-1431 |
2.51e-18 |
|
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: 85.85 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG----------KENATREDVKRACKFAAIDEFIESL 1342
Cdd:cd03296 56 SGTILFGGEDATDVPVQE-RNV-GFVFQHYALFrHMTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRY 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIK 1421
Cdd:cd03296 134 PAQ-----------LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEeALE 202
|
170
....*....|
gi 156095386 1422 RSDKIVVFNN 1431
Cdd:cd03296 203 VADRVVVMNK 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
356-664 |
2.82e-18 |
|
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: 86.54 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 356 NNLYEIINRKPlvennqdGKKLKDIKKIQFKNvrfhydtrkdvEIYK---------DLNFTLTEGKTYAFVGESGCGKST 426
Cdd:cd03294 4 KGLYKIFGKNP-------QKAFKLLAKGKSKE-----------EILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKST 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 427 ILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRSK-IGVVSQDPLLFSN-SIKNNIKYSLyslkDLEALSEESNEdgf 502
Cdd:cd03294 66 LLRCINRLIEPTSGKVLIDgqDIAAMSRKELRELRRKkISMVFQSFALLPHrTVLENVAFGL----EVQGVPRAERE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 503 ssqsdsnsrnscrakcagdlndmiqttdsteliqvRKNYETIEdsevvsvskKVLIHDFVSALPDKyetlvgsnaskLSG 582
Cdd:cd03294 139 -----------------------------------ERAAEALE---------LVGLEGWEHKYPDE-----------LSG 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 583 GQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLsnrENGSTV 661
Cdd:cd03294 164 GMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDeALRLGDRIAIM---KDGRLV 240
|
...
gi 156095386 662 DVD 664
Cdd:cd03294 241 QVG 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
402-677 |
2.91e-18 |
|
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: 85.47 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSKIGVVSQDPLLFSN-SIKNN 479
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDItNLPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 IKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKNYETIEDSEVVSVSKKVLIh 559
Cdd:cd03299 92 IAYGL---------------------------------------------------KKRKVDKKEIERKVLEIAEMLGI- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 560 dfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLK--GNENRITII-I 636
Cdd:cd03299 120 ----------DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK---EKLREELKkiRKEFGVTVLhV 186
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 156095386 637 AHRLSTIRyantifVLSNR----ENGSTVDVDVLGEDPTKDSNEK 677
Cdd:cd03299 187 THDFEEAW------ALADKvaimLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1274-1450 |
3.01e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.58 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYN-LKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN------ATREDVKRACKFAAIDEFIESLPn 1344
Cdd:PRK13644 56 KGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPetQFVGRTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSP- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1345 qydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSD 1424
Cdd:PRK13644 135 ----------KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG-KTIVYITHNLEELHDAD 203
|
170 180
....*....|....*....|....*.
gi 156095386 1425 KIVVFnnpDRtgSFVQAQGTHEELLS 1450
Cdd:PRK13644 204 RIIVM---DR--GKIVLEGEPENVLS 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
61-307 |
3.11e-18 |
|
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: 86.84 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 61 LLGVSFVCATISGGTLPFFVSV---FGVIMKNMNLgenVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFL 137
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLlidDVIPAGDLSL---LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 138 KSVFYQDGQFHDNNP-G---SKLTSDLDfyleQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC 213
Cdd:cd07346 80 RHLQRLSLSFFDRNRtGdlmSRLTSDVD----AVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 214 GVICNKKVK-----INKKTSLLYNNntmsiIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMIN 288
Cdd:cd07346 156 LRYFRRRIRkasreVRESLAELSAF-----LQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
|
250
....*....|....*....
gi 156095386 289 GFILASYAFGFWYGTRIII 307
Cdd:cd07346 231 LLTALGTALVLLYGGYLVL 249
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1274-1448 |
3.44e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.93 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLR-------------NLFSivSQepmlfnmSIYENIKFGKE--NATREDVKrackfAAIDEF 1338
Cdd:PRK11153 59 SGRVLVDGQDLTALSEKELRkarrqigmifqhfNLLS--SR-------TVFDNVALPLElaGTPKAEIK-----ARVTEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 IE--SLPNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1416
Cdd:PRK11153 125 LElvGLSDKADR----YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 156095386 1417 IASIKR---------SDKIV-------VFNNP--DRTGSFVQAQgTHEEL 1448
Cdd:PRK11153 201 MDVVKRicdrvavidAGRLVeqgtvseVFSHPkhPLTREFIQST-LHLDL 249
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1273-1427 |
5.08e-18 |
|
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: 84.12 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICD--YNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFA-------AIDEFIESL 1342
Cdd:cd03262 53 DSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFpHLTVLENITLAPIKVKGMSKAEAEERAlellekvGLADKADAY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKR 1422
Cdd:cd03262 133 PAQ-----------LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFARE 200
|
....*.
gi 156095386 1423 -SDKIV 1427
Cdd:cd03262 201 vADRVI 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
383-637 |
6.16e-18 |
|
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: 84.09 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDvNLKWWRSKI 462
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-YSIRT-DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNsiknnikyslysLKDLEALseesnedgfssqsdsnsRNSCRAKCagdlndmiqttdsteliqvrknye 542
Cdd:cd03263 78 GYCPQFDALFDE------------LTVREHL-----------------RFYARLKG------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tIEDSEVVSVSKKVLIHDfvsALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03263 105 -LPKSEIKEEVELLLRVL---GLTDKANKR----ARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLI 176
|
250
....*....|....*
gi 156095386 623 NNLKgnENRiTIIIA 637
Cdd:cd03263 177 LEVR--KGR-SIILT 188
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
383-643 |
1.45e-17 |
|
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: 83.98 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG-DVIINDsHNLKDVNLKWWRSK 461
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFG-ERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDpllfsnsiknnikyslyslkdlealseesnedgfsSQSDSNSRNSCRakcagdlnDMIQT--TDSTELiqvrk 539
Cdd:COG1119 80 IGLVSPA-----------------------------------LQLRFPRDETVL--------DVVLSgfFDSIGL----- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nYETIEDSEVVSVskKVLIHDF-VSALPDK-YETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG1119 112 -YREPTDEQRERA--RELLELLgLAHLADRpFGTL--------SQGEQRRVLIARALVKDPELLILDEPTAGLDLGAREL 180
|
250 260
....*....|....*....|....*.
gi 156095386 618 VQKTINNLKGNENRITIIIAHRLSTI 643
Cdd:COG1119 181 LLALLDKLAAEGAPTLVLVTHHVEEI 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1270-1450 |
1.99e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.37 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1270 LFKNSGKILLDGVDICDY-NLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN------ATREDVKRACKFAAIDEFIE 1340
Cdd:PRK13633 60 LIPSEGKVYVDGLDTSDEeNLWDIRNKAGMVFQNPdnQIVATIVEEDVAFGPENlgippeEIRERVDESLKKVGMYEYRR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 SLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1420
Cdd:PRK13633 140 HAPHL-----------LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA 208
|
170 180 190
....*....|....*....|....*....|
gi 156095386 1421 KRSDKIVVFNnpdrTGSFVQaQGTHEELLS 1450
Cdd:PRK13633 209 VEADRIIVMD----SGKVVM-EGTPKEIFK 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
402-676 |
2.30e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN----DSHNLKDVnlkwWRSKIGVVSQDPLLFSN-SI 476
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvRFRSPRDA----QAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 477 KNNIkyslyslkdleALSEESNEDGFSsqsdsnsrnscrakcagDLNDMIQTTdsTELIqvrknyETIEdsevVSVSkkv 556
Cdd:COG1129 97 AENI-----------FLGREPRRGGLI-----------------DWRAMRRRA--RELL------ARLG----LDID--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 557 lihdfvsalPDkyeTLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVqKTINNLKgnENRITII 635
Cdd:COG1129 134 ---------PD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLF-RIIRRLK--AQGVAII 194
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 156095386 636 -IAHRLSTIRY-ANTIFVLsnReNGSTVdvdvlGEDPTKDSNE 676
Cdd:COG1129 195 yISHRLDEVFEiADRVTVL--R-DGRLV-----GTGPVAELTE 229
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1164-1415 |
2.48e-17 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 83.18 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSrpNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEP------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFS---IVSQEPMLF-NMSIYENI---KF 1316
Cdd:COG3638 56 -----------------------------TSGEILVDGQDVTALRGRALRRLRRrigMIFQQFNLVpRLSVLTNVlagRL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 GKENA--------TREDVKRAckFAAIDEFieSLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:COG3638 107 GRTSTwrsllglfPPEDRERA--LEALERV--GLADKAYQRAD----QLSGGQQQRVAIARALVQEPKLILADEPVASLD 178
|
250 260
....*....|....*....|....*...
gi 156095386 1389 -SNSEKLIEkTIVDIKDKADKTIITIAH 1415
Cdd:COG3638 179 pKTARQVMD-LLRRIAREDGITVVVNLH 205
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1164-1450 |
2.71e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.92 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYK----DLTFSCESKKTTAIVGETGSGKSTVM----SLLMrfydlkndhhivfkneqtgeSS 1235
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPFERralyDVNVSIPSGSYVAIIGHTGSGKSTLLqhlnGLLQ--------------------PT 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1236 KEQMQQGDEEQNVGMKNANefssskegadgqsstlfknsgkilldgvdicdynLKDLRNLFSIVSQ--EPMLFNMSIYEN 1313
Cdd:PRK13634 61 SGTVTIGERVITAGKKNKK----------------------------------LKPLRKKVGIVFQfpEHQLFEETVEKD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1314 IKFGKEN--ATREDVKRACKfaaidEFIE--SLPNQYDTNvGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:PRK13634 107 ICFGPMNfgVSEEDAKQKAR-----EMIElvGLPEELLAR-SPF--ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1390 NSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHK----GT-VFLQGTPREIFA 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1177-1431 |
2.73e-17 |
|
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: 82.38 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1177 PNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtGEsskeqMQQgdeeqnvgMKNANEF 1256
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAIL------------------GE-----MQT--------LEGKVHW 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1257 SSSKEGADGQSSTLFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLFNMSIYENIKFGKE-NATR-EDVKRACkfaA 1334
Cdd:cd03290 61 SNKNESEPSFEATRSRNRYSV-------------------AYAAQKPWLLNATVEENITFGSPfNKQRyKAVTDAC---S 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1335 IDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITI 1413
Cdd:cd03290 119 LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLV 198
|
250
....*....|....*...
gi 156095386 1414 AHRIASIKRSDKIVVFNN 1431
Cdd:cd03290 199 THKLQYLPHADWIIAMKD 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
383-663 |
2.77e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.08 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHY-DTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGD--VIINDSHNLKDVNLKWWR 459
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPA--LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnsKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQDPllfsnsiknnikyslyslkDLEALSEESNED-GFSSQSDSNSRNscrakcagdlndmiqttdstELIQVr 538
Cdd:PRK13640 84 EKVGIVFQNP-------------------DNQFVGATVGDDvAFGLENRAVPRP--------------------EMIKI- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 539 knyetiedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:PRK13640 124 ----------VRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 156095386 619 QKTINNLKgNENRITII-IAHRLSTIRYANTIFVLSNRE---NGSTVDV 663
Cdd:PRK13640 183 LKLIRKLK-KKNNLTVIsITHDIDEANMADQVLVLDDGKllaQGSPVEI 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
390-611 |
3.44e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.30 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 390 FHYDT----RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVV 465
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-HPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 466 SQDPllfSNSIknNIKYSLYSLKDLEALseesnedgfssqsdsnsrnscrakcagdLNDMIQTTDSTELIqvrknYETIE 545
Cdd:PRK15112 93 FQDP---STSL--NPRQRISQILDFPLR----------------------------LNTDLEPEQREKQI-----IETLR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 546 DsevvsvskkvlihdfVSALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK15112 135 Q---------------VGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
383-654 |
5.02e-17 |
|
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: 81.47 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGkTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNlkWWRSKI 462
Cdd:cd03264 1 LQLENLTKRYGKKRAL---DGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ--KLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNsiknnikyslysLKDLEALseesnedgfssqsdsnsRNSCRAKcagdlnDMIQTTdsteliqvrknye 542
Cdd:cd03264 75 GYLPQEFGVYPN------------FTVREFL-----------------DYIAWLK------GIPSKE------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiEDSEVVSVSKKVLIHDFVsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03264 107 --VKARVDEVLELVNLGDRA----KKK-------IGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL 173
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 623 NNLkgNENRITIIIAHRLSTIRY-ANTIFVLSN 654
Cdd:cd03264 174 SEL--GEDRIVILSTHIVEDVESlCNQVAVLNK 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
383-639 |
5.97e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.13 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDVIINdSHNL-----KD 452
Cdd:PRK14239 6 LQVSDLSVYYNKKKAL---NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYN-GHNIysprtDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 453 VNLkwwRSKIGVVSQDPLLFSNSIKNNIKYSLY--SLKDLEALseesnedgfssqsDSNSRNSCRAKCAGDlndmiqttd 530
Cdd:PRK14239 82 VDL---RKEIGMVFQQPNPFPMSIYENVVYGLRlkGIKDKQVL-------------DEAVEKSLKGASIWD--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 531 steliqvrknyetiedsEVvsvskKVLIHDfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:PRK14239 137 -----------------EV-----KDRLHD---------------SALGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
250 260
....*....|....*....|....*....
gi 156095386 611 DNKSEYLVQKTINNLKgneNRITIIIAHR 639
Cdd:PRK14239 180 DPISAGKIEETLLGLK---DDYTMLLVTR 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1164-1415 |
6.51e-17 |
|
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: 81.30 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03292 1 IEFINVTKTY--PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYK----------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEQnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYN---LKDLRNLFSIVSQE-PMLFNMSIYENIKFGKE 1319
Cdd:cd03292 50 EEL-------------------------PTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQDfRLLPDRNVYENVAFALE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 ------NATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:cd03292 105 vtgvppREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
250 260
....*....|....*....|..
gi 156095386 1394 LIEKTIVDIkDKADKTIITIAH 1415
Cdd:cd03292 174 EIMNLLKKI-NKAGTTVVVATH 194
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1162-1420 |
7.23e-17 |
|
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: 82.59 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYLSRPNVpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqq 1241
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR--------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKEN 1320
Cdd:cd03289 53 ----------------------------LLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDpYGKWS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 atREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03289 105 --DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK 182
|
250 260
....*....|....*....|
gi 156095386 1401 diKDKADKTIITIAHRIASI 1420
Cdd:cd03289 183 --QAFADCTVILSEHRIEAM 200
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1179-1450 |
8.35e-17 |
|
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: 80.94 E-value: 8.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1179 VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfkneqtgesskeqmqqgdeeqnvgmknanefss 1258
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR--------------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1259 skegadgqsstlfknSGKILLDGVDIcdynlkDLRNLFSI-------VSQEPMLF-NMSIYENIKFGKENATREDVKRAc 1330
Cdd:cd03224 54 ---------------SGSIRFDGRDI------TGLPPHERaragigyVPEGRRIFpELTVEENLLLGAYARRRAKRKAR- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1331 kfaaIDEFIESLP------NQYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIE---KTIVD 1401
Cdd:cd03224 112 ----LERVYELFPrlkerrKQL-------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL---APKIVEeifEAIRE 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1402 IKDKaDKTIITI---AHRIASIkrSDKIVVFnnpdRTGSFVqAQGTHEELLS 1450
Cdd:cd03224 178 LRDE-GVTILLVeqnARFALEI--ADRAYVL----ERGRVV-LEGTAAELLA 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1164-1419 |
8.43e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.60 E-value: 8.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSrpnVPIYKDLTFSCESKKTTAIVGETGSGKST---VMSLLmrfyDLKNDHHIVFKNEQTGESSKEQMQ 1240
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLL----ETPDSGQLNIAGHQFDFSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 QGDE-EQNVGMknanefssskegadgqsstLFKNsgkilldgvdicdYNL----KDLRNLFsivsQEPM-LFNMSiyeni 1314
Cdd:COG4161 76 AIRLlRQKVGM-------------------VFQQ-------------YNLwphlTVMENLI----EAPCkVLGLS----- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1315 kfgKENAtredVKRACKFAA---IDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNs 1391
Cdd:COG4161 115 ---KEQA----REKAMKLLArlrLTDKADRFPLH-----------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE- 175
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 1392 eklIEKTIVDIKDKADKTIIT---------IAHRIAS 1419
Cdd:COG4161 176 ---ITAQVVEIIRELSQTGITqvivtheveFARKVAS 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1183-1450 |
1.21e-16 |
|
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: 80.94 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskeg 1262
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRP-------------------------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstlfkNSGKILLDGVDICdyNLK-DLRNLFSIVS--QEPMLF-NMSIYENIKFGKENATREDVKRACKFAAIDEF 1338
Cdd:cd03219 53 ----------TSGSVLFDGEDIT--GLPpHEIARLGIGRtfQIPRLFpELTVLENVMVAAQARTGSGLLLARARREEREA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 IES---------LPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDKaDK 1408
Cdd:cd03219 121 RERaeellervgLADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEELAE-LIRELRER-GI 194
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 156095386 1409 TIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:cd03219 195 TVLLVEHDMDVVMSlADRVTVLDQ----GR-VIAEGTPDEVRN 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1243-1455 |
1.39e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.68 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 DEEQNVGMKNANEFSSSK--------EGADGQSST------LFKN-SGKILLDGVDICDYNLKDLRNLFSIVSQEP--ML 1305
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKgewvsiigQNGSGKSTTarlidgLFEEfEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1306 FNMSIYENIKFGKENatrEDVKRACKFAAIDEFIESLpNQYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATS 1385
Cdd:PRK13642 95 VGATVEDDVAFGMEN---QGIPREEMIKRVDEALLAV-NMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1386 SLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAQGTHEELLSVQDGV 1455
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVM----KAGEIIKEAAPSELFATSEDMV 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
383-613 |
1.82e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.07 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LKWWRSK 461
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG----QDIThVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGDLNDMIQTTDSTELIQVRkn 540
Cdd:PRK09452 88 VNTVFQSYALFPHmTVFENVAFGL--------------------------------RMQKTPAAEITPRVMEALRMVQ-- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 541 yetiedsevvsvskkvlihdfvsalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK09452 134 ----------------------------LEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
403-614 |
2.42e-16 |
|
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: 82.46 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN-----DSHnlKDVNLKWWRSKIGVVSQDPLLFSN-SI 476
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqDSA--RGIFLPPHRRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 477 KNNIKYSLyslkdlealseesnedgfssqsdsnsRNSCRAKCAGDLNDMIQTTDsteliqvrknyetIEDsevvsvskkv 556
Cdd:COG4148 95 RGNLLYGR--------------------------KRAPRAERRISFDEVVELLG-------------IGH---------- 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 557 lihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:COG4148 126 ---------------LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1274-1448 |
2.67e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.07 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG-------KENaTREDVKRACKFAAIDEFIESLPNQ 1345
Cdd:PRK11432 60 EGQIFIDGEDVTHRSIQQ-RDI-CMVFQSYALFpHMSLGENVGYGlkmlgvpKEE-RKQRVKEALELVDLAGFEDRYVDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1346 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSD 1424
Cdd:PRK11432 137 -----------ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHdQSEAFAVSD 205
|
170 180
....*....|....*....|....
gi 156095386 1425 KIVVFNNpdrtGSFVQaQGTHEEL 1448
Cdd:PRK11432 206 TVIVMNK----GKIMQ-IGSPQEL 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1161-1460 |
3.05e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1161 KGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHhivfkneqtgesskeqmq 1240
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSK------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKE 1319
Cdd:PRK14246 67 ------------------------------IKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpHLSIYDNIAYPLK 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATREDvKRACKfAAIDEFIESL---PNQYDTNVGPyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:PRK14246 117 SHGIKE-KREIK-KIVEECLRKVglwKEVYDRLNSP-ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIE 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1397 KTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNnpdRTGSFVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PRK14246 194 KLITELKNEI--AIVIVSHNPQQVARVADYVAFL---YNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
383-681 |
3.44e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.68 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTR----------KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdSHNLKD 452
Cdd:PRK15079 9 LEVADLKVHFDIKdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL-GKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 453 VNLKWW---RSKIGVVSQDPLLfsnsiknnikySLyslkdlealseesnedgfssqsdsNSRNScrakcagdLNDMIQTT 529
Cdd:PRK15079 88 MKDDEWravRSDIQMIFQDPLA-----------SL------------------------NPRMT--------IGEIIAEP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 530 dsteliqVRKNYETIEDSEVVSVSKKVLIHdfVSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSS 609
Cdd:PRK15079 125 -------LRTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 610 LDNKSEYLVqktINNLKG--NENRITII-IAHRLSTIRYantifvLSNRengstVDVDVLG---EDPTKDSNEKNEKH 681
Cdd:PRK15079 192 LDVSIQAQV---VNLLQQlqREMGLSLIfIAHDLAVVKH------ISDR-----VLVMYLGhavELGTYDEVYHNPLH 255
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1357-1431 |
3.64e-16 |
|
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: 77.47 E-value: 3.64e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIeKTIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERLF-KVIRRLRAQ-GVAVIFISHRLDEVFEiADRVTVLRD 157
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1319-1416 |
3.64e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ENATREDVKRACKFAAIDEFIESLpnqyDTnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG4178 453 EAFSDAELREALEAVGLGHLAERL----DE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527
|
90
....*....|....*...
gi 156095386 1399 IVDIKDKAdkTIITIAHR 1416
Cdd:COG4178 528 LREELPGT--TVISVGHR 543
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1275-1429 |
4.09e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.89 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1275 GKILLDGVDI--CDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG--------KENATREDVKRACKFAAIDEFIESLP 1343
Cdd:PRK14267 64 GEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFpHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQYDTNvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRS 1423
Cdd:PRK14267 144 NDYPSN-------LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARV 214
|
....*.
gi 156095386 1424 DKIVVF 1429
Cdd:PRK14267 215 SDYVAF 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
383-654 |
4.20e-16 |
|
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: 77.08 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN----DSHNLKDVnlkwW 458
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgkevSFASPRDA----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 459 RSKIGVVSQdpllfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvr 538
Cdd:cd03216 74 RAGIAMVYQ----------------------------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 539 knyetiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
250 260 270
....*....|....*....|....*....|....*...
gi 156095386 619 QKTINNLKgnENRITII-IAHRLSTI-RYANTIFVLSN 654
Cdd:cd03216 122 FKVIRRLR--AQGVAVIfISHRLDEVfEIADRVTVLRD 157
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1268-1427 |
5.05e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEnaTREDVKRACKFAA-IDEF 1338
Cdd:PRK10247 47 STLLKivaslispTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPWQ--IRNQQPDPAIFLDdLERF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 ieSLPNQ-YDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:PRK10247 125 --ALPDTiLTKNI----AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDK 198
|
170
....*....|
gi 156095386 1418 ASIKRSDKIV 1427
Cdd:PRK10247 199 DEINHADKVI 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1268-1453 |
5.59e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.85 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFKN--------SGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFG------KENATREDVKRACK 1331
Cdd:PRK13652 44 STLFRHfngilkptSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1332 FAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1411
Cdd:PRK13652 124 MLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 156095386 1412 TIAHRIASI-KRSDKIVVFNNpdrtGSFVqAQGTHEELLSVQD 1453
Cdd:PRK13652 193 FSTHQLDLVpEMADYIYVMDK----GRIV-AYGTVEEIFLQPD 230
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
825-1119 |
6.19e-16 |
|
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: 79.90 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAgglypLFALLYAKYVGTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd07346 2 LLALLLLLLAT-----ALGLALPLLTKLLIDDVIPAGDLsllLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 902 RLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGT---YFI 978
Cdd:cd07346 77 DLFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLlplYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 979 FMRVFAIRARiAANKDVEKKRvnqpgtafvynsdDEIFKdpsfLIQEAFYNMNTVIIYGLEDYFctliEKAIDYSNKGQK 1058
Cdd:cd07346 155 ILRYFRRRIR-KASREVRESL-------------AELSA----FLQESLSGIRVVKAFAAEERE----IERFREANRDLR 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1059 RKTLINSMLWGFSQSAQFFINSFA----YWFGSFLIRRGTIQVDDfmksLFTFLftgSYAGKLMS 1119
Cdd:cd07346 213 DANLRAARLSALFSPLIGLLTALGtalvLLYGGYLVLQGSLTIGE----LVAFL---AYLGMLFG 270
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
395-638 |
6.41e-16 |
|
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: 78.47 E-value: 6.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDVIINDSHNLKDVnlkwWRSKIGVVSQDPLL 471
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQ----FQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 472 FSN-SIKNNIKYSLYSlkdleALSEESNEdgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsevv 550
Cdd:cd03234 93 LPGlTVRETLTYTAIL-----RLPRKSSD--------------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 551 SVSKKVlihDFVSALPDKYETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNE 629
Cdd:cd03234 117 AIRKKR---VEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL-ARR 192
|
....*....
gi 156095386 630 NRITIIIAH 638
Cdd:cd03234 193 NRIVILTIH 201
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
402-644 |
6.54e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDVIINDS--HNLKDVNLKWWRSKIGVVSQDPllfsNS 475
Cdd:PRK15134 303 KNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQplHNLNRRQLLPVRHRIQVVFQDP----NS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 476 iknnikyslySLkdlealseesnedgfssqsdsNSRnscrakcagdLNdMIQTTDstELIQVRKNYETIEDSE--VVSVS 553
Cdd:PRK15134 374 ----------SL---------------------NPR----------LN-VLQIIE--EGLRVHQPTLSAAQREqqVIAVM 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 554 KKVLIHdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseylVQKTI-NNLKG--NEN 630
Cdd:PRK15134 410 EEVGLD---PETRHRY-------PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT----VQAQIlALLKSlqQKH 475
|
250
....*....|....*
gi 156095386 631 RIT-IIIAHRLSTIR 644
Cdd:PRK15134 476 QLAyLFISHDLHVVR 490
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
99-343 |
6.66e-16 |
|
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: 80.17 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 99 IIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNP-G---SKLTSDLDfyleQVNAGIGTK 174
Cdd:cd18542 41 LALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARtGdlmSRCTSDVD----TIRRFLAFG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 175 FITIFtYASAFLGLYIWSLFK-NARLTLCITCVFPLIYICGVICNKKV-----KINKKTSLLynnNTMsiIEEALVGIRT 248
Cdd:cd18542 117 LVELV-RAVLLFIGALIIMFSiNWKLTLISLAIIPFIALFSYVFFKKVrpafeEIREQEGEL---NTV--LQENLTGVRV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 249 VVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISDlsnqqpnndfhggsviSIL 328
Cdd:cd18542 191 VKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVING----------------EIT 254
|
250
....*....|....*..
gi 156095386 329 LGVLI--SMFMLTIILP 343
Cdd:cd18542 255 LGELVafISYLWMLIWP 271
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
383-613 |
7.32e-16 |
|
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: 78.54 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSK 461
Cdd:cd03296 3 IEVRNVSKRFGDFVALD---DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG----EDAtDVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEALSEesnedgfssqsdsnsrNSCRAKcAGDLNDMIQttdsteliqvrkn 540
Cdd:cd03296 76 VGFVFQHYALFRHmTVFDNVAFGLRVKPRSERPPE----------------AEIRAK-VHELLKLVQ------------- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 541 yetiedsevvsvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03296 126 ---------------------LDWLADRY-------PAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
381-656 |
9.04e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.37 E-value: 9.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 381 KKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRS 460
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPllfsnsiknnikyslyslkDLEALSEESNED-GFSSQSDSNSRnscrakcagdlNDMIQTTDSTELiqvrk 539
Cdd:PRK13642 82 KIGMVFQNP-------------------DNQFVGATVEDDvAFGMENQGIPR-----------EEMIKRVDEALL----- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyetiedsevvsvskKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:PRK13642 127 ---------------AVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 620 KTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGE 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1275-1450 |
9.26e-16 |
|
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: 80.54 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1275 GKILLDGVDICD----YNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKENATREDvkRACKFAAIDEF--IESLpnqyd 1347
Cdd:TIGR02142 52 GEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFpHLSVRGNLRYGMKRARPSE--RRISFERVIELlgIGHL----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1348 tnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKI 1426
Cdd:TIGR02142 125 --LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRV 202
|
170 180
....*....|....*....|....
gi 156095386 1427 VVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:TIGR02142 203 VVLED----GR-VAAAGPIAEVWA 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
383-669 |
1.05e-15 |
|
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: 78.69 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDT------RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVN 454
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 455 LKWWRSKIGVVSQDpllfsnsiknnikyslyslkdlealseesnedgfsSQSDSNSRNSCRAKCAGDLNDMiqtTDSTEL 534
Cdd:TIGR02769 83 RRAFRRDVQLVFQD-----------------------------------SPSAVNPRMTVRQIIGEPLRHL---TSLDES 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 535 IQVRKNYETIEDSEVVSvskkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:TIGR02769 125 EQKARIAELLDMVGLRS--------EDADKLP-----------RQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 615 EYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLsnrENGSTVDVDVLGED 669
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVqSFCQRVAVM---DKGQIVEECDVAQL 238
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1352-1416 |
1.18e-15 |
|
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: 76.04 E-value: 1.18e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1352 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikdkADKTIITIAHR 1416
Cdd:cd03223 87 PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHR 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1196-1428 |
1.39e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1196 AIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegADgqsstlfknSG 1275
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQ---------------------------------------------PD---------SG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1276 KILLDG--VDIcdYNLKDLRNLfSI--VSQEPMLF-NMSIYENIKFGKENATREDVKRAckfAAIDEfIESLPNQYDTNV 1350
Cdd:COG3845 61 EILIDGkpVRI--RSPRDAIAL-GIgmVHQHFMLVpNLTVAENIVLGLEPTKGGRLDRK---AARAR-IRELSERYGLDV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1351 GPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDkADKTIITIAHRIASIKR-SDKI 1426
Cdd:COG3845 134 DPDAKveDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE-ILRRLAA-EGKSIIFITHKLREVMAiADRV 211
|
..
