|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
47-1263 |
0e+00 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 597.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 47 RLYMLVGTLAAIIHGVALPLMMLIFGDMTdsfasvgnvsknsTNMSeadkramfakLEEEMTTYAYYYTGIGAGVLIVAY 126
Cdd:PTZ00265 59 RKLLGVSFVCATISGGTLPFFVSVFGVIM-------------KNMN----------LGENVNDIIFSLVLIGIFQFILSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 127 IqvSFWCL--AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGF 204
Cdd:PTZ00265 116 I--SSFCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 205 TRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLG 284
Cdd:PTZ00265 194 FKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 285 IKKAITANISMGAAFLLIYASYALAFWYGTSLVIS--------KEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARG 356
Cdd:PTZ00265 274 LKANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 357 AAYEVFKIIDNKPSIDSfSKSGHKPDNIQgNLEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLM 436
Cdd:PTZ00265 354 ATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 437 QRLYDPLDGMVSI-DGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG--------------RED----------- 490
Cdd:PTZ00265 432 ERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDgndsqenknkr 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 491 -----------------VTMDEIEKAVKEANA---------------YDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIA 538
Cdd:PTZ00265 512 nscrakcagdlndmsntTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIA 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 539 RALVRNPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVI---------------------- 594
Cdd:PTZ00265 592 RAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedpt 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 595 -------------------------AGFDGGVIVEQGNHDELMREK-GIYFKLVMTQTA--------GNEIELGNEACKS 640
Cdd:PTZ00265 672 kdnkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKVsskkssnnDNDKDSDMKSSAY 751
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 641 KD-----EIDNLDMSSKDSGSSLIRRRSTRKSICGPHDQDR--KLSTKEALDEDVPPA-SFWRILKLNSTEWPYFVVGIF 712
Cdd:PTZ00265 752 KDsergyDPDEMNGNSKHENESASNKKSCKMSDENASENNAggKLPFLRNLFKRKPKApNNLRIVYREIFSYKKDVTIIA 831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 713 CAII-NGGLQPAFSVIFSKVVGVFTNGGPPETqrqNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKS 791
Cdd:PTZ00265 832 LSILvAGGLYPVFALLYAKYVSTLFDFANLEA---NSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFEN 908
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 792 MLRQDVSWFDDPKNTTGALTTRLANDAAQVKGATGSRLaVIFQNIANLgtgIIISLIYGWQLTLLLLAIVPIIAIagvVE 871
Cdd:PTZ00265 909 ILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNI-VIFTHFIVL---FLVSMVMSFYFCPIVAAVLTGTYF---IF 981
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 872 MKMLSGQA-LKDKKELEGSGK---------------------IATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMK 929
Cdd:PTZ00265 982 MRVFAIRArLTANKDVEKKEInqpgtvfaynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKR 1061
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 930 KAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKATVSASHIIRIIE 1009
Cdd:PTZ00265 1062 KTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLII 1141
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1010 KTPEIDSYSTQGLK---PNMLEGNVQFSGVVFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-- 1084
Cdd:PTZ00265 1142 RKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlk 1221
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1085 ----------------------------------------------------PMAGSVFLDGKEIKQLNVQWLRAQLGIV 1112
Cdd:PTZ00265 1222 ndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIV 1301
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1113 SQEPILFDCSIAENIAYGDNSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHI 1192
Cdd:PTZ00265 1302 SQEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKI 1379
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1193 LLLDEATSALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVIQNGK-----VKEHGTHQQLL-AQKGI 1262
Cdd:PTZ00265 1380 LLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGV 1457
|
.
gi 153791547 1263 Y 1263
Cdd:PTZ00265 1458 Y 1458
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
38-628 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 545.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 38 MFRYAgWLDRLYMLVGTLAAIIHGVALPLMMLIFGDMTDSFASVGNVSKnstnmseadkramfakleeeMTTYAYYYTGI 117
Cdd:COG1132 12 LLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA--------------------LLLLLLLLLGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 118 GAGVLIVAYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFF 197
Cdd:COG1132 71 ALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 198 GGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNL 277
Cdd:COG1132 151 GALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 278 EEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGA 357
Cdd:COG1132 231 EELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALAS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 358 AYEVFKIIDNKPSIDSfSKSGHKPDNIQGNLEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQ 437
Cdd:COG1132 311 AERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 438 RLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFD 517
Cdd:COG1132 388 RFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 518 TLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGF 597
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVL 547
|
570 580 590
....*....|....*....|....*....|.
gi 153791547 598 DGGVIVEQGNHDELMREKGIYFKLVMTQTAG 628
Cdd:COG1132 548 DDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
50-361 |
1.38e-178 |
|
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: 529.16 E-value: 1.38e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 50 MLVGTLAAIIHGVALPLMMLIFGDMTDSFASVGNVSKNSTNMSEADKRAMFAKLEEEMTTYAYYYTGIGAGVLIVAYIQV 129
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 130 SFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWK 209
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 210 LTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAI 289
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 290 TANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEV 361
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
689-1273 |
2.87e-170 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 517.80 E-value: 2.87e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 689 PPASFWRILKLNSTEWPYFVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETqrqnSNLFSLLFLILGIISFITFFL 768
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA----LLLLLLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 769 QGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLI 848
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 849 YGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAM 928
Cdd:COG1132 159 IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 929 KKAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKATVSASHIIRII 1008
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1009 EKTPEI-DSYSTQGLKPnmLEGNVQFSGVVFNYPtrPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA 1087
Cdd:COG1132 319 DEPPEIpDPPGAVPLPP--VRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1088 GSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGD 1167
Cdd:COG1132 395 GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1168 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKV 1247
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
570 580
....*....|....*....|....*.
gi 153791547 1248 KEHGTHQQLLAQKGIYFSMVSVQAGA 1273
Cdd:COG1132 553 VEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1031-1270 |
7.99e-153 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 458.54 E-value: 7.99e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFDCSIAENIAYGDNSRVVsyEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1190
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSVQ 1270
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
389-625 |
2.01e-152 |
|
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: 457.77 E-value: 2.01e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 389 EFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGV 468
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 469 VSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 548
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 549 LLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 625
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
707-1004 |
1.54e-149 |
|
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: 453.27 E-value: 1.54e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGG----------------PPETQRQNSNLFSLLFLILGIISFITFFLQG 770
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGmtnitgnssglnssagPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 771 FTFGKAGEILTKRLRYMVFKSMLRQDVSWFddPKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYG 850
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 851 WQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKK 930
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 931 AHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLM-TFENVLLVFSAIVFGAMAVGQVSSFAPdYAKATVSASHI 1004
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYsIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
697-1014 |
3.52e-144 |
|
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: 439.19 E-value: 3.52e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 697 LKLNSTEWPYFVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPEtQRQNSNLFSLLFLILGIISFITFFLQGFTFGKA 776
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDE-LRSEANFWALMFLVLAIVAGIAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 777 GEILTKRLRYMVFKSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLL 856
Cdd:cd18578 80 GERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 857 LLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGI 936
Cdd:cd18578 160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 937 TFSFTQAMMYFSYAACFRFGAYLVTQQLMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKATVSASHIIRIIEKTPEI 1014
Cdd:cd18578 240 GFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
117-626 |
1.04e-143 |
|
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: 452.75 E-value: 1.04e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 117 IGAGVLIVAYIQVSF-----WCLA-AGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMF 189
Cdd:COG2274 198 LAIGLLLALLFEGLLrllrsYLLLrLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 190 FQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKE 269
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 270 LERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTvfFSVLIGAF--SVGQASPN 347
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIA--FNILSGRFlaPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 348 IEAFANARGAAYEVFKIIDNKPSIDSFSKSGHKPdNIQGNLEFKNIHFSYPSRkEVQILKGLNLKVKSGQTVALVGNSGC 427
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP-RLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 428 GKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYD 507
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 508 FIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLST 587
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490 500 510
....*....|....*....|....*....|....*....
gi 153791547 588 VRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQT 626
Cdd:COG2274 673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
135-622 |
3.20e-140 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 443.39 E-value: 3.20e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 135 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVI 214
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 215 LAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANIS 294
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 295 MGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLtvffSVLIGAFSVGQASPNIEAFAN----ARGAAYEVFKIIDNKPS 370
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSgmmqAVGASEKVFEYLDRKPN 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 371 IDSfsKSGHKPDNIQGNLEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSID 450
Cdd:TIGR00958 464 IPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 451 GQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGG 530
Cdd:TIGR00958 542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 531 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAalDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDE 610
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699
|
490
....*....|..
gi 153791547 611 LMREKGIYFKLV 622
Cdd:TIGR00958 700 LMEDQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
680-1271 |
1.74e-137 |
|
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: 436.19 E-value: 1.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 680 TKEALDEDVPPASFWRILKLNSTEWPYFVVGIFCAIINGGLQ---PAFS-VIFSKVVGvftnggppeTQRQNS-NLFSLL 754
Cdd:COG2274 131 TPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLAlatPLFTqVVIDRVLP---------NQDLSTlWVLAIG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 755 FLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKGATGSRLAVIFQ 834
Cdd:COG2274 202 LLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 835 NIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGsgkIATEAIENFRTVVSLTRE-- 909
Cdd:COG2274 279 DLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLfqpRLRRLSREESEASAKRQS---LLVETLRGIETIKALGAEsr 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 910 --QKFETMYAQSLqipyRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFeNVLLVFSAIVFGAMA-VGQ 986
Cdd:COG2274 356 frRRWENLLAKYL----NARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 987 VSSFAPDYAKATVSASHIIRIIEKTPEIDSYSTQGLKPNmLEGNVQFSGVVFNYPTRpSIPVLQGLSLEVKKGQTLALVG 1066
Cdd:COG2274 431 LIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1067 SSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSYEEIVRAAK 1146
Cdd:COG2274 509 RSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAAR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1147 EANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVI 1226
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 153791547 1227 AHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSVQA 1271
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
50-361 |
2.96e-130 |
|
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: 401.85 E-value: 2.96e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 50 MLVGTLAAIIHGVALPLMMLIFGDMTDSFASVGNVSKNStnmseadkramfAKLEEEMTTYAYYYTGIGAGVLIVAYIQV 129
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSP------------DEFLDDVNKYALYFVYLGIGSFVLSYIQT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 130 SFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWK 209
Cdd:cd18577 69 ACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 210 LTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAI 289
Cdd:cd18577 149 LTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 290 TANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEV 361
Cdd:cd18577 229 VSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
138-625 |
1.23e-128 |
|
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: 407.93 E-value: 1.23e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 138 RQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAI 217
Cdd:TIGR02204 88 RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 218 SPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGA 297
Cdd:TIGR02204 168 VPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 298 AFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFKIIDNKPSIDSFSKS 377
Cdd:TIGR02204 248 VIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 378 GHKPDNIQGNLEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI 457
Cdd:TIGR02204 328 KTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 458 NVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAI 537
Cdd:TIGR02204 408 DPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAI 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 538 ARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGI 617
Cdd:TIGR02204 488 ARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGL 567
|
....*...