gi 156095386 1427 VV 1428
Cdd:COG3845 212 TV 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1175-1401 |
1.44e-15 |
|
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: 77.13 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1175 SRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknan 1254
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA----------------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1255 efssskegadGQSSTLfknSGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKF----GKENATREDVKRA 1329
Cdd:COG4133 50 ----------GLLPPS---AGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKpELTVRENLRFwaalYGLRADREAIDEA 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1330 CKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:COG4133 116 LEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
403-654 |
1.56e-15 |
|
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: 79.77 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS---HNLKDVNLKWWRSKIGVVSQDPLLFSN-SIKN 478
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 479 NIKYSLyslkdlealseesnedgfsSQSDSNSRNSCRAKCagdlndmiqttdsTELIQVrknyetiedsevvsvskkvli 558
Cdd:TIGR02142 95 NLRYGM-------------------KRARPSERRISFERV-------------IELLGI--------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 559 hdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITII-IA 637
Cdd:TIGR02142 122 -----------GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLH-AEFGIPILyVS 189
|
250
....*....|....*...
gi 156095386 638 HRLSTI-RYANTIFVLSN 654
Cdd:TIGR02142 190 HSLQEVlRLADRVVVLED 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
406-611 |
1.63e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 79.62 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 406 FTLTEGKTYAFVGESGCGKSTI---LKLIERlydPTEGDVIInDSHNLKDVN---LKWWRSKIGVVSQDPllfsnsiknn 479
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYY-QGQDLLKADpeaQKLLRQKIQIVFQNP---------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 ikY-SLYSLKDLEALSEESNEdgfssqsdsnsrnscrakcagdlndmIQTTDSTeliQVRKnyetiedSEVVSVSKKV-L 557
Cdd:PRK11308 102 --YgSLNPRKKVGQILEEPLL--------------------------INTSLSA---AERR-------EKALAMMAKVgL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 156095386 558 IHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11308 144 RPEHYDRYPHMF-----------SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1164-1449 |
1.87e-15 |
|
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: 77.82 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlknDHHivfkneQTgesskeqmqqgd 1243
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG------DLP------PT------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegaDGQSSTLFknsGKILlDGVDIcdynlKDLRNLFSIVS---QEPMLFNMSIYENI---KFG 1317
Cdd:COG1119 57 --------------------YGNDVRLF---GERR-GGEDV-----WELRKRIGLVSpalQLRFPRDETVLDVVlsgFFD 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 K----ENATREDVKRAckFAAIDEF-IESLPNQydtnvgPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNS 1391
Cdd:COG1119 108 SiglyREPTDEQRERA--RELLELLgLAHLADR------PFG-TLSQGEQRRVLIARALVKDPELLILDEPTAGLDlGAR 178
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1392 EKLIEkTIVDIKDKADKTIITIAHRIASIKRS-DKIVVFnnpdRTGSfVQAQGTHEELL 1449
Cdd:COG1119 179 ELLLA-LLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLL----KDGR-VVAAGPKEEVL 231
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
830-1116 |
2.28e-15 |
|
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: 78.86 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 830 LSIMVAGGLYPLFALLYAKYVGTLFD-------------------FANLEANSNKYSLYILVIAIAMFISETLKNYYNNV 890
Cdd:cd18558 6 LCAIIHGGLLPAFMVIFGDMTDSFTNggmtnitgnssglnssagpFEKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 891 IGEKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAA 970
Cdd:cd18558 86 AAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 971 VLTGTYFIFMRVFAIRARI-AANKDVEKKRVNQPGTafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKA 1049
Cdd:cd18558 164 VILAISPVLGLSAVVWAKIlSGFTDKEKKAYAKAGA----------------VAEEVLEAFRTVIAFGGQQKEETRYAQN 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1050 IDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGK 1116
Cdd:cd18558 228 LEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQ 294
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1299-1450 |
2.30e-15 |
|
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: 79.37 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1299 VSQEPMLF-NMSIYENIKFGKENATREDvkRACKFAAIDEF--IESLPNQYDTNvgpygksLSGGQKQRIAIARALLREP 1375
Cdd:COG4148 82 VFQEARLFpHLSVRGNLLYGRKRAPRAE--RRISFDEVVELlgIGHLLDRRPAT-------LSGGERQRVAIGRALLSSP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1376 KILLLDEATSSLD--SNSEKL--IEKtivdIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:COG4148 153 RLLLMDEPLAALDlaRKAEILpyLER----LRDELDIPILYVSHSLDEVARlADHVVLLEQ----GR-VVASGPLAEVLS 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1164-1428 |
2.58e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.33 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYK----DLTFSCESKKTTAIVGETGSGKSTvmslLMRFYDlkndhhivfkneqtgesskeqm 1239
Cdd:PRK13641 3 IKFENVDYIY--SPGTPMEKkgldNISFELEEGSFVALVGHTGSGKST----LMQHFN---------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 qqgdeeqnvgmknanefssskegadgqsSTLFKNSGKILLDGVDIC----DYNLKDLRNLFSIVSQ--EPMLFNMSIYEN 1313
Cdd:PRK13641 55 ----------------------------ALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQfpEAQLFENTVLKD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1314 IKFGKEN--ATREDVK-RACKFAAIDEFIESLPNQydtnvGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:PRK13641 107 VEFGPKNfgFSEDEAKeKALKWLKKVGLSEDLISK-----SPF--ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 1391 SEKLIEKTIVDIKdKADKTIITIAHRIASI-KRSDKIVV 1428
Cdd:PRK13641 180 GRKEMMQLFKDYQ-KAGHTVILVTHNMDDVaEYADDVLV 217
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1273-1459 |
3.11e-15 |
|
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: 76.81 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFAA-IDEF-IESLPNQYdt 1348
Cdd:cd03218 53 DSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEElLEEFhITHLRKSK-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1349 nvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT---------IAHRiAS 1419
Cdd:cd03218 131 -----ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdhnvretlsITDR-AY 204
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 156095386 1420 IKRSDKIVvfnnpdrtgsfvqAQGTHEELLSVQDgVYKKY 1459
Cdd:cd03218 205 IIYEGKVL-------------AEGTPEEIAANEL-VRKVY 230
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
825-1109 |
3.54e-15 |
|
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: 77.85 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLYPLFALLyakyVGTLFDfaNLEANSNKYSLYILVIAI-AMF----ISETLKNYYNNVIGEKVEKTM 899
Cdd:cd18552 1 LALAILGMILVAATTAALAWL----LKPLLD--DIFVEKDLEALLLVPLAIiGLFllrgLASYLQTYLMAYVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 900 KLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP---IVAAVLTGTY 976
Cdd:cd18552 75 RNDLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWkltLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 977 FIFMRVFAIRARIAANKdvekkrvNQPGTAFVYNsddeifkdpsfLIQEAFYNMNTVIIYGLEDY----FCTLIEKAIDY 1052
Cdd:cd18552 153 ALPIRRIGKRLRKISRR-------SQESMGDLTS-----------VLQETLSGIRVVKAFGAEDYeikrFRKANERLRRL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1053 SNKGQKRKTLINSMlwgfSQsaqfFINSFA----YWFGSFLIRRGTIQVDDFMkSLFTFLF 1109
Cdd:cd18552 215 SMKIARARALSSPL----ME----LLGAIAialvLWYGGYQVISGELTPGEFI-SFITALL 266
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1184-1428 |
3.63e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 78.62 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEQTgesskeqmqqgdeeqnvgmknanefssskega 1263
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE------------EPT-------------------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 dgqsstlfknSGKILLDGVDICDYNLKDLRNL---FSIVSQEPM--LfN--MSIYENIKFGKENATREDVkrackfAAID 1336
Cdd:COG4608 72 ----------SGEILFDGQDITGLSGRELRPLrrrMQMVFQDPYasL-NprMTVGDIIAEPLRIHGLASK------AERR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1337 EFIESL-------PNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SnseklIEKTIV----DIKD 1404
Cdd:COG4608 135 ERVAELlelvglrPEHADR----YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvS-----IQAQVLnlleDLQD 205
|
250 260
....*....|....*....|....*
gi 156095386 1405 KADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:COG4608 206 ELGLTYLFISHDLSVVRHiSDRVAV 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
383-611 |
4.35e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.92 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnLKDVNLKwwRSKI 462
Cdd:PRK11000 4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR-MNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmiqtTDSTElIQVRKNy 541
Cdd:PRK11000 78 GMVFQSYALYPHlSVAENMSFGL--------------------------------KLAG--------AKKEE-INQRVN- 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etiEDSEVVSvskkvLIHdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11000 116 ---QVAEVLQ-----LAH------------LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1268-1417 |
4.51e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.20 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFKN--------SGKILLDGVDIcDYNLKDLRNL---FSIVSQEP--MLFNMSIYENIKFG------KENATREDVKR 1328
Cdd:PRK13636 46 STLFQNlngilkpsSGRILFDGKPI-DYSRKGLMKLresVGMVFQDPdnQLFSASVYQDVSFGavnlklPEDEVRKRVDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAAIdEFIESLPNQYdtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADK 1408
Cdd:PRK13636 125 ALKRTGI-EHLKDKPTHC----------LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGL 193
|
....*....
gi 156095386 1409 TIITIAHRI 1417
Cdd:PRK13636 194 TIIIATHDI 202
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1153-1443 |
5.55e-15 |
|
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: 80.72 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1153 KIKNSNDIKGKIEIMD-VNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqt 1231
Cdd:TIGR01271 412 KIKQNNKARKQPNGDDgLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM------------------ 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1232 GESskeqmqqgdeeqnvgmknanefssskEGADGQsstlFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLFNMSIY 1311
Cdd:TIGR01271 474 GEL--------------------------EPSEGK----IKHSGRI-------------------SFSPQTSWIMPGTIK 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1312 ENIKFG--KENATREDVKRACKfaaIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:TIGR01271 505 DNIIFGlsYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1390 NSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFNNPDR--TGSFVQAQG 1443
Cdd:TIGR01271 582 VTEKEIFESCL-CKLMSNKTRILVTSKLEHLKKADKILLLHEGVCyfYGTFSELQA 636
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
383-661 |
6.90e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.71 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVE--IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVNLKW 457
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtliTSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 458 WRSKIGVVSQDP--LLFSNSIknnikyslysLKDLealseesnedGFSSQSDSNSRnscrakcagdlndmiqttdsteli 535
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETV----------LKDV----------AFGPQNFGVSQ------------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 536 qvrknyetiEDSEVVSVSKKVLIHdfVSalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK13649 119 ---------EEAEALAREKLALVG--IS------ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 156095386 616 YLVQKTINNLkgNENRITIIIAHRL--STIRYANTIFVLsnrENGSTV 661
Cdd:PRK13649 182 KELMTLFKKL--HQSGMTIVLVTHLmdDVANYADFVYVL---EKGKLV 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
385-654 |
7.24e-15 |
|
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: 74.51 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 385 FKNVRF---HYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDVIINDshnlKDVNLKWWR 459
Cdd:cd03213 6 FRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING----RPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQDPLLFSN-SIKNNIKYSlyslkdlealseesnedgfssqsdsnsrnscrAKCAGdlndmiqttdsteliqvr 538
Cdd:cd03213 82 KIIGYVPQDDILHPTlTVRETLMFA--------------------------------AKLRG------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 539 knyetiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:cd03213 112 -----------------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
250 260 270
....*....|....*....|....*....|....*...
gi 156095386 619 QKTINNLkGNENRITIIIAHRLSTIRYA--NTIFVLSN 654
Cdd:cd03213 151 MSLLRRL-ADTGRTIICSIHQPSSEIFElfDKLLLLSQ 187
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1268-1398 |
7.27e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.28 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICdyNLKDLR--NLFSIVSQEPML---FNMSIYENI----KFGKenatREDVKRAC 1330
Cdd:COG1101 46 STLLNaiagslppDSGSILIDGKDVT--KLPEYKraKYIGRVFQDPMMgtaPSMTIEENLalayRRGK----RRGLRRGL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1331 KFAAIDEFIES-------LPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIEKT 1398
Cdd:COG1101 120 TKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpKTAALVLELT 191
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
383-652 |
8.33e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.66 E-value: 8.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHY-DTRKDVEIY--KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWR 459
Cdd:PRK13633 5 IKCKNVSYKYeSNEESTEKLalDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQDPllfSNSIknnikyslyslkdLEALSEEsnEDGFssqsdsnsrnscrakcaGDLNDMIQTtdstELIQVRk 539
Cdd:PRK13633 85 NKAGMVFQNP---DNQI-------------VATIVEE--DVAF-----------------GPENLGIPP----EEIRER- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyetIEDSevvsvSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:PRK13633 125 ----VDES-----LKKVGMYEYRRHAP-----------HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 620 KTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:PRK13633 185 NTIKELNKKYGITIILITHYMEEAVEADRIIVM 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-1420 |
1.00e-14 |
|
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: 79.95 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 340 IILPNITEYMKslEATNNLYEIINrkplvENNQDGKKLKDIKKIQFKNVRFHYdtrkdVEIYKDLNFTLTEGKTYAFVGE 419
Cdd:TIGR01271 393 VEMVNVTASWD--EGIGELFEKIK-----QNNKARKQPNGDDGLFFSNFSLYV-----TPVLKNISFKLEKGQLLAVAGS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 420 SGCGKSTILKLIERLYDPTEGDViindSHNlkdvnlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealseesne 499
Cdd:TIGR01271 461 TGSGKSSLLMMIMGELEPSEGKI----KHS----------GRISFSPQTSWIMPGTIKDNIIFGL--------------- 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 500 dgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyeTIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASK 579
Cdd:TIGR01271 512 -------------------------------------------SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGIT 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY-LVQKTINNLKGNENRItiIIAHRLSTIRYANTIFVLSNREN- 657
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRI--LVTSKLEHLKKADKILLLHEGVCy 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 658 --GSTVDVDvlGEDPTKDSNEKNEKHDKQEKGGKNSS---------ANQKIGNAGSYI------IEQGTHDALMKNKNGI 720
Cdd:TIGR01271 627 fyGTFSELQ--AKRPDFSSLLLGLEAFDNFSAERRNSiltetlrrvSIDGDSTVFSGPetikqsFKQPPPEFAEKRKQSI 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 721 YYTMINNQKVSSKSSSNNDNDKDSDMKSSIYKDSERGYD--PDEANGNAKNESASAKKSEKMSDAK--------ASNTNA 790
Cdd:TIGR01271 705 ILNPIASARKFSFVQMGPQKAQATTIEDAVREPSERKFSlvPEDEQGEESLPRGNQYHHGLQHQAQrrqsvlqlMTHSNR 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 791 G-GRLAFLRNLFKRKPKAP-----------------------------------------NNLRVV------YREIFSYK 822
Cdd:TIGR01271 785 GeNRREQLQTSFRKKSSITqqnelaseldiysrrlskdsvyeiseeineedlkecfaderENVFETttwntyLRYITTNR 864
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 823 KDIAIIALSIM-----VAGGLYPLFaLLYAKYVGTLFDFANLEANSNKYSLYilviaiAMFISETLKNYYNNVIGEKVEK 897
Cdd:TIGR01271 865 NLVFVLIFCLViflaeVAASLLGLW-LITDNPSAPNYVDQQHANASSPDVQK------PVIITPTSAYYIFYIYVGTADS 937
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 898 TMKLRLFENI-MYQEISFFDQDSHAPGLLS------AHINRdvhlLKTGLVNN--------------IVIFThFIVLFL- 955
Cdd:TIGR01271 938 VLALGFFRGLpLVHTLLTVSKRLHEQMLHSvlqapmAVLNT----MKAGRILNrftkdmaiiddmlpLTLFD-FIQLTLi 1012
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 956 ------VSTVMSFYFcpIVAAVLTGTYFIFMRVFAIRAriaankDVEKKRVNQPGTAFVYnsddeifkdpSFLIQeAFYN 1029
Cdd:TIGR01271 1013 vlgaifVVSVLQPYI--FIAAIPVAVIFIMLRAYFLRT------SQQLKQLESEARSPIF----------SHLIT-SLKG 1073
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1030 MNTVIIYGLEDYFCTLIEKAIDysnkgqkrktlINSMLWgfsqsaqFFINSFAYWFgsfLIRRGTIQVDDFMKSLF-TFL 1108
Cdd:TIGR01271 1074 LWTIRAFGRQSYFETLFHKALN-----------LHTANW-------FLYLSTLRWF---QMRIDIIFVFFFIAVTFiAIG 1132
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1109 FTGSYAGKL-------MSLKG----------DSENAKLSFERYYPLITRKSLIDVRDNGGIKIKNSNDI----------- 1160
Cdd:TIGR01271 1133 TNQDGEGEVgiiltlaMNILStlqwavnssiDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKYQLSTVLvienphaqkcw 1212
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1161 --KGKIEIMDVNFRYLSRPNVpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeq 1238
Cdd:TIGR01271 1213 psGGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR------------------------ 1267
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1239 mqqgdeeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGK 1318
Cdd:TIGR01271 1268 -------------------------------LLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PY 1315
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:TIGR01271 1316 EQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKT 1395
|
1210 1220
....*....|....*....|..
gi 156095386 1399 IVdiKDKADKTIITIAHRIASI 1420
Cdd:TIGR01271 1396 LK--QSFSNCTVILSEHRVEAL 1415
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1174-1428 |
1.10e-14 |
|
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: 74.12 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1174 LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmkna 1253
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA---------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1254 nefssskegadGQSSTLfKNSGKILLDGVDIcdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGkenatredvkrackf 1332
Cdd:cd03213 57 -----------GRRTGL-GVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHpTLTVRETLMFA--------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1333 AAIdefieslpnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIIT 1412
Cdd:cd03213 107 AKL-------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG-RTIIC 166
|
250
....*....|....*...
gi 156095386 1413 IAHRIAS--IKRSDKIVV 1428
Cdd:cd03213 167 SIHQPSSeiFELFDKLLL 184
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
383-644 |
1.10e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 75.43 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH-----NLKDVNLKW 457
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 458 WRSKIGVVSQdpllfsnsiknniKYSLYS-LKDLEALSEesnedgfssqsdsnsrnscrAKCagdlndmiqttdsteliQ 536
Cdd:COG4161 80 LRQKVGMVFQ-------------QYNLWPhLTVMENLIE--------------------APC-----------------K 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 537 VRKNYETIEDSEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:COG4161 110 VLGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
250 260
....*....|....*....|....*....
gi 156095386 617 LVQKTINNLKGNEnrIT-IIIAHRLSTIR 644
Cdd:COG4161 179 QVVEIIRELSQTG--ITqVIVTHEVEFAR 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
402-626 |
1.34e-14 |
|
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: 74.78 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDV---------NLKwwRSKIGVVSQ----- 467
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLaqaspreilALR--RRTIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 468 ----------DPLLfsnsiknnikyslyslkdlealseesnEDGFSsqsdsnsRNSCRAKcAGDLndmiqttdsteLIQV 537
Cdd:COG4778 106 prvsaldvvaEPLL---------------------------ERGVD-------REEARAR-AREL-----------LARL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 538 RknyetiedsevvsvskkvlihdfvsaLPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG4778 140 N--------------------------LP---ERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAV 190
|
....*....
gi 156095386 618 VQKTINNLK 626
Cdd:COG4778 191 VVELIEEAK 199
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
396-643 |
1.39e-14 |
|
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: 74.18 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShnlKDVNLKWWRSKIGVVSQDPLLFSNs 475
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---SYQKNIEALRRIGALIEAPGFYPN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 476 iknnikyslyslkdleaLSEEsnedgfssqsdSNSRNSCRAKcagdlndmiqttdsteliqvrknyeTIEDSEVVSVSKK 555
Cdd:cd03268 87 -----------------LTAR-----------ENLRLLARLL-------------------------GIRKKRIDEVLDV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 556 VLIHDfvsaLPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnrITII 635
Cdd:cd03268 114 VGLKD----SAKK-------KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG--ITVL 180
|
....*....
gi 156095386 636 IA-HRLSTI 643
Cdd:cd03268 181 ISsHLLSEI 189
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
580-664 |
1.59e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN-LKGnenrITII-IAHRLSTIRYANTIFVLSNREN 657
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPG----TTVIsVGHRSTLAAFHDRVLELTGDGS 561
|
....*..
gi 156095386 658 GSTVDVD 664
Cdd:COG4178 562 WQLLPAE 568
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1268-1411 |
1.78e-14 |
|
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: 74.48 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLF-NMSIYENIKFGKENATREDVKrackfaaIDE 1337
Cdd:TIGR03410 40 TTLLKtlmgllpvKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFpRLTVEENLLTGLAALPRRSRK-------IPD 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1338 FIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1411
Cdd:TIGR03410 113 EIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAIL 186
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1164-1449 |
1.82e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.73 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4604 2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR----------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqssTLFKNSGKILLDGVDICDYNLKDL-RNLfSIVSQEPMlFNM--SIYENIKFG--- 1317
Cdd:COG4604 50 -------------------------LLPPDSGEVLVDGLDVATTPSRELaKRL-AILRQENH-INSrlTVRELVAFGrfp 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 --KENATREDVkrackfAAIDEFI-----ESLPNQY-DTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:COG4604 103 ysKGRLTAEDR------EIIDEAIayldlEDLADRYlDE--------LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1390 NSEKLIEKTIVDIKDKADKTIITIAHRI--ASiKRSDKIVVFNNpdrtGSfVQAQGTHEELL 1449
Cdd:COG4604 169 KHSVQMMKLLRRLADELGKTVVIVLHDInfAS-CYADHIVAMKD----GR-VVAQGTPEEII 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1184-1417 |
1.96e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.04 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKSTvmsLLMRFYDLKndhhivfkneqtgESSKEQMQQGDeeqnvgMKNANEFssskega 1263
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKST---LVTHFNGLI-------------KSKYGTIQVGD------IYIGDKK------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 DGQSSTLFKNSGKIlldgvdicdYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN--ATREDVKRACKFaaideFI 1339
Cdd:PRK13631 95 NNHELITNPYSKKI---------KNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVAlgVKKSEAKKLAKF-----YL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1340 ESLPNQYD-TNVGPYGksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRI 1417
Cdd:PRK13631 161 NKMGLDDSyLERSPFG--LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTM 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
383-656 |
2.03e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN------DSHNLKDVnlk 456
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikyDKKSLLEV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 457 wwRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdleaLSEESNEDgfssqsdsnsrnscRAKCAgdlndmiqttdstel 534
Cdd:PRK13639 77 --RKTVGIVFQNPddQLFAPTVEEDVAFGPLNLG----LSKEEVEK--------------RVKEA--------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 535 iqvrknyetiedsevvsvSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK13639 122 ------------------LKAVGMEGFENKPP-----------HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 156095386 615 EYLVQKTINNLkgNENRITIIIA-HRLSTI-RYANTIFVLSNRE 656
Cdd:PRK13639 173 ASQIMKLLYDL--NKEGITIIIStHDVDLVpVYADKVYVMSDGK 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
383-649 |
2.24e-14 |
|
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: 73.67 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWwRSKI 462
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-EPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSNsiknnikyslysLKDLEALSeesnedgFSSQSDSNSRNscrakcAGDLNDMIQTTDSTELIQVRknye 542
Cdd:COG4133 78 AYLGHADGLKPE------------LTVRENLR-------FWAALYGLRAD------REAIDEALEAVGLAGLADLP---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:COG4133 129 ----------------------------------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
250 260
....*....|....*....|....*..
gi 156095386 623 NNLKGNeNRITIIIAHRLSTIRYANTI 649
Cdd:COG4133 175 AAHLAR-GGAVLLTTHQPLELAAARVL 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1273-1448 |
2.56e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.28 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLKDLRNLFsiVSQEPMLF-NMSIYENIKFG------KENATREDVKRacKFAAIDEFI--ESLP 1343
Cdd:PRK10851 55 TSGHIRFHGTDVSRLHARDRKVGF--VFQHYALFrHMTVFDNIAFGltvlprRERPNAAAIKA--KVTQLLEMVqlAHLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQYDTNvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKR 1422
Cdd:PRK10851 131 DRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHdQEEAMEV 203
|
170 180
....*....|....*....|....*.
gi 156095386 1423 SDKIVVFNNpdrtGSFVQAqGTHEEL 1448
Cdd:PRK10851 204 ADRVVVMSQ----GNIEQA-GTPDQV 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1164-1431 |
2.56e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.77 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTvmsLLMRFydlkNDHHIVfkneqtgesskeqmQQGd 1243
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHL----NGIYLP--------------QRG- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknsgKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENA 1321
Cdd:PRK13647 61 --------------------------------RVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAFGPVNM 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 --TREDVKR----ACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK13647 109 glDKDEVERrveeALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 1396 eKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1431
Cdd:PRK13647 178 -MEILDRLHNQGKTVIVATHDVdLAAEWADQVIVLKE 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
371-611 |
2.86e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.91 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 371 NQDGKKLKDIKKiqfknvRFHYDTRKDveiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNL 450
Cdd:PRK11432 3 QKNFVVLKNITK------RFGSNTVID-----NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 451 KDVNLKwwRSKIGVVSQDPLLFSN-SIKNNIKyslYSLKDLEALSEESNEdgfssqsdsnsrnscRAKCAGDLNDMiqtt 529
Cdd:PRK11432 71 THRSIQ--QRDICMVFQSYALFPHmSLGENVG---YGLKMLGVPKEERKQ---------------RVKEALELVDL---- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 530 dsteliqvrknyETIEDSEVvsvskkvlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSS 609
Cdd:PRK11432 127 ------------AGFEDRYV----------------------------DQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
..
gi 156095386 610 LD 611
Cdd:PRK11432 167 LD 168
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
383-652 |
3.14e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.06 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVE---IYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVNLK 456
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErraLY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErviTAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 457 WWRSKIGVVSQDP--LLFSNSIknnikyslysLKDLealseesnedgfssqsdsnsrnscrakCAGDLNDMIQTTDSTel 534
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETV----------EKDI---------------------------CFGPMNFGVSEEDAK-- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 535 iqvRKNYETIedsEVVSVSKKVLIHD-FvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK13634 123 ---QKAREMI---ELVGLPEELLARSpF-----------------ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 156095386 614 SEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAaRYADQIVVM 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
383-611 |
3.67e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.64 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRkdveiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNlkwwRSK 461
Cdd:COG3840 2 LRLDDLTYRYGDF-----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPPA----ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIkyslyslkdleALseesnedGFSSqsdsnsrnSCRakcagdLNDmiqttdsteliqvrkn 540
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNI-----------GL-------GLRP--------GLK------LTA---------------- 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 541 yetIEDSEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG3840 105 ---EQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1275-1450 |
3.92e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.23 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1275 GKILLDGVDICDYNLKDLRNL----FSIVSQE-PMLFNMSIYENIKFGKENA------TREDVKRACKFAAIDEFIESLP 1343
Cdd:PRK10070 83 GQVLIDGVDIAKISDAELREVrrkkIAMVFQSfALMPHMTVLDNTAFGMELAginaeeRREKALDALRQVGLENYAHSYP 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR- 1422
Cdd:PRK10070 163 DE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRi 231
|
170 180
....*....|....*....|....*...
gi 156095386 1423 SDKIVVFNNpdrtGSFVQAqGTHEELLS 1450
Cdd:PRK10070 232 GDRIAIMQN----GEVVQV-GTPDEILN 254
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1262-1448 |
4.31e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1262 GADG-QSSTLFK--------NSGKILLDGVDICDynLKDLRNLFSIVSQEPMLF-NMSIYENIKFG------KENATRED 1325
Cdd:PRK11607 52 GASGcGKSTLLRmlagfeqpTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMTVEQNIAFGlkqdklPKAEIASR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1326 VKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1405
Cdd:PRK11607 130 VNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILER 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 156095386 1406 ADKTIITIAH-RIASIKRSDKIVVFNNpdrtGSFVQAqGTHEEL 1448
Cdd:PRK11607 199 VGVTCVMVTHdQEEAMTMAGRIAIMNR----GKFVQI-GEPEEI 237
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1268-1447 |
4.83e-14 |
|
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: 73.92 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDLRNL-----FsivsQEPMLF-NMSIYENIKFG---------------- 1317
Cdd:COG0411 44 TTLFNlitgfyrpTSGRILFDGRDITGLPPHRIARLgiartF----QNPRLFpELTVLENVLVAaharlgrgllaallrl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -----KENATREDVKRACKFAAIDEFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-S 1391
Cdd:COG0411 120 prarrEEREARERAEELLERVGLADRADEPA-----------GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeT 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1392 EKLIEkTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEE 1447
Cdd:COG0411 189 EELAE-LIRRLRDERGITILLIEHDMDLVMGlADRIVVLDF----GR-VIAEGTPAE 239
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1164-1458 |
5.07e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.72 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRY------LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesske 1237
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKML------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1238 qmqqgdeeqnVGMknanefssskegadgQSSTlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPmlfNMSIYENIKFG 1317
Cdd:COG4167 60 ----------AGI---------------IEPT----SGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTSLNPRLNIG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -------KENATREDVKRACKFAAIDEFIESLPNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:COG4167 108 qileeplRLNTDLTAEEREERIFATLRLVGLLPEHANF----YPHMLSSGQKQRVALARALILQPKIIIADEALAALDMS 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1391 SEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAQGTHEELLSVQDGVYKK 1458
Cdd:COG4167 184 VRSQIINLMLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQ----GEVVEYGKTAEVFANPQHEVTKR 248
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1164-1448 |
5.40e-14 |
|
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: 72.92 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqTGEsskeqmqqgd 1243
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML------------------TGE---------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKF-----G 1317
Cdd:cd03263 52 --------------------------LRPTSGTAYINGYSI-RTDRKAARQSLGYCPQFDALFdELTVREHLRFyarlkG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KENATREDVkrackfaaIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:cd03263 105 LPKSEIKEE--------VELLLRvlGLTDKANKRA----RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAI 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1396 EKTIVDIkdKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEEL 1448
Cdd:cd03263 173 WDLILEV--RKGRSIILTTHSMDEAEAlCDRIAIMSD----GK-LRCIGSPQEL 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1147-1450 |
5.48e-14 |
|
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: 74.12 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1147 RDNGGIKIKNSNDikgkieimDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivf 1226
Cdd:cd03291 26 QENNDRKHSSDDN--------NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLIL------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1227 kneqtgesskeqmqqGDEEQnvgmknanefssskegadgqSSTLFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLF 1306
Cdd:cd03291 85 ---------------GELEP--------------------SEGKIKHSGRI-------------------SFSSQFSWIM 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1307 NMSIYENIKFG--KENATREDVKRACKfaaIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEAT 1384
Cdd:cd03291 111 PGTIKENIIFGvsYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1385 SSLDSNSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFNNPDR--TGSFVQAQGTHEELLS 1450
Cdd:cd03291 188 GYLDVFTEKEIFESCV-CKLMANKTRILVTSKMEHLKKADKILILHEGSSyfYGTFSELQSLRPDFSS 254
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1268-1431 |
5.50e-14 |
|
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: 72.61 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK-NSGKILLDGVDICDYNLKdLRNLFSIVSQEPMLF-NMSIYENIKF----GKENATREDvkrackfAAIDEFIEs 1341
Cdd:cd03264 46 ATLTPpSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYpNFTVREFLDYiawlKGIPSKEVK-------ARVDEVLE- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1342 lpnqyDTNVGPYGK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRI 1417
Cdd:cd03264 117 -----LVNLGDRAKkkigSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIV 189
|
170
....*....|....*
gi 156095386 1418 ASIKRS-DKIVVFNN 1431
Cdd:cd03264 190 EDVESLcNQVAVLNK 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1181-1431 |
6.59e-14 |
|
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: 72.69 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1181 IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLM-RFYDLKNDHHIVFKNEQtgESSKEQMQqgdeeqnvgmknanefsss 1259
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgRVEGGGTTSGQILFNGQ--PRKPDQFQ------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1260 kegadgqsstlfknsgkilldgvDICDYNLKDLRNLFSIVSQEPMLFnmsiYENIKFGKENATREDVKRACkfaaidefI 1339
Cdd:cd03234 81 -----------------------KCVAYVRQDDILLPGLTVRETLTY----TAILRLPRKSSDAIRKKRVE--------D 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1340 ESLPNQYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRia 1418
Cdd:cd03234 126 VLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA-RRNRIVILTIHQ-- 202
|
250
....*....|...
gi 156095386 1419 siKRSDKIVVFNN 1431
Cdd:cd03234 203 --PRSDLFRLFDR 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
383-663 |
8.00e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.82 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNLKWWRSK 461
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSNsiknnikyslyslkdLEALSeesnedgfssqsdsnsrnscrakcagdlNDMIQTtdstelIQVRKny 541
Cdd:PRK09493 79 AGMVFQQFYLFPH---------------LTALE----------------------------NVMFGP------LRVRG-- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etiedsevvsvSKKVLIHDFVSALPDKyetlVGSNA------SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK09493 108 -----------ASKEEAEKQARELLAK----VGLAErahhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 156095386 616 YLVQKTINNLkGNENRITIIIAHRLSTIRYANT--IFVLSNR--ENGSTVDV 663
Cdd:PRK09493 173 HEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASrlIFIDKGRiaEDGDPQVL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1183-1432 |
8.73e-14 |
|
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: 75.88 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskeg 1262
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLR------------------------------------------------ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstLFKNSGKILLDGVDICDYNLKDLRNL---FSIVSQEPM-LFN--MSIYENI-------KFGKENATREDvkRA 1329
Cdd:COG4172 335 -------LIPSEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDPFgSLSprMTVGQIIaeglrvhGPGLSAAERRA--RV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1330 CkfAAIDEfieslpnqydtnVG--P-----YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDsnseKLIEKTIVDI 1402
Cdd:COG4172 406 A--EALEE------------VGldPaarhrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILDL 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1403 -KDKADKT-----IIT--------IAHRIASIKRSdKIV-------VFNNP 1432
Cdd:COG4172 468 lRDLQREHglaylFIShdlavvraLAHRVMVMKDG-KVVeqgpteqVFDAP 517
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
402-673 |
8.98e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.07 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKW-WRSKIGVVSQDPLLFSN-SIK 477
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIAKISDAELREvRRKKIAMVFQSFALMPHmTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 478 NNIKYSLyslkDLEALSEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsEVVSVSKKVL 557
Cdd:PRK10070 125 DNTAFGM----ELAGINAEERRE-----------------------------------------------KALDALRQVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 558 IHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
Cdd:PRK10070 154 LENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFIS 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 638 HRL-STIRYANTIFVLSNRENGSTVDVDVLGEDPTKD 673
Cdd:PRK10070 223 HDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1270-1388 |
1.21e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.92 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1270 LFKNSGKILLDGVDiCDYNLKDLRNLfSIVSQEPMLFN-MSIYENIKFG-----KENAT-REDVKRACKFAAIDEFIESL 1342
Cdd:PRK10771 49 LTPASGSLTLNGQD-HTTTPPSRRPV-SMLFQENNLFShLTVAQNIGLGlnpglKLNAAqREKLHAIARQMGIEDLLARL 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 156095386 1343 PNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK10771 127 PGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1171-1428 |
1.78e-13 |
|
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: 71.24 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1171 FRYLSRPNVPIyKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgm 1250
Cdd:cd03266 11 FRDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRML-------------------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1251 knanefssskegadgqsSTLFK-NSGKILLDGVDICDYNLKDLRNLfSIVSQEPMLFN-MSIYENIKFgkeNATREDVKR 1328
Cdd:cd03266 52 -----------------AGLLEpDAGFATVDGFDVVKEPAEARRRL-GFVSDSTGLYDrLTARENLEY---FAGLYGLKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAAIDEFIESLpnqydtNVGPY----GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:cd03266 111 DELTARLEELADRL------GMEELldrrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA 184
|
250 260
....*....|....*....|....*
gi 156095386 1405 kADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03266 185 -LGKCILFSTHIMQEVERlCDRVVV 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1273-1418 |
2.05e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.66 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLKD--LRNLFSIVSQEPMLF-NMSIYENIKFGKENatredVKRACKFAAIDEFIESLpnqydTN 1349
Cdd:PRK09493 54 TSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQFYLFpHLTALENVMFGPLR-----VRGASKEEAEKQARELL-----AK 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1350 VG------PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIA 1418
Cdd:PRK09493 124 VGlaerahHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP---ELRHEVLKVMQDLAEEgmTMVIVTHEIG 197
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
383-654 |
2.36e-13 |
|
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: 70.77 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVnlkwwRSKI 462
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSN-SIKNNIKY--SLYSLKDLEALSEesnedgfssqsdsnsrnscrakcagdlndmiqttdSTELIqvrK 539
Cdd:cd03269 73 GYLPEERGLYPKmKVIDQLVYlaQLKGLKKEEARRR-----------------------------------IDEWL---E 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 NYEtIEDSEvvsvSKKVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:cd03269 115 RLE-LSEYA----NKRV---------------------EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168
|
250 260 270
....*....|....*....|....*....|....*.
gi 156095386 620 KTINNLKGNENRItIIIAHRLSTI-RYANTIFVLSN 654
Cdd:cd03269 169 DVIRELARAGKTV-ILSTHQMELVeELCDRVLLLNK 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
383-652 |
2.38e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.17 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEI--YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH---NLKDVNLKW 457
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 458 WRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLkdlealseesnedGFSSQsdsnsrnscRAKcagdlndmiqttdsteli 535
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEFGPKNF-------------GFSED---------EAK------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 536 qvrknyetiedSEVVSVSKKVlihdfvsALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK13641 123 -----------EKALKWLKKV-------GLS---EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
250 260 270
....*....|....*....|....*....|....*...
gi 156095386 616 YLVQKTINNLKgNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK13641 182 KEMMQLFKDYQ-KAGHTVILVTHNMDDVaEYADDVLVL 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1164-1419 |
3.55e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRFYDLkndhhivFKNEQTGESSKEQmqqgd 1243
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSS----LLRVLNL-------LEMPRSGTLNIAG----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknaNEFSSSKEGADGQSSTLFKNSGKILLDgvdicdYNLkdlrnlfsivsqEPmlfNMSIYENI--------K 1315
Cdd:PRK11124 64 ----------NHFDFSKTPSDKAIRELRRNVGMVFQQ------YNL------------WP---HLTVQQNLieapcrvlG 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 FGKENAtredVKRACKFAA---IDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNse 1392
Cdd:PRK11124 113 LSKDQA----LARAEKLLErlrLKPYADRFPLH-----------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE-- 175
|
250 260 270
....*....|....*....|....*....|....*.
gi 156095386 1393 klIEKTIVDIKDKADKTIIT---------IAHRIAS 1419
Cdd:PRK11124 176 --ITAQIVSIIRELAETGITqvivtheveVARKTAS 209
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
580-657 |
3.56e-13 |
|
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: 69.10 E-value: 3.56e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnenrITII-IAHRLSTIRYANTIFVLSNREN 657
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG-----ITVIsVGHRPSLWKFHDRVLDLDGEGG 165
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1268-1462 |
3.94e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 71.26 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLF--------KNSGKILLDGVDIcDYNLKDL---RNLFSIVSQEP--MLFNMSIYENIKFG------KENATREDVKR 1328
Cdd:PRK13639 42 STLFlhfngilkPTSGEVLIKGEPI-KYDKKSLlevRKTVGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdK 1408
Cdd:PRK13639 121 ALKAVGMEGFENKPPHH-----------LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-I 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1409 TIITIAHRIASI-KRSDKIVVFNNpdrtGSFVqAQGTHEELLSVQDGVYKKYVKL 1462
Cdd:PRK13639 189 TIIISTHDVDLVpVYADKVYVMSD----GKII-KEGTPKEVFSDIETIRKANLRL 238
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1271-1450 |
4.42e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1271 FKNSGKILLDGVDICDY-NLKDLRNLFSIVSQEPMLFNMSIYENIKFGKenatredvkRACKFAAIDEFiESLPNQYDTN 1349
Cdd:PRK14271 77 YRYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGV---------RAHKLVPRKEF-RGVAQARLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1350 VGPYGK----------SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIAS 1419
Cdd:PRK14271 147 VGLWDAvkdrlsdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQ 224
|
170 180 190
....*....|....*....|....*....|..
gi 156095386 1420 IKR-SDKIVVFNNpdrtGSFVQaQGTHEELLS 1450
Cdd:PRK14271 225 AARiSDRAALFFD----GRLVE-EGPTEQLFS 251
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
402-611 |
6.79e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS--HNLKDVNLKWWRSKIGVVSQDPLlfsnsiknn 479
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplAKLNRAQRKAFRRDIQMVFQDSI--------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 ikyslyslkdlealseesnedgfssqSDSNSRNSCRAKCAGDLNDMIQTTDSTELIQVRKNYETIEdsevvsvskkvLIH 559
Cdd:PRK10419 100 --------------------------SAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVD-----------LDD 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 156095386 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10419 143 SVLDKRP-----------PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1176-1452 |
7.38e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1176 RPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEQTG-ESSKEQMqqgdeeqnvgmknan 1254
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLL------------EQAGgLVQCDKM--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1255 efssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNL-FSIVSQEPM-----LFNM--SIYENIK----FGKENAT 1322
Cdd:PRK10261 79 ---------------LLRRRSRQVIELSEQSAAQMRHVRGAdMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREEAM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REdVKRACKFAAIDEfieslpnqYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:PRK10261 144 VE-AKRMLDQVRIPE--------AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVL 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 156095386 1403 KDKADKTIITIAHriasikrsDKIVVFNNPDRTgsFVQAQGTHEELLSVQ 1452
Cdd:PRK10261 215 QKEMSMGVIFITH--------DMGVVAEIADRV--LVMYQGEAVETGSVE 254
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1177-1450 |
8.62e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1177 PNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkNEQTGEsskeqMQQGDEEQNvgmknanef 1256
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNY-----------QPDAGS-----ILIDGQEMR--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1257 ssskegadgqsstlFKNSGKILLDGVdicdynlkdlrnlfSIVSQEPMLF-NMSIYENI-------KFG--KENATREDV 1326
Cdd:PRK11288 70 --------------FASTTAALAAGV--------------AIIYQELHLVpEMTVAENLylgqlphKGGivNRRLLNYEA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1327 KRacKFAAIDEFIEslPnqyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIeKTIVDIKDK 1405
Cdd:PRK11288 122 RE--QLEHLGVDID--P---DTPL----KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLF-RVIRELRAE 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1406 AdKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQ-----AQGTHEELLS 1450
Cdd:PRK11288 190 G-RVILYVSHRMEEIFAlCDAITVF----KDGRYVAtfddmAQVDRDQLVQ 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
393-611 |
1.23e-12 |
|
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: 68.93 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 393 DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVnlkwwRSKIGVVSQDP 469
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvVKEPAEA-----RRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 470 LLFSN-SIKNNIKY--SLYSLKDLEALseesnedgfssqsdsnsrnscrakcaGDLNDMIQTTDSTELIQVRknyetied 546
Cdd:cd03266 88 GLYDRlTARENLEYfaGLYGLKGDELT--------------------------ARLEELADRLGMEELLDRR-------- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 547 sevvsvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:cd03266 134 ------------------------------VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
397-681 |
1.39e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.31 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL---YDP---TEGDVII--NDSHNLKDVNLkwwRSKIGVVSQD 468
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYfgKDIFQIDAIKL---RKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 469 PLLFSN-SIKNNIKYSLYSlkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdstELIQVRKNYETIEDS 547
Cdd:PRK14246 99 PNPFPHlSIYDNIAYPLKS----------------------------------------------HGIKEKREIKKIVEE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 548 EVVSVSKKVLIHDFVSalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKg 627
Cdd:PRK14246 133 CLRKVGLWKEVYDRLN-----------SPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 156095386 628 NENRITIIIAHRLSTIRYANTIFVLSnreNGSTVDVDVLGEDPTKDSNEKNEKH 681
Cdd:PRK14246 201 NEIAIVIVSHNPQQVARVADYVAFLY---NGELVEWGSSNEIFTSPKNELTEKY 251
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
400-643 |
1.43e-12 |
|
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: 69.88 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNN 479
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI-DGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 IkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrKNYETIEDSEVVSVSKKVLIH 559
Cdd:cd03289 97 L----------------------------------------------------------DPYGKWSDEEIWKVAEEVGLK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTinnLKGNENRITIIIA-H 638
Cdd:cd03289 119 SVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKT---LKQAFADCTVILSeH 195
|
....*
gi 156095386 639 RLSTI 643
Cdd:cd03289 196 RIEAM 200
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
383-613 |
1.45e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.02 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVnlKWWRSKI 462
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHV--PPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesNEDGFSsqsdsnsrnscRAKCAGDLNDMIQttdsteliqvrkny 541
Cdd:PRK11607 94 NMMFQSYALFPHmTVEQNIAFGL-------------KQDKLP-----------KAEIASRVNEMLG-------------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 542 etiedsevvsvskkvLIH--DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK11607 136 ---------------LVHmqEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
383-636 |
1.90e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.10 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDV-IINDSHNLKDVNLK 456
Cdd:PRK14267 5 IETVNLRVYYG---SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVrLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 457 WWRSKIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagDLNDMIQTTDstELi 535
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHlTIYDNVAIGV------------------------------------KLNGLVKSKK--EL- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 536 qvrknyetieDSEVVSVSKKvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK14267 123 ----------DERVEWALKK-------AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
250 260
....*....|....*....|.
gi 156095386 616 YLVQKTINNLKgneNRITIII 636
Cdd:PRK14267 186 AKIEELLFELK---KEYTIVL 203
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
397-654 |
2.13e-12 |
|
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: 68.13 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWW---RSKIGVVSQDPLLFS 473
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 474 NSIKNNIKYslyslkdlealseesnEDGFSSQSDSNSRNSCRAKCAGDLndmiqttdsteliqvrknyetiedsevvsvs 553
Cdd:cd03290 93 ATVEENITF----------------GSPFNKQRYKAVTDACSLQPDIDL------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 554 kkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRI 632
Cdd:cd03290 126 -----------LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRT 194
|
250 260
....*....|....*....|..
gi 156095386 633 TIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03290 195 LVLVTHKLQYLPHADWIIAMKD 216
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1308-1430 |
2.42e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.44 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1308 MSIYENIKFG------KENATREDVKRACKFAAIDEFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLD 1381
Cdd:PRK11000 90 LSVAENMSFGlklagaKKEEINQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 156095386 1382 EATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFN 1430
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLD 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1358-1432 |
2.85e-12 |
|
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: 67.84 E-value: 2.85e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1358 SGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIEKtIVDIKDkADKTIITIAHRIASIKR-SDKIVVFNNP 1432
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAaNRAVVVEL-IEEAKA-RGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1176-1415 |
3.08e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1176 RPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrFYDLKNdhhivfkneqtgesskeqmqqgdeeqnvgmknane 1255
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKG----------------------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1256 fssskegadgqsstlFKNSGKILLDGVDIcdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFAA 1334
Cdd:TIGR00955 79 ---------------VKGSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIpTLTVREHLMFQAHLRMPRRVTKKEKRER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1335 IDEFIE--SLPNQYDTNVGPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTI 1410
Cdd:TIGR00955 141 VDEVLQalGLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKG-KTI 219
|
....*
gi 156095386 1411 ITIAH 1415
Cdd:TIGR00955 220 ICTIH 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
383-638 |
3.20e-12 |
|
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: 70.99 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL--YDPTEGDVIINDSHNLKdvnlkwwRS 460
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEK-------CG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQdpllfsnsIKNNIKYSLYSLKDLEAlseesnedGFSSQSDSNSRNsCRAKCAgdlnDMIQTT-----DSTELI 535
Cdd:TIGR03269 71 YVERPSK--------VGEPCPVCGGTLEPEEV--------DFWNLSDKLRRR-IRKRIA----IMLQRTfalygDDTVLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 536 QVRKNYETIEDSEVVSVSKKVLIHDFVsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:TIGR03269 130 NVLEALEEIGYEGKEAVGRAVDLIEMV-----QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA 204
|
250 260
....*....|....*....|...
gi 156095386 616 YLVQKTINNLKGNENRITIIIAH 638
Cdd:TIGR03269 205 KLVHNALEEAVKASGISMVLTSH 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1274-1428 |
5.25e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLF-NMSIYENIKFGKE--NATREDvkrackFAAIDEFIESLPNQYDTN 1349
Cdd:PRK13549 61 EGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkELSVLENIFLGNEitPGGIMD------YDAMYLRAQKLLAQLKLD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1350 VGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLdSNSEKLIEKTIV-DIKDKaDKTIITIAHRIASIKR-SDK 1425
Cdd:PRK13549 135 INPATPvgNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIIrDLKAH-GIACIYISHKLNEVKAiSDT 212
|
...
gi 156095386 1426 IVV 1428
Cdd:PRK13549 213 ICV 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1308-1431 |
8.01e-12 |
|
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: 66.72 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1308 MSIYENIKFGKeNATREDVKRACKFAAIDEFIESLPNQYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:TIGR01184 69 LTVRENIALAV-DRVLPDLSKSERRAIVEEHIALVGLTEAADKRP--GQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 156095386 1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1431
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVdEALLLSDRVVMLTN 190
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1184-1430 |
8.95e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.73 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSceSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfkneqtgesskeqmqqGDEEQNVGMKNANEfssskega 1263
Cdd:PRK13645 31 SLTFK--KNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV----------------GDYAIPANLKKIKE-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 dgqsstlfknsgkilldgvdicdynLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN--ATREDVkrackFAAIDEFI 1339
Cdd:PRK13645 85 -------------------------VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNlgENKQEA-----YKKVPELL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1340 E--SLPNQYdTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:PRK13645 135 KlvQLPEDY-VKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNM 211
|
250
....*....|....
gi 156095386 1418 ASIKR-SDKIVVFN 1430
Cdd:PRK13645 212 DQVLRiADEVIVMH 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1187-1388 |
1.02e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.07 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1187 FSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgq 1266
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLL------------------------------------------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1267 ssTLFKN--SGKILLDGVDICDYN---LKDLRNLFSIVSQ-----------------EPMLFNMSIyenikfgkenaTRE 1324
Cdd:PRK11308 62 --TMIETptGGELYYQGQDLLKADpeaQKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSL-----------SAA 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1325 DvkRACKFAAIDEFIESLPNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11308 129 E--RREKALAMMAKVGLRPEHYDR----YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1292-1450 |
1.10e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1292 LRNLFSIVSQEPMLFNMSIYENIKFGKE-NATRedVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARA 1370
Cdd:PLN03130 677 IRGTVAYVPQVSWIFNATVRDNILFGSPfDPER--YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARA 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1371 LLREPKILLLDEATSSLDSN-SEKLIEKTIVDikDKADKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAQGTHEELL 1449
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHvGRQVFDKCIKD--ELRGKTRVLVTNQLHFLSQVDRIILVHE-----GMIKEEGTYEELS 827
|
.
gi 156095386 1450 S 1450
Cdd:PLN03130 828 N 828
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1179-1450 |
1.13e-11 |
|
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: 69.33 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1179 VPIYKDLTFSCESKKTTAIVGETGSGKS----TVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknan 1254
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLL------------------------------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1255 efssskegADGQSSTlfknSGKILLDGVDICDYNLKDLRNL----FSIVSQEPM-----LFNMS--IYENIKFgKENATR 1323
Cdd:COG4172 61 --------PDPAAHP----SGSILFDGQDLLGLSERELRRIrgnrIAMIFQEPMtslnpLHTIGkqIAEVLRL-HRGLSG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRAckfaAID----------EF-IESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:COG4172 128 AAARAR----ALEllervgipdpERrLDAYPHQ-----------LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQ 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1393 KLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQaQGTHEELLS 1450
Cdd:COG4172 193 AQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVM----RQGEIVE-QGPTAELFA 246
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
382-613 |
1.89e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.56 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LKWWRS 460
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG----RVVNeLEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 461 KIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmiqtTDSTElIQVRk 539
Cdd:PRK11650 77 DIAMVFQNYALYPHmSVRENMAYGL--------------------------------KIRG--------MPKAE-IEER- 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 540 nyetiedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK11650 115 ---------VAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
376-669 |
2.28e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 376 KLKDIKKIqfknvrFHYDTRKDVEIYKDLNFTLTEGKtyaFV---GESGCGKSTILKLIERLYDPTEGDVIINDshnlKD 452
Cdd:COG1101 3 ELKNLSKT------FNPGTVNEKRALDGLNLTIEEGD---FVtviGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 453 V-NLK-WWRSK-IGVVSQDPLL---FSNSIKNNIkySLYSLKdlealseeSNEDGFSSQSDSNSRNSCRAKCAG-DLNdm 525
Cdd:COG1101 70 VtKLPeYKRAKyIGRVFQDPMMgtaPSMTIEENL--ALAYRR--------GKRRGLRRGLTKKRRELFRELLATlGLG-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 526 iqttdsteliqvrknyetiedsevvsvskkvlihdfvsaLPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDE 605
Cdd:COG1101 138 ---------------------------------------LENRLDTKVGL----LSGGQRQALSLLMATLTKPKLLLLDE 174
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 606 ATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLsnrENGSTVdVDVLGED 669
Cdd:COG1101 175 HTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEqALDYGNRLIMM---HEGRII-LDVSGEE 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1262-1431 |
2.31e-11 |
|
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: 64.93 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1262 GADGQ-SSTLFK--------NSGKILLDGVDICDyNLKDLRNLFSIVSqEPMLF-NMSIYENIKFgkeNATREDVKRAck 1331
Cdd:cd03268 33 GPNGAgKTTTMKiilglikpDSGEITFDGKSYQK-NIEALRRIGALIE-APGFYpNLTARENLRL---LARLLGIRKK-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1332 faAIDEFIE--SLPNQYDTNVGPYgkSLsgGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKT 1409
Cdd:cd03268 106 --RIDEVLDvvGLKDSAKKKVKGF--SL--GMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG-IT 178
|
170 180
....*....|....*....|...
gi 156095386 1410 IITIAHRIASI-KRSDKIVVFNN 1431
Cdd:cd03268 179 VLISSHLLSEIqKVADRIGIINK 201
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
65-309 |
2.35e-11 |
|
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: 66.41 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 65 SFVCATISGGT---LPFFVS--VFGVIMKNMnlGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKS 139
Cdd:cd18572 1 AFVFLVVAALSelaIPHYTGavIDAVVADGS--REAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 140 VFYQDGQFHD-NNPG---SKLTSDLDfyleQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIcgv 215
Cdd:cd18572 79 LLRQDIAFFDaTKTGeltSRLTSDCQ----KVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 216 ICNKKVKINKKTSLLYNN---NTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFIL 292
Cdd:cd18572 152 ITKVYGRYYRKLSKEIQDalaEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQN 231
|
250
....*....|....*..
gi 156095386 293 ASYAFGFWYGTRIIISD 309
Cdd:cd18572 232 GTQVLVLFYGGHLVLSG 248
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
383-662 |
2.49e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-----SHNLKDVNLKW 457
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 458 WRSKIGVVSQdpllfsnsiknniKYSLYS-LKDLEALSEesnedgfssqsdsnsrnscrAKCagdlndmiqttdsteliQ 536
Cdd:PRK11124 80 LRRNVGMVFQ-------------QYNLWPhLTVQQNLIE--------------------APC-----------------R 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 537 VRKNYETIEDSEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:PRK11124 110 VLGLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 156095386 617 LVQKTINNLKgnENRIT-IIIAHRLSTIRYANTIFVLsnRENGSTVD 662
Cdd:PRK11124 179 QIVSIIRELA--ETGITqVIVTHEVEVARKTASRVVY--MENGHIVE 221
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
64-355 |
3.13e-11 |
|
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: 66.12 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 64 VSFVCATISGGTLPFFV-SVFGVIMKNMNLG-----ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFL 137
Cdd:cd18780 3 IALLVSSGTNLALPYFFgQVIDAVTNHSGSGgeealRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 138 KSVFYQDGQFHD-NNPG---SKLTSDldfylEQV--NAGIGTKFITIFTYASAFLGLYIwsLFK-NARLTLCITCVFPLI 210
Cdd:cd18780 83 SAIIAQEIAFFDvTRTGellNRLSSD-----TQVlqNAVTVNLSMLLRYLVQIIGGLVF--MFTtSWKLTLVMLSVVPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFnlSEKLYSKYTLKANLmeSLHIGMINGF 290
Cdd:cd18780 156 SIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY--SEKINESYLLGKKL--ARASGGFNGF 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 291 ILA----SYAFGFWYGTRIIISDlsnqqpnnDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
Cdd:cd18780 232 MGAaaqlAIVLVLWYGGRLVIDG--------ELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGAS 292
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
383-652 |
3.34e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDV--EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVNLKW 457
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 458 WRSKIGVVSQDP--LLFSNSIknnikyslysLKDLealseesnedGFSSQSDSNSRNSCRAKCAgdlndmiqttdsteli 535
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETV----------LKDV----------AFGPQNFGIPKEKAEKIAA---------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 536 qvrknyetiEDSEVVSVSKkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK13643 126 ---------EKLEMVGLAD-----EFWEKSP-----------FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
250 260 270
....*....|....*....|....*....|....*...
gi 156095386 616 YLVQKTINNLKgNENRITIIIAHRLSTIR-YANTIFVL 652
Cdd:PRK13643 181 IEMMQLFESIH-QSGQTVVLVTHLMDDVAdYADYVYLL 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
383-654 |
3.42e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnLKDVNLKWWRSKI 462
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-VNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDP--LLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcaGDLNdmiQTTDSTELiqvrkn 540
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAF-------------------------------------GPVN---MGLDKDEV------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 yetieDSEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13647 116 -----ERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
|
250 260 270
....*....|....*....|....*....|....*.
gi 156095386 621 TINNLkgNENRITIIIA-HRLS-TIRYANTIFVLSN 654
Cdd:PRK13647 180 ILDRL--HNQGKTVIVAtHDVDlAAEWADQVIVLKE 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-611 |
4.08e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.93 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDVIInDSHNLKDVNLK 456
Cdd:PRK14247 3 KIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYL-DGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 457 WWRSKIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagDLNDMIQTtdSTELI 535
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNlSIFENVALGL------------------------------------KLNRLVKS--KKELQ 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 536 Q-VRKNYETIEdsevvsvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK14247 121 ErVRWALEKAQ-------------------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
383-625 |
4.45e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.01 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKwwRSKI 462
Cdd:PRK13536 42 IDLAGVSKSY---GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA--RARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQdpllFSNSiknnikyslyslkDLEALSEESnedgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRKNYE 542
Cdd:PRK13536 117 GVVPQ----FDNL-------------DLEFTVREN-------------------------------------LLVFGRYF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 TIEDSEVVSVSKKVLihDFvSALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK13536 143 GMSTREIEAVIPSLL--EF-ARLESKADARV----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL 215
|
...