gi 153791547 618 YFKLVMTQ 625
Cdd:TIGR02204 568 YARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
679-1267 |
1.82e-126 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 406.80 E-value: 1.82e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 679 STKEALDEDVPPAS-FWRILKLNSTEWPYFVVGIF---CAIINGGLQPAFSvifSKVVG-VFTNGGPPETQRqnsNLFSL 753
Cdd:TIGR00958 134 SEKEAEQGQSETADlLFRLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIDtLGGDKGPPALAS---AIFFM 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 754 LflILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIF 833
Cdd:TIGR00958 208 C--LLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 834 QNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTRE---- 909
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEegea 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 910 QKFETMYAQSLQIPYRNAMKKAhVFGITFSFTQAMMYFSYAACfrfGAYLVTQQLMTFENvLLVFsaiVFGAMAVGQ--- 986
Cdd:TIGR00958 364 SRFKEALEETLQLNKRKALAYA-GYLWTTSVLGMLIQVLVLYY---GGQLVLTGKVSSGN-LVSF---LLYQEQLGEavr 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 987 -VSSFAPDYAKATVSASHIIRIIEKTPEIDSysTQGLKPNMLEGNVQFSGVVFNYPTRPSIPVLQGLSLEVKKGQTLALV 1065
Cdd:TIGR00958 436 vLSYVYSGMMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALV 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1066 GSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSYEEIVRAA 1145
Cdd:TIGR00958 514 GPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAA 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1146 KEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEalDKAREGRTCIV 1225
Cdd:TIGR00958 592 KAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLL 669
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 153791547 1226 IAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMV 1267
Cdd:TIGR00958 670 IAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
737-1270 |
1.14e-116 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 375.96 E-value: 1.14e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 737 NGGPPETQRQNSNLFSLLFLILGIISFITFFlQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLAN 816
Cdd:TIGR02204 47 HGFSKDSSGLLNRYFAFLLVVALVLALGTAA-RFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 817 DAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEA 896
Cdd:TIGR02204 124 DTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGET 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 897 IENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTF-ENVLLVFS 975
Cdd:TIGR02204 204 LGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAgTLGQFVFY 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 976 AiVFGAMAVGQVSSFAPDYAKATVSASHIIRIIEKTPEIDSYSTQGLKPNMLEGNVQFSGVVFNYPTRPSIPVLQGLSLE 1055
Cdd:TIGR02204 284 A-VMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1056 VKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYG--DNS 1133
Cdd:TIGR02204 363 VRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDAT 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1134 RvvsyEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEA 1213
Cdd:TIGR02204 443 D----EEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQA 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1214 LDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSVQ 1270
Cdd:TIGR02204 519 LETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
692-1270 |
2.40e-114 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 369.43 E-value: 2.40e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 692 SFWRILKLNSTEWPYFVVGIFCAIINGGLQPafsvIFSKVVGVFTNGGPPETQRQNSNLFSLLFLILGIISFITFFLQGF 771
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATES----TLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 772 TFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGW 851
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 852 QLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRtVVSLTREQKFET-MYAQSLQIPYRNAMKK 930
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYR-VVKLFGGQAYETrRFDAVSNRNRRLAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 931 AHVFGITFSFTQ-----AMMYFSYAACFRFGA-YLVTQQLMTF-ENVLLVFSAIvfgamavGQVSSFAPDYAKATVSASH 1003
Cdd:TIGR02203 234 TSAGSISSPITQliaslALAVVLFIALFQAQAgSLTAGDFTAFiTAMIALIRPL-------KSLTNVNAPMQRGLAAAES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1004 IIRIIEKTPEIDsysTQGLKPNMLEGNVQFSGVVFNYPTRpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY 1083
Cdd:TIGR02203 307 LFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1084 DPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSyEEIVRAAKEANIHQFIDSLPDKYNT 1163
Cdd:TIGR02203 383 EPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADR-AEIERALAAAYAQDFVDKLPLGLDT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1164 RVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQ 1243
Cdd:TIGR02203 462 PIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMD 541
|
570 580
....*....|....*....|....*..
gi 153791547 1244 NGKVKEHGTHQQLLAQKGIYFSMVSVQ 1270
Cdd:TIGR02203 542 DGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
123-621 |
1.04e-113 |
|
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: 367.89 E-value: 1.04e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 123 IVAYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFII 202
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 203 GFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKR 282
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 283 LGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVFFSVLIGAFSVGQASPNIEA-FANARGAAYEV 361
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFITAMIALIRPLKSLTNVNApMQRGLAAAESL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 362 FKIIDNKPSIDsfsKSGHKPDNIQGNLEFKNIHFSYPSRkEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD 441
Cdd:TIGR02203 308 FTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 442 PLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGR-EDVTMDEIEKAVKEANAYDFIMKLPHQFDTLV 520
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 521 GERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGG 600
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
490 500
....*....|....*....|.
gi 153791547 601 VIVEQGNHDELMREKGIYFKL 621
Cdd:TIGR02203 544 RIVERGTHNELLARNGLYAQL 564
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
259-632 |
3.20e-113 |
|
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: 367.61 E-value: 3.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 259 TVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVltvffsVLIGA 338
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDF------VLVNA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 339 F----------------SVGQASPNIEAfanargaayeVFKIIDNKPSIDSfsksghKPDNI-----QGNLEFKNIHFSY 397
Cdd:COG5265 304 YliqlyiplnflgfvyrEIRQALADMER----------MFDLLDQPPEVAD------APDAPplvvgGGEVRFENVSFGY 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 398 -PSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLF 476
Cdd:COG5265 368 dPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLF 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 477 ATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 556
Cdd:COG5265 445 NDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 557 LDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTAGNEIE 632
Cdd:COG5265 525 LDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAE 600
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
129-625 |
1.11e-111 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 362.80 E-value: 1.11e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 129 VSFWCLA--AGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDD------------VSKINEGigdkigmffqamA 194
Cdd:PRK11176 84 ISSYCISwvSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREG------------A 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 195 TFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYN 274
Cdd:PRK11176 152 SIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 275 NNLEEAKRLGIKKAITANISMGAAFLLiyASYALAF-WYGTSL-VISKEYSIGQVlTVFFSVLIGAFSVGQASPNIEA-F 351
Cdd:PRK11176 232 KVSNRMRQQGMKMVSASSISDPIIQLI--ASLALAFvLYAASFpSVMDTLTAGTI-TVVFSSMIALMRPLKSLTNVNAqF 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 352 ANARGAAYEVFKIIDNKPSIDSfskSGHKPDNIQGNLEFKNIHFSYPSrKEVQILKGLNLKVKSGQTVALVGNSGCGKST 431
Cdd:PRK11176 309 QRGMAACQTLFAILDLEQEKDE---GKRVIERAKGDIEFRNVTFTYPG-KEVPALRNINFKIPAGKTVALVGRSGSGKST 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 432 TVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDV-TMDEIEKAVKEANAYDFIM 510
Cdd:PRK11176 385 IANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFIN 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 511 KLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRN 590
Cdd:PRK11176 465 KMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK 544
|
490 500 510
....*....|....*....|....*....|....*
gi 153791547 591 ADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 625
Cdd:PRK11176 545 ADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
388-621 |
5.05e-108 |
|
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: 339.59 E-value: 5.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:cd03251 1 VEFKNVTFRYPG-DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 547
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 548 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 621
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1031-1263 |
1.16e-106 |
|
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: 335.74 E-value: 1.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFDCSIAENIAYGDnsRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1190
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIY 1263
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
388-621 |
8.35e-104 |
|
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: 328.04 E-value: 8.35e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:cd03253 1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 547
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 548 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 621
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1006-1276 |
3.83e-103 |
|
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: 340.26 E-value: 3.83e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1006 RIIEKTPEI-DSYSTQGLKPNmlEGNVQFSGVVFNY-PTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY 1083
Cdd:COG5265 334 DLLDQPPEVaDAPDAPPLVVG--GGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1084 DPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYG--DNSRvvsyEEIVRAAKEANIHQFIDSLPDKY 1161
Cdd:COG5265 409 DVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGrpDASE----EEVEAAARAAQIHDFIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1162 NTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVV 1241
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
250 260 270
....*....|....*....|....*....|....*
gi 153791547 1242 IQNGKVKEHGTHQQLLAQKGIYFSMVSVQAGAKRS 1276
Cdd:COG5265 565 LEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
386-616 |
1.77e-100 |
|
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: 318.79 E-value: 1.77e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 386 GNLEFKNIHFSYpsRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI 465
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNP 545
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 546 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKG 616
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1031-1270 |
1.01e-99 |
|
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: 317.25 E-value: 1.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPtrPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFDCSIAENIAYGDNSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1190
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSVQ 1270
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
754-1272 |
3.87e-99 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 328.52 E-value: 3.87e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 754 LFLILGIISFITFFLQGFTFGKageiLTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIF 833
Cdd:PRK11176 74 LMILRGITSFISSYCISWVSGK----VVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALITVV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 834 QNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIA-GVVE-------------MKMLSG---QALKDKKELEGSGKIATEa 896