gi 156095386 623 NNL 625
Cdd:PRK13536 216 RSL 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1163-1448 |
4.50e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRYLSRpnVPIY----KDLTFSCESKKTTAIVGETGSGKSTV---MSLLMrfydLKNDHHI--VFKNEQTGE 1233
Cdd:PRK13651 2 QIKVKNIVKIFNKK--LPTElkalDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALL----LPDTGTIewIFKDEKNKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1234 SSKEQMQQGDEeqnvgmknanefssskegaDGQSSTLFKNSGKIlldgvdicdynlKDLRNLFSIVSQ--EPMLFNMSIY 1311
Cdd:PRK13651 76 KTKEKEKVLEK-------------------LVIQKTRFKKIKKI------------KEIRRRVGVVFQfaEYQLFEQTIE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1312 ENIKFG-------KENATredvKRACKFAAIdefiESLPNQYdTNVGPYGksLSGGQKQRIAIARALLREPKILLLDEAT 1384
Cdd:PRK13651 125 KDIIFGpvsmgvsKEEAK----KRAAKYIEL----VGLDESY-LQRSPFE--LSGGQKRRVALAGILAMEPDFLVFDEPT 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1385 SSLDSNSEKLIEKtIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNNpdrtGSFVQAQGTHEEL 1448
Cdd:PRK13651 194 AGLDPQGVKEILE-IFDNLNKQGKTIILVTHDLDNVlEWTKRTIFFKD----GKIIKDGDTYDIL 253
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
62-291 |
4.91e-11 |
|
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: 65.50 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 62 LGVSFVCATISGGT---LPFFVS-VFGVIMKNMNLGENVN-----DIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTL 132
Cdd:cd18547 1 LILVIILAIISTLLsvlGPYLLGkAIDLIIEGLGGGGGVDfsgllRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 133 ------KIEFLkSVFYqdgqFHDNNPG---SKLTSDLDfyleQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCI 203
Cdd:cd18547 81 rkdlfeKLQRL-PLSY----FDTHSHGdimSRVTNDVD----NISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 204 TCVFPLIYICGVIcnkkvkINKKTSLLYNNNTMSI------IEEALVGIRTVVSYCGENTILKKFN-LSEKLYsKYTLKA 276
Cdd:cd18547 152 LVTVPLSLLVTKF------IAKRSQKYFRKQQKALgelngyIEEMISGQKVVKAFNREEEAIEEFDeINEELY-KASFKA 224
|
250
....*....|....*
gi 156095386 277 NLMESLhIGMINGFI 291
Cdd:cd18547 225 QFYSGL-LMPIMNFI 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1179-1396 |
5.24e-11 |
|
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: 64.38 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1179 VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknAnefss 1258
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLL----------------------------------------A----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1259 skeGADGQSStlfknsGKILLDGVDICDYN---LKDLRN-LFSIVSQEPMLF-NMSIYENIK-----FGKENAtREDVKR 1328
Cdd:COG4181 60 ---GLDRPTS------GTVRLAGQDLFALDedaRARLRArHVGFVFQSFQLLpTLTALENVMlplelAGRRDA-RARARA 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1329 ACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIE 1396
Cdd:COG4181 130 LLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGNLDAaTGEQIID 187
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1350-1446 |
5.95e-11 |
|
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: 62.97 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1350 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03222 65 YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYlSDRIHV 144
|
90
....*....|....*....
gi 156095386 1429 F-NNPDRTGSFVQAQGTHE 1446
Cdd:cd03222 145 FeGEPGVYGIASQPKGTRE 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
402-652 |
6.06e-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: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLkwwRS-------KIGVVSQDPLLFSN 474
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG----KPVRI---RSprdaialGIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 475 -SIKNNIkyslyslkdleALSEESNEDGFSSqsdsnsRNSCRAKcagdlndmiqttdsteliqvrknyetiedsevvsvs 553
Cdd:COG3845 95 lTVAENI-----------VLGLEPTKGGRLD------RKAARAR------------------------------------ 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 554 kkvlihdfVSALPDKY------ETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVqKTINNLK 626
Cdd:COG3845 122 --------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELF-EILRRLA 188
|
250 260
....*....|....*....|....*...
gi 156095386 627 gnENRITII-IAHRLSTIR-YANTIFVL 652
Cdd:COG3845 189 --AEGKSIIfITHKLREVMaIADRVTVL 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1268-1450 |
6.48e-11 |
|
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: 63.85 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDIcdynlkdlRNL---------FSIVSQEPMLF-NMSIYENIKFG-----KENATRE 1324
Cdd:COG0410 43 TTLLKaisgllppRSGSIRFDGEDI--------TGLpphriarlgIGYVPEGRRIFpSLTVEENLLLGayarrDRAEVRA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1325 DVKRACK-FAAIDEFIESLpnqydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIEK---TIV 1400
Cdd:COG0410 115 DLERVYElFPRLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEifeIIR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1401 DIKDkADKTIITI---AHRIASIkrSDKIVVFnnpdRTGSFVqAQGTHEELLS 1450
Cdd:COG0410 181 RLNR-EGVTILLVeqnARFALEI--ADRAYVL----ERGRIV-LEGTAAELLA 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
398-652 |
6.49e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKIGVVSQDPLLFSN-SI 476
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 477 KNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrAKCAGDLNDMiqttdsTELIQvrknyetiedseVVSVSKKv 556
Cdd:PRK15439 104 KENILFGL-------------------------------PKRQASMQKM------KQLLA------------ALGCQLD- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 557 lihdfvsalPDkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKtINNLKGNENRItII 635
Cdd:PRK15439 134 ---------LD-------SSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSR-IRELLAQGVGI-VF 195
|
250
....*....|....*...
gi 156095386 636 IAHRLSTIR-YANTIFVL 652
Cdd:PRK15439 196 ISHKLPEIRqLADRISVM 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
383-653 |
7.23e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.87 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN----DSHNLKDVNLkww 458
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpiDYSRKGLMKL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 459 RSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdleaLSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQ 536
Cdd:PRK13636 81 RESVGMVFQDPdnQLFSASVYQDVSFGAVNLK----LPED---------------------------------------E 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 537 VRKNYETIedsevvsvskkvLIHDFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:PRK13636 118 VRKRVDNA------------LKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 617 LVQKTINNLKgNENRITIIIA-HRLSTIR-YANTIFVLS 653
Cdd:PRK13636 179 EIMKLLVEMQ-KELGLTIIIAtHDIDIVPlYCDNVFVMK 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
383-656 |
7.95e-11 |
|
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: 61.70 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdvnlkwwRSKI 462
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQdpllfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03221 66 GYFEQ--------------------------------------------------------------------------- 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 623 NNLKGnenrITIIIAH-R--LSTIryANTIFVLSNRE 656
Cdd:cd03221 114 KEYPG----TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1178-1431 |
8.28e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1178 NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqGDEEQNVgmknanefs 1257
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM----------------------------GHPKYEV--------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1258 sskegadgqsstlfkNSGKILLDGVDICDYNLKD--LRNLFsiVS-QEP--------MLFNMSIYeNIKFGKENATREDV 1326
Cdd:COG0396 55 ---------------TSGSILLDGEDILELSPDEraRAGIF--LAfQYPveipgvsvSNFLRTAL-NARRGEELSAREFL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1327 KRACKFAAI----DEFIESlpnqyDTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:COG0396 117 KLLKEKMKElgldEDFLDR-----YVNEG-----FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL 186
|
250 260 270
....*....|....*....|....*....|.
gi 156095386 1403 KDKaDKTIITIAH--RIASIKRSDKIVVFNN 1431
Cdd:COG0396 187 RSP-DRGILIITHyqRILDYIKPDFVHVLVD 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1308-1388 |
9.54e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.25 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1308 MSIYENIKFGKENA------TREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLD 1381
Cdd:PRK11650 91 MSVRENMAYGLKIRgmpkaeIEERVAEAARILELEPLLDRKPRE-----------LSGGQRQRVAMGRAIVREPAVFLFD 159
|
....*..
gi 156095386 1382 EATSSLD 1388
Cdd:PRK11650 160 EPLSNLD 166
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1171-1460 |
9.65e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.04 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1171 FRY----LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeq 1246
Cdd:PRK15112 14 FRYrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKML---------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1247 nvgmknanefssskegadgqSSTLFKNSGKILLDGVDIC--DYNLKDLRnlFSIVSQEPmlfNMSIYENIKFG------- 1317
Cdd:PRK15112 60 --------------------AGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDP---STSLNPRQRISqildfpl 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KENATREDVKRACKFAAIDEFIESLPNqydtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:PRK15112 115 RLNTDLEPEQREKQIIETLRQVGLLPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1398 TIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PRK15112 191 LMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQ----GEVVERGSTADVLASPLHELTKRLI 250
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1273-1382 |
9.87e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.51 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLkDLRNLFSI--VSQEPMLF-NMSIYENIK-----FGKENATREDvkracKFAA-IDEF-IESL 1342
Cdd:COG1137 56 DSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFrKLTVEDNILavlelRKLSKKEREE-----RLEElLEEFgITHL 129
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDE 1382
Cdd:COG1137 130 RKSK-------AYSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1356-1427 |
1.17e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.88 E-value: 1.17e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIV 1427
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVdYALRYCERIV 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1268-1448 |
1.35e-10 |
|
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: 62.77 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK-NSGKILLDGVDI-CDynLKDLRNLFSIVSQEPMLFN-MSIYENIKFgkeNATREDVKRACKFAAIDEFIE--SL 1342
Cdd:cd03265 47 TTLLKpTSGRATVAGHDVvRE--PREVRRRIGIVFQDLSVDDeLTGWENLYI---HARLYGVPGAERRERIDELLDfvGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQYDTNVGPYgkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-K 1421
Cdd:cd03265 122 LEAADRLVKTY----SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQ 197
|
170 180
....*....|....*....|....*..
gi 156095386 1422 RSDKIVVFNNpdrtGSFVqAQGTHEEL 1448
Cdd:cd03265 198 LCDRVAIIDH----GRII-AEGTPEEL 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
396-611 |
1.37e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH--NLKDVNLKWWRSKIGVVSQDPLLfS 473
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidTLSPGKLQALRRDIQFIFQDPYA-S 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 474 NSIKNNIKYSLyslkdLEALSEESNEDGFSSQSdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsEVVSVS 553
Cdd:PRK10261 414 LDPRQTVGDSI-----MEPLRVHGLLPGKAAAA-----------------------------------------RVAWLL 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 554 KKV-LIHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10261 448 ERVgLLPEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1163-1450 |
1.40e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmRFYDLKNDHHIVFKNeqtgesskeqmqqg 1242
Cdd:PRK10619 5 KLNVIDLHKRYGEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeQNVGMKNANefssskegaDGQSSTLFKNsgkilldgvdicdyNLKDLRNLFSIVSQEPMLFN-MSIYENIK------ 1315
Cdd:PRK10619 67 ---QTINLVRDK---------DGQLKVADKN--------------QLRLLRTRLTMVFQHFNLWShMTVLENVMeapiqv 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 --FGKENAtREDVKRACKFAAIDEFIEslpnqydtnvGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseK 1393
Cdd:PRK10619 121 lgLSKQEA-RERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP---E 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1394 LIEKTIVDIKDKAD--KTIITIAHRIASIKRSDKIVVFNNPDRtgsfVQAQGTHEELLS 1450
Cdd:PRK10619 187 LVGEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVIFLHQGK----IEEEGAPEQLFG 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
386-610 |
1.46e-10 |
|
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: 62.84 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 386 KNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWW---RSK 461
Cdd:cd03224 4 ENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDItGLPPHeraRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvRKN 540
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLLLGAYARRR------------------------------------------------AKR 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 YETIEDsevvsvskkvlIHDFVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:cd03224 109 KARLER-----------VYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
402-652 |
1.46e-10 |
|
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: 62.84 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNlkwwRSKIGVVS--QDPLLFSN-SI 476
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeDITGLPPHE----IARLGIGRtfQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 477 KNNIKYSLYSlkdlealseeSNEDGFSSQSDSNSRNSCRAKCAgdlndmiqttdstELIqvrknyetiedsevvsvskkv 556
Cdd:cd03219 93 LENVMVAAQA----------RTGSGLLLARARREEREARERAE-------------ELL--------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 557 lihDFVsALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLdNKSEylVQKTINNLKG-NENRITI- 634
Cdd:cd03219 129 ---ERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAAGL-NPEE--TEELAELIRElRERGITVl 197
|
250
....*....|....*....
gi 156095386 635 IIAHRLSTI-RYANTIFVL 652
Cdd:cd03219 198 LVEHDMDVVmSLADRVTVL 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1299-1388 |
1.47e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.51 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1299 VSQEPMLF-NMSIYENIKFGKENATREdvkracKFAAIDEF--IESLPNQYdtnvgPYgkSLSGGQKQRIAIARALLREP 1375
Cdd:PRK11144 81 VFQDARLFpHYKVRGNLRYGMAKSMVA------QFDKIVALlgIEPLLDRY-----PG--SLSGGEKQRVAIGRALLTAP 147
|
90
....*....|...
gi 156095386 1376 KILLLDEATSSLD 1388
Cdd:PRK11144 148 ELLLMDEPLASLD 160
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1163-1428 |
1.60e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.34 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRYLSRPNVpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneQTGESSKEQMqqg 1242
Cdd:PTZ00243 658 KTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEI-----------SEGRVWAERS--- 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstlfknsgkilldgvdicdynlkdlrnlFSIVSQEPMLFNMSIYENIKF-GKENA 1321
Cdd:PTZ00243 723 -----------------------------------------------------IAYVPQQAWIMNATVRGNILFfDEEDA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TR-EDVKRACKFAAiDefIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTI 1399
Cdd:PTZ00243 750 ARlADAVRVSQLEA-D--LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECF 826
|
250 260
....*....|....*....|....*....
gi 156095386 1400 vdIKDKADKTIITIAHRIASIKRSDKIVV 1428
Cdd:PTZ00243 827 --LGALAGKTRVLATHQVHVVPRADYVVA 853
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1356-1429 |
1.71e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 61.87 E-value: 1.71e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKRSDKIVVF 1429
Cdd:NF040873 119 ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1274-1428 |
1.84e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDI---CDYNLKDLRNLFSIVSQEP-------MLFNMSIYENIKFGKENATREDVKRACKfaAIDEFIESLP 1343
Cdd:PRK15079 75 DGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPlaslnprMTIGEIIAEPLRTYHPKLSRQEVKDRVK--AMMLKVGLLP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADK----TIITIAHRIAS 1419
Cdd:PRK15079 153 NL----INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS----IQAQVVNLLQQLQRemglSLIFIAHDLAV 224
|
170
....*....|
gi 156095386 1420 IKR-SDKIVV 1428
Cdd:PRK15079 225 VKHiSDRVLV 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
383-636 |
2.22e-10 |
|
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: 62.00 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVnlKWWRSKI 462
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLL------FSNSIknnIKYSLYSLKDLEAlseesnedgfssqsdsnsrnscRAKCAgdlndmiQTTDSTELIQ 536
Cdd:cd03265 76 GIVFQDLSVddeltgWENLY---IHARLYGVPGAER----------------------RERID-------ELLDFVGLLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 537 VRknyetiedsevvsvskkvlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:cd03265 124 AA----------------------------DRL-------VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
250 260
....*....|....*....|
gi 156095386 617 LVQKTINNLKgNENRITIII 636
Cdd:cd03265 169 HVWEYIEKLK-EEFGMTILL 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1269-1450 |
2.45e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.48 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1269 TLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGK----------ENATREDVKRACKFAAIDE 1337
Cdd:PRK09536 52 TLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1338 FIeslpnqyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKlieKTIVDIKDKAD--KTIITIAH 1415
Cdd:PRK09536 132 FA-------DRPV----TSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV---RTLELVRRLVDdgKTAVAAIH 197
|
170 180 190
....*....|....*....|....*....|....*.
gi 156095386 1416 RIASIKR-SDKIVVFnnpdrTGSFVQAQGTHEELLS 1450
Cdd:PRK09536 198 DLDLAARyCDELVLL-----ADGRVRAAGPPADVLT 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
383-661 |
2.51e-10 |
|
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: 61.74 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNlkwwRSK 461
Cdd:cd03298 1 VRLDKIRFSYG-----EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPA----DRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLY-SLKdleaLSEESNEdgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrk 539
Cdd:cd03298 72 VSMLFQENNLFAHlTVEQNVGLGLSpGLK----LTAEDRQ---------------------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 540 nyetiedsEVVSVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:cd03298 108 --------AIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 156095386 620 KTINNLKGNENRITIIIAHRLSTIR--YANTIFVlsnrENGSTV 661
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKrlAQRVVFL----DNGRIA 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
345-638 |
2.93e-10 |
|
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: 64.44 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 345 ITEYMKSLEATNNLYEIINRKPLVennqdgkKLKDIKKiqfknvRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGK 424
Cdd:TIGR03269 257 VAVFMEGVSEVEKECEVEVGEPII-------KVRNVSK------RYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 425 STILKLIERLYDPTEGDVIINDSHNLKDVNLKWW----RSK--IGVVSQDpllfsnsiknnikYSLYSLKD-LEALsees 497
Cdd:TIGR03269 324 TTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPdgrgRAKryIGILHQE-------------YDLYPHRTvLDNL---- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 498 nedgfssqsdsnsrnscrakcagdlndmiqttdsTELIqvrknyeTIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNA 577
Cdd:TIGR03269 387 ----------------------------------TEAI-------GLELPDELARMKAVITLKMVGFDEEKAEEILDKYP 425
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSH 486
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1139-1428 |
2.98e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.59 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1139 TRKSLIDVRDnggikiknsndikgkieiMDVNFrylSRP--NVPIYKDLTFSCESKKTTAIVGETGSGKS----TVMSLL 1212
Cdd:PRK09473 8 QADALLDVKD------------------LRVTF---STPdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1213 MrfydlkndhhivfKNEQTGESSKeqmQQGDEEQNVGMKNANEFSSSKegadgqsstlfknsgkilldgvdicdynlkdl 1292
Cdd:PRK09473 67 A-------------ANGRIGGSAT---FNGREILNLPEKELNKLRAEQ-------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1293 rnlFSIVSQEPML-FN--MSIYENI--------KFGKENATREDVKR--ACKFAAIDEFIESLPNQYdtnvgpygkslSG 1359
Cdd:PRK09473 99 ---ISMIFQDPMTsLNpyMRVGEQLmevlmlhkGMSKAEAFEESVRMldAVKMPEARKRMKMYPHEF-----------SG 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1360 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR---IASIkrSDKIVV 1428
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlgvVAGI--CDKVLV 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
390-653 |
3.07e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 390 FHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND--------------SHNLKDV-N 454
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitNPYSKKIkN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 455 LKWWRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdlealseesnedgfssqsdsNSRNSCRAKCAGDLNDMiqttdst 532
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALG--------------------VKKSEAKKLAKFYLNKM------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 533 eliqvrknyetiedsevvsvskkvlihdfvsALPDKYetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:PRK13631 164 -------------------------------GLDDSY---LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156095386 613 KSEYLVQKTINNLKGNeNRITIIIAHRLSTI-RYANTIFVLS 653
Cdd:PRK13631 210 KGEHEMMQLILDAKAN-NKTVFVITHTMEHVlEVADEVIVMD 250
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
404-612 |
3.11e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVII--NDSHNLKDVNLKWWRSKIGVVSQDP-LLFSNSIKNNI 480
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsgHDITRLKNREVPFLRRQIGMIFQDHhLLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 481 KYSLyslkdleALSEESNEDgfssqsdsnsrnsCRAKCAGDLndmiqttDSTELIQVRKNYETiedsevvsvskkvlihd 560
Cdd:PRK10908 101 AIPL-------IIAGASGDD-------------IRRRVSAAL-------DKVGLLDKAKNFPI----------------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 156095386 561 fvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:PRK10908 137 ------------------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
398-644 |
3.39e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.42 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdvnlkwwrskigvVSQDPLLFSNSIK 477
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN------------------INYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 478 NNIKYSLYSLKDLEALSEESNEdgfssqsdSNSRNSCRAKCAGDLNDMIQTTDSTELIQVRknyetiedsevvsVSKKVL 557
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENL--------YIGRHLTKKVCGVNIIDWREMRVRAAMMLLR-------------VGLKVD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 558 IHDFVSalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQkTINNLKgNENRITIII 636
Cdd:PRK09700 139 LDEKVA---------------NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEvDYLFL-IMNQLR-KEGTAIVYI 201
|
....*...
gi 156095386 637 AHRLSTIR 644
Cdd:PRK09700 202 SHKLAEIR 209
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
94-308 |
3.61e-10 |
|
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: 62.89 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 94 ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNN-PG---SKLTSDLDFyLEQVna 169
Cdd:cd18575 33 ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTrTGevlSRLTTDTTL-IQTV-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 170 gIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTV 249
Cdd:cd18575 110 -VGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTV 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 250 VSYCGENTILKKFN-LSEKLYsKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIIS 308
Cdd:cd18575 189 QAFTREDAERQRFAtAVEAAF-AAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLA 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
366-640 |
3.83e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 366 PLVENNQDGKKLKDIKkiqfkNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDP--TEGD 441
Cdd:PRK09473 1 TVPLAQQQADALLDVK-----DLRVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 442 VIINDSH--NLKDVNLKWWRS-KIGVVSQDPLLfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakc 518
Cdd:PRK09473 76 ATFNGREilNLPEKELNKLRAeQISMIFQDPMT----------------------------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 519 agDLNDMIQTTDstELIQVRKNYETIEDSEVVSVSKKVLihDFVSaLPDKYETLvGSNASKLSGGQKQRISIARAIIRNP 598
Cdd:PRK09473 109 --SLNPYMRVGE--QLMEVLMLHKGMSKAEAFEESVRML--DAVK-MPEARKRM-KMYPHEFSGGMRQRVMIAMALLCRP 180
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156095386 599 KILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1183-1431 |
4.05e-10 |
|
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: 61.14 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdLKNDHHIVFKNEQTGESSKEQMQQGDEEQNvgmknanefssskeg 1262
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII-LPDSGEVLFDGKPLDIAARNRIGYLPEERG--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstLFKNSgKILldgvDICDYnLKDLRNLfsivsqepmlfnmsiyenikfGKENATREdvkrackfaaIDEFIESL 1342
Cdd:cd03269 81 -------LYPKM-KVI----DQLVY-LAQLKGL---------------------KKEEARRR----------IDEWLERL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 pnqydtNVGPYGKS----LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIA 1418
Cdd:cd03269 117 ------ELSEYANKrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQME 189
|
250
....*....|....
gi 156095386 1419 SIKR-SDKIVVFNN 1431
Cdd:cd03269 190 LVEElCDRVLLLNK 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1178-1450 |
4.25e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1178 NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefs 1257
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL------------------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1258 sskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGKE-------NATRED---V 1326
Cdd:PRK11231 52 ------------LTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRELVAYGRSpwlslwgRLSAEDnarV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1327 KRACKFAAIDEFIESLPNqydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1406
Cdd:PRK11231 120 NQAMEQTRINHLADRRLT-----------DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQG 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 156095386 1407 dKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:PRK11231 189 -KTVVTVLHDLNQASRyCDHLVVLAN----GHVM-AQGTPEEVMT 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
383-611 |
4.59e-10 |
|
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: 61.30 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVN----LKW 457
Cdd:COG4181 9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG-QDLFALDedarARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 458 WRSKIGVVSQDPLLfsnsiknnikysLYSLKDLE--ALSEESnedgfssQSDSNSRNscRAKcagdlndmiqttdsTELi 535
Cdd:COG4181 88 RARHVGFVFQSFQL------------LPTLTALEnvMLPLEL-------AGRRDARA--RAR--------------ALL- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 536 qvrknyetiedsEVVSVSKKVlihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4181 132 ------------ERVGLGHRL------DHYP-----------AQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
403-668 |
4.91e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTL-TEGKTYAFvGESGCGKSTILKLIERLYDPTEGDVIINDsHNL----KDVNLKWWRSKIGVVSQDPLLFSN-SI 476
Cdd:PRK11144 16 TVNLTLpAQGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLfdaeKGICLPPEKRRIGYVFQDARLFPHyKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 477 KNNIKYSlyslkdlealseesnedgfssqsdsnsrnsCRAKCAGDLNDMIQTTDsteliqvrknyetIEdsevvsvskkv 556
Cdd:PRK11144 94 RGNLRYG------------------------------MAKSMVAQFDKIVALLG-------------IE----------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 557 lihdfvsALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD--NKSE---YL--VQKTINnlkgne 629
Cdd:PRK11144 120 -------PLLDRY-------PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlpRKREllpYLerLAREIN------ 179
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 156095386 630 nrITII-IAHRLSTI-RYANTIFVLsnrENGSTVDVDVLGE 668
Cdd:PRK11144 180 --IPILyVSHSLDEIlRLADRVVVL---EQGKVKAFGPLEE 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1184-1393 |
5.19e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.07 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkNDHHIvfkneqtgesskeqmqqgdeeqnvgmknanefssskega 1263
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLL-------NGLHV--------------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 dgqsstlfKNSGKILLDGVDIC----DYNLKDLRNLFSIVSQ--EPMLFNMSIYENIKFGKEN---ATREDVKRACKFAA 1334
Cdd:PRK13649 59 --------PTQGSVRVDDTLITstskNKDIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgvSQEEAEALAREKLA 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1335 IDEFIESLpnqYDTNvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:PRK13649 131 LVGISESL---FEKN--PF--ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
402-638 |
5.59e-10 |
|
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: 61.33 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdshnlkdvnlkwwrskiGVVSQDP-----LLFSNsi 476
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE-----------------GKQITEPgpdrmVVFQN-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 477 knnikYSLYSLKdlealseesnedgfssqsdsnsrnSCRAKCAGDLNDMIQTTDSTEliqvrknYETIEDSEVVSVSkkv 556
Cdd:TIGR01184 63 -----YSLLPWL------------------------TVRENIALAVDRVLPDLSKSE-------RRAIVEEHIALVG--- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 557 lihdfVSALPDKYETlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRIT-II 635
Cdd:TIGR01184 104 -----LTEAADKRPG-------QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI-WEEHRVTvLM 170
|
...
gi 156095386 636 IAH 638
Cdd:TIGR01184 171 VTH 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1272-1449 |
6.32e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1272 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQEP----MLFNMSIYENI------KFGKENATredVKRACKFAAIDEFIE 1340
Cdd:PRK10762 304 RTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSVKENMsltalrYFSRAGGS---LKHADEQQAVSDFIR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 SL----PNQyDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHR 1416
Cdd:PRK10762 381 LFniktPSM-EQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSE 454
|
170 180 190
....*....|....*....|....*....|....
gi 156095386 1417 IASI-KRSDKIVVFNNPDRTGSFVQAQGTHEELL 1449
Cdd:PRK10762 455 MPEVlGMSDRILVMHEGRISGEFTREQATQEKLM 488
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
381-652 |
6.79e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.95 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 381 KKIQFKNVRFHYDTRKDVEiYKDLN---FTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVN 454
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFE-FKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaiPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 455 -LKWWRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdlealseESNEDGFssqsdsnsrnscraKCAGDLNDMIQttds 531
Cdd:PRK13645 84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-------ENKQEAY--------------KKVPELLKLVQ---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 532 teliqvrknyetiedsevvsvskkvlihdfvsaLPDKYetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK13645 139 ---------------------------------LPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 156095386 612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVM 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
387-671 |
6.98e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 387 NVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIeRLYDPTEGDviindshnlkdvnlkwwrskigvV 465
Cdd:PRK10261 19 NIAFMQE-QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGL-----------------------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 466 SQDPLLFSNSIKNNIkyslyslkdleALSEesnedgfssQSDSNSRNSCRAKCAgdlndMIQTTDSTELIQVRKNYETIE 545
Cdd:PRK10261 74 QCDKMLLRRRSRQVI-----------ELSE---------QSAAQMRHVRGADMA-----MIFQEPMTSLNPVFTVGEQIA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 546 DS----------EVVSVSKKVLihDFVSaLPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK10261 129 ESirlhqgasreEAMVEAKRML--DQVR-IPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQ 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 616 YLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRENGSTVDVDVLGEDPT 671
Cdd:PRK10261 205 AQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1353-1395 |
8.44e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 8.44e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK15134 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
59-347 |
9.08e-10 |
|
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: 61.70 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 59 RKLLGVSFVCATISGGT---LPFFVSVF---GVIMKNMNLGenvndIIFSLVLIGIFqfILSFISSFCMD----VVTTKI 128
Cdd:cd18549 1 KKLFFLDLFCAVLIAALdlvFPLIVRYIiddLLPSKNLRLI-----LIIGAILLALY--ILRTLLNYFVTywghVMGARI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 129 LKTLKIEFLKSVFYQDGQFHDNNP-G---SKLTSDLdFYL-EQVNAGIGTKFITIFTyasaFLGLYIWSLFKNARLTLCI 203
Cdd:cd18549 74 ETDMRRDLFEHLQKLSFSFFDNNKtGqlmSRITNDL-FDIsELAHHGPEDLFISIIT----IIGSFIILLTINVPLTLIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 204 TCVFPLIYICGVICNKKVK-----INKKTSLLYnnntmSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANL 278
Cdd:cd18549 149 FALLPLMIIFTIYFNKKMKkafrrVREKIGEIN-----AQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYK 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 279 MESLHIGMINGFI----LASYAFGFW--YGTRIIISDLsnqqpnndfhggsvISILLgvLISMFMLTI-ILPNITE 347
Cdd:cd18549 224 AMAYFFSGMNFFTnllnLVVLVAGGYfiIKGEITLGDL--------------VAFLL--YVNVFIKPIrRLVNFTE 283
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1240-1450 |
9.35e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.33 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 QQGDEEQNVGMKNAN-EFSSSKEGA-DGQS----STLFKN--------SGKILLDGVDIC----DYNLKDLRNLFSIVSQ 1301
Cdd:PRK13646 13 QKGTPYEHQAIHDVNtEFEQGKYYAiVGQTgsgkSTLIQNinallkptTGTVTVDDITIThktkDKYIRPVRKRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1302 --EPMLFNMSIYENIKFGKENaTREDVKRAcKFAAIDEFIESLPNQYDTNVGPYgkSLSGGQKQRIAIARALLREPKILL 1379
Cdd:PRK13646 93 fpESQLFEDTVEREIIFGPKN-FKMNLDEV-KNYAHRLLMDLGFSRDVMSQSPF--QMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1380 LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQaQGTHEELLS 1450
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKE----GSIVS-QTSPKELFK 235
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
826-1115 |
9.59e-10 |
|
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: 61.38 E-value: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 826 AIIALSIMVAGGL-YPLFallyakyVGTLFDFANLEANSNK---YSLY--------ILVI-AIAMFisetLKNYYNNVIG 892
Cdd:cd18573 1 ALALLLVSSAVTMsVPFA-------IGKLIDVASKESGDIEifgLSLKtfalallgVFVVgAAANF----GRVYLLRIAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 893 EKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLsahINR---DVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVA 969
Cdd:cd18573 70 ERIVARLRKRLFKSILRQDAAFFDK--NKTGEL---VSRlssDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 970 AVLTGT---YFIFMRVFAIRARIAANKdvekkrvnqpgtafVYNSDDEIFKdpsfLIQEAFYNMNTVIIYGLEDYFCTLI 1046
Cdd:cd18573 145 LVMLLVvppIAVGAVFYGRYVRKLSKQ--------------VQDALADATK----VAEERLSNIRTVRAFAAERKEVERY 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1047 EKAIDYSNKGQKRKTLINSMLWGfsqSAQFFINSFAY---WFGSFLIRRGTIQVDDfmksLFTFLFTGSYAG 1115
Cdd:cd18573 207 AKKVDEVFDLAKKEALASGLFFG---STGFSGNLSLLsvlYYGGSLVASGELTVGD----LTSFLMYAVYVG 271
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
833-1120 |
9.85e-10 |
|
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: 61.35 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 833 MVAGGLYPLFALLYAKYVGTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMY 909
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTaslNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 910 QEISFFDQDSHapGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGT---YFIFMRVF--A 984
Cdd:cd18576 82 LPLSFFHERRV--GELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATvpvVVLVAVLFgrR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 985 IRaRIAankdveKKRVNQPGTAFVYnsddeifkdpsflIQEAFYNMNTVIIYGLEDY----FCTLIEKAIDYSNKGQKrk 1060
Cdd:cd18576 160 IR-KLS------KKVQDELAEANTI-------------VEETLQGIRVVKAFTREDYeierYRKALERVVKLALKRAR-- 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1061 tlINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDfmksLFTFLF-TGSYAGKLMSL 1120
Cdd:cd18576 218 --IRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGD----LVAFLLyTLFIAGSIGSL 272
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1265-1412 |
1.10e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.68 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1265 GQSSTLF-------KNSGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLFN-MSIYENIKFGKEnaTREDVKRACKFAAI 1335
Cdd:PRK10895 41 GKTTTFYmvvgivpRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRrLSVYDNLMAVLQ--IRDDLSAEQREDRA 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1336 DEFIESLPNQYDTNvgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1412
Cdd:PRK10895 119 NELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLIT 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
392-636 |
1.14e-09 |
|
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: 60.25 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 392 YDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNL-KWWRSKIGVVSQDPL 470
Cdd:cd03218 10 YGKRKVV---NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG-QDITKLPMhKRARLGIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 471 LFSN-SIKNNIKYSLYSLKDLEALSEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsev 549
Cdd:cd03218 86 IFRKlTVEENILAVLEIRGLSKKEREEKLEE------------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 550 vsvskkvLIHDFvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnE 629
Cdd:cd03218 117 -------LLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK--D 181
|
....*..
gi 156095386 630 NRITIII 636
Cdd:cd03218 182 RGIGVLI 188
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1357-1417 |
1.21e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 60.65 E-value: 1.21e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV 195
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
390-636 |
1.22e-09 |
|
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: 60.42 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 390 FHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdvnLKWWRSKIGVVSQDP 469
Cdd:cd03267 27 FKRKYR-EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--------LVPWKRRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 470 LLFSNsiKNNIKYslyslkDLEALseesneDGFSsqsdsnsrnscrakcagdLNDMIQTTDSTELiqvRKNYETIedSEV 549
Cdd:cd03267 98 VVFGQ--KTQLWW------DLPVI------DSFY------------------LLAAIYDLPPARF---KKRLDEL--SEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 550 VSVskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNE 629
Cdd:cd03267 141 LDL-----------------EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY--NR 201
|
....*..
gi 156095386 630 NRITIII 636
Cdd:cd03267 202 ERGTTVL 208
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1274-1428 |
1.22e-09 |
|
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: 62.53 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLF-NMSIYENIKFGKE---NATRED----VKRACKFAA---IDEFIES 1341
Cdd:TIGR02633 57 DGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVAENIFLGNEitlPGGRMAynamYLRAKNLLRelqLDADNVT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1342 LPnqydtnVGPYGkslsGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIK 1421
Cdd:TIGR02633 137 RP------VGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHG-VACVYISHKLNEVK 205
|
....*...
gi 156095386 1422 R-SDKIVV 1428
Cdd:TIGR02633 206 AvCDTICV 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
374-611 |
1.24e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.39 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 374 GKKLkdikkIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIndSHNLkdv 453
Cdd:COG0488 312 GKKV-----LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--GETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 454 nlkwwrsKIGVVSQdpllfsnsiknnikyslyslkDLEALSEESNedgfssqsdsnsrnscrakcagdlndMIQttdstE 533
Cdd:COG0488 379 -------KIGYFDQ---------------------HQEELDPDKT--------------------------VLD-----E 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 534 LIQVRKNYETIEdsevvsvskkvlIHDFVSAL---PDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:COG0488 400 LRDGAPGGTEQE------------VRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
.
gi 156095386 611 D 611
Cdd:COG0488 464 D 464
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1164-1455 |
1.45e-09 |
|
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: 60.59 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLS------RPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskE 1237
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL---------------------E 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1238 QMQQGdeeqNVGMKnanefssskegadGQSSTLFKNSGKilldgvdicdynlKDLRNLFSIVSQE-PMLFN--MSIYENI 1314
Cdd:TIGR02769 62 KPAQG----TVSFR-------------GQDLYQLDRKQR-------------RAFRRDVQLVFQDsPSAVNprMTVRQII 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1315 KFGKENATRED-VKRACKFAAIDEFIESLPNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:TIGR02769 112 GEPLRHLTSLDeSEQKARIAELLDMVGLRSEDADK----LPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQA 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1394 LIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAQGTHEELLSVQDGV 1455
Cdd:TIGR02769 188 VILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDK----GQIVEECDVAQLLSFKHPAG 246
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
396-644 |
1.47e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.15 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG-----DVIINDSHNLKDVN--LKWWRSKIGVVSQD 468
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKglIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 469 PLLFSNsiknnikyslyslkdlealseesnedgfssqsdsnsRNScrakcagdLNDMIQTTdstelIQVRKnyetIEDSE 548
Cdd:PRK11264 94 FNLFPH------------------------------------RTV--------LENIIEGP-----VIVKG----EPKEE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 549 VVSVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLKG- 627
Cdd:PRK11264 121 ATARARELLAKVGLAGKETSY-------PRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE---LVGEVLNTIRQl 190
|
250
....*....|....*...
gi 156095386 628 -NENRITIIIAHRLSTIR 644
Cdd:PRK11264 191 aQEKRTMVIVTHEMSFAR 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
394-611 |
1.50e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.42 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDVIINDshnlKDVN-LKWWRSKIGVVSQDP 469
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNG----RRLTaLPAEQRRIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 470 LLFSN-SIKNNIKYSLyslkdlealseesnedgfssqSDSNSRNSCRAKCAgdlndmiQTTDSTELiqvrknyetiedse 548
Cdd:COG4136 86 LLFPHlSVGENLAFAL---------------------PPTIGRAQRRARVE-------QALEEAGL-------------- 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 549 vvsvskkvliHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4136 124 ----------AGFADRDPAT-----------LSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
399-651 |
1.69e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKN 478
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG-QTINLVRDKDGQLKVADKNQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 479 NIKYSLYS-LKDLEALSEESnedgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRKNYETIEDSEVVSVSKKVL 557
Cdd:PRK10619 98 FQHFNLWShMTVLENVMEAP-------------------------------------IQVLGLSKQEARERAVKYLAKVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 558 IHDfvsALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIA 637
Cdd:PRK10619 141 IDE---RAQGKY-------PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVT 209
|
250
....*....|....*.
gi 156095386 638 HRLSTIRYANT--IFV 651
Cdd:PRK10619 210 HEMGFARHVSShvIFL 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1174-1388 |
1.71e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1174 LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqGDEEqnvgmkna 1253
Cdd:COG0488 6 KSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA----------------------------GELE-------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1254 nefssskegADgqsstlfknSGKILLDgvdicdynlKDLRnlFSIVSQEPMLF-NMSIYENIKFG--------------- 1317
Cdd:COG0488 50 ---------PD---------SGEVSIP---------KGLR--IGYLPQEPPLDdDLTVLDTVLDGdaelraleaeleele 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -KENATREDVKRA----CKFAAIDEF-----IESL-------PNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLL 1380
Cdd:COG0488 101 aKLAEPDEDLERLaelqEEFEALGGWeaearAEEIlsglgfpEEDLDRPVS----ELSGGWRRRVALARALLSEPDLLLL 176
|
....*...
gi 156095386 1381 DEATSSLD 1388
Cdd:COG0488 177 DEPTNHLD 184
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
578-652 |
1.87e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 1.87e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVAL 226
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
65-309 |
1.99e-09 |
|
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: 60.58 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 65 SFVCATISGGT---LPFFV-SVFGVIMKNMNLGeNVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSV 140
Cdd:cd18576 1 GLILLLLSSAIglvFPLLAgQLIDAALGGGDTA-SLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 141 FYQDGQFHDNN-PG---SKLTSDldfyLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVI 216
Cdd:cd18576 80 QRLPLSFFHERrVGeltSRLSND----VTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 217 CNKKV-KINKKT--SLlynNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILA 293
Cdd:cd18576 156 FGRRIrKLSKKVqdEL---AEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFG 232
|
250
....*....|....*.
gi 156095386 294 SYAFGFWYGTRIIISD 309
Cdd:cd18576 233 AIVAVLWYGGRLVLAG 248
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1353-1418 |
2.18e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.76 E-value: 2.18e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--KTIITIAHRIA 1418
Cdd:PRK11264 141 YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMS 205
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
61-308 |
2.47e-09 |
|
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: 60.22 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 61 LLGVSfvcatiSGGTL--PFFV-----SVFGVIMKNMNLGENVNdiIFSLVLIGIFQF--ILSFISSFCMDVVTTKILKT 131
Cdd:cd18573 4 LLLVS------SAVTMsvPFAIgklidVASKESGDIEIFGLSLK--TFALALLGVFVVgaAANFGRVYLLRIAGERIVAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 132 LKIEFLKSVFYQDGQFHDNNP----GSKLTSDLDFYLEQV--NAGIGTKFItIFTYASAFLGLYIwslfkNARLTLCITC 205
Cdd:cd18573 76 LRKRLFKSILRQDAAFFDKNKtgelVSRLSSDTSVVGKSLtqNLSDGLRSL-VSGVGGIGMMLYI-----SPKLTLVMLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 206 VFPLIYICGVICNKKVKinKKTSLLYNN--NTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLH 283
Cdd:cd18573 150 VVPPIAVGAVFYGRYVR--KLSKQVQDAlaDATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLF 227
|
250 260
....*....|....*....|....*
gi 156095386 284 IGMINGFILASYAFGFWYGTRIIIS 308
Cdd:cd18573 228 FGSTGFSGNLSLLSVLYYGGSLVAS 252
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1164-1388 |
2.75e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.40 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqTGEsskeqmqqgd 1243
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL------------------SGE---------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGKENAT 1322
Cdd:PRK13548 52 --------------------------LSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVVAMGRAPHG 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1323 REDVKRAckfAAIDEFIESlpnqydTNVGPYGK----SLSGGQKQRIAIARALLR------EPKILLLDEATSSLD 1388
Cdd:PRK13548 106 LSRAEDD---ALVAAALAQ------VDLAHLAGrdypQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
403-654 |
3.07e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDP----TEGDVIINDSHNLK--DVNLKWWR-SKIGVVSQDPLLFSN 474
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHasEQTLRGVRgNKIAMIFQEPMVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 475 SIkNNIKYSLYslkdlEALSEESNEdgfssqsdsnSRNSCRAkcagdlnDMIQTTDSTELIQVRKNyetiedsevvsvsk 554
Cdd:PRK15134 107 PL-HTLEKQLY-----EVLSLHRGM----------RREAARG-------EILNCLDRVGIRQAAKR-------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 555 kvlIHDFvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
Cdd:PRK15134 150 ---LTDY---------------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLL 211
|
250 260
....*....|....*....|.
gi 156095386 635 IIAHRLSTIR-YANTIFVLSN 654
Cdd:PRK15134 212 FITHNLSIVRkLADRVAVMQN 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
388-445 |
3.07e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.32 E-value: 3.07e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 388 VRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN 445
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1337-1429 |
3.13e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1337 EFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIA 1414
Cdd:PRK13409 436 EIIKplQLERLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVD 511
|
90
....*....|....*.
gi 156095386 1415 HRIASIKR-SDKIVVF 1429
Cdd:PRK13409 512 HDIYMIDYiSDRLMVF 527
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
864-1123 |
3.15e-09 |
|
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: 59.96 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 864 NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNN 943
Cdd:cd18780 42 NQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDV--TRTGELLNRLSSDTQVLQNAVTVN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 944 IVIFTHFIVLFLVSTVMSFYFCPivaaVLTGTYFIFMRVFAIRARIAANKDVEKKRVNQPGTAfvynsddeifkDPSFLI 1023
Cdd:cd18780 120 LSMLLRYLVQIIGGLVFMFTTSW----KLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALA-----------AASTVA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1024 QEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDD---F 1100
Cdd:cd18780 185 EESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLltsF 264
|
250 260
....*....|....*....|...
gi 156095386 1101 MksLFTFLFTGSYAGkLMSLKGD 1123
Cdd:cd18780 265 L--LYTLTVAMSFAF-LSSLYGD 284
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
825-1134 |
3.56e-09 |
|
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: 59.77 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAgglypLFALLYAKYVGTLFDF---ANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18570 5 ILILLLSLLIT-----LLGIAGSFFFQILIDDiipSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 902 RLFENIMYQEISFFdqDSHAPGLLSAHIN-----RDV--HLLKTGLVNNIVIFTHFIVLFLVSTVMsFYFCPIVAAVLTG 974
Cdd:cd18570 80 GYFKHLLKLPLSFF--ETRKTGEIISRFNdankiREAisSTTISLFLDLLMVIISGIILFFYNWKL-FLITLLIIPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 975 TYFIFMRVF--AIRARIAANKDVEkkrvnqpgtafvynsddeifkdpSFLIqEAFYNMNTVIIYGLEDYFCTLIEKAIDY 1052
Cdd:cd18570 157 IILLFNKPFkkKNREVMESNAELN-----------------------SYLI-ESLKGIETIKSLNAEEQFLKKIEKKFSK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1053 SNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFM--KSLFTFlFTGSyAGKLMSLKGDSENAKLS 1130
Cdd:cd18570 213 LLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIafNALLGY-FLGP-IENLINLQPKIQEAKVA 290
|
....
gi 156095386 1131 FERY 1134
Cdd:cd18570 291 ADRL 294
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1355-1431 |
3.77e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.74 E-value: 3.77e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEkLIEKTIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4152 128 EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPvNVE-LLKDVIRELAAK-GTTVIFSSHQMELVEElCDRIVIINK 204
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1274-1431 |
4.27e-09 |
|
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: 57.44 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNL-FSIVSQEPM---LF-NMSIYENIkfgkenatredvkrackfaaidefieSLPNQydt 1348
Cdd:cd03215 54 SGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVlDLSVAENI--------------------------ALSSL--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1349 nvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKR-SDKIV 1427
Cdd:cd03215 105 --------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGlCDRIL 175
|
....
gi 156095386 1428 VFNN 1431
Cdd:cd03215 176 VMYE 179
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1341-1429 |
4.49e-09 |
|
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: 60.95 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1420
Cdd:COG1245 444 GLEKLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLI 519
|
90
....*....|
gi 156095386 1421 KR-SDKIVVF 1429
Cdd:COG1245 520 DYiSDRLMVF 529
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
369-654 |
4.68e-09 |
|
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: 59.10 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 369 ENNQDGKKLKDIKKIQFKNVRFHYDTrkdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdvIINDSh 448
Cdd:cd03291 26 QENNDRKHSSDDNNLFFSNLCLVGAP-----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--KIKHS- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 449 nlkdvnlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnSRNSCRAKcagdlndmiqt 528
Cdd:cd03291 98 -----------GRISFSSQFSWIMPGTIKENIIFGV-------------------------SYDEYRYK----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 529 tdsteliqvrknyetiedsevvSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
Cdd:cd03291 131 ----------------------SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 156095386 609 SLDNKSEYLV-QKTINNLKGNENRitIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03291 189 YLDVFTEKEIfESCVCKLMANKTR--ILVTSKMEHLKKADKILILHE 233
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
378-472 |
4.88e-09 |
|
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: 60.58 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 378 KDIKKIQFKNVRFHYDTRKDVEIYK--DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNL 455
Cdd:COG4615 323 ADFQTLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG-QPVTADNR 401
|
90
....*....|....*..
gi 156095386 456 KWWRSKIGVVSQDPLLF 472
Cdd:COG4615 402 EAYRQLFSAVFSDFHLF 418
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1339-1429 |
5.03e-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: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 IESLpnqYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1418
Cdd:cd03237 105 IEQI---LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDII 177
|
90
....*....|..
gi 156095386 1419 SIKR-SDKIVVF 1429
Cdd:cd03237 178 MIDYlADRLIVF 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1183-1451 |
5.16e-09 |
|
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: 60.59 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEQTGESskeqmqqgdeeqnVGMKNANEFSSSKEG 1262
Cdd:TIGR03269 17 KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEK-------------CGYVERPSKVGEPCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 ADGQSSTLFKnsgkilLDGVDICDYNLKDLRNLFSIVSQEPMLF--NMSIYENIKFGKENA---TREDVKRACkfaaidE 1337
Cdd:TIGR03269 84 VCGGTLEPEE------VDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIgyeGKEAVGRAV------D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1338 FIESLpnQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:TIGR03269 152 LIEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260 270
....*....|....*....|....*....|....*
gi 156095386 1418 ASI-KRSDKIVVFNNpdrtGSFVQaQGTHEELLSV 1451
Cdd:TIGR03269 230 EVIeDLSDKAIWLEN----GEIKE-EGTPDEVVAV 259
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1330-1433 |
5.17e-09 |
|
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: 56.61 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1330 CKFAAIDEFIESLPNQY-DTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD-----IK 1403
Cdd:smart00382 33 VIYIDGEDILEEVLDQLlLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLK 112
|
90 100 110
....*....|....*....|....*....|....*.
gi 156095386 1404 DKADKTIITIAHRIASIK------RSDKIVVFNNPD 1433
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGpallrrRFDRRIVLLLIL 148
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
99-309 |
5.88e-09 |
|
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: 58.94 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 99 IIFSLVLIG--IFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIG 172
Cdd:cd18544 41 LLLALLYLGllLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVgrlvTRVTNDTEALNELFTSGLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 173 TKFITIFTyasaFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVK-----INKKTSLLynnNTMsiIEEALVGIR 247
Cdd:cd18544 121 TLIGDLLL----LIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRkayreVREKLSRL---NAF--LQESISGMS 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 248 TVVSYCGENTILKKFN-LSEKLYsKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISD 309
Cdd:cd18544 192 VIQLFNREKREFEEFDeINQEYR-KANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSG 253
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1357-1431 |
6.76e-09 |
|
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: 55.92 E-value: 6.76e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQvATKIIELED 142
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1269-1449 |
7.00e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1269 TLF----KNSGKILLDGVDICDYN-LKDLRNLFSIVSQE----------PMLFNmSIYENIKFGKENATREDVKRACKFA 1333
Cdd:PRK10982 293 TLFgireKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyaylDIGFN-SLISNIRNYKNKVGLLDNSRMKSDT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1334 --AIDEFIESLPNQYdTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTII 1411
Cdd:PRK10982 372 qwVIDSMRVKTPGHR-TQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGII 445
|
170 180 190
....*....|....*....|....*....|....*....
gi 156095386 1412 TIAHRIAS-IKRSDKIVVFNNPDRTGSFVQAQGTHEELL 1449
Cdd:PRK10982 446 IISSEMPElLGITDRILVMSNGLVAGIVDTKTTTQNEIL 484
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
389-445 |
8.40e-09 |
|
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: 57.54 E-value: 8.40e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 389 RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN 445
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
825-1097 |
8.66e-09 |
|
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: 58.57 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLY-PLF------ALLYAKYVGTLFDFANLeansNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEK 897
Cdd:cd18547 3 LVIILAIISTLLSVLgPYLlgkaidLIIEGLGGGGGVDFSGL----LRILLLLLGLYLLSALFSYLQNRLMARVSQRTVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 898 TMKLRLFENIMYQEISFFDQdsHAPG-LLSAHINrDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP---IVAAVLT 973
Cdd:cd18547 79 DLRKDLFEKLQRLPLSYFDT--HSHGdIMSRVTN-DVDNISQALSQSLTQLISSILTIVGTLIMMLYISPlltLIVLVTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 974 GTYFIFMRVFAIRARIAAnkdveKKRVNQPG--TAFvynsddeifkdpsflIQEAFYNMNTVIIYGLEDY----FCTLIE 1047
Cdd:cd18547 156 PLSLLVTKFIAKRSQKYF-----RKQQKALGelNGY---------------IEEMISGQKVVKAFNREEEaieeFDEINE 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1048 KAIDYSNKGQKRKTLINSMLwgfsqsaqFFINSFAY----WFGSFLIRRGTIQV 1097
Cdd:cd18547 216 ELYKASFKAQFYSGLLMPIM--------NFINNLGYvlvaVVGGLLVINGALTV 261
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
404-611 |
1.10e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 57.28 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 404 LNFTLT--EGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS-HNLKDVNlkwwRSKIGVVSQDPLLFSN-SIKNN 479
Cdd:PRK10771 16 MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTTTPPS----RRPVSMLFQENNLFSHlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 IKYSLY-SLKdleaLSEESNEdgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsEVVSVSKKVLI 558
Cdd:PRK10771 92 IGLGLNpGLK----LNAAQRE------------------------------------------------KLHAIARQMGI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 156095386 559 HDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10771 120 EDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
399-611 |
1.17e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.56 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDViindSHNLKDVNLKWWRS-KIGVVSQDPLLFSN-SI 476
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI----RFHGTDVSRLHARDrKVGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 477 KNNIKYSLYSLKDLEALSeesnedgfssqsdsnsRNSCRAKCAgDLNDMIQttdsteliqvrknyetiedsevvsvskkv 556
Cdd:PRK10851 92 FDNIAFGLTVLPRRERPN----------------AAAIKAKVT-QLLEMVQ----------------------------- 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 557 LIHdfvsaLPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10851 126 LAH-----LADRY-------PAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
386-625 |
1.25e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 386 KNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdSHNLKDVnlkwwRSKIGVV 465
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-TAPLAEA-----REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 466 SQDP-LLFSNSIKNNIKYSL---YSLKDLEALSEESNEDgfssqsdsnsrnscRAkcagdlndmiqttdsteliqvrkny 541
Cdd:PRK11247 87 FQDArLLPWKKVIDNVGLGLkgqWRDAALQALAAVGLAD--------------RA------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etiedsevvsvskkvliHDFVSALpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:PRK11247 128 -----------------NEWPAAL---------------SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 175
|
....
gi 156095386 622 INNL 625
Cdd:PRK11247 176 IESL 179
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
825-1118 |
1.31e-08 |
|
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: 57.83 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAgglyplFALLYAKYVGTLFDFANLEANSN---KYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18542 3 LAILALLLATA------LNLLIPLLIRRIIDSVIGGGLREllwLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 902 RLFENIMYQEISFFDqdsHAP-GLLSAHINRDV----HLLKTGL---VNNIVIFT-HFIVLFLVSTVMSFY---FCPIVa 969
Cdd:cd18542 77 DLYDHLQRLSFSFHD---KARtGDLMSRCTSDVdtirRFLAFGLvelVRAVLLFIgALIIMFSINWKLTLIslaIIPFI- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 970 avltgtyFIFMRVFAIRARiaankdvekkrvnqpgtafvynsddEIFKDpsflIQEAFYNMNTVI---IYG--------L 1038
Cdd:cd18542 153 -------ALFSYVFFKKVR-------------------------PAFEE----IREQEGELNTVLqenLTGvrvvkafaR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1039 EDYfctLIEKaIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFA----YWFGSFLIRRGTIQVDDfmksLFTFLftgSYA 1114
Cdd:cd18542 197 EDY---EIEK-FDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQivlvLWVGGYLVINGEITLGE----LVAFI---SYL 265
|
....
gi 156095386 1115 GKLM 1118
Cdd:cd18542 266 WMLI 269
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1356-1388 |
1.38e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.77 E-value: 1.38e-08
10 20 30
....*....|....*....|....*....|...
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1164-1415 |
1.51e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.82 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYK----DLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgeSSKEQM 1239
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHL---------------------NGLLQP 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 QQGdeEQNVGMKNANEFSSSKEgadgqsstlfknsgkilldgvdicdynLKDLRNLFSIVSQEP--MLFNMSIYENIKFG 1317
Cdd:PRK13643 59 TEG--KVTVGDIVVSSTSKQKE---------------------------IKPVRKKVGVVFQFPesQLFEETVLKDVAFG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KEN--ATREDVKR--ACKFAAI---DEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:PRK13643 110 PQNfgIPKEKAEKiaAEKLEMVglaDEFWEKSPFE-----------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
250 260
....*....|....*....|....*
gi 156095386 1391 SEKLIEKTIVDIKdKADKTIITIAH 1415
Cdd:PRK13643 179 ARIEMMQLFESIH-QSGQTVVLVTH 202
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
383-670 |
1.55e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.89 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKwwRSKI 462
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA--RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQ-DPLLFSNSIKNNIK-YSLYSlkdlealseesnedGFSSQSdsnsrnsCRAKCAGDLndmiqttdsteliqvrkn 540
Cdd:PRK13537 83 GVVPQfDNLDPDFTVRENLLvFGRYF--------------GLSAAA-------ARALVPPLL------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 yetiedsevvsvskkvlihDFvSALPDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13537 124 -------------------EF-AKLENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 621 TINNLKGNENRITII---------IAHRLSTIRYANTI-----FVLSNRENGSTVdVDVLGEDP 670
Cdd:PRK13537 180 RLRSLLARGKTILLTthfmeeaerLCDRLCVIEEGRKIaegapHALIESEIGCDV-IEIYGPDP 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1179-1434 |
1.56e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.35 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1179 VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefss 1258
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL---------------------------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1259 skeGADGQSStlfknSGKILLDGVDICDYNLKDL----RNLFSIVSQE-PMLFNMSIYENIKF-----GKENATREdvKR 1328
Cdd:PRK10535 55 ---GCLDKPT-----SGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSHLTAAQNVEVpavyaGLERKQRL--LR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAA---IDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1405
Cdd:PRK10535 125 AQELLQrlgLEDRVEYQPSQ-----------LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 1406 ADKTIITI--------AHRIASIKrsDKIVVFNNPDR 1434
Cdd:PRK10535 194 GHTVIIVThdpqvaaqAERVIEIR--DGEIVRNPPAQ 228
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1338-1443 |
1.75e-08 |
|
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: 55.79 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1338 FIESLPNQYDTNVG--PYGK---SLSGGQKQRIAIARALLREPK--ILLLDEATSSLDSNS-EKLIE--KTIVDIKDkad 1407
Cdd:cd03238 64 FIDQLQFLIDVGLGylTLGQklsTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDiNQLLEviKGLIDLGN--- 140
|
90 100 110
....*....|....*....|....*....|....*..
gi 156095386 1408 kTIITIAHRIASIKRSDKIVVFN-NPDRTGSFVQAQG 1443
Cdd:cd03238 141 -TVILIEHNLDVLSSADWIIDFGpGSGKSGGKVVFSG 176
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1307-1384 |
1.76e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1307 NMSIYENI---------KFGKENATREDvkrackfAAIDEFIESL----PNQyDTNVGpygkSLSGGQKQRIAIARALLR 1373
Cdd:COG1129 344 DLSIRENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLriktPSP-EQPVG----NLSGGNQQKVVLAKWLAT 411
|
90
....*....|.
gi 156095386 1374 EPKILLLDEAT 1384
Cdd:COG1129 412 DPKVLILDEPT 422
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1356-1389 |
1.81e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.99 E-value: 1.81e-08
10 20 30
....*....|....*....|....*....|....