Cdd:PRK11176 148 REGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVVSkrfrnisknmqntMGQVTTsaeQMLKGHKEVLIFGGQEVE- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 897 IENFRTVVSLTREQKFETMYAQSLQIPyrnamkkahVFGITFSFtqAMMYFSYAACFRfgayLVTQQLmTFENVLLVFSA 976
Cdd:PRK11176 227 TKRFDKVSNRMRQQGMKMVSASSISDP---------IIQLIASL--ALAFVLYAASFP----SVMDTL-TAGTITVVFSS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 977 IvFGAM----AVGQVSSfapDYAKATVSASHIIRIIEKTPEIDsysTQGLKPNMLEGNVQFSGVVFNYPTRpSIPVLQGL 1052
Cdd:PRK11176 291 M-IALMrplkSLTNVNA---QFQRGMAACQTLFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDN 1132
Cdd:PRK11176 363 NFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYART 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1133 SRVvSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQE 1212
Cdd:PRK11176 443 EQY-SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQA 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1213 ALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSVQAG 1272
Cdd:PRK11176 522 ALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
289-625 |
9.81e-99 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 327.69 E-value: 9.81e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 289 ITANISMGAAFLLiyasyalafwyGTSLVISKEYSIGQVLTV--FFSVLIGAFSvgqaspNIEAFAN----ARGAAYEVF 362
Cdd:PRK13657 248 AASTITMLAILVL-----------GAALVQKGQLRVGEVVAFvgFATLLIGRLD------QVVAFINqvfmAAPKLEEFF 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 363 KIIDNKPSIDsfsKSGHKPD--NIQGNLEFKNIHFSYPSRKevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLY 440
Cdd:PRK13657 311 EVEDAVPDVR---DPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 441 DPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLV 520
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVV 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 521 GERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGG 600
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
330 340
....*....|....*....|....*
gi 153791547 601 VIVEQGNHDELMREKGIYFKLVMTQ 625
Cdd:PRK13657 546 RVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1029-1261 |
3.75e-97 |
|
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: 309.93 E-value: 3.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1029 GNVQFSGVVFNYptRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQ 1108
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1109 LGIVSQEPILFDCSIAENIAYGDNSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 1188
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1189 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKG 1261
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
135-616 |
1.15e-96 |
|
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: 320.94 E-value: 1.15e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 135 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVI 214
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 215 LAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRlgikkaitanIS 294
Cdd:COG4988 165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRK----------RT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 295 MGA---AFL-------LIYASYALAfwygtSLVISKEYSIGQV-LTVFFSVLIgafsvgqASPniEAF------------ 351
Cdd:COG4988 235 MKVlrvAFLssavlefFASLSIALV-----AVYIGFRLLGGSLtLFAALFVLL-------LAP--EFFlplrdlgsfyha 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 352 -ANARGAAYEVFKIIDnKPSIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKS 430
Cdd:COG4988 301 rANGIAAAEKIFALLD-APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKS 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 431 TTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIM 510
Cdd:COG4988 378 TLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVA 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 511 KLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRN 590
Cdd:COG4988 458 ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ 537
|
490 500
....*....|....*....|....*.
gi 153791547 591 ADVIAGFDGGVIVEQGNHDELMREKG 616
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1022-1247 |
1.45e-89 |
|
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: 288.99 E-value: 1.45e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1022 LKPNMLEGNVQFSGVVFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN 1101
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1102 VQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIA 1181
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1182 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKV 1247
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
695-1261 |
1.85e-89 |
|
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: 300.91 E-value: 1.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 695 RILKLNSTEWPYFVVGIFCAIINGGLQPAFSVIFSKVV-GVFTNGGPPETQRQnsnLFSLLFLILGIISFITFFLQGFTF 773
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLaGLIIGGAPLSALLP---LLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 774 gKAGEILTKRLRYMVFKSMLRQDVSWFDDPKntTGALTTRLAndaAQVKGATG--SR------LAVIfqniANLGTGIII 845
Cdd:COG4988 84 -RAAARVKRRLRRRLLEKLLALGPAWLRGKS--TGELATLLT---EGVEALDGyfARylpqlfLAAL----VPLLILVAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 846 SLIYgWQLTLLLLAIVPIIAIAgvveMkMLSGQALKDKKElegsgkiateaiENFRTVVSL------------------- 906
Cdd:COG4988 154 FPLD-WLSGLILLVTAPLIPLF----M-ILVGKGAAKASR------------RQWRALARLsghfldrlrglttlklfgr 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 907 TREQKfETMYAQSLQipYRNA-MKkahVFGITF--SFT-QAMMYFSYAAC-FRFGAYLVTQQlMTFENVLLVF--SAIVF 979
Cdd:COG4988 216 AKAEA-ERIAEASED--FRKRtMK---VLRVAFlsSAVlEFFASLSIALVaVYIGFRLLGGS-LTLFAALFVLllAPEFF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 980 gaMAVGQVSSFAPDYAKATVSASHIIRIIEKTPEIDSYSTQGLkPNMLEGNVQFSGVVFNYPTRPsiPVLQGLSLEVKKG 1059
Cdd:COG4988 289 --LPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPL-PAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1060 QTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVSYE 1139
Cdd:COG4988 364 ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1140 EIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE 1219
Cdd:COG4988 442 ELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK 521
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 153791547 1220 GRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKG 1261
Cdd:COG4988 522 GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
135-621 |
4.69e-89 |
|
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: 300.14 E-value: 4.69e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 135 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVskinegigDKIGMFF-QAMATFFGGFIIGFTrgwkLTLV 213
Cdd:COG4987 82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----AVAF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 214 ILAISPVLGLS-------AGIWAKILSSFTDKELHAYAKA--GAVAEEVLAAIR---TVIAFGGQKKELERYNNNLEEAK 281
Cdd:COG4987 150 LAFFSPALALVlalglllAGLLLPLLAARLGRRAGRRLAAarAALRARLTDLLQgaaELAAYGALDRALARLDAAEARLA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 282 RLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFFSVLiGAFSVgqASPNIEAFAN---ARGAA 358
Cdd:COG4987 230 AAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAL-ALFEA--LAPLPAAAQHlgrVRAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 359 YEVFKIIDNKPSIDSFSKSGHKPDniQGNLEFKNIHFSYPSRKEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQR 438
Cdd:COG4987 307 RRLNELLDAPPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 439 LYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDT 518
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 519 LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFD 598
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|...
gi 153791547 599 GGVIVEQGNHDELMREKGIYFKL 621
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQL 566
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
146-626 |
2.58e-86 |
|
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: 296.27 E-value: 2.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 146 KFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEGIGDK-----IGMFFqaMATFFGgfiIGFTRGWKLTLVILAISPV 220
Cdd:TIGR01846 217 RLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSaltvvLDLLF--VVVFLA---VMFFYSPTLTGVVIGSLVC 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 221 LGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFL 300
Cdd:TIGR01846 291 YALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 301 LIYASYALAFWYGTSLVISKEYSIGQVltVFFSVLIGAFS--VGQASPNIEAFANARGAAYEVFKIIdNKPSiDSFSKSG 378
Cdd:TIGR01846 371 IQKLTFAILLWFGAHLVIGGALSPGQL--VAFNMLAGRVTqpVLRLAQLWQDFQQTGIALERLGDIL-NSPT-EPRSAGL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 379 HKPDNIQGNLEFKNIHFSY-PSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI 457
Cdd:TIGR01846 447 AALPELRGAITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 458 NVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAI 537
Cdd:TIGR01846 525 DPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAI 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 538 ARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGI 617
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGL 684
|
....*....
gi 153791547 618 YFKLVMTQT 626
Cdd:TIGR01846 685 YARLWQQQS 693
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
46-371 |
5.01e-86 |
|
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: 282.80 E-value: 5.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 46 DRLYMLVGTLAAIIHGVALPLMMLIFGDMTDSFASVGNvsknstnmseadkramfAKLEEEMTTYAYYYTGIGAGVLIVA 125
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDD-----------------DELRSEANFWALMFLVLAIVAGIAY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 126 YIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFD--VHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIG 203
Cdd:cd18578 70 FLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 204 FTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRL 283
Cdd:cd18578 150 FVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 284 GIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFK 363
Cdd:cd18578 230 GLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFR 309
|
....*...
gi 153791547 364 IIDNKPSI 371
Cdd:cd18578 310 LLDRKPEI 317
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
388-625 |
1.34e-85 |
|
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: 278.22 E-value: 1.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:cd03252 1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 547
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 548 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 625
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
381-602 |
9.21e-85 |
|
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: 275.50 E-value: 9.21e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 381 PDNIQGNLEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVR 460
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 YLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARA 540
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 541 LVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVI 602
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
780-1268 |
3.30e-83 |
|
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: 283.58 E-value: 3.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 780 LTKRLRYMVFKSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGATgsrLAVIFQNIANLGTGIIISLIYGWQLTLLLLA 859
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLR--SGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 860 IVPIIAIAGVVeMKMLSGQALK--DKKELEGSGKIATEAIENFRTVVSLT---REQKFETMYAQSLQiPYRNAMKKAHVF 934
Cdd:COG4987 161 LALGLLLAGLL-LPLLAARLGRraGRRLAAARAALRARLTDLLQGAAELAaygALDRALARLDAAEA-RLAAAQRRLARL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 935 -GITFSFTQAMMYFSYAACFRFGAYLVTQQlmTFENVLLVfsAIVFGAMA----VGQVSSFAPDYAKATVSASHIIRIIE 1009
Cdd:COG4987 239 sALAQALLQLAAGLAVVAVLWLAAPLVAAG--ALSGPLLA--LLVLAALAlfeaLAPLPAAAQHLGRVRAAARRLNELLD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1010 KTPEIDSYSTQGLKPNmlEGNVQFSGVVFNYPTRPSiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS 1089
Cdd:COG4987 315 APPAVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1090 VFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKG 1169
Cdd:COG4987 392 ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGG 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1170 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKE 1249
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
490
....*....|....*....