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1274-1387 |
1.90e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNL-KDLRNLFSIVSQEPMLFN-MSIYENIKFGKENATREDVKRAckfaaIDEFIESLPNQYDTNVG 1351
Cdd:PRK11614 59 SGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQER-----IKWVYELFPRLHERRIQ 133
|
90 100 110
....*....|....*....|....*....|....*.
gi 156095386 1352 PYGkSLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:PRK11614 134 RAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1184-1431 |
2.29e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKS----TVMSLLmrfydlkndhhivfkneqtgESSKEQMQQGDeeqnvgmknanefsss 1259
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLL--------------------PSPPVVYPSGD---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1260 kegadgqsstlfknsgkILLDGVDICDYNLKDLR----NLFSIVSQEPM-----LFNM--SIYENIKFGKeNATREdvkr 1328
Cdd:PRK15134 71 -----------------IRFHGESLLHASEQTLRgvrgNKIAMIFQEPMvslnpLHTLekQLYEVLSLHR-GMRRE---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ackfAAIDEFIESLP----NQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:PRK15134 129 ----AARGEILNCLDrvgiRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQ 204
|
250 260
....*....|....*....|....*...
gi 156095386 1405 KADKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:PRK15134 205 ELNMGLLFITHNLSIVRKlADRVAVMQN 232
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
99-307 |
2.40e-08 |
|
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: 57.04 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 99 IIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNP-G---SKLTSDLDFyLEQVnAGIGTK 174
Cdd:cd18541 42 YALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRtGdlmARATNDLNA-VRMA-LGPGIL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 175 FI--TIFTYASAFlglyIWSLFKNARLTLCITCVFPLIYICGVICNKKV-----KINKKTSLLYNnntmsIIEEALVGIR 247
Cdd:cd18541 120 YLvdALFLGVLVL----VMMFTISPKLTLIALLPLPLLALLVYRLGKKIhkrfrKVQEAFSDLSD-----RVQESFSGIR 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 248 TVVSYCGENTILKKF-NLSEKLYSKyTLKANLMESLHIGMINGFILASYAFGFWYGTRIII 307
Cdd:cd18541 191 VIKAFVQEEAEIERFdKLNEEYVEK-NLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVI 250
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
387-611 |
3.19e-08 |
|
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: 58.16 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 387 NVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDVIINDsHNLKDVNLKWWR--- 459
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG-QDLLGLSERELRrir 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 -SKIGVVSQDPL-----LFSnsIKNNIKYSLySLKdlEALSeesnedgfssqsdsnsRNSCRAKCAgDLndmiqttdste 533
Cdd:COG4172 91 gNRIAMIFQEPMtslnpLHT--IGKQIAEVL-RLH--RGLS----------------GAAARARAL-EL----------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 534 LIQVRknyetiedsevvsvskkvlihdfvsaLPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4172 138 LERVG--------------------------IPDP-ERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
392-654 |
3.31e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 56.73 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 392 YDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDvNLKWWRSKIGVVSQDP-- 469
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE-NIREVRKFVGLVFQNPdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 470 LLFSNSIKNNIKYSLYSLkdleALSEesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyETIEdSEV 549
Cdd:PRK13652 90 QIFSPTVEQDIAFGPINL----GLDE----------------------------------------------ETVA-HRV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 550 VSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 629
Cdd:PRK13652 119 SSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETY 187
|
250 260
....*....|....*....|....*.
gi 156095386 630 NRITIIIAHRLSTI-RYANTIFVLSN 654
Cdd:PRK13652 188 GMTVIFSTHQLDLVpEMADYIYVMDK 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1298-1446 |
3.43e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1298 IVSQEPMLF-NMSIYENIKFG--KENATREDVKrackfaaidEFIESLPNQYDTNVGpyGKSLSGGQKQRIAIARALLRE 1374
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILFGlpKRQASMQKMK---------QLLAALGCQLDLDSS--AGSLEVADRQIVEILRGLMRD 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1375 PKILLLDEATSSLD-SNSEKLIEKtIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQAQGTHE 1446
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSR-IRELLAQ-GVGIVFISHKLPEIRQlADRISVM----RDGTIALSGKTAD 226
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
396-638 |
3.46e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDVIINDShNLKDVNLKWwRSKIGVVsqdpLLFS 473
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGE-SILDLEPEE-RAHLGIF----LAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 474 NSIKnnikyslyslkdleaLSEESNEDGFssqsdsnsRNSCRAKcagdlndmiqttdsteliqvRKNYETIEDSEVvsvs 553
Cdd:CHL00131 92 YPIE---------------IPGVSNADFL--------RLAYNSK--------------------RKFQGLPELDPL---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 554 kkvlihDFVSALPDKYEtLVGSNASKL--------SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:CHL00131 125 ------EFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL 197
|
250
....*....|...
gi 156095386 626 KGNENRItIIIAH 638
Cdd:CHL00131 198 MTSENSI-ILITH 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1190-1415 |
3.90e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1190 ESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknEQTGESS--KEQMQQGDEEQNVGMKNANEfssskeGADGQS 1267
Cdd:PRK10584 34 KRGETIALIGESGSGKSTLLAILAGLDD-----------GSSGEVSlvGQPLHQMDEEARAKLRAKHV------GFVFQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFKNsgkilldgvdicdynLKDLRNLfsivsQEPMLfnmsiyenIKFGKENATREDVKRACKFAAIDEFIESLPNQyd 1347
Cdd:PRK10584 97 FMLIPT---------------LNALENV-----ELPAL--------LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1348 tnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1415
Cdd:PRK10584 147 ---------LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
403-647 |
4.07e-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: 57.84 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDVIINDShnlkdvnlkwwRSKIGVVSQDPLLFSNSIKNNIKY 482
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 483 SLYSlkdlealsEESNEDGFSSQsdsnsrnscrakcagDLNDMIQTTDSTELIQVRKNYETIED-SEVvsvskkvlihdf 561
Cdd:TIGR00954 538 PDSS--------EDMKRRGLSDK---------------DLEQILDNVQLTHILEREGGWSAVQDwMDV------------ 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 562 vsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKgnENRITII-IAHRL 640
Cdd:TIGR00954 583 ------------------LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE---GYMYRLCR--EFGITLFsVSHRK 639
|
....*..
gi 156095386 641 STIRYAN 647
Cdd:TIGR00954 640 SLWKYHE 646
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1268-1428 |
4.51e-08 |
|
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: 54.84 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK----------NSGKILLDGVDICDynlkdlrnlfsivsqepmlfnMSIYENIKFG-----KENATREDVKrackf 1332
Cdd:cd03217 40 STLAKtimghpkyevTEGEILFKGEDITD---------------------LPPEERARLGiflafQYPPEIPGVK----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1333 aaIDEFIESLpnqydtNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIIT 1412
Cdd:cd03217 94 --NADFLRYV------NEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLI 159
|
170
....*....|....*...
gi 156095386 1413 IAH--RIASIKRSDKIVV 1428
Cdd:cd03217 160 ITHyqRLLDYIKPDRVHV 177
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
399-631 |
5.16e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShnlkdvnlkwwrskigvvsqdPLlfsNSIKN 478
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ---------------------PM---SKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 479 NIKYSLyslkdlealseESNEDGFSSQ-----SDSNSrnscrakcagdlndmIQTTDSTELIQVRKNYETIEDSevvsvs 553
Cdd:PRK11629 79 AAKAEL-----------RNQKLGFIYQfhhllPDFTA---------------LENVAMPLLIGKKKPAEINSRA------ 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 554 kkvliHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylvQKTINNLKGNENR 631
Cdd:PRK11629 127 -----LEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN----ADSIFQLLGELNR 193
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1268-1436 |
5.46e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDL----RNLFSIVSQEPMLFNMSIYENIKFGK--ENATREDVKRACKfA 1333
Cdd:PRK10908 42 STLLKlicgierpSAGKIWFSGHDITRLKNREVpflrRQIGMIFQDHHLLMDRTVYDNVAIPLiiAGASGDDIRRRVS-A 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1334 AIDEF-----IESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADK 1408
Cdd:PRK10908 121 ALDKVglldkAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGV 188
|
170 180
....*....|....*....|....*....
gi 156095386 1409 TIITIAHRIASI-KRSDKIVVFNNPDRTG 1436
Cdd:PRK10908 189 TVLMATHDIGLIsRRSYRMLTLSDGHLHG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1353-1433 |
6.03e-08 |
|
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: 57.12 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI---------ASIKRS 1423
Cdd:TIGR03269 424 YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMdfvldvcdrAALMRD 503
|
90
....*....|
gi 156095386 1424 DKIVVFNNPD 1433
Cdd:TIGR03269 504 GKIVKIGDPE 513
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
890-1101 |
6.34e-08 |
|
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: 56.01 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 890 VIGEKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKT--------GLVNNIVIFTHFIVLFLVSTVMS 961
Cdd:cd18574 68 VVGERVAARLRNDLFSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSsfkqcvsqGLRSVTQTVGCVVSLYLISPKLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 962 FYFCPIV-AAVLTGTYF-IFMRVFAIRAriaankdveKKRVNQP-GTAFvynsddeifkdpsfliqEAFYNMNTVIIYGL 1038
Cdd:cd18574 146 LLLLVIVpVVVLVGTLYgSFLRKLSRRA---------QAQVAKAtGVAD-----------------EALGNIRTVRAFAM 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1039 EDYFCTLiekaidYSNKGQKRKTLiNSML---WGFSQS-AQFFINSFA---YWFGSFLIRRGTIQVDDFM 1101
Cdd:cd18574 200 EDRELEL------YEEEVEKAAKL-NEKLglgIGIFQGlSNLALNGIVlgvLYYGGSLVSRGELTAGDLM 262
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
400-654 |
8.41e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 55.02 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdvnlkwwrskigvvsqdpllfsnsiknn 479
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD--------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 ikyslyslKDLEALSeesnedgfssqsdsnSRNSCRAkcagdLNDMIQTTDSTELIQVRKNYE-------------TIED 546
Cdd:PRK11231 64 --------KPISMLS---------------SRQLARR-----LALLPQHHLTPEGITVRELVAygrspwlslwgrlSAED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 547 SEVVSVSkkvlIHDF-VSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:PRK11231 116 NARVNQA----MEQTrINHLADR-------RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMREL 184
|
250 260 270
....*....|....*....|....*....|
gi 156095386 626 KgNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:PRK11231 185 N-TQGKTVVTVLHDLNqASRYCDHLVVLAN 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1274-1418 |
9.12e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF----NMSIYENIKFGkenatREDVKRACK-----FAAIDEFIESLP 1343
Cdd:COG3845 312 SGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRglvpDMSVAENLILG-----RYRRPPFSRggfldRKAIRAFAEELI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQYD---TNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK--------AD-KTII 1411
Cdd:COG3845 387 EEFDvrtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgaavllisEDlDEIL 466
|
....*..
gi 156095386 1412 TIAHRIA 1418
Cdd:COG3845 467 ALSDRIA 473
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
403-673 |
1.02e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPT---EGDVI----------INDSHnlkdvnlkwwRSKIGVVSQD- 468
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILfdgevcrfkdIRDSE----------ALGIVIIHQEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 469 ---PLLfsnSIKNNIkyslyslkdleALSEESNEDGFSSQSDSNSRnscrakcagdlndmiqttdSTELIqvrknyetie 545
Cdd:NF040905 88 aliPYL---SIAENI-----------FLGNERAKRGVIDWNETNRR-------------------ARELL---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 546 dsevvsvsKKVlihdfvsALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVQkTINN 624
Cdd:NF040905 125 --------AKV-------GLDESPDTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LLLE 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 156095386 625 LKgnENRIT-IIIAHRLSTIRY-ANTIFVLsnrENGSTVD-VDVLGEDPTKD 673
Cdd:NF040905 185 LK--AQGITsIIISHKLNEIRRvADSITVL---RDGRTIEtLDCRADEVTED 231
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
826-1114 |
1.25e-07 |
|
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: 54.80 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 826 AIIALsIMVAGGLyplFALLYAkyVGTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVekTMKLR 902
Cdd:cd18575 1 ALIAL-LIAAAAT---LALGQG--LRLLIDQGFAAGNTallNRAFLLLLAVALVLALASALRFYLVSWLGERV--VADLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 903 --LFENIMYQEISFFDqdSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP--------IVAAVL 972
Cdd:cd18575 73 kaVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltllvllVIPLVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 973 tgtyfIFMRVFAIRARIAAnkdvekkRVNQPGTAfvynsddeifkDPSFLIQEAFYNMNTVIIYGLEDY----FCTLIEK 1048
Cdd:cd18575 151 -----LPIILFGRRVRRLS-------RASQDRLA-----------DLSAFAEETLSAIKTVQAFTREDAerqrFATAVEA 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1049 AIDYSnkgqKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDfmksLFTFLFtgsYA 1114
Cdd:cd18575 208 AFAAA----LRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGE----LSQFVF---YA 262
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
829-1109 |
1.27e-07 |
|
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: 54.86 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 829 ALSIMVaggLYPLFALLYAKYVGTLFDFANLEANSNK--YSLYILVIAIAMF-ISETLKNYYNNVIGEKVEKTMKLRLFE 905
Cdd:cd18572 1 AFVFLV---VAALSELAIPHYTGAVIDAVVADGSREAfyRAVLLLLLLSVLSgLFSGLRGGCFSYAGTRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 906 NIMYQEISFFDQdsHAPGLLSAHINRDV--------HLLKTGLVNNIVIFTHFIVLFLVS---TVMSFYFCPIVAAVlTG 974
Cdd:cd18572 78 SLLRQDIAFFDA--TKTGELTSRLTSDCqkvsdplsTNLNVFLRNLVQLVGGLAFMFSLSwrlTLLAFITVPVIALI-TK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 975 TYFIFMRVFA--IRARIA-ANKDVEkkrvnqpgtafvynsddeifkdpsfliqEAFYNMNTVIIYGLEDYFCTLIEKAID 1051
Cdd:cd18572 155 VYGRYYRKLSkeIQDALAeANQVAE----------------------------EALSNIRTVRSFATEEREARRYERALD 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1052 -YSNKGQKRKTLINSMLWgFSQSAQFFINSFAYWFGSFLIRRGTIQVDdfmkSLFTFLF 1109
Cdd:cd18572 207 kALKLSVRQALAYAGYVA-VNTLLQNGTQVLVLFYGGHLVLSGRMSAG----QLVTFML 260
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
390-656 |
1.29e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.63 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 390 FHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN-DSHNLKDVNLKWWRSKIGVVSQD 468
Cdd:PRK13638 9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgKPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 469 P--LLFSNSIKNNIKYSLYSLKDLEalseesnedgfssqsdsnsrnscrAKCAGDLNDMIQTTDSTELIQvrknyETIEd 546
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVPE------------------------AEITRRVDEALTLVDAQHFRH-----QPIQ- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 547 sevvsvskkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
Cdd:PRK13638 136 --------------------------------CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
250 260 270
....*....|....*....|....*....|.
gi 156095386 627 GNENRItIIIAHRLSTI-RYANTIFVLSNRE 656
Cdd:PRK13638 184 AQGNHV-IISSHDIDLIyEISDAVYVLRQGQ 213
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
569-649 |
1.36e-07 |
|
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: 53.10 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 569 YETLvGSNASKLSGGQKQRISIARAIIRNPK--ILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRYA 646
Cdd:cd03238 78 YLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTV-ILIEHNLDVLSSA 155
|
...
gi 156095386 647 NTI 649
Cdd:cd03238 156 DWI 158
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1353-1430 |
1.39e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 1.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFN 1430
Cdd:PRK10261 460 YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMY 538
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
397-638 |
1.41e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 54.30 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI---ERlYDPTEGDVIindshnLKDVNLKWW----RSK--IGVVSQ 467
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSIL------LDGEDILELspdeRARagIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 468 DPLlfsnSIKNnikyslYSLKDLeaLSEESNEDGFSSQSDSNSRNSCRAKCAgDLN---DMIqttdsteliqvrknyeti 544
Cdd:COG0396 85 YPV----EIPG------VSVSNF--LRTALNARRGEELSAREFLKLLKEKMK-ELGldeDFL------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 545 eDSEVvsvskkvlihdfvsalpdkyetlvgsNASkLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
Cdd:COG0396 134 -DRYV--------------------------NEG-FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNK 185
|
250
....*....|....
gi 156095386 625 LKgNENRITIIIAH 638
Cdd:COG0396 186 LR-SPDRGILIITH 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
571-641 |
1.48e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 1.48e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 571 TLVGSNASK--LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLS 641
Cdd:TIGR00955 156 TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPS 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1181-1388 |
1.52e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1181 IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEQTgesskeqmqqgdeeqnvgmknaNEFSSSK 1260
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPM----------------------SKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1261 EGadgqsstlfknsgkilldgvdicdynlkDLRN--LFSIVSQEPMLFNMSIYENIKF----GKENATREDVKRACKFAA 1334
Cdd:PRK11629 81 KA----------------------------ELRNqkLGFIYQFHHLLPDFTALENVAMplliGKKKPAEINSRALEMLAA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1335 IDefIESLPNQYDTnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11629 133 VG--LEHRANHRPS-------ELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
580-654 |
1.73e-07 |
|
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: 53.30 E-value: 1.73e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRY--ANTIFVLSN 654
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLR-EEGKSVLIITHYQRLLDYikPDRVHVLYD 180
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1357-1417 |
1.76e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.94 E-value: 1.76e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
415-641 |
1.78e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.33 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 415 AFVGESGCGKSTILKLIERLYDPTEG-----DVIINDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKd 489
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHK- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 490 lealseesnedgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRKNYETIEDSEVVSVSKKVLIHDFVSALPdky 569
Cdd:PRK14271 130 ---------------------------------------------LVPRKEFRGVAQARLTEVGLWDAVKDRLSDSP--- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 570 etlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRIT-IIIAHRLS 641
Cdd:PRK14271 162 --------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA---DRLTvIIVTHNLA 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1176-1399 |
1.80e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.34 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1176 RPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDH-HIVFKNEQTGESS-KEQMQQgdeeqnVGMKNA 1253
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL--LPPAAgTIKLDGGDIDDPDvAEACHY------LGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1254 nefssskegadgqsstlfknsgkilldgvdicdynLKDlrnlfsivsqepmlfNMSIYENIKFGKE--NATREDVKRACK 1331
Cdd:PRK13539 84 -----------------------------------MKP---------------ALTVAENLEFWAAflGGEELDIAAALE 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1332 FAAIDEfIESLPNQYdtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PRK13539 114 AVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
403-669 |
1.90e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPT---EGDVIINDS----HNLKDVNlkwwRSKIGVVSQDPLLFSN- 474
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEelqaSNIRDTE----RAGIAIIHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 475 SIKNNIkyslyslkdleALSEESNEDGFSsqsdsnsrnscrakcagDLNDMIQTTDsTELIQVRKNyetiedsevVSVSK 554
Cdd:PRK13549 98 SVLENI-----------FLGNEITPGGIM-----------------DYDAMYLRAQ-KLLAQLKLD---------INPAT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 555 KVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITI 634
Cdd:PRK13549 140 PV---------------------GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACI 197
|
250 260 270
....*....|....*....|....*....|....*.
gi 156095386 635 IIAHRLSTI-RYANTIFVLSNRENGSTVDVDVLGED 669
Cdd:PRK13549 198 YISHKLNEVkAISDTICVIRDGRHIGTRPAAGMTED 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1268-1449 |
2.34e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLFNMSIYENI------------KFGKENatREDV 1326
Cdd:PRK10575 51 STLLKmlgrhqppSEGEILLDAQPLESWSSKAFaRKVAYLPQQLPAAEGMTVRELVaigrypwhgalgRFGAAD--REKV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1327 KRACKFAAIDEFIESLPNqydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1406
Cdd:PRK10575 129 EEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQER 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 156095386 1407 DKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVqAQGTHEELL 1449
Cdd:PRK10575 198 GLTVIAVLHDINMAARyCDYLVAL----RGGEMI-AQGTPAELM 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
400-652 |
2.46e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPllfsnSIKNN 479
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-DGEHIQHYASKEVARRIGLLAQNA-----TTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 IkyslySLKDLEALSEESNEDGFSsqsdsnsrnscrakcagdlndmiqttdsteliQVRKnyetiEDSEVVSVSKKvlih 559
Cdd:PRK10253 96 I-----TVQELVARGRYPHQPLFT--------------------------------RWRK-----EDEEAVTKAMQ---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 560 dfVSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
Cdd:PRK10253 130 --ATGITH----LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHD 203
|
250
....*....|....
gi 156095386 640 LS-TIRYANTIFVL 652
Cdd:PRK10253 204 LNqACRYASHLIAL 217
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
570-655 |
2.68e-07 |
|
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: 51.61 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN-----NLKGNENRITIIIAHRLSTIR 644
Cdd:smart00382 51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLTVILTTNDEKDLG 130
|
90
....*....|.
gi 156095386 645 YANTIFVLSNR 655
Cdd:smart00382 131 PALLRRRFDRR 141
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
405-652 |
3.23e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.14 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPtegDVIIN-DSHNLKDVNL---------KWWRSKIGVVSQDPLLF-- 472
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKD---NWHVTaDRFRWNGIDLlklsprerrKIIGREIAMIFQEPSSCld 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 473 -SNSIKNNIKyslyslkdlEALSEESNEDGFSSqsdsnsrnscRAkcagdlndmiqttdsteliQVRKNYetiedseVVS 551
Cdd:COG4170 104 pSAKIGDQLI---------EAIPSWTFKGKWWQ----------RF-------------------KWRKKR-------AIE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 552 VSKKVLIHDfvsalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENR 631
Cdd:COG4170 139 LLHRVGIKD--------HKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARL--NQLQ 208
|
250 260
....*....|....*....|....
gi 156095386 632 ITII--IAHRLSTI-RYANTIFVL 652
Cdd:COG4170 209 GTSIllISHDLESIsQWADTITVL 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
580-635 |
3.27e-07 |
|
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: 52.91 E-value: 3.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITII 635
Cdd:TIGR03410 132 LSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLR-AEGGMAIL 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1164-1453 |
3.32e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.62 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFrylSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegaDGQsstLFKNSGKILLDGVDI---CDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKE 1319
Cdd:PRK11831 54 --------------------GGQ---IAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQSGALFtDMNVFDNVAYPLR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATR--EDVKRACKFAAidefIESLPNQYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:PRK11831 111 EHTQlpAPLLHSTVMMK----LEAVGLRGAAKLMP--SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1398 TIVDIKDKADKTIITIAH---RIASIKRSDKIVvfnnpdrTGSFVQAQGTHEELLSVQD 1453
Cdd:PRK11831 185 LISELNSALGVTCVVVSHdvpEVLSIADHAYIV-------ADKKIVAHGSAQALQANPD 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1355-1430 |
3.53e-07 |
|
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: 53.11 E-value: 3.53e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFN 1430
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVID 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1268-1454 |
4.31e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLFN-MSIYENIKFGKeNATRE-------DVKRAC 1330
Cdd:PRK09700 45 STLMKvlsgihepTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDeLTVLENLYIGR-HLTKKvcgvniiDWREMR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1331 KFAAIDEFIESLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIekTIVDIKDKADKT 1409
Cdd:PRK09700 124 VRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRKEGTA 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 156095386 1410 IITIAHRIASIKR-SDKIVVFNNPDRTGSFVQAQGTHEELLSVQDG 1454
Cdd:PRK09700 198 IVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
385-654 |
4.76e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 385 FKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdSHNLKDVNLKWWRSKIG 463
Cdd:PTZ00243 1311 FEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVN-GREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 464 VVSQDPLLFSNSIKNNIkyslyslkD--LEALSEEsnedgfssqsdsnsrnscrakcagdlndmiqTTDSTELIQVRKny 541
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNV--------DpfLEASSAE-------------------------------VWAALELVGLRE-- 1426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etiedsEVVSVSKKVlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILIL-DEATSSLDNKSEYLVQK 620
Cdd:PTZ00243 1427 ------RVASESEGI-------------DSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQA 1487
|
250 260 270
....*....|....*....|....*....|....
gi 156095386 621 TINNLKGNENRITiiIAHRLSTIRYANTIFVLSN 654
Cdd:PTZ00243 1488 TVMSAFSAYTVIT--IAHRLHTVAQYDKIIVMDH 1519
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
411-614 |
4.85e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.47 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 411 GKTYAFVGESGCGKSTILKLIERLYDPTEGDVII--NDSHNLKDVNLKWWRSK-IGVVSQDPLLFS--NSIKNnikysly 485
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgQPLHQMDEEARAKLRAKhVGFVFQSFMLIPtlNALEN------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 486 slKDLEALseesnedgFSSQSDSNSRNSCRakcagdlndmiqttdstELIqvrknyetiedsEVVSVSKKvLIHdfvsaL 565
Cdd:PRK10584 109 --VELPAL--------LRGESSRQSRNGAK-----------------ALL------------EQLGLGKR-LDH-----L 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 156095386 566 PdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK10584 144 P-----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
377-473 |
5.23e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 377 LKDIKKIQFKNVRFHYDTRK-DVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNL 455
Cdd:PRK10522 317 FPDWQTLELRNVTFAYQDNGfSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTAEQP 392
|
90
....*....|....*...
gi 156095386 456 KWWRSKIGVVSQDPLLFS 473
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFD 410
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
825-1100 |
5.94e-07 |
|
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: 52.80 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALsIMVAgglypLFALLYAKYVGTLFD-FANLEANSN---KYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMK 900
Cdd:cd18541 3 LGILFL-ILVD-----LLQLLIPRIIGRAIDaLTAGTLTASqllRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 901 LRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLK--TG-----LVNNIVIFThFIVLFLVS-----TVMSFYFCPIV 968
Cdd:cd18541 77 NDLFAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRmaLGpgilyLVDALFLGV-LVLVMMFTispklTLIALLPLPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 969 AAVLtgtyFIFMRVfaIRARIaankdvekkRVNQpgtafvynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCTLIEK 1048
Cdd:cd18541 154 ALLV----YRLGKK--IHKRF---------RKVQ-----------EAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDK 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1049 AidysNKGQKRKTLINSMLWGFSQSAQFFINSFAY----WFGSFLIRRGTIQVDDF 1100
Cdd:cd18541 208 L----NEEYVEKNLRLARVDALFFPLIGLLIGLSFlivlWYGGRLVIRGTITLGDL 259
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1177-1428 |
5.96e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1177 PNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneqtgesskeqmQQGDEEqnvgmknanef 1256
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-----------------------PHGSYE----------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1257 ssskegadgqsstlfknsGKILLDGvDICDYnlKDLRNlfS------IVSQE----PMLfnmSIYENIKFGKENATR--- 1323
Cdd:NF040905 58 ------------------GEILFDG-EVCRF--KDIRD--SealgivIIHQElaliPYL---SIAENIFLGNERAKRgvi 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 ---EDVKRACKFAAIDEFIESlPnqyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTI 1399
Cdd:NF040905 112 dwnETNRRARELLAKVGLDES-P---DTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LL 182
|
250 260 270
....*....|....*....|....*....|
gi 156095386 1400 VDIKDKADKTIItIAHRIASIKR-SDKIVV 1428
Cdd:NF040905 183 LELKAQGITSII-ISHKLNEIRRvADSITV 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1347-1415 |
6.04e-07 |
|
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: 53.79 E-value: 6.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1347 DTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1415
Cdd:TIGR03719 156 DADVT----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTH 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1333-1428 |
6.36e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.30 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1333 AAIDEFIE--SLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTI 1410
Cdd:PRK13536 151 AVIPSLLEfaRLESKADARVS----DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARG-KTI 225
|
90
....*....|....*....
gi 156095386 1411 ITIAHRIASIKR-SDKIVV 1428
Cdd:PRK13536 226 LLTTHFMEEAERlCDRLCV 244
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1262-1450 |
6.64e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1262 GADG-QSSTLFKN--------SGKILLDG--VDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN---ATRED 1325
Cdd:PRK13638 34 GANGcGKSTLFMNlsgllrpqKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYTDIDSDIAFSLRNlgvPEAEI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1326 VKRackfaaIDEFIESLPNQYDTNvGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1405
Cdd:PRK13638 114 TRR------VDEALTLVDAQHFRH-QPI-QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 156095386 1406 ADKTIITiAHRIASIKR-SDKIVVFnnpdRTGSfVQAQGTHEELLS 1450
Cdd:PRK13638 186 GNHVIIS-SHDIDLIYEiSDAVYVL----RQGQ-ILTHGAPGEVFA 225
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
825-1095 |
6.80e-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: 52.90 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAgglypLFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAM---FISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18555 5 ISILLLSLLLQ-----LLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFllyGLFSFLRGYIIIKLQTKLDKSLMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 902 RLFENIMYQEISFFDQDShaPGLLSAHINRDVHL-------LKTGLVNNIVIFTHFIVLFLVSTVMSFYfcpivaaVLTG 974
Cdd:cd18555 80 DFFEHLLKLPYSFFENRS--SGDLLFRANSNVYIrqilsnqVISLIIDLLLLVIYLIYMLYYSPLLTLI-------VLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 975 TYFIFMRVFAIRARIaankdvekKRVNQpgTAFVYNSddeifKDPSFLIqEAFYNMNTVIIYGLEDYFCT----LIEKAI 1050
Cdd:cd18555 151 GLLIVLLLLLTRKKI--------KKLNQ--EEIVAQT-----KVQSYLT-ETLYGIETIKSLGSEKNIYKkwenLFKKQL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 156095386 1051 DYSnkgqKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTI 1095
Cdd:cd18555 215 KAF----KKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
580-652 |
6.85e-07 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 51.47 E-value: 6.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLSTIRYANTIFVL 652
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1307-1454 |
6.92e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1307 NMSIYENIK-----FGKENAT-REDVKRACKFAaidefieSLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLL 1380
Cdd:PRK13537 94 DFTVRENLLvfgryFGLSAAAaRALVPPLLEFA-------KLENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVL 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1381 DEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKR-SDKIVVFNNPDRTgsfvqAQGTHEELLSVQDG 1454
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERlCDRLCVIEEGRKI-----AEGAPHALIESEIG 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
403-652 |
7.11e-07 |
|
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: 52.35 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LK-WWRSKIGVVS--QDPLLFSN-SIK 477
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG----RDITgLPpHRIARLGIARtfQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 478 NNIKYSLYSlkdleALSEESNEDGFSSQSDSNSRNSCRAKCAgdlndmiqttdstELIqvrknyetiedsevvsvskkvl 557
Cdd:COG0411 98 ENVLVAAHA-----RLGRGLLAALLRLPRARREEREARERAE-------------ELL---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 558 ihDFVSaLPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQkTINNLKGNENrITI-I 635
Cdd:COG0411 138 --ERVG-LADRADEPAGN----LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAE-LIRRLRDERG-ITIlL 208
|
250
....*....|....*...