gi 153791547 1250 HGTHQQLLAQKGIYFSMVS 1268
Cdd:COG4987 550 QGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
50-339 |
4.83e-83 |
|
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: 272.59 E-value: 4.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 50 MLVGTLAAIIHGVALPLMMLIFGDMTDSFASVGNVSKNSTNMseadkramfakleeemttYAYYYTGIGAGVLIVAYIQV 129
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNV------------------YSLALLLLGLAQFILSFLQS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 130 SFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWK 209
Cdd:pfam00664 63 YLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 210 LTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAI 289
Cdd:pfam00664 143 LTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 153791547 290 TANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQ--VLTVFFSVLIGAF 339
Cdd:pfam00664 223 ANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
833-1261 |
7.81e-82 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 280.31 E-value: 7.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 833 FQNIANLGTGIIISLIYGWQLTLLLLAIVPI-IAIAGVVEMKMLSGQALKDKKELEGSGKiATEAIENFRTVVSLTR-EQ 910
Cdd:PRK13657 138 LATLVALVVLLPLALFMNWRLSLVLVVLGIVyTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRiEA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 911 KFETM--YAQSL---QIPYRNAMkkAHVFGIT-FSFTQAMMyfsyaACFRFGAYLVTQQLMTfenVLLVFSAIVFGAMAV 984
Cdd:PRK13657 217 ETQALrdIADNLlaaQMPVLSWW--ALASVLNrAASTITML-----AILVLGAALVQKGQLR---VGEVVAFVGFATLLI 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 985 G---QVSSFAPDYAKATVSASHIIRIIEKTPEIDSysTQGLK-PNMLEGNVQFSGVVFNYPTRPsiPVLQGLSLEVKKGQ 1060
Cdd:PRK13657 287 GrldQVVAFINQVFMAAPKLEEFFEVEDAVPDVRD--PPGAIdLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQ 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1061 TLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSYEE 1140
Cdd:PRK13657 363 TVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1141 IVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREG 1220
Cdd:PRK13657 441 MRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKG 520
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 153791547 1221 RTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKG 1261
Cdd:PRK13657 521 RTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
707-1004 |
1.82e-81 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 269.34 E-value: 1.82e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGG----PPETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTK 782
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGsgesSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 783 RLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVP 862
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 863 IIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQ 942
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 943 AMMYFSYAACFRFGAYLVTQQLMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKATVSASHI 1004
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
388-600 |
5.53e-80 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 260.01 E-value: 5.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIrygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKI 547
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153791547 548 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGG 600
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1031-1270 |
7.52e-80 |
|
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: 262.42 E-value: 7.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYptRPSIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQL 1109
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1110 GIVSQEPILFDCSIAENIAYGDNSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 1189
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1190 PHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSV 1269
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 153791547 1270 Q 1270
Cdd:cd03252 237 Q 237
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
690-1263 |
4.55e-79 |
|
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: 276.05 E-value: 4.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 690 PASFWRILK--LNSTE--WPYFVVGIFCAIINGGLQPAFSVIFSKVVGVftnggppetQRQNSNLFSLLflilgIISFIT 765
Cdd:TIGR03796 138 KPSLLRALWrrLRGSRgaLLYLLLAGLLLVLPGLVIPAFSQIFVDEILV---------QGRQDWLRPLL-----LGMGLT 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 766 FFLQGFtfgkageiLTK-RLRYMV--------------FKSMLRQDVSWFDdpKNTTGALTTRLANdAAQVKGATGSRLA 830
Cdd:TIGR03796 204 ALLQGV--------LTWlQLYYLRrleiklavgmsarfLWHILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 831 VIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQ 910
Cdd:TIGR03796 273 TTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLES 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 911 ----KFETMYAQSLqipyrNAMKKAHVFGITFS-FTQAMMYFSYAACFRFGAYLVTQQLMT------FENVLLVFSAIVF 979
Cdd:TIGR03796 353 dffsRWAGYQAKLL-----NAQQELGVLTQILGvLPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVN 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 980 GAMAVGQ-VSSFAPDYAKATVSASHIIRIIEKTPEIDSYSTQglKPNMLEGNVQFSGVVFNY-PTRPsiPVLQGLSLEVK 1057
Cdd:TIGR03796 428 NLVGFGGtLQELEGDLNRLDDVLRNPVDPLLEEPEGSAATSE--PPRRLSGYVELRNITFGYsPLEP--PLIENFSLTLQ 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1058 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVS 1137
Cdd:TIGR03796 504 PGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IP 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1138 YEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdkA 1217
Cdd:TIGR03796 582 DADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--R 659
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 153791547 1218 REGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIY 1263
Cdd:TIGR03796 660 RRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1031-1246 |
4.02e-78 |
|
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: 254.62 E-value: 4.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPSiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFDCSIAENIaygdnsrvvsyeeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQP 1190
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGK 1246
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
191-624 |
1.08e-77 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 268.68 E-value: 1.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 191 QAMATFFGGFII---GFTRGWKLTLVILaispVLGLSAGIWAKILSSFTDK-----ELHAYAKAGAVAEEV--LAAIRTV 260
Cdd:TIGR01192 136 QHLATFVALFLLiptAFAMDWRLSIVLM----VLGILYILIAKLVMQRTKNgqaavEHHYHNVFKHVSDSIsnVSVVHSY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 261 IAFGGQKKELERYNNNLEEAK---------RLGIKKaITANISMGAAFLLiyasyalafwyGTSLVISKEYSIGQVLTV- 330
Cdd:TIGR01192 212 NRIEAETSALKQFTNNLLSAQypvldwwalASGLNR-MASTISMMCILVI-----------GTVLVIKGELSVGEVIAFi 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 331 -FFSVLIGAFSvgQASPNIEAFANARGAAYEVFKIIDNKPSIDSFSKSGHKPdNIQGNLEFKNIHFSYPSRKevQILKGL 409
Cdd:TIGR01192 280 gFANLLIGRLD--QMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELP-NVKGAVEFRHITFEFANSS--QGVFDV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 410 NLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRE 489
Cdd:TIGR01192 355 SFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGRE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 490 DVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAAL 569
Cdd:TIGR01192 435 GATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAI 514
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 570 DKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMT 624
Cdd:TIGR01192 515 DALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
792-1270 |
5.94e-76 |
|
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: 266.44 E-value: 5.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 792 MLRQDVSWFDdpKNTTGALTTRlANDAAQVK----GAT-GSRLAVIFqNIANLGtgiiISLIYGWQLTL--LLLAIVpII 864
Cdd:TIGR03797 219 LLRLPVSFFR--QYSTGDLASR-AMGISQIRrilsGSTlTTLLSGIF-ALLNLG----LMFYYSWKLALvaVALALV-AI 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 865 AIAGVVEMKMLSgqalKDKKELEGSGKIATEAIENFRTVVSLtR----EQKFETMYAQ--SLQIpyRNAMKKAHVFGITF 938
Cdd:TIGR03797 290 AVTLVLGLLQVR----KERRLLELSGKISGLTVQLINGISKL-RvagaENRAFARWAKlfSRQR--KLELSAQRIENLLT 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 939 SFTQAMMYFSYAACFRFGAYLVTQQLMTFeNVLLVFSAIvFGA--MAVGQVSSFAPDYAKATVSASHIIRIIEKTPEIDS 1016
Cdd:TIGR03797 363 VFNAVLPVLTSAALFAAAISLLGGAGLSL-GSFLAFNTA-FGSfsGAVTQLSNTLISILAVIPLWERAKPILEALPEVDE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1017 YSTQglkPNMLEGNVQFSGVVFNYptRPSIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGK 1095
Cdd:TIGR03797 441 AKTD---PGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1096 EIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsrVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGG 1175
Cdd:TIGR03797 516 DLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGG 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1176 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQ 1255
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDE 670
|
490
....*....|....*
gi 153791547 1256 LLAQKGIYFSMVSVQ 1270
Cdd:TIGR03797 671 LMAREGLFAQLARRQ 685
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
975-1272 |
1.24e-75 |
|
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: 265.84 E-value: 1.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 975 SAIVFGAMAVGQVSSF--------AP---------DYAKATVSASHIIRIIEKTPEIDSYSTQGLkPNmLEGNVQFSGVV 1037
Cdd:TIGR01846 385 HLVIGGALSPGQLVAFnmlagrvtQPvlrlaqlwqDFQQTGIALERLGDILNSPTEPRSAGLAAL-PE-LRGAITFENIR 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1038 FNY-PTRPsiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEP 1116
Cdd:TIGR01846 463 FRYaPDSP--EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQEN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 ILFDCSIAENIAYGDNSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1196
Cdd:TIGR01846 541 VLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1197 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSVQAG 1272
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
678-1244 |
2.09e-75 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 275.37 E-value: 2.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 678 LSTKEALDEDVPPASFWRIL-KLNSTEWPYFV--------------VGIFCAIINGGLQPAFSVIFSKVVGVFTNGgppe 742
Cdd:PTZ00265 18 LSIKDEVEKELNKKGTFELYkKIKTQKIPFFLpfkclpashrkllgVSFVCATISGGTLPFFVSVFGVIMKNMNLG---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 743 tQRQNSNLFSLLflILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDDpkNTTGALTTRLANDAAQVK 822
Cdd:PTZ00265 94 -ENVNDIIFSLV--LIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDN--NPGSKLTSDLDFYLEQVN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 823 GATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSgqaLKDKKEL---EGSGKIATEAIEN 899
Cdd:PTZ00265 169 AGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVK---INKKTSLlynNNTMSIIEEALVG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 900 FRTVVSLTRE----QKF---ETMYAQslQIPYRNAMKKAHVfGITFSFTQAmmyfSYAACFRFGAYLVTQQLMTFE---- 968
Cdd:PTZ00265 246 IRTVVSYCGEktilKKFnlsEKLYSK--YILKANFMESLHI-GMINGFILA----SYAFGFWYGTRIIISDLSNQQpnnd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 969 ----NVLLVFSAIVFGAMAVGQVSSFAPDYAKATVSASHIIRIIEKTPEIDSYSTQGLKPNMLEgnVQFSGVVFNYPTRP 1044
Cdd:PTZ00265 319 fhggSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKK--IQFKNVRFHYDTRK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1045 SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFL-DGKEIKQLNVQWLRAQLGIVSQEPILFDCSI 1123
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 AENIAY------------------------GDNSR-------------------------------VVSYEEIVRAAKEA 1148
Cdd:PTZ00265 477 KNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakcagdlndmsnttdsneliemrknyqTIKDSEVVDVSKKV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1149 NIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVI 1226
Cdd:PTZ00265 557 LIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIII 636
|
650
....*....|....*...
gi 153791547 1227 AHRLSTIQNADLIVVIQN 1244
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLSN 654
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
707-982 |
1.30e-73 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 246.02 E-value: 1.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETQRQNsnLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 786
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALN--VYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 787 MVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 866
Cdd:pfam00664 79 KLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 867 AGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMY 946
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 153791547 947 FSYAACFRFGAYLVTQQLMTFEN--VLLVFSAIVFGAM 982
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
391-1266 |
1.33e-69 |
|
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: 257.57 E-value: 1.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 391 KNIHFSYpSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGqdirtiNVRYlreiigvVS 470
Cdd:TIGR00957 640 HNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------SVAY-------VP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 471 QEPVLFATTIAENIRYGREdvTMDEIEKAVKEANAY--DFIMkLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 548
Cdd:TIGR00957 706 QQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 549 LLDEATSALDTEseaVVQAALDKA------REGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLV 622
Cdd:TIGR00957 783 LFDDPLSAVDAH---VGKHIFEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 623 MTQtAGNEIELGNE---------ACKSKDEIDNLDMSSKDSGSSLIRRRSTRKSICGphDQDRKLSTKEALDEDVPPASF 693
Cdd:TIGR00957 860 RTY-APDEQQGHLEdswtalvsgEGKEAKLIENGMLVTDVVGKQLQRQLSASSSDSG--DQSRHHGSSAELQKAEAKEET 936
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 694 WRILKLN---------STEWPYF-VVGIFC--AIINGGLQPAFSVIFSKV-VGVFTNGGPPETQRQNSNLFSLLFLILGI 760
Cdd:TIGR00957 937 WKLMEADkaqtgqvelSVYWDYMkAIGLFItfLSIFLFVCNHVSALASNYwLSLWTDDPMVNGTQNNTSLRLSVYGALGI 1016
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 761 ISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIAN-L 839
Cdd:TIGR00957 1017 LQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvI 1094
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 840 GTGIIISLIygwqlTLLLLAIVPIIAIAGVVEMKMLSGQAlKDKKELEgsgkiateaienfrtvvSLTREQKF----ETM 915
Cdd:TIGR00957 1095 GALIVILLA-----TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLE-----------------SVSRSPVYshfnETL 1151
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 916 YAQSLQIPYRNAMKKAHVFGITFSFTQAMmYFSYAACFRFGAYlvtqQLMTFENVLLVFSAIvfgaMAVGQVSSFAPDYA 995
Cdd:TIGR00957 1152 LGVSVIRAFEEQERFIHQSDLKVDENQKA-YYPSIVANRWLAV----RLECVGNCIVLFAAL----FAVISRHSLSAGLV 1222
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 996 KATVSAS--------HIIRI-------IEKTPEIDSYS-TQGLKPNMLE-----------GNVQFSGVVFNYptRPSIP- 1047
Cdd:TIGR00957 1223 GLSVSYSlqvtfylnWLVRMssemetnIVAVERLKEYSeTEKEAPWQIQetappsgwpprGRVEFRNYCLRY--REDLDl 1300
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENI 1127
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 aygDNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1207
Cdd:TIGR00957 1381 ---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1208 KVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSM 1266
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
386-606 |
7.59e-69 |
|
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: 230.55 E-value: 7.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 386 GNLEFKNIHFSYPSrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI 465
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNP 545
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 546 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 606
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1029-1247 |
1.18e-68 |
|
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: 229.78 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1029 GNVQFSGVVFNYPTRPsIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQ 1108
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1109 LGIVSQEPILFDCSIAENIAYGDnsRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 1188
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1189 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKV 1247
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
157-625 |
4.64e-67 |
|
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: 240.63 E-value: 4.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 157 GWFDVHDVGELNTRlTDDVSKINEGIGDKigMFFQAMATFFGGFIIG--FTRGWKLTLVILAISPVLGLSAGIWAKILss 234
Cdd:TIGR03797 225 SFFRQYSTGDLASR-AMGISQIRRILSGS--TLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVLGLLQ-- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 235 fTDKELHAYAKAGAVAEEVLAAIRTVIAF---GGQKKELERYNNNLEEAKRLGIKKAITANI--SMGAAFLLIyASYALa 309
Cdd:TIGR03797 300 -VRKERRLLELSGKISGLTVQLINGISKLrvaGAENRAFARWAKLFSRQRKLELSAQRIENLltVFNAVLPVL-TSAAL- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 310 FWYGTSLVISKEYSIGQVLTvfFSVLIGAF--SVGQASPNIEAfANARGAAYEVFK-IIDNKPSIDSfskSGHKPDNIQG 386
Cdd:TIGR03797 377 FAAAISLLGGAGLSLGSFLA--FNTAFGSFsgAVTQLSNTLIS-ILAVIPLWERAKpILEALPEVDE---AKTDPGKLSG 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 387 NLEFKNIHFSYpSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREII 466
Cdd:TIGR03797 451 AIEVDRVTFRY-RPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFATTIAENIrYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPK 546
Cdd:TIGR03797 530 GVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPR 608
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 547 ILLLDEATSALDTESEAVVQAALDKAREGRttIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 625
Cdd:TIGR03797 609 ILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
100-622 |
5.59e-66 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 245.71 E-value: 5.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 100 FAKLEEEMTTYAYYYTGIGAGVLIVAYIQvSFWCLAAGRQIHK-IRQKFFHAIMNQEIGWFD--VHDVGELNTRLTDDVS 176
Cdd:PTZ00265 858 FANLEANSNKYSLYILVIAIAMFISETLK-NYYNNVIGEKVEKtMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVH 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 177 KINEGIGDKIGMFFQAMATFFGGFIIGF----------TRGWKLTLVILAISPVLGLSAGIWAK-------ILSSFTDKE 239
Cdd:PTZ00265 937 LLKTGLVNNIVIFTHFIVLFLVSMVMSFyfcpivaavlTGTYFIFMRVFAIRARLTANKDVEKKeinqpgtVFAYNSDDE 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 240 LhaYAKAGAVAEEVLAAIRTVIAFGgqkkeLERYNNNLEEA----KRLGIKKAITAN-----ISMGAAFLLiyasYALAF 310
Cdd:PTZ00265 1017 I--FKDPSFLIQEAFYNMNTVIIYG-----LEDYFCNLIEKaidySNKGQKRKTLVNsmlwgFSQSAQLFI----NSFAY 1085
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 311 WYGTSLVISKEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFKIIDNKPSIDSFSKSGHKPDN---IQGN 387
Cdd:PTZ00265 1086 WFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGK 1165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLD----------------------- 444
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgd 1245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 445 -------------------------------GMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTM 493
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATR 1325
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 494 DEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAAL---- 569
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdik 1405
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 570 DKAreGRTTIVIAHRLSTVRNADVIAGFD-----GGVIVEQGNHDELMR-EKGIYFKLV 622
Cdd:PTZ00265 1406 DKA--DKTIITIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLSvQDGVYKKYV 1462
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
749-1259 |
1.60e-65 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 232.72 E-value: 1.60e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 749 NLFSLLFLILGIISFITF-----FLQGFTFGKAGEILTKRLRYMVFKSMLRQDVswfddpkNTTGALTTRLANDAAQVKG 823
Cdd:COG4618 55 SVDTLLMLTLLALGLYAVmglldAVRSRILVRVGARLDRRLGPRVFDAAFRAAL-------RGGGGAAAQALRDLDTLRQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 824 ATGSR--------------LAVIFqnianlgtgiIISLIYGWqltLLLLAIVPIIAIAGVVEMkmLSGQALKDKKELEG- 888
Cdd:COG4618 128 FLTGPglfalfdlpwapifLAVLF----------LFHPLLGL---LALVGALVLVALALLNER--LTRKPLKEANEAAIr 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 889 SGKIATEAIENFRTVVSL-------TREQKfETMYAQSLQIpyrNAMKKAHVFG-ITFSFTQAMMYFSYAAcfrfGAYLV 960
Cdd:COG4618 193 ANAFAEAALRNAEVIEAMgmlpalrRRWQR-ANARALALQA---RASDRAGGFSaLSKFLRLLLQSAVLGL----GAYLV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 961 TQQLMTFenvllvfSAIVFGAMAVGQVssFAP-DYA----KATVSA----SHIIRIIEKTPEiDSYSTQGLKPnmlEGNV 1031
Cdd:COG4618 265 IQGEITP-------GAMIAASILMGRA--LAPiEQAiggwKQFVSArqayRRLNELLAAVPA-EPERMPLPRP---KGRL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYPTRPSiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGI 1111
Cdd:COG4618 332 SVENLTVVPPGSKR-PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQEPILFDCSIAENIA-YGDnsrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1190
Cdd:COG4618 411 LPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDP 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
350-594 |
1.40e-64 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 229.10 E-value: 1.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 350 AFANARGAAYEVFKIIDNKPSIDSFSKSGHKPDNIQgnLEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGK 429
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 430 STTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFI 509
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 510 MKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVR 589
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
....*
gi 153791547 590 NADVI 594
Cdd:TIGR02857 522 LADRI 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
386-607 |
1.90e-64 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 217.75 E-value: 1.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 386 GNLEFKNIHFSYPSRKEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI 465
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFATTIAENI----RYgredvTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARAL 541