gi 156095386 636 IAHRLSTI-RYANTIFVL 652
Cdd:COG0411 209 IEHDMDLVmGLADRIVVL 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
386-607 |
7.20e-07 |
|
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: 51.91 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 386 KNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWW---RSK 461
Cdd:COG0410 7 ENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDItGLPPHriaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEALSEesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkn 540
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRA--------------------------------------------- 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 541 yeTIEDsevvsvskkvlIHDFVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEAT 607
Cdd:COG0410 115 --DLER-----------VYELFPRLKERRRQRAGT----LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
825-1117 |
7.21e-07 |
|
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: 52.78 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLYPLFALLYA--KY-VGTLFDFANLeansNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18544 3 LALLLLLLATALELLGPLLIKRAidDYiVPGQGDLQGL----LLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 902 RLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIV-IFTHFIVLFLVSTVMsFYFCPIVAAVLTGT---YF 977
Cdd:cd18544 79 DLFSHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGLVtLIGDLLLLIGILIAM-FLLNWRLALISLLVlplLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 978 IFMRVFAIRARiAANKDVEKK--RVNqpgtAFvynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFctliEKAIDYSNK 1055
Cdd:cd18544 156 LATYLFRKKSR-KAYREVREKlsRLN----AF---------------LQESISGMSVIQLFNREKRE----FEEFDEINQ 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1056 GQKRKTLINSMLWGFSQSAQFFINSFAY----WFGSFLIRRGTIQVDdfmkSLFTFLftgSYAGKL 1117
Cdd:cd18544 212 EYRKANLKSIKLFALFRPLVELLSSLALalvlWYGGGQVLSGAVTLG----VLYAFI---QYIQRF 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1355-1415 |
7.61e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 7.61e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdikdKADKTIITIAH 1415
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSH 399
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
383-611 |
8.71e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.17 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYD-TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdVNLKWWRSK 461
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG------VPVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQ-DPLLFSNSIKNNIKYSLySLKDLealseesnedgfssqsdsnSRNSCRAKCAgdlndmiqttdstELIQvrkn 540
Cdd:COG4525 78 RGVVFQkDALLPWLNVLDNVAFGL-RLRGV-------------------PKAERRARAE-------------ELLA---- 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 541 yetiedsevvsvskKVLIHDFVSALPdkYEtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4525 121 --------------LVGLADFARRRI--WQ---------LSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1193-1439 |
9.48e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1193 KTTAIVGETGSGKSTVMSLLMRFYDlKNDHHIVFKNEQTgesskeqmqqgdeeqnvgmknanEFSSSKegaDGQSSTLfk 1272
Cdd:PRK10762 31 RVMALVGENGAGKSTMMKVLTGIYT-RDAGSILYLGKEV-----------------------TFNGPK---SSQEAGI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 nsgkilldgvdicdynlkdlrnlfSIVSQEPMLF-NMSIYENIKFGKENAT---REDVKRAckFAAIDEFIESLPNQY-- 1346
Cdd:PRK10762 82 ------------------------GIIHQELNLIpQLTIAENIFLGREFVNrfgRIDWKKM--YAEADKLLARLNLRFss 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1347 DTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIeKTIVDIKDKaDKTIITIAHRIASI-KRSD 1424
Cdd:PRK10762 136 DKLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELKSQ-GRGIVYISHRLKEIfEICD 209
|
250
....*....|....*
gi 156095386 1425 KIVVFnnpdRTGSFV 1439
Cdd:PRK10762 210 DVTVF----RDGQFI 220
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
62-358 |
9.74e-07 |
|
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: 52.05 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 62 LGVSFVCATISGGT---LPFFVsvfGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLK 138
Cdd:cd18551 1 LILALLLSLLGTAAslaQPLLV---KNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 139 SVFYQDGQFHDNN-PG---SKLTSDldfyLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICG 214
Cdd:cd18551 78 RLLRLPVSFFDRRrSGdlvSRVTND----TTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 215 VICNKKVkinKKTSLLYNNNT---MSIIEEALVGIRTVVSYCGENTILKKFN-LSEKLYsKYTLKANLMESLHIGMINGF 290
Cdd:cd18551 154 LPLGRRI---RKASKRAQDALgelSAALERALSAIRTVKASNAEERETKRGGeAAERLY-RAGLKAAKIEALIGPLMGLA 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 291 ILASYAFGFWYGT-RIIISDLSnqqpnndfhggsvisilLGVLIS--MFMLTIILP------NITEYMKSLEATNNL 358
Cdd:cd18551 230 VQLALLVVLGVGGaRVASGALT-----------------VGTLVAflLYLFQLITPlsqlssFFTQLQKALGALERI 289
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
383-654 |
9.94e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 52.42 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNlkwwRSKI 462
Cdd:COG4152 2 LELKGLTKRFGDKTAV---DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLDPED----RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPLLFSN-SIKNNIKYsLYSLKDLealseesnedgfssqsdsnSRNSCRAKcagdLNDMIQTTDstelIQVRKNy 541
Cdd:COG4152 74 GYLPEERGLYPKmKVGEQLVY-LARLKGL-------------------SKAEAKRR----ADEWLERLG----LGDRAN- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 etiedsevvsvsKKVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD--NKSeyLVQ 619
Cdd:COG4152 125 ------------KKV---------------------EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpvNVE--LLK 169
|
250 260 270
....*....|....*....|....*....|....*..
gi 156095386 620 KTINNLKgnENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:COG4152 170 DVIRELA--AKGTTVIFSsHQMELVeELCDRIVIINK 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
386-626 |
9.98e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.82 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 386 KNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNL----KWWRSK 461
Cdd:PRK10895 7 KNLAKAYKGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD----EDISLlplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLealSEESNEDgfssqsdsnsrnscRAKcagdlndmiqttdsteliqvrkn 540
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQIRDDL---SAEQRED--------------RAN----------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 541 yETIEDSEVvsvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK10895 120 -ELMEEFHI--------------------EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
....*.
gi 156095386 621 TINNLK 626
Cdd:PRK10895 179 IIEHLR 184
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
827-1109 |
1.14e-06 |
|
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: 52.05 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 827 IIALSIMVAGGLyplFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFEN 906
Cdd:cd18551 2 ILALLLSLLGTA---ASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 907 IMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIV-IFTH-------FIVLFLVSTVMSFyfcpIVAAVLTGTYFI 978
Cdd:cd18551 79 LLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPqLVTGvltvvgaVVLMFLLDWVLTL----VTLAVVPLAFLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 979 FMRVFAIRARIAANkdvekkrvNQPGTAfVYNSDdeifkdpsflIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQK 1058
Cdd:cd18551 153 ILPLGRRIRKASKR--------AQDALG-ELSAA----------LERALSAIRTVKASNAEERETKRGGEAAERLYRAGL 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1059 RKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMkSLFTFLF 1109
Cdd:cd18551 214 KAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLV-AFLLYLF 263
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
580-655 |
1.32e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 1.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVqKTINNLKgNENRITIIIAHRLstiryaNTIFVLSNR 655
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAReIEQLF-RVIRELR-AEGRVILYVSHRM------EEIFALCDA 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1347-1415 |
1.46e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 1.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1347 DTNVGPygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1415
Cdd:PRK11819 158 DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG----TVVAVTH 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1272-1396 |
1.46e-06 |
|
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: 50.57 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1272 KNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFiESLPNQYdtnvg 1351
Cdd:cd03231 52 PLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----- 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 156095386 1352 pygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03231 126 -----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1355-1416 |
1.87e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.73 E-value: 1.87e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1416
Cdd:COG2401 135 KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1355-1419 |
1.94e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.57 E-value: 1.94e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIAS 1419
Cdd:PLN03211 205 RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKG-KTIVTSMHQPSS 268
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
399-614 |
2.05e-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: 52.24 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnlkdvnlkwwrsKIGVVSQDPLLFSN-SIK 477
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI------------KVGYLPQEPQLDPTkTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 478 NNIKYSLYSLKDLEALSEESNEDGFSSQSDSNSRnscrAKCAGDLNDMIQTTDSTELiqvrknyetieDSEVvSVSKKVL 557
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRFNEISAKYAEPDADFDKL----AAEQAELQEIIDAADAWDL-----------DSQL-EIAMDAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 558 ihdfvsALPDKyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:TIGR03719 151 ------RCPPW-----DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
866-1097 |
2.19e-06 |
|
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: 51.31 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 866 YSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFdqDSHAPG-LLSAHINrDVH----LLKTGL 940
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFF--DSRPVGkILSRVIN-DVNslsdLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 941 VNnivIFTHFIVLFLVSTVMsFYF-------CPIVAAVLtgtyFIFMRVFAIRARIAAnKDVEKKRVNQpgTAFvynsdd 1013
Cdd:cd18545 119 IN---LIPDLLTLVGIVIIM-FSLnvrlalvTLAVLPLL----VLVVFLLRRRARKAW-QRVRKKISNL--NAY------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1014 eifkdpsflIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRG 1093
Cdd:cd18545 182 ---------LHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGG 252
|
....
gi 156095386 1094 TIQV 1097
Cdd:cd18545 253 AITV 256
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1173-1422 |
2.25e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1173 YLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkNDHHIVFKNEQTgESSKEQMQQGDEEQNVgmkn 1252
Cdd:PRK11147 10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLL-DDGRIIYEQDLI-VARLQQDPPRNVEGTV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1253 aneFSSSKEGADGQSSTLfKNSGKILLD-GVDICDYNLKDLRNLfsivsQEpmlfnmsiyeniKFGKENATREDVKrack 1331
Cdd:PRK11147 84 ---YDFVAEGIEEQAEYL-KRYHDISHLvETDPSEKNLNELAKL-----QE------------QLDHHNLWQLENR---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1332 faaIDEFIESLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTII 1411
Cdd:PRK11147 139 ---INEVLAQLGLDPDAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SII 207
|
250
....*....|.
gi 156095386 1412 TIAHRIASIKR 1422
Cdd:PRK11147 208 FISHDRSFIRN 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
579-652 |
2.32e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 2.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVM 227
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
825-1109 |
2.45e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 51.00 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLYPlfallyAKYVGTLFDFANLEANS----NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMK 900
Cdd:cd18778 3 LTLLCALLSTLLGLVP------PWLIRELVDLVTIGSKSlgllLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 901 LRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAV-LTGTYFI- 978
Cdd:cd18778 77 SDLYDKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLtLIPIPFLa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 979 -FMRVFAIRARIAAnkdvekkRVNQpgtafvynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDYfctliEKAiDYSNKGQ 1057
Cdd:cd18778 155 lGAWLYSKKVRPRY-------RKVR-----------EALGELNALLQDNLSGIREIQAFGREEE-----EAK-RFEALSR 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1058 K-RKTLINSM-LWGFSQSAQFFINSFAY----WFGSFLIRRGTIQVDDfmksLFTFLF 1109
Cdd:cd18778 211 RyRKAQLRAMkLWAIFHPLMEFLTSLGTvlvlGFGGRLVLAGELTIGD----LVAFLL 264
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1308-1450 |
2.53e-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: 51.75 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1308 MSIYENIKFG--KENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGkSLSGGQKQRIAIARALLREPKILLLDEATS 1385
Cdd:TIGR02633 354 LGVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1386 SLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDKIVVFNNPDRTGSFVQAQGTHEELLS 1450
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVlGLSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
383-638 |
2.81e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.03 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDT-RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG-------DVIINDSHNLKDVN 454
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 455 lkwwRSKIGVVSQdpllfsnsiknniKYSLyslkdLEALSEESNedgfssqsdsnsrnscrakcagdlndmiqttdstel 534
Cdd:PRK10535 85 ----REHFGFIFQ-------------RYHL-----LSHLTAAQN------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 535 IQVRKNYETIEDSEVVSVSKKVLIHdfvSALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK10535 107 VEVPAVYAGLERKQRLLRAQELLQR---LGLEDR----VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
250 260
....*....|....*....|....
gi 156095386 615 EYLVQKTINNLKgNENRITIIIAH 638
Cdd:PRK10535 180 GEEVMAILHQLR-DRGHTVIIVTH 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
383-640 |
3.34e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.11 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdvIINDSHNLKdvnlkwwrskI 462
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--VIKRNGKLR----------I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQdpllfsnsiknniKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlnDMIQTTDSTELIQVRKNye 542
Cdd:PRK09544 70 GYVPQ-------------KLYL---------------------------------------DTTLPLTVNRFLRLRPG-- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 543 tIEDSEVVSVSKKVlihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK09544 96 -TKKEDILPALKRV-----------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
250
....*....|....*...
gi 156095386 623 NNLKGNENRITIIIAHRL 640
Cdd:PRK09544 164 DQLRRELDCAVLMVSHDL 181
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
571-653 |
3.77e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.42 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 571 TLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRYA--N 647
Cdd:PLN03211 197 TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSRVYQmfD 275
|
....*.
gi 156095386 648 TIFVLS 653
Cdd:PLN03211 276 SVLVLS 281
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1335-1431 |
4.01e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.47 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1335 IDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1412
Cdd:COG4586 135 LDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILL 210
|
90 100
....*....|....*....|
gi 156095386 1413 IAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4586 211 TSHDMDDIEAlCDRVIVIDH 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
394-622 |
4.68e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.10 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnlkdvnlkwwrskigvvSQDPLLFS 473
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-----------------IDDPDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 474 NSI----KNNIKyslyslkdlEALSEESNEDGFssqsdsnsrnscrAKCAGDLNDMIqttdsteliqvrknYETIEDsev 549
Cdd:PRK13539 74 ACHylghRNAMK---------PALTVAENLEFW-------------AAFLGGEELDI--------------AAALEA--- 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 550 vsvskkVLIHDfVSALPDKYetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK13539 115 ------VGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
394-654 |
5.43e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 50.61 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVII--NDSHNLKDVNLKwwrSKIGVVSQD-PL 470
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagDDVEALSARAAS---RRVASVPQDtSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 471 LFSNSIKNNIkyslyslkdlealseesnEDGfssqsdsnsRNSCRAKCAgdlndmiqTTDSTELIQVRKNYETIEdsevv 550
Cdd:PRK09536 89 SFEFDVRQVV------------------EMG---------RTPHRSRFD--------TWTETDRAAVERAMERTG----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 551 svskkvlihdfVSALPDKYETlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseylVQKTINNLK---- 626
Cdd:PRK09536 129 -----------VAQFADRPVT-------SLSGGERQRVLLARALAQATPVLLLDEPTASLD------INHQVRTLElvrr 184
|
250 260 270
....*....|....*....|....*....|
gi 156095386 627 -GNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:PRK09536 185 lVDDGKTAVAAIHDLDlAARYCDELVLLAD 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
579-611 |
5.82e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 49.31 E-value: 5.82e-06
10 20 30
....*....|....*....|....*....|...
gi 156095386 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11248 128 QLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
404-640 |
5.88e-06 |
|
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: 51.17 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV--NLKWWRSKIGVVSQDPLLFsnsikNNIK 481
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----KDIetNLDAVRQSLGMCPQHNILF-----HHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 482 YSLYSLkdlealseesnedgFSSQSDSNSRNSCRAkcagDLNDMIQTTDstelIQVRKNYEtiedsevvsvskkvlihdf 561
Cdd:TIGR01257 1020 VAEHIL--------------FYAQLKGRSWEEAQL----EMEAMLEDTG----LHHKRNEE------------------- 1058
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 562 vsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 640
Cdd:TIGR01257 1059 ---------------AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1322-1418 |
7.14e-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: 50.55 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD----SNSEKLI 1395
Cdd:COG1245 180 VRELLEKVDERGKLDELAEklGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLI 255
|
90 100
....*....|....*....|...
gi 156095386 1396 EKTIvdikdKADKTIITIAHRIA 1418
Cdd:COG1245 256 RELA-----EEGKYVLVVEHDLA 273
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1164-1431 |
7.77e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.45 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqGD 1243
Cdd:COG0488 316 LELEGLSKSY---GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA----------------------------GE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEqnvgmknanefssskegADgqsstlfknSGKILLdGVdicdyNLKdlrnlFSIVSQEPMLF--NMSIYENIKFGKENA 1321
Cdd:COG0488 365 LE-----------------PD---------SGTVKL-GE-----TVK-----IGYFDQHQEELdpDKTVLDELRDGAPGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVkRAckfaaideFIESL---PNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG0488 408 TEQEV-RG--------YLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
250 260 270
....*....|....*....|....*....|....*....
gi 156095386 1399 IVDIkdkaDKTIITIAH------RIAsikrsDKIVVFNN 1431
Cdd:COG0488 475 LDDF----PGTVLLVSHdryfldRVA-----TRILEFED 504
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
580-658 |
7.93e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.37 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 580 LSGGQKQ------RISIARAIIRNPKILILDEATSSLD--NKSEYLVQkTINNLKGNENRITIIIAHRLSTIRYANTIFV 651
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeeNIEESLAE-IIEERKSQKNFQLIVITHDEELVDAADHIYR 194
|
....*..
gi 156095386 652 LSNRENG 658
Cdd:cd03240 195 VEKDGRQ 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
578-669 |
8.34e-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: 50.21 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNeNRITIIIAHRLSTIR-YANTIFVLSNRE 656
Cdd:TIGR02633 140 GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKaVCDTICVIRDGQ 218
|
90
....*....|...
gi 156095386 657 NGSTVDVDVLGED 669
Cdd:TIGR02633 219 HVATKDMSTMSED 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
382-651 |
8.79e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.31 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 382 KIQFKNVRFHYDTRKDVEI--YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDV--IINDSHNLKDVNLKW 457
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 458 W---------------------RSKIGVVSQ--DPLLFSNSIKNNIKYSLYSLKdleALSEESNEdgfssqsdsnsrnsc 514
Cdd:PRK13651 82 KvleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMG---VSKEEAKK--------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 515 RAKcagdlnDMIqttdsteliqvrknyetiedsEVVsvskkvlihdfvsALPDKYetlVGSNASKLSGGQKQRISIARAI 594
Cdd:PRK13651 144 RAA------KYI---------------------ELV-------------GLDESY---LQRSPFELSGGQKRRVALAGIL 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 595 IRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIA-HRL-STIRYAN-TIFV 651
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNL--NKQGKTIILVtHDLdNVLEWTKrTIFF 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1357-1415 |
9.00e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.96 E-value: 9.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1415
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
76-309 |
9.12e-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: 49.10 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 76 LPFFVSVF--GVIM-KNMNLgenVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVF---------YQ 143
Cdd:cd18568 21 LPLFTQIIldRVLVhKNISL---LNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLslplsffasRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 144 DG----QFHDNNpgsKLTSDLdfyleqVNAGIGT--KFITIFTYASAFLglyiwslFKNARLTLCITCVFPLIYICGVIC 217
Cdd:cd18568 98 VGdiitRFQENQ---KIRRFL------TRSALTTilDLLMVFIYLGLMF-------YYNLQLTLIVLAFIPLYVLLTLLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 218 NKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFnlsEKLYSKYtLKANL-MESLHI--GMINGFI-LA 293
Cdd:cd18568 162 SPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRW---ENKFAKA-LNTRFrGQKLSIvlQLISSLInHL 237
|
250
....*....|....*.
gi 156095386 294 SYAFGFWYGTRIIISD 309
Cdd:cd18568 238 GTIAVLWYGAYLVISG 253
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1357-1459 |
9.27e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.83 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR---IASIkrSDKIVVFNNpd 1433
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDmklVMGI--SDRIYVVNQ-- 229
|
90 100
....*....|....*....|....*.
gi 156095386 1434 rtGSFVqAQGTHEELLSVQDgVYKKY 1459
Cdd:PRK11300 230 --GTPL-ANGTPEEIRNNPD-VIKAY 251
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1353-1428 |
9.80e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 9.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRS-DKIVV 1428
Cdd:PRK11022 150 YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAaHKIIV 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
580-654 |
9.82e-06 |
|
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: 47.81 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIahrLST-----IRYANTIFVLSN 654
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA--DAGKAVLL---ISSeldelLGLCDRILVMYE 179
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
99-337 |
1.01e-05 |
|
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: 49.00 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 99 IIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNP-G---SKLTSDLDFYLEQVNAGIGTK 174
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPvGkilSRVINDVNSLSDLLSNGLINL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 175 FITIFTyasaFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKV-----KINKKTSLLYnnntmSIIEEALVGIRTV 249
Cdd:cd18545 122 IPDLLT----LVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRArkawqRVRKKISNLN-----AYLHESISGIRVI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 250 VSYCGENTILKKF-NLSEKLYSKYtLKANLMESLH---IGMINGFilaSYAFGFWYGTRIIISDlsnqqpnndfhggsvi 325
Cdd:cd18545 193 QSFAREDENEEIFdELNRENRKAN-MRAVRLNALFwplVELISAL---GTALVYWYGGKLVLGG---------------- 252
|
250
....*....|..
gi 156095386 326 SILLGVLISMFM 337
Cdd:cd18545 253 AITVGVLVAFIG 264
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1274-1415 |
1.05e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIyenikfGKENATREDvkrackfAAIDEFIESLPNQYDTNVGPy 1353
Cdd:PRK10522 377 SGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEGKPANP-------ALVEKWLERLKMAHKLELED- 442
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1354 GK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1415
Cdd:PRK10522 443 GRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
570-645 |
1.10e-05 |
|
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: 48.52 E-value: 1.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRY 645
Cdd:cd03236 130 RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV-LVVEHDLAVLDY 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
371-484 |
1.10e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.99 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 371 NQDGKKLKDIKKIQFknvrfhydTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH-- 448
Cdd:PRK11831 1 EQSVANLVDMRGVSF--------TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENip 72
|
90 100 110
....*....|....*....|....*....|....*..
gi 156095386 449 NLKDVNLKWWRSKIGVVSQDPLLFSN-SIKNNIKYSL 484
Cdd:PRK11831 73 AMSRSRLYTVRKRMSMLFQSGALFTDmNVFDNVAYPL 109
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1322-1418 |
1.29e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PRK13409 180 VRELLKKVDERGKLDEVVErlGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLI 255
|
90
....*....|....*....
gi 156095386 1400 VDIKDkaDKTIITIAHRIA 1418
Cdd:PRK13409 256 RELAE--GKYVLVVEHDLA 272
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
578-652 |
1.30e-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: 49.78 E-value: 1.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRY-ANTIFVL 652
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
94-341 |
2.28e-05 |
|
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: 47.89 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 94 ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPgsklTSDLDF------YLEQV 167
Cdd:cd18555 39 NLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRS----SGDLLFransnvYIRQI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 168 nagIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIR 247
Cdd:cd18555 115 ---LSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 248 TVVSYCGENTILKKFnlsEKLYSK---YTLKANLMESLHIGMINGFILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSV 324
Cdd:cd18555 192 TIKSLGSEKNIYKKW---ENLFKKqlkAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVI--------NGELTLGEL 260
|
250
....*....|....*..
gi 156095386 325 ISILlgVLISMFMLTII 341
Cdd:cd18555 261 IAFS--SLAGSFLTPIV 275
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
404-611 |
2.30e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.86 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQD-PLLFSNSIKNNIKY 482
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-QPLESWSSKAFARKVAYLPQQlPAAEGMTVRELVAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 483 SLYSLKDleALSEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknYETIEDSeVVSVSKKVLIHDFV 562
Cdd:PRK10575 109 GRYPWHG--ALGRFGAAD----------------------------------------REKVEEA-ISLVGLKPLAHRLV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 156095386 563 SAlpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10575 146 DS---------------LSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1272-1442 |
2.47e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1272 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQE-PMLFNMSIYENIKFGK---------ENATREDVKrackfAAIDEFie 1340
Cdd:PRK10982 50 KDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQRSVMDNMWLGRyptkgmfvdQDKMYRDTK-----AIFDEL-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 slpnqyDTNVGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIE---KTIVDIKDKAdKTIITIAH 1415
Cdd:PRK10982 123 ------DIDIDPRAKvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNhlfTIIRKLKERG-CGIVYISH 192
|
170 180
....*....|....*....|....*...
gi 156095386 1416 RIASIKR-SDKIVVFnnpdRTGSFVQAQ 1442
Cdd:PRK10982 193 KMEEIFQlCDEITIL----RDGQWIATQ 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
406-611 |
2.60e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 406 FTLTEGKTYAFVGESGCGKSTILKLI--ERLYDptEGDVIINdshnlKDVnlkwwrskigVVS---QDPllfsnsiKNNI 480
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILngEVLLD--DGRIIYE-----QDL----------IVArlqQDP-------PRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 481 KYSLYS------------LKDLEALSEESNEDgfssQSDSNsrnscrakcagdLNDMIQttdstelIQvrknyETIEDSE 548
Cdd:PRK11147 80 EGTVYDfvaegieeqaeyLKRYHDISHLVETD----PSEKN------------LNELAK-------LQ-----EQLDHHN 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 549 VVSVSKKvlIHDFVSAL---PDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11147 132 LWQLENR--INEVLAQLgldPDA-------ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
580-625 |
2.71e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 2.71e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL 451
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
383-652 |
2.74e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.67 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKI 462
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 463 GVVSQDPllfsnsiknnikyslyslkDLEALSEESNED-GFSSQsdsnsrNSCRAKcagdlndmiqttdstelIQVRKNY 541
Cdd:PRK13644 80 GIVFQNP-------------------ETQFVGRTVEEDlAFGPE------NLCLPP-----------------IEIRKRV 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 542 ETiedsevvsvskkvlihdfvsALPD-KYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13644 118 DR--------------------ALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
250 260 270
....*....|....*....|....*....|..
gi 156095386 621 TINNLKgNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:PRK13644 178 RIKKLH-EKGKTIVYITHNLEELHDADRIIVM 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
580-654 |
2.78e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 47.46 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 580 LSGGQKQRISIARAIIR------NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
Cdd:PRK13548 135 LSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLL 214
|
..
gi 156095386 653 SN 654
Cdd:PRK13548 215 HQ 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
566-645 |
3.08e-05 |
|
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: 47.02 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 566 PDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
Cdd:cd03237 102 PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDY 181
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1357-1421 |
3.27e-05 |
|
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: 48.59 E-value: 3.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATS--SLDsnseklIEKTIVDIKDKADKTIITIAHRIASIK 1421
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSavSVD------VEGYMYRLCREFGITLFSVSHRKSLWK 643
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1357-1420 |
4.12e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 4.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI 1420
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEG-KTMLVSTHNLGSV 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1274-1417 |
4.55e-05 |
|
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: 48.47 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKFGKENATREDVKRACKFAAIdefIESLPNQYDTNvgP 1352
Cdd:TIGR01257 984 SGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEEAQLEMEAM---LEDTGLHHKRN--E 1057
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRI 1417
Cdd:TIGR01257 1058 EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
400-639 |
4.92e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.10 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY--DPTEGDVIINDshnlkdvnLKWWRSKIGVvsqdpllfsnsik 477
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD--------NQFGREASLI------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 478 nnikyslyslkdlealseesneDGFSSQSDsnsrnscrakcagdlndmiqTTDSTELIQVRKNyetiedSEVVSVSKKVl 557
Cdd:COG2401 104 ----------------------DAIGRKGD--------------------FKDAVELLNAVGL------SDAVLWLRRF- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 558 ihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIA 637
Cdd:COG2401 135 --------------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL-ARRAGITLVVA 193
|
...
gi 156095386 638 -HR 639
Cdd:COG2401 194 tHH 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
570-607 |
5.24e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.71 E-value: 5.24e-05
10 20 30
....*....|....*....|....*....|....*...
gi 156095386 570 ETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEAT 607
Cdd:COG1129 389 EQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
386-611 |
5.29e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.46 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 386 KNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVI-------INDSHNLKDVNLKW- 457
Cdd:PRK11701 10 RGLTKLYGPRKGCR---DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqLRDLYALSEAERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 458 WRSKIGVVSQDP---LLFSNSIKNNIKYSLYSLKDlealseesnedgfssqsdsnsRNSCRakcagdlndmIQTTDSTEL 534
Cdd:PRK11701 87 LRTEWGFVHQHPrdgLRMQVSAGGNIGERLMAVGA---------------------RHYGD----------IRATAGDWL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 535 IQVRKNYETIEDsevvsvskkvlihdfvsaLPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11701 136 ERVEIDAARIDD------------------LPTTF-----------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
402-649 |
5.38e-05 |
|
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: 48.09 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 402 KDLNFTLTEGKTYAFVGESGCGKSTILK------LIERLY----DPTEGDVIINDSHnlkdvnlkwwRSKIGVVSQDPLL 471
Cdd:TIGR00630 625 KNITVSIPLGLFTCITGVSGSGKSTLINdtlypaLANRLNgaktVPGRYTSIEGLEH----------LDKVIHIDQSPIG 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 472 FSnSIKNNIKYS--LYSLKDLEALSEESNEDGFSsqsdsNSRNS-------CrAKCAGD---------LNDMIQTTDS-- 531
Cdd:TIGR00630 695 RT-PRSNPATYTgvFDEIRELFAETPEAKVRGYT-----PGRFSfnvkggrC-EACQGDgvikiemhfLPDVYVPCEVck 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 532 -----TELIQVRKNYETIEDSEVVSVSKKvliHDFVSALPD---KYETLV---------GSNASKLSGGQKQRISIARAI 594
Cdd:TIGR00630 768 gkrynRETLEVKYKGKNIADVLDMTVEEA---YEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKEL 844
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 595 IR---NPKILILDEATSSLD----NKSEYLVQKTINnlKGNEnriTIIIAHRLSTIRYANTI 649
Cdd:TIGR00630 845 SKrstGRTLYILDEPTTGLHfddiKKLLEVLQRLVD--KGNT---VVVIEHNLDVIKTADYI 901
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
579-645 |
5.88e-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: 45.26 E-value: 5.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDY 137
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
575-636 |
6.04e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 46.18 E-value: 6.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII 636
Cdd:COG1137 132 SKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLK--ERGIGVLI 191
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
403-611 |
6.58e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVII----NDSHNLKDvnlkwwRSKIGVVSQdpllfsnsikn 478
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpVDAGDIAT------RRRVGYMSQ----------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 479 niKYSLYS-------LkDLEA----LSEEsnedgfssqsDSNSRnscrakcagdLNDMIQTTDsteliqvrknyetieds 547
Cdd:NF033858 347 --AFSLYGeltvrqnL-ELHArlfhLPAA----------EIAAR----------VAEMLERFD----------------- 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 548 evvsvskkvlIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:NF033858 387 ----------LADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
578-625 |
6.59e-05 |
|
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: 47.13 E-value: 6.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 156095386 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL 449
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
59-309 |
7.44e-05 |
|
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: 46.28 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 59 RKLLGVSFVCAtisggtlpFFVSVFGVIMK-----------NMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTK 127
Cdd:cd18570 1 KKLLILILLLS--------LLITLLGIAGSfffqiliddiiPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 128 ILKTLKIEFLKSVFYQDGQFHDNNPGSKLTS---DLDFYLEQVNAGIGTKFITIFT--YASAFLGLYIWSLFknarltlC 202
Cdd:cd18570 73 LDIRLILGYFKHLLKLPLSFFETRKTGEIISrfnDANKIREAISSTTISLFLDLLMviISGIILFFYNWKLF-------L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 203 ITCVFPLIYICGVICNKKV--KINKKTSLLYNNNTMSIIeEALVGIRTVVSYCGENTILKKFnlsEKLYSKYtLKANLME 280
Cdd:cd18570 146 ITLLIIPLYILIILLFNKPfkKKNREVMESNAELNSYLI-ESLKGIETIKSLNAEEQFLKKI---EKKFSKL-LKKSFKL 220
|
250 260 270
....*....|....*....|....*....|....