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 542 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 607
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
388-1267 |
6.86e-63 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 236.03 E-value: 6.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDgMVSIDgqdirtinvryLREIIG 467
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV-----------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIRYGrEDVTMDEIEKAVKeanaydfIMKLPHQFD-------TLVGERGAQLSGGQKQRIAIARA 540
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFG-SDFESERYWRAID-------VTALQHDLDllpgrdlTEIGERGVNISGGQKQRVSMARA 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 541 LVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREkGIYF 619
Cdd:PLN03232 755 VYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-GSLF 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 620 KLVMtQTAGnEIELGNEACKSKDEIDNL------DMSSKDSGSSLIRRRstRKSIcgphdqdrkLSTKEALDEDVppASF 693
Cdd:PLN03232 834 KKLM-ENAG-KMDATQEVNTNDENILKLgptvtiDVSERNLGSTKQGKR--GRSV---------LVKQEERETGI--ISW 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 694 WRILKLNSTEWPYFVVGIF--CAIinggLQPAFSVIFSKVVGVFTNGGPPETQRqnSNLFSLLFLILGIISFITFFLQGF 771
Cdd:PLN03232 899 NVLMRYNKAVGGLWVVMILlvCYL----TTEVLRVSSSTWLSIWTDQSTPKSYS--PGFYIVVYALLGFGQVAVTFTNSF 972
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 772 TFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKgatgsrlavifQNIANLGTGIIISLiygW 851
Cdd:PLN03232 973 WLISSSLHAAKRLHDAMLNSILRAPMLFFH--TNPTGRVINRFSKDIGDID-----------RNVANLMNMFMNQL---W 1036
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 852 QL--TLLLLAIVPIIAIAGVVEMKMLSGQAL-------KDKKELEGSGKIAT-----EAIENFRTVVSLTREQKFETMYA 917
Cdd:PLN03232 1037 QLlsTFALIGTVSTISLWAIMPLLILFYAAYlyyqstsREVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMAKING 1116
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 918 QSL--QIPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFENV---LLVFSAIVFGAMA-VGQVSSFA 991
Cdd:PLN03232 1117 KSMdnNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTmglLLSYTLNITTLLSgVLRQASKA 1196
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 992 PDYAKATVSASHIIRIIEKTPEIDSySTQGLKPNMLEGNVQFSGVVFNYptRPSIP-VLQGLSLEVKKGQTLALVGSSGC 1070
Cdd:PLN03232 1197 ENSLNSVERVGNYIDLPSEATAIIE-NNRPVSGWPSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGA 1273
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1071 GKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENI-AYGDNSRVVSYEEIVRAakeaN 1149
Cdd:PLN03232 1274 GKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDADLWEALERA----H 1349
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1150 IHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHR 1229
Cdd:PLN03232 1350 IKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHR 1429
|
890 900 910
....*....|....*....|....*....|....*....
gi 153791547 1230 LSTIQNADLIVVIQNGKVKEHGTHQQLLAQKG-IYFSMV 1267
Cdd:PLN03232 1430 LNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMV 1468
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
986-1242 |
1.53e-62 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 223.32 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 986 QVSSFAPDYAKATVSASHIIRIIEKTPEIDSYSTQGLKPNMLEgnVQFSGVVFNYPTRPsiPVLQGLSLEVKKGQTLALV 1065
Cdd:TIGR02857 279 QLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALV 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1066 GSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVSYEEIVRAA 1145
Cdd:TIGR02857 355 GPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREAL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1146 KEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV 1225
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
|
250
....*....|....*..
gi 153791547 1226 IAHRLSTIQNADLIVVI 1242
Cdd:TIGR02857 513 VTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1029-1252 |
1.81e-62 |
|
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: 212.35 E-value: 1.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1029 GNVQFSGVVFNYptRP-SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA 1107
Cdd:cd03244 1 GDIEFKNVSLRY--RPnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEPILFDCSIAENIA----YGDnsrvvsyEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIA 1183
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpfgeYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1184 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGT 1252
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
755-1270 |
2.19e-62 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 224.60 E-value: 2.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 755 FLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQ 834
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD--TQPVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 835 NIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAgvvemkMLSGQalkdkkelegsgKIATEAIENFRTVVSLTREQKFET 914
Cdd:PRK10790 149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVV------MVIYQ------------RYSTPIVRRVRAYLADINDGFNEV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 915 MYAQSLQIPYRNAMKkahvFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFE-----NVLLVFSAIVFGAMAVGQVSS 989
Cdd:PRK10790 211 INGMSVIQQFRQQAR----FGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSalilcGLLMLFGFSASGTIEVGVLYA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 990 FApDY------------------AKATVSASHIIRIIEKTPEIDSYSTQGLKpnmlEGNVQFSGVVFNYptRPSIPVLQG 1051
Cdd:PRK10790 287 FI-SYlgrlneplielttqqsmlQQAVVAGERVFELMDGPRQQYGNDDRPLQ----SGRIDIDNVSFAY--RDDNLVLQN 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1052 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGd 1131
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1132 nsRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQ 1211
Cdd:PRK10790 439 --RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1212 EALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSVQ 1270
Cdd:PRK10790 517 QALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
104-618 |
3.60e-62 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 223.05 E-value: 3.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 104 EEEMTTYA-YYYTGIGAGVLIVAYIQVSFWCL----AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKI 178
Cdd:PRK10789 27 EQHMTTGQiLMWIGTMVLIAVVVYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 179 NEGIGDKIGMFFQAMATFFGGFIIGFTR-GWKLTLVILAISPVLGLsagiwakILSSFTDKELHAYAKAGAV-------A 250
Cdd:PRK10789 107 VFAAGEGVLTLVDSLVMGCAVLIVMSTQiSWQLTLLALLPMPVMAI-------MIKRYGDQLHERFKLAQAAfsslndrT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 251 EEVLAAIRTVIAFGgqkkeLERYNNNL--EEAKRLGIKKAITANISM---GAAFLLIYASYALAFWYGTSLVISKEYSIG 325
Cdd:PRK10789 180 QESLTSIRMIKAFG-----LEDRQSALfaADAEDTGKKNMRVARIDArfdPTIYIAIGMANLLAIGGGSWMVVNGSLTLG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 326 QvLTVFFSVLigafsvGQASPNIEAFA---N--ARG-AAY-EVFKIIDNKPSIdsfsKSGHKP-DNIQGNLEFKNIHFSY 397
Cdd:PRK10789 255 Q-LTSFVMYL------GLMIWPMLALAwmfNivERGsAAYsRIRAMLAEAPVV----KDGSEPvPEGRGELDVNIRQFTY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 398 PsRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFA 477
Cdd:PRK10789 324 P-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 TTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 557
Cdd:PRK10789 403 DTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 558 DTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIY 618
Cdd:PRK10789 483 DGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
977-1266 |
5.42e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 222.78 E-value: 5.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 977 IVFGAMA--------------VGQVSSfapdyakatvSASHIIRIIEKTPEIDSYSTQGLKPNmlEGNVQFSGVVFNYPT 1042
Cdd:PRK11160 283 FVFAALAafealmpvagafqhLGQVIA----------SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1043 RPSiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCS 1122
Cdd:PRK11160 351 QPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSAT 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 IAENIAYgdnsrvvsyeeivrAAKEANIHQFIDSL-----------PDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPH 1191
Cdd:PRK11160 430 LRDNLLL--------------AAPNASDEALIEVLqqvgleklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAP 495
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1192 ILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSM 1266
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
730-1270 |
9.84e-61 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 219.20 E-value: 9.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 730 KVVGVFTNGgppETQRQNSNLFSLLFL-ILGIISFITFFLQGF----TFGkAGEILTKRLRYMVFKSMLRQDVSWFddPK 804
Cdd:PRK10789 16 KVVGIIVDG---VTEQHMTTGQILMWIgTMVLIAVVVYLLRYVwrvlLFG-ASYQLAVELREDFYRQLSRQHPEFY--LR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 805 NTTGALTTRLANDAAQVKGATGSR-LAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIA-----GVVEMKMLSGQ 878
Cdd:PRK10789 90 HRTGDLMARATNDVDRVVFAAGEGvLTLVDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMikrygDQLHERFKLAQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 879 A----LKDKkelegsgkiATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHV---FGITFSFTQAMmyfSYAA 951
Cdd:PRK10789 170 AafssLNDR---------TQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIdarFDPTIYIAIGM---ANLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 952 CFRFGAYLVTQqlmtfenvllvfsaivfGAMAVGQVSSFA--------PDYAKATV-------SA--SHIIRIIEKTPEI 1014
Cdd:PRK10789 238 AIGGGSWMVVN-----------------GSLTLGQLTSFVmylglmiwPMLALAWMfnivergSAaySRIRAMLAEAPVV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1015 DSystqGLKPNMLE-GNVQFSGVVFNYPTRpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLD 1093
Cdd:PRK10789 301 KD----GSEPVPEGrGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1094 GKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLS 1173
Cdd:PRK10789 376 DIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD--ATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1174 GGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTH 1253
Cdd:PRK10789 454 GGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNH 533
|
570
....*....|....*..
gi 153791547 1254 QQLLAQKGIYFSMVSVQ 1270
Cdd:PRK10789 534 DQLAQQSGWYRDMYRYQ 550
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
385-614 |
1.31e-60 |
|
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: 218.46 E-value: 1.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 385 QGNLEFKNIHFSYPSRKEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLRE 464
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 IIGVVSQEPVLFATTIAENI-RYGreDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVR 543
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 544 NPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
123-622 |
1.13e-59 |
|
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: 219.23 E-value: 1.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 123 IVAYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQAMATFFG-GFI 201
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILVIvGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 202 IGFtRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQ----KKELERYNNNL 277
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEaerySKIDSEFGDYL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 278 EEAKRLGIKKAITANISMGAAFLLIyasyALAFWYGTSLVISKEYSIGQVLTvfFSVLIGAF-----SVGQASPNIEAFA 352
Cdd:TIGR01193 369 NKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLIT--FNALLSYFltpleNIINLQPKLQAAR 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 353 NARGAAYEVFKIidnkPSIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKEvqILKGLNLKVKSGQTVALVGNSGCGKSTT 432
Cdd:TIGR01193 443 VANNRLNEVYLV----DSEFINKKKRTELNNLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGKSTL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 433 VQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG-REDVTMDEIEKAVKEANAYDFIMK 511
Cdd:TIGR01193 517 AKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIEN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 512 LPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREgRTTIVIAHRLSTVRNA 591
Cdd:TIGR01193 597 MPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS 675
|
490 500 510
....*....|....*....|....*....|.
gi 153791547 592 DVIAGFDGGVIVEQGNHDELMREKGIYFKLV 622
Cdd:TIGR01193 676 DKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
214-585 |
1.33e-58 |
|
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: 211.84 E-value: 1.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 214 ILAISPVLGLSAGIWAKILSSFTdKELHAYAKAGAVAEEVLAAIR---TVIAFGGQKKELERYNNNLEEAKRLGIKKAIT 290
Cdd:TIGR02868 158 ILAAGLLLAGFVAPLVSLRAARA-AEQALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 291 ANISMGAAFLLIYASYALAFWYGTSLVISKEYSiGQVLTVFFSVLIGAFSVGQASPN-IEAFANARGAAYEVFKIIDNKP 369
Cdd:TIGR02868 237 TALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLAAFEAFAALPAaAQQLTRVRAAAERIVEVLDAAG 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 370 SIDSFSKSGHKPDNIQG-NLEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVS 448
Cdd:TIGR02868 316 PVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 449 IDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLS 528
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLS 473
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 529 GGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 585
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
391-1267 |
5.14e-58 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 220.76 E-value: 5.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 391 KNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPL-DGMVSIDGqdirtiNVRYlreiigvV 469
Cdd:PLN03130 618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsDASVVIRG------TVAY-------V 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 470 SQEPVLFATTIAENIRYGREdVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 549
Cdd:PLN03130 685 PQVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 550 LDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREkGIYFKLVMtQTAG 628
Cdd:PLN03130 764 FDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN-GPLFQKLM-ENAG 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 629 NEIELGNEACKSKDEIDNLDMSSKDSGSSLIRRRSTRKSicgPHDQDRKLSTKEALDEDVPPasfWRIL-KLNSTEWPYF 707
Cdd:PLN03130 842 KMEEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKK---SKEGKSVLIKQEERETGVVS---WKVLeRYKNALGGAW 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 708 VVGI--FCAIinggLQPAFSVIFSKVVGVFTNGGPPETQRqnSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLR 785
Cdd:PLN03130 916 VVMIlfLCYV----LTEVFRVSSSTWLSEWTDQGTPKTHG--PLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLH 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 786 YMVFKSMLRQDVSWFDdpKNTTGALTTRLANDaaqvkgatgsrLAVIFQNIANLGTGIIISLiygWQL--TLLLLAIVPI 863
Cdd:PLN03130 990 DAMLGSILRAPMSFFH--TNPLGRIINRFAKD-----------LGDIDRNVAVFVNMFLGQI---FQLlsTFVLIGIVST 1053
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 864 IAIAGVVEMKML----------SGQALKDKKELEGSGKIAT--EAIENFRTVVSLTREQKFETMYAQSLQIPYRNA---M 928
Cdd:PLN03130 1054 ISLWAIMPLLVLfygaylyyqsTAREVKRLDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTlvnM 1133
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 929 KKAHVFGITFSFTQAMMYFSYA--ACFRFGAYLVTQQLMTFENVLLVFSAIVFGAM-AVGQVSSFAPDYAKATVSASHII 1005
Cdd:PLN03130 1134 SSNRWLAIRLETLGGLMIWLTAsfAVMQNGRAENQAAFASTMGLLLSYALNITSLLtAVLRLASLAENSLNAVERVGTYI 1213
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1006 RI-IEKTPEIDSYSTQGLKPNmlEGNVQFSGVVFNYptRPSIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY 1083
Cdd:PLN03130 1214 DLpSEAPLVIENNRPPPGWPS--SGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIV 1289
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1084 DPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENI-AYGDNSRVVSYEEIVRaakeANIHQFIDSLPDKYN 1162
Cdd:PLN03130 1290 ELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdPFNEHNDADLWESLER----AHLKDVIRRNSLGLD 1365
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1163 TRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKarEGRTC--IVIAHRLSTIQNADLIV 1240
Cdd:PLN03130 1366 AEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRIL 1443
|
890 900
....*....|....*....|....*...
gi 153791547 1241 VIQNGKVKEHGTHQQLLAQKGIYFS-MV 1267
Cdd:PLN03130 1444 VLDAGRVVEFDTPENLLSNEGSAFSkMV 1471
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
357-621 |
4.98e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.14 E-value: 4.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 357 AAYEVFKIIDNKPSIdSFSKSgHKPDNIQGNLEFKNIHFSYPSRkEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLM 436
Cdd:PRK11160 310 SARRINEITEQKPEV-TFPTT-STAAADQVSLTLNNVSFTYPDQ-PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 437 QRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTmDEIEKAVKEANAYDFIMKLPHQF 516
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 517 DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAG 596
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260
....*....|....*....|....*
gi 153791547 597 FDGGVIVEQGNHDELMREKGIYFKL 621
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
711-1269 |
1.14e-55 |
|
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: 207.28 E-value: 1.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 711 IFCAIINGGLQPAFSVIFSKVVGVFTnggpPETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFK 790
Cdd:TIGR01193 162 VIAAIIVTLISIAGSYYLQKIIDTYI----PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 791 SMLRQDVSWFDDPKntTGALTTRLAnDAAQVKGATGSRLAVIFQNIANLgtgIIISLIYGWQ---LTLLLLAIVPIIAIA 867
Cdd:TIGR01193 238 HLFELPMSFFSTRR--TGEIVSRFT-DASSIIDALASTILSLFLDMWIL---VIVGLFLVRQnmlLFLLSLLSIPVYAVI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 868 GVVEMKMLSGQalkDKKELEGSGKIATEAIENF---RTVVSLTREQ--------KFETMYAQSLQIPYRNAMKKAHVFGI 936
Cdd:TIGR01193 312 IILFKRTFNKL---NHDAMQANAVLNSSIIEDLngiETIKSLTSEAeryskidsEFGDYLNKSFKYQKADQGQQAIKAVT 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 937 TFSFTQAMMYFsyaacfrfGAYLVTQQLMTFENvLLVFSAIV-FGAMAVGQVSSFAPDYAKATVSASHIIRIIEKTPEId 1015
Cdd:TIGR01193 389 KLILNVVILWT--------GAYLVMRGKLTLGQ-LITFNALLsYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEF- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1016 SYSTQGLKPNMLEGNVQFSGVVFNYPTrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGK 1095
Cdd:TIGR01193 459 INKKKRTELNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1096 EIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGdNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGG 1175
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGG 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1176 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQ 1255
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
570
....*....|....
gi 153791547 1256 LLAQKGIYFSMVSV 1269
Cdd:TIGR01193 695 LLDRNGFYASLIHN 708
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
116-632 |
1.02e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 201.87 E-value: 1.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 116 GIGAGvLIVAYIQVSFwcLAAGRQ--------------IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEG 181
Cdd:PRK10790 62 GLVAG-LAAAYVGLQL--LAAGLHyaqsllfnraavgvVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 182 IGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKiLSSFTDKELHAY-AKAGAVAEEVLAAIrTV 260
Cdd:PRK10790 139 YVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQR-YSTPIVRRVRAYlADINDGFNEVINGM-SV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 261 IAfggQKKELERYNNNLEEAKRLGIKKAITA----------NISMGAAFLLIyasyALAFWYGtslvISKEYSIG-QVLT 329
Cdd:PRK10790 217 IQ---QFRQQARFGERMGEASRSHYMARMQTlrldgfllrpLLSLFSALILC----GLLMLFG----FSASGTIEvGVLY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 330 VFFSVLiGAFSvgqaSPNIE------AFANARGAAYEVFKIIDNkpsidsfSKSGHKPDNI---QGNLEFKNIHFSYpsR 400
Cdd:PRK10790 286 AFISYL-GRLN----EPLIElttqqsMLQQAVVAGERVFELMDG-------PRQQYGNDDRplqSGRIDIDNVSFAY--R 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 401 KEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTI 480
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 481 AENIRYGReDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 560
Cdd:PRK10790 432 LANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 561 SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTAGNEIE 632
Cdd:PRK10790 511 TEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELA 582
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
350-618 |
2.69e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 197.37 E-value: 2.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 350 AFANARGAAYEVFKIIDnkpSIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGK 429
Cdd:PRK11174 313 AKAQAVGAAESLVTFLE---TPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 430 STtvqLMQRL--YDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYD 507
Cdd:PRK11174 390 TS---LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 508 FIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLST 587
Cdd:PRK11174 467 FLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
250 260 270
....*....|....*....|....*....|.