gi 156095386 281 SLhIGMINGFI--LASYAFG---FWYGTRIIISD 309
Cdd:cd18570 221 GK-LSNLQSSIkgLISLIGSlliLWIGSYLVIKG 253
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
570-655 |
7.72e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYanti 649
Cdd:PRK13409 444 ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDY---- 519
|
....*.
gi 156095386 650 fvLSNR 655
Cdd:PRK13409 520 --ISDR 523
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
826-989 |
8.29e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 46.35 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 826 AIIALSIMVAGglyPLFALLYAKYVGTLFD--FANLEANSNKYSLYILVIA-----IAMFISETLKNYYNNVIGEKVEKT 898
Cdd:cd18563 1 LILGFLLMLLG---TALGLVPPYLTKILIDdvLIQLGPGGNTSLLLLLVLGlagayVLSALLGILRGRLLARLGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 899 MKLRLFENIMYQEISFFdqDSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVA-AVLTGTYF 977
Cdd:cd18563 78 LRRDLYEHLQRLSLSFF--DKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLAlLVLIPVPL 155
|
170
....*....|..
gi 156095386 978 IFMRVFAIRARI 989
Cdd:cd18563 156 VVWGSYFFWKKI 167
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1356-1448 |
8.50e-05 |
|
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: 47.32 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1356 SLSGGQKQRIAIARALLRE---PKILLLDEATSSL---DSNseKLIEkTIVDIKDKADkTIITIAHRIASIKRSDKIVVF 1429
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIK--KLLE-VLQRLVDKGN-TVVVIEHNLDVIKTADYIIDL 904
|
90 100
....*....|....*....|.
gi 156095386 1430 nNPD--RTGSFVQAQGTHEEL 1448
Cdd:TIGR00630 905 -GPEggDGGGTVVASGTPEEV 924
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
575-651 |
9.41e-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: 47.09 E-value: 9.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFV 651
Cdd:COG1245 451 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1356-1450 |
9.49e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASI-KRSDKIVVFNNPDR 1434
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVlGLSDRVLVMHEGKL 483
|
90
....*....|....*.
gi 156095386 1435 TGSFVQAQGTHEELLS 1450
Cdd:PRK13549 484 KGDLINHNLTQEQVME 499
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1170-1429 |
9.53e-05 |
|
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: 45.60 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1170 NFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvg 1249
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPP------------------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1250 mknanefssskegadgqsstlfkNSGKILLDGvdicdynlkDLRNLFSI-VSQEPMLfnmSIYENIKFgkeNATREDVKR 1328
Cdd:cd03220 75 -----------------------DSGTVTVRG---------RVSSLLGLgGGFNPEL---TGRENIYL---NGRLLGLSR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAAIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKtIVDIKDK 1405
Cdd:cd03220 117 KEIDEKIDEIIEfsELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRR-LRELLKQ 191
|
250 260
....*....|....*....|....*
gi 156095386 1406 AdKTIITIAHRIASIKR-SDKIVVF 1429
Cdd:cd03220 192 G-KTVILVSHDPSSIKRlCDRALVL 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
579-643 |
9.91e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 9.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI 643
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR-DEGKTMLVSTHNLGSV 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
569-654 |
1.06e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 569 YETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANT 648
Cdd:PRK10982 385 HRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDR 460
|
....*.
gi 156095386 649 IFVLSN 654
Cdd:PRK10982 461 ILVMSN 466
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
395-611 |
1.13e-04 |
|
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: 44.66 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnLKDVNLKWWRSkigvvsqdpLLF-- 472
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-LAEQRDEPHEN---------ILYlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 473 -SNSIKNnikyslyslkdleALSEESNEDGFSSQSDSNSRNSCRAKCAGDLNDmiqttdsteliqvrknyetIEDsevvs 551
Cdd:TIGR01189 80 hLPGLKP-------------ELSALENLHFWAAIHGGAQRTIEDALAAVGLTG-------------------FED----- 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 552 vskkvlihdfvsaLPdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:TIGR01189 123 -------------LP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1322-1446 |
1.32e-04 |
|
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: 45.44 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS----NSEKLI 1395
Cdd:cd03236 107 VGELLKKKDERGKLDELVDqlELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrlNAARLI 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1396 EKTIVDikdkaDKTIITIAHRIASIKR-SDKI-VVFNNPDRTGSFVQAQGTHE 1446
Cdd:cd03236 183 RELAED-----DNYVLVVEHDLAVLDYlSDYIhCLYGEPGAYGVVTLPKSVRE 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
580-611 |
1.87e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 1.87e-04
10 20 30
....*....|....*....|....*....|..
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1356-1396 |
2.20e-04 |
|
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: 43.89 E-value: 2.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:TIGR01189 127 QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
398-643 |
2.24e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLKwwRSK------IGVVSQD-PL 470
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG----KEIDFK--SSKealengISMVHQElNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 471 LFSNSIKNNIKYSLYSLKDLEAlseesnedgfssqsdsnsrnscrakcagDLNDMIQTTdsteliqvrknyETIEDSEVV 550
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKGMFV----------------------------DQDKMYRDT------------KAIFDELDI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 551 SVSKKVLIhdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnEN 630
Cdd:PRK10982 125 DIDPRAKV-------------------ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK--ER 183
|
250
....*....|....
gi 156095386 631 RITII-IAHRLSTI 643
Cdd:PRK10982 184 GCGIVyISHKMEEI 197
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
580-625 |
2.60e-04 |
|
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: 43.77 E-value: 2.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1356-1396 |
2.83e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIE 1396
Cdd:PLN03073 627 TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
380-499 |
2.94e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.99 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 380 IKKIQFKNVRfhydtrkdveIYKDLNFTLTEGKTyAFVGESGCGKSTILKLIERLYDPTEGDVI-INDSHNLKDVNLK-- 456
Cdd:COG3593 3 LEKIKIKNFR----------SIKDLSIELSDDLT-VLVGENNSGKSSILEALRLLLGPSSSRKFdEEDFYLGDDPDLPei 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 156095386 457 ----WWRSKIGVVSQDplLFSNSIKNNIKYSLYSLKdlEALSEESNE 499
Cdd:COG3593 72 eielTFGSLLSRLLRL--LLKEEDKEELEEALEELN--EELKEALKA 114
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
570-652 |
3.00e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRY-ANT 648
Cdd:PRK13409 203 ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL--AEGKYVLVVEHDLAVLDYlADN 280
|
....
gi 156095386 649 IFVL 652
Cdd:PRK13409 281 VHIA 284
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
577-643 |
3.02e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.21 E-value: 3.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
557-663 |
3.02e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 557 LIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIR-----NP--KILILDEATSSLDNKSEYLVQKTINNL--KG 627
Cdd:PRK03695 106 ALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDVAQQAALDRLLSELcqQG 183
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 156095386 628 nenrITIIIA-HRLS-TIRYANTIFVLSNRE---NGSTVDV 663
Cdd:PRK03695 184 ----IAVVMSsHDLNhTLRHADRVWLLKQGKllaSGRRDEV 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1319-1389 |
4.21e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 4.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1319 ENATREDvkRACKFAAIDEFIESLPNQYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:TIGR00956 173 DGVSREE--YAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1358-1388 |
4.79e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.76 E-value: 4.79e-04
10 20 30
....*....|....*....|....*....|.
gi 156095386 1358 SGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1270-1388 |
4.79e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.38 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1270 LFKNSGKILLDGVDICDYNLKDL---RNLFSivSQEPMLFNMSIYENIKFGKENATREDVKRAckfaAIDEFIES--LPN 1344
Cdd:PRK03695 45 LLPGSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPFAMPVFQYLTLHQPDKTRTEAVAS----ALNEVAEAlgLDD 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1345 QYDTNVGpygkSLSGGQKQRIAIARALLR-------EPKILLLDEATSSLD 1388
Cdd:PRK03695 119 KLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
570-663 |
5.05e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.66 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 570 ETLVGSNASKLSGGQKQRISIARAI---------IRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PRK13547 136 TALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDP 215
|
90 100
....*....|....*....|....*..
gi 156095386 641 S-TIRYANTIFVLSNRE---NGSTVDV 663
Cdd:PRK13547 216 NlAARHADRIAMLADGAivaHGAPADV 242
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
577-611 |
5.16e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 5.16e-04
10 20 30
....*....|....*....|....*....|....*
gi 156095386 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:NF033858 134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1306-1422 |
5.33e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.53 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1306 FNMSI--YENIKFgkeNA-----TREDVKRacKFAAIDEFIEsLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKIL 1378
Cdd:COG1134 99 FHPELtgRENIYL---NGrllglSRKEIDE--KFDEIVEFAE-LGDFIDQPV----KTYSSGMRARLAFAVATAVDPDIL 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 156095386 1379 LLDEATSSLDSN-SEKLIEKtIVDIKDKAdKTIITIAHRIASIKR 1422
Cdd:COG1134 169 LVDEVLAVGDAAfQKKCLAR-IRELRESG-RTVIFVSHSMGAVRR 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1355-1401 |
5.73e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 5.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS 485
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1181-1450 |
6.32e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.44 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1181 IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHhiVFKNeqtgessKEQMQQgdeeqnvgmknanefSSSK 1260
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH--VWLD-------GEHIQH---------------YASK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1261 EGAdgqsstlfKNSGKILLDGVDICDYNLKDL--RNLFSivsQEPMLfnmsiyenIKFGKENAtrEDVKRACKFAAIDEf 1338
Cdd:PRK10253 78 EVA--------RRIGLLAQNATTPGDITVQELvaRGRYP---HQPLF--------TRWRKEDE--EAVTKAMQATGITH- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 iesLPNQ-YDTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:PRK10253 136 ---LADQsVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
|
250 260 270
....*....|....*....|....*....|....
gi 156095386 1418 ASIKR-SDKIVVFnnpdRTGSFVqAQGTHEELLS 1450
Cdd:PRK10253 205 NQACRyASHLIAL----REGKIV-AQGAPKEIVT 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
394-635 |
6.55e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.54 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKwwrsKIGVV----SQ 467
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyVPFKRRKEFAR----RIGVVfgqrSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 468 dpLLFsnsiknnikyslyslkDLEALseesnedgfssqsdsnsrnscrakcagdlndmiqttDSTELIqvRKNYEtIEDS 547
Cdd:COG4586 107 --LWW----------------DLPAI------------------------------------DSFRLL--KAIYR-IPDA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 548 EVvsvskKVLIHDFVSAL--PDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:COG4586 130 EY-----KKRLDELVELLdlGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY 200
|
250
....*....|
gi 156095386 626 KgNENRITII 635
Cdd:COG4586 201 N-RERGTTIL 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
580-624 |
7.40e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 7.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1360-1415 |
7.65e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 7.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1360 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADKTIITIAH 1415
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLE----DVLNERNSTMIIISH 210
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
579-652 |
7.95e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 7.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINVL 232
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1325-1413 |
8.33e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1325 DVKRACKFAAIDEFIE--SLPNQYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PLN03140 985 EVSKEEKMMFVDEVMElvELDNLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
90
....*....|..
gi 156095386 1402 IKDKADKTIITI 1413
Cdd:PLN03140 1065 TVDTGRTVVCTI 1076
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
571-643 |
9.06e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 9.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 571 TLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVqKTINNLKgNENRITIIIAHRLSTI 643
Cdd:PRK10762 137 KLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELK-SQGRGIVYISHRLKEI 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1307-1459 |
9.11e-04 |
|
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: 43.85 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1307 NMSIYENIKFgKENATREDVKRACKFAAIDEFIESLpnQYDTNVG-PY------GKSLSGGQKQRIAIARAL-------- 1371
Cdd:TIGR00630 435 ELSIREAHEF-FNQLTLTPEEKKIAEEVLKEIRERL--GFLIDVGlDYlslsraAGTLSGGEAQRIRLATQIgsgltgvl 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1372 --LREPKILLLDEATssldsnsEKLIEkTIVDIKDKADkTIITIAHRIASIKRSDKIVvfnnpD------RTGSFVQAQG 1443
Cdd:TIGR00630 512 yvLDEPSIGLHQRDN-------RRLIN-TLKRLRDLGN-TLIVVEHDEDTIRAADYVI-----DigpgagEHGGEVVASG 577
|
170
....*....|....*.
gi 156095386 1444 THEELLSVQDGVYKKY 1459
Cdd:TIGR00630 578 TPEEILANPDSLTGQY 593
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
555-649 |
1.07e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 555 KVLIHDFVSALPdkyetlVGSNASKLSGGQKQRISIARAIIRNPK---ILILDEATSSLDNKSEYLVQKTINNLKgNENR 631
Cdd:PRK00635 1681 QALIDNGLGYLP------LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLV-SLGH 1753
|
90
....*....|....*...
gi 156095386 632 ITIIIAHRLSTIRYANTI 649
Cdd:PRK00635 1754 SVIYIDHDPALLKQADYL 1771
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
382-442 |
1.13e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 382 KIQF--KNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKL-IERLyDPTEGDV 442
Cdd:PRK11147 317 KIVFemENVNYQIDGKQLV---KDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGRI 376
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1358-1415 |
1.24e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.32 E-value: 1.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1358 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAH 1415
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1310-1460 |
1.26e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1310 IYENIKFGKE-NATREDVkrACKFAAIDEFIESLPNQYDTNVG--PYGK---SLSGGQKQRIAIARALL---REPKILLL 1380
Cdd:PRK00635 1649 VYEGKHFGQLlQTPIEEV--AETFPFLKKIQKPLQALIDNGLGylPLGQnlsSLSLSEKIAIKIAKFLYlppKHPTLFLL 1726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1381 DEATSSLDSNSEKLIEK---TIVDIkdkaDKTIITIAHRIASIKRSDKIVVFN-NPDRTGSFVQAQGTHEELLSVQDGVY 1456
Cdd:PRK00635 1727 DEIATSLDNQQKSALLVqlrTLVSL----GHSVIYIDHDPALLKQADYLIEMGpGSGKTGGKILFSGPPKDISASKDSLL 1802
|
....
gi 156095386 1457 KKYV 1460
Cdd:PRK00635 1803 KTYM 1806
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1357-1391 |
1.32e-03 |
|
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: 41.86 E-value: 1.32e-03
10 20 30
....*....|....*....|....*....|....*
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
570-625 |
1.36e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 1.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILI-LDEATSSLDNKSEYLVQKTINNL 625
Cdd:TIGR00956 892 DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1356-1402 |
1.50e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 1.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 156095386 1356 SLSGGQkQRIA-IARALLREPKILLLDEATSSLDSNSEKLIeKTIVDI 1402
Cdd:PRK10938 401 SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLV-RRFVDV 446
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
824-1097 |
1.61e-03 |
|
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: 42.18 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 824 DIAIIALSIMVAGGLYPLFAL-LYAKYVGtlfdfanleaNSNKYSLYILVIAIAM-FISET----LKNYYNNVIGEKVEK 897
Cdd:cd18566 6 QVLLASLFINILALATPLFILqVYDRVIP----------NESIPTLQVLVIGVVIaILLESllrlLRSYILAWIGARFDH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 898 TMKLRLFENIMYQEISFFDQDSHapgllSAHINR--DVHLLK---TGLVNNIVIFTHFIVLFLVstVMSFY-----FCPI 967
Cdd:cd18566 76 RLSNAAFEHLLSLPLSFFEREPS-----GAHLERlnSLEQIReflTGQALLALLDLPFVLIFLG--LIWYLggklvLVPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 968 VAAVLtgtyFIFMRVF---AIRARIAANKDVEKKRVNqpgtafvynsddeifkdpsFLIqEAFYNMNTVIIYGLEDYFC- 1043
Cdd:cd18566 149 VLLGL----FVLVAILlgpILRRALKERSRADERRQN-------------------FLI-ETLTGIHTIKAMAMEPQMLr 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1044 ---TLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFInsfaYWFGSFLIRRGTIQV 1097
Cdd:cd18566 205 ryeRLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAV----VAFGALLVINGDLTV 257
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
580-638 |
1.68e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
99-311 |
2.05e-03 |
|
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: 41.76 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 99 IIFSLVLIGIFQFI-LSFISSFCMDVVTTkilktLKIEFLKSVFYQDGQFHDNNPG----SKLTSDL-DF--YLEQVnAG 170
Cdd:cd18574 48 LLGLYLLQSLLTFAyISLLSVVGERVAAR-----LRNDLFSSLLRQDIAFFDTHRTgelvNRLTADVqEFksSFKQC-VS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 171 IGTKFITIFtyASAFLGLYIWSlfknARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVV 250
Cdd:cd18574 122 QGLRSVTQT--VGCVVSLYLIS----PKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVR 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 251 SYCGENTILKKFNLSEKLYSKytLKANLmeSLHIGM--------INGFILASYAFGfwyGTRIIISDLS 311
Cdd:cd18574 196 AFAMEDRELELYEEEVEKAAK--LNEKL--GLGIGIfqglsnlaLNGIVLGVLYYG---GSLVSRGELT 257
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
581-651 |
2.40e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 2.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 581 SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRYANTIFV 651
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLR-DGKRSFIIVTHYQRILDYIKPDYV 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1355-1399 |
2.50e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 2.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PRK13538 128 RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1269-1388 |
2.51e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1269 TLF----KNSGKILLDGVDICDYNLKDL-----------RNLFSIVSQEPMLFNMS--IYENIKF----GKENATREDVK 1327
Cdd:PRK15439 308 TLYglrpARGGRIMLNGKEINALSTAQRlarglvylpedRQSSGLYLDAPLAWNVCalTHNRRGFwikpARENAVLERYR 387
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1328 RA--CKFAAIDEFIeslpnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK15439 388 RAlnIKFNHAEQAA---------------RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
400-442 |
2.71e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 156095386 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDV 442
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1356-1412 |
2.77e-03 |
|
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: 42.31 E-value: 2.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1412
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT 2126
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1352-1428 |
3.03e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 3.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1352 PYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVV 1428
Cdd:PRK15093 156 PY--ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINV 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
578-614 |
3.48e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 3.48e-03
10 20 30
....*....|....*....|....*....|....*..
gi 156095386 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1326-1413 |
3.78e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1326 VKRACKFAAIDEFIESLP-NQY-DTNVGPYGKSLSGGQKQRIAIARALLREPKILL-LDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:TIGR00956 869 VSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
90
....*....|.
gi 156095386 1403 KDKADKTIITI 1413
Cdd:TIGR00956 949 ADHGQAILCTI 959
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
569-616 |
3.81e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 3.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 156095386 569 YETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:TIGR00956 198 RNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAL 246
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
578-611 |
5.44e-03 |
|
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: 39.94 E-value: 5.44e-03
10 20 30
....*....|....*....|....*....|....
gi 156095386 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:cd03233 117 RGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
374-447 |
5.58e-03 |
|
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: 41.07 E-value: 5.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 374 GKKLKDiKKIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS 447
Cdd:TIGR03719 315 GPRLGD-KVIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET 384
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
380-685 |
5.88e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 40.66 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 380 IKKIQFKNVRFHydtrKDVEIYKDLNFTLtegktyaFVGESGCGKSTILKLIERLYDPTEgdviindSHNLKDVNLKWWR 459
Cdd:pfam13175 3 IKSIIIKNFRCL----KDTEIDLDEDLTV-------LIGKNNSGKSSILEALDIFLNNKE-------KFFEDDFLVLYLK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 460 SKIGVVSQDPLLFSNSIKNN---IKYSLYSLKDLEALSEESNEDGFSSQSDSNSRNSCRAKCAGDLNDMIQTTDSTelIQ 536
Cdd:pfam13175 65 DVIKIDKEDLNIFENISFSIdieIDVEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISD--LK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 537 VRKNYETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKlsggqkqrisiaraiirnPKILILDEATSSLDNKSEY 616
Cdd:pfam13175 143 KYLKQFKIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEK------------------EEIKVDKEDLKKLINELEK 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 617 LVQKTINNLKGNENRITIIIAHRlstiryantifvlSNRENGSTVDVDVLGEDPTKDSNEKNEKHDKQE 685
Cdd:pfam13175 205 SINYHENVLENLQIKKLLISADR-------------NASDEDSEKINSLLGALKQRIFEEALQEELELT 260
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
400-615 |
6.04e-03 |
|
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: 39.78 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNLKDVNLKWWRSKIGVVSQdpllfsnsikNN 479
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDFQRDSIARGLLYLGHA----------PG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 480 IKYSLYSLKDLEALSeesnedgfssqsDSNSRNSCRakcagdlndmiqttdsTELIQVrkNYETIEDSEVVSvskkvlih 559
Cdd:cd03231 84 IKTTLSVLENLRFWH------------ADHSDEQVE----------------EALARV--GLNGFEDRPVAQ-------- 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 560 dfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:cd03231 126 --------------------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
62-309 |
6.42e-03 |
|
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: 40.21 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 62 LGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDII--FSLVLIGIF--QFILSFISSFCMDVVTTKI--------- 128
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLlgLALLLLGAYllRALLNFLRIYLNHVAEQKVvadlrsdly 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 129 --LKTLKIEFlksvfyqdgqFHDNNPG---SKLTSDLDfYLEQVNA-GIGTKFITIFTyasaFLGLYIWSLFKNARLTLc 202
Cdd:cd18778 81 dkLQRLSLRY----------FDDRQTGdlmSRVINDVA-NVERLIAdGIPQGITNVLT----LVGVAIILFSINPKLAL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 203 ITCV-FPLIYICGVICNKKV----KINKKTSLLYNnntmSIIEEALVGIRTVVSYCGENTILKKFN-LSEKlYSKYTLKA 276
Cdd:cd18778 145 LTLIpIPFLALGAWLYSKKVrpryRKVREALGELN----ALLQDNLSGIREIQAFGREEEEAKRFEaLSRR-YRKAQLRA 219
|
250 260 270
....*....|....*....|....*....|...
gi 156095386 277 NLMESLHIGMINGFILASYAFGFWYGTRIIISD 309
Cdd:cd18778 220 MKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAG 252
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1293-1388 |
6.65e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1293 RNLFsivsqePMLfnmSIYENIKF-----GKENATREdvkrackfAAIDEFIESlpnqydTNVGPY-----GKsLSGGQK 1362
Cdd:NF033858 87 KNLY------PTL---SVFENLDFfgrlfGQDAAERR--------RRIDELLRA------TGLAPFadrpaGK-LSGGMK 142
|
90 100
....*....|....*....|....*.
gi 156095386 1363 QRIAIARALLREPKILLLDEATSSLD 1388
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
192-346 |
6.80e-03 |
|
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: 40.07 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 192 SLFKNARLTLCITCVFPLIYICGVICNKKV-----KINKKTSLLynNNtmsIIEEALVGIRTVVSYCGENTILKKFNLSE 266
Cdd:cd18548 134 AFRINPKLALILLVAIPILALVVFLIMKKAiplfkKVQKKLDRL--NR---VVRENLTGIRVIRAFNREDYEEERFDKAN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 267 KLYSKYTLKAN-LMESLHIGM---INGFILASYAFGfwyGTRIIISDLSNqqpnndfhgGSVISI---LLGVLISMFMLT 339
Cdd:cd18548 209 DDLTDTSLKAGrLMALLNPLMmliMNLAIVAILWFG---GHLINAGSLQV---------GDLVAFinyLMQILMSLMMLS 276
|
....*..
gi 156095386 340 IILPNIT 346
Cdd:cd18548 277 MVFVMLP 283
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
865-1101 |
7.10e-03 |
|
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: 40.07 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 865 KYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQDShAPGLlsahINR---DVHLLKTGLV 941
Cdd:cd18548 40 RTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFG-TSSL----ITRltnDVTQVQNFVM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 942 NNIVIFTHFIVLFLVSTVMSFY--------FCPIVAAVLTGTYFIFMRVFAIRARIAANKDvekkRVNQpgtafvynsdd 1013
Cdd:cd18548 115 MLLRMLVRAPIMLIGAIIMAFRinpklaliLLVAIPILALVVFLIMKKAIPLFKKVQKKLD----RLNR----------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1014 eifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKAidysNKGQKRKTLINSMLWGFSQSAQFFINSFA----YWFGSFL 1089
Cdd:cd18548 180 --------VVRENLTGIRVIRAFNREDYEEERFDKA----NDDLTDTSLKAGRLMALLNPLMMLIMNLAivaiLWFGGHL 247
|
250
....*....|..
gi 156095386 1090 IRRGTIQVDDFM 1101
Cdd:cd18548 248 INAGSLQVGDLV 259
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
580-611 |
7.38e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 7.38e-03
10 20 30
....*....|....*....|....*....|..
gi 156095386 580 LSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
825-1055 |
7.45e-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: 40.18 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLYpLFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLF 904
Cdd:cd18580 1 VLLLLLLLLLLAFLS-QFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 905 ENIMYQEISFFDqdSHAPGLLsahINR---DVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP---IVAAVLTGTYFI 978
Cdd:cd18580 80 RSVLRAPMSFFD--TTPSGRI---LNRfskDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPyflIVLPPLLVVYYL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 979 FMRVFairarIAANKDVekKRVnqpgtafvynsdDEIFKDPSF-LIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNK 1055
Cdd:cd18580 155 LQRYY-----LRTSRQL--RRL------------ESESRSPLYsHFSETLSGLSTIRAFGWQERFIEENLRLLDASQR 213
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
574-614 |
7.51e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 7.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 156095386 574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
825-991 |
8.19e-03 |
|
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: 40.16 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 825 IAIIALSIMVAGGLYPLFALLYAKyvgtLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLRE----IIDDALPQGDLgllVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 902 RLFENIMYQEISFFdqDSHAPGLLSAHINRDVHLLK-------TGLVNN--IVIFThFIVLFLVS---TVMSFYFCPIva 969
Cdd:cd18550 77 QLYAHLQRMSLAFF--TRTRTGEIQSRLNNDVGGAQsvvtgtlTSVVSNvvTLVAT-LVAMLALDwrlALLSLVLLPL-- 151
|
170 180
....*....|....*....|....
gi 156095386 970 avltgtyFIFM--RVFAIRARIAA 991
Cdd:cd18550 152 -------FVLPtrRVGRRRRKLTR 168
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1355-1452 |
8.59e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSeklIEkTIVDIKDKADKTIITIAH----------RIASIKrSD 1424
Cdd:PRK15064 437 KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IE-SLNMALEKYEGTLIFVSHdrefvsslatRIIEIT-PD 511
|
90 100
....*....|....*....|....*...
gi 156095386 1425 KIVVFnnpdrtgsfvqaQGTHEELLSVQ 1452
Cdd:PRK15064 512 GVVDF------------SGTYEEYLRSQ 527
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
186-308 |
8.68e-03 |
|
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: 39.77 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 186 LGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKV--------KINKKTSLLYNnntmsiieEALVGIRTVVSYCGENT 257
Cdd:cd18540 131 IGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKIlkayrkvrKINSRITGAFN--------EGITGAKTTKTLVREEK 202
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 156095386 258 ILKKF-NLSEKLYsKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIIS 308
Cdd:cd18540 203 NLREFkELTEEMR-RASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLA 253
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| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
841-1078 |
9.16e-03 |
|
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: 39.78 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 841 LFALLY--AKYVGTLF-----DFANLEANSNKYSLYILVIAI--AMFISETLKNYYN---NVIGEKV---------EKTM 899
Cdd:cd18579 4 LLKLLEdlLSLAQPLLlglliSYLSSYPDEPLSEGYLLALALflVSLLQSLLLHQYFflsFRLGMRVrsalssliyRKAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 900 KLrlfenimyqeiSFFDQDSHAPG----LLSAHINRdvhllktglVNNIVIFTHFIVLFLVSTVMSFY----------FC 965
Cdd:cd18579 84 RL-----------SSSARQETSTGeivnLMSVDVQR---------IEDFFLFLHYLWSAPLQIIVALYllyrllgwaaLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 966 PIVAAVLT--GTYFIFMRVFAIRARIAANKDvekKRVNqpgtafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFC 1043
Cdd:cd18579 144 GLGVLLLLipLQAFLAKLISKLRKKLMKATD---ERVK--------------------LTNEILSGIKVIKLYAWEKPFL 200
|
250 260 270
....*....|....*....|....*....|....*
gi 156095386 1044 TLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFI 1078
Cdd:cd18579 201 KRIEELRKKELKALRKFGYLRALNSFLFFSTPVLV 235
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|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
824-986 |
9.71e-03 |
|
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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 39.81 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 824 DIAIIALSIMVagglyplFALLYAKYVGTLFDFA-NLEANSNKYSLYILVIAIAMFisET----LKNYYNNVIGEKVEKT 898
Cdd:cd18783 6 DVAIASLILHV-------LALAPPIFFQIVIDKVlVHQSYSTLYVLTIGVVIALLF--EGilgyLRRYLLLVATTRIDAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 899 MKLRLFENIMYQEISFFDQdsHAPGLLSAHIN-----RDV---HLLKTGL-VNNIVIFthFIVLFLVSTVMSFY---FCP 966
Cdd:cd18783 77 LALRTFDRLLSLPIDFFER--TPAGVLTKHMQqieriRQFltgQLFGTLLdATSLLVF--LPVLFFYSPTLALVvlaFSA 152
|
170 180
....*....|....*....|
gi 156095386 967 IVAAVLtgtyFIFMRVFAIR 986
Cdd:cd18783 153 LIALII----LAFLPPFRRR 168
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