gi 153791547 588 VRNADVIAGFDGGVIVEQGNHDELMREKGIY 618
Cdd:PRK11174 547 LAQWDQIWVMQDGQIVQQGDYAELSQAGGLF 577
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1052-1266 |
1.47e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 195.45 E-value: 1.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1052 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGD 1131
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1132 NSrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQ 1211
Cdd:PRK11174 448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1212 EALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSM 1266
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1028-1259 |
6.13e-52 |
|
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: 192.56 E-value: 6.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1028 EGNVQFSGVVFnYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA 1107
Cdd:TIGR01842 314 EGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEPILFDCSIAENIA-YGDNsrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARAL 1186
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARAL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1187 VRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
313-614 |
1.08e-50 |
|
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: 188.71 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 313 GTSLVISKEYSIGQVLTVffSVLIG-AFS-VGQASPNIEAFANARGAAYEVFKIIDNKPSIDSfsksgHKP-DNIQGNLE 389
Cdd:TIGR01842 246 GAYLAIDGEITPGMMIAG--SILVGrALApIDGAIGGWKQFSGARQAYKRLNELLANYPSRDP-----AMPlPEPEGHLS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 390 FKNIHFSYPSRKEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVV 469
Cdd:TIGR01842 319 VENVTIVPPGGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 470 SQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 549
Cdd:TIGR01842 398 PQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVV 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 550 LDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
388-613 |
1.42e-50 |
|
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: 187.80 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI 465
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 ---IGVVSQEPV--LFAT-TIAENIRYG---REDVTMDEIEKAVKEANA-----YDFIMKLPHQFdtlvgergaqlSGGQ 531
Cdd:COG1123 341 rrrVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAERRERVAELLErvglpPDLADRYPHEL-----------SGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 532 KQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVE 604
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
....*....
gi 153791547 605 QGNHDELMR 613
Cdd:COG1123 486 DGPTEEVFA 494
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
388-615 |
1.86e-50 |
|
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: 178.29 E-value: 1.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPV--LFATTIAENIRYGRE--DVTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIAR 539
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPEnlGLPREEIRERVEEAlelvGLEHLADRPPHE-----------LSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 615
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
389-600 |
5.20e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 173.42 E-value: 5.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 389 EFKNIHFSYPSRKEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGV 468
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 469 VSQEP--VLFATTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 544
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGG 600
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
388-611 |
9.44e-49 |
|
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: 173.14 E-value: 9.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLDGMVSIDGQDIRTINVR-- 460
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 YLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDEI-EKAVKEANAYDFIMKLPHqfdtlvgerGAQLSGGQKQ 533
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKAALWDEVKDRLH---------ALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 534 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 611
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
388-602 |
3.23e-48 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 169.70 E-value: 3.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIrygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKI 547
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 548 LLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDGGVI 602
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1031-1260 |
7.17e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 170.59 E-value: 7.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPtrPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPI--LFDCSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 1184
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1185 ALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGTHQQLLAQK 1260
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
53-361 |
1.64e-47 |
|
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: 171.97 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 53 GTLAAIIHGVALPLMMLIFGDMTDsfasvgnvsknstNMSEADKRAMFAKLeeemttyAYYYTGIGAGVLIVAYIQVSFW 132
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLID-------------TIIKGGDLDVLNEL-------ALILLAIYLLQSVFTFVRYYLF 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 133 CLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTL 212
Cdd:cd18557 61 NIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 213 VILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITAN 292
Cdd:cd18557 141 VLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANA 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 293 ISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLT-VFFSVLIgAFSVGQASPNIEAFANARGAAYEV 361
Cdd:cd18557 221 LFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILYTIMV-ASSVGGLSSLLADIMKALGASERV 289
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1031-1259 |
2.91e-47 |
|
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: 177.79 E-value: 2.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPS--IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWL 1105
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1106 RAQLGIVSQEPIL-FDC--SIAENIAYG-DNSRVVSYEEIVRAAKEAnIHQ------FIDSLPDkyntrvgdkgtQLSGG 1175
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-LERvglppdLADRYPH-----------ELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1176 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGT 1252
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
....*..
gi 153791547 1253 HQQLLAQ 1259
Cdd:COG1123 489 TEEVFAN 495
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1031-1256 |
2.98e-47 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 168.90 E-value: 2.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEI--KQLNVQ 1103
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1104 WLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVS----YEEIVRAA-KEANihqfidsLPDKYNTRVgdKGTQLSGGQKQ 1178
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKlkeeLDERVEEAlRKAA-------LWDEVKDRL--HALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1179 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQL 1256
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1032-1247 |
3.36e-47 |
|
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: 166.62 E-value: 3.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYP-TRPsiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:cd03246 2 EVENVSFRYPgAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFDCSIAENIaygdnsrvvsyeeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQP 1190
Cdd:cd03246 80 YLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIQNGKV 1247
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1047-1247 |
4.32e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 167.69 E-value: 4.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAEN 1126
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYGDNSRVVSY-EEIVRAAkeanIHQFidSLPDKY-NTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1204
Cdd:COG4619 94 LPFPFQLRERKFdRERALEL----LERL--GLPPDIlDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153791547 1205 ESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:COG4619 164 ENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
388-606 |
8.92e-47 |
|
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: 167.68 E-value: 8.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI- 465
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 --IGVVSQEPVL-------FATTIAENIRYGREDVTMDEIEKAVKEA-----NAYDFIMKLPHQfdtlvgergaqLSGGQ 531
Cdd:cd03257 82 keIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPHE-----------LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 532 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 606
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
53-344 |
7.50e-46 |
|
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: 167.43 E-value: 7.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 53 GTLAAIIHGVALPLMMLIFGDMTDSfasvgnVSKNSTNMSEADKRAMfakleeemTTYAYYYTGIGAGVLIVAYIQVSFW 132
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDA------VTNHSGSGGEEALRAL--------NQAVLILLGVVLIGSIATFLRSWLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 133 CLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTL 212
Cdd:cd18780 67 TLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 213 VILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITAN 292
Cdd:cd18780 147 VMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASG 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 153791547 293 ISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVFfsvLIGAFSVGQA 344
Cdd:cd18780 227 GFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGL-LTSF---LLYTLTVAMS 274
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
388-583 |
2.59e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 162.68 E-value: 2.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENI----RYGREDVTMDEIEKAVKEANaydfimkLPHQF-DTLVGErgaqLSGGQKQRIAIARALV 542
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153791547 543 RNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 583
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
406-555 |
6.11e-45 |
|
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: 159.35 E-value: 6.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLF-ATTIAENI 484
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 485 RYGREdvtMDEIEKAVKEANAYDFI--MKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 555
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1032-1246 |
7.37e-45 |
|
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: 161.48 E-value: 7.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYPTRPSiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGI 1111
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQEP--ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLPDKyNTRvgdkgtQLSGGQKQRIAIARALVRQ 1189
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDR-SPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1190 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGK 1246
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1033-1230 |
8.19e-45 |
|
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: 171.00 E-value: 8.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1033 FSGVVFNYPTRPsiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIV 1112
Cdd:TIGR02868 337 LRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1113 SQEPILFDCSIAEN--IAYGDnsrvVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1190
Cdd:TIGR02868 415 AQDAHLFDTTVRENlrLARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRL 1230
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
388-606 |
1.48e-44 |
|
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: 159.40 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINvRYLREIIG 467
Cdd:cd03247 1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIrygredvtmdeiekavkeanaydfimklphqfdtlvgerGAQLSGGQKQRIAIARALVRNPKI 547
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 548 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 606
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1031-1251 |
1.71e-44 |
|
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: 159.02 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPSiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAQLG 1110
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFDCSIAENIaygdnsrvvsyeeivraakeanihqfidslpdkyntrvgdkGTQLSGGQKQRIAIARALVRQP 1190
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHG 1251
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
388-611 |
3.29e-44 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 160.44 E-value: 3.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSR-KEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI- 465
Cdd:cd03258 2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 --IGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKE----------ANAYdfimklPhqfdtlvgergAQLSGG 530
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVLEllelvgledkADAY------P-----------AQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 531 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQGN 607
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETtQSILALLRDINRELGLTIVlITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....
gi 153791547 608 HDEL 611
Cdd:cd03258 225 VEEV 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
386-606 |
4.88e-44 |
|
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: 158.73 E-value: 4.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 386 GNLEFKNIHFSYPSRKEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI 465
Cdd:cd03369 5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFATTIAENI-RYGREDvtMDEIEKAVKeanaydfimklphqfdtlVGERGAQLSGGQKQRIAIARALVRN 544
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 606
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
388-613 |
5.57e-44 |
|
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: 160.35 E-value: 5.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSR-KEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREII 466
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEP---------VlfATTIAENIRYGREDVTMDEIEKAVKEAN-AYDFIMKLPHQfdtlvgergaqLSGGQKQRIA 536
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPHQ-----------LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 537 IARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHD 609
Cdd:COG1124 149 IARALILEPELLLLDEPTSALD----VSVQAEiLNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224
|
....
gi 153791547 610 ELMR 613
Cdd:COG1124 225 DLLA 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1029-1252 |
5.92e-44 |
|
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: 158.73 E-value: 5.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1029 GNVQFSGVVFNYptRPSIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA 1107
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEPILFDCSIAENIaygDNSRVVSYEEIVRAakeanihqfidslpdkynTRVGDKGTQLSGGQKQRIAIARALV 1187
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1188 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGT 1252
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
388-607 |
7.86e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 162.94 E-value: 7.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI- 465
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 --IGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKE----------ANAYdfimklPhqfdtlvgergAQLSGG 530
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKRVAEllelvglsdkADAY------P-----------SQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 531 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGN 607
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
388-613 |
1.44e-43 |
|
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: 167.00 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP---LDGMVSIDGQDIRTINVRYLRE 464
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 IIGVVSQEP--VLFATTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDtlvgERGAQLSGGQKQRIAIARA 540
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVLELLE---AVGLERRLD----RYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 541 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMR 613
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
388-611 |
2.43e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 157.85 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI--RTINVRYLREI 465
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFA-TTIAENIRYGREDVT-MDEiEKAVKEANAY-------DFIMKLPHQfdtlvgergaqLSGGQKQRIA 536
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPIKVKkMSK-AEAEERAMELlervglaDKADAYPAQ-----------LSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 537 IARALVRNPKILLLDEATSALDTE--SEaVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPElvGE-VLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
388-613 |
4.12e-43 |
|
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: 157.45 E-value: 4.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-- 465
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 -IGVVSQEPVLF-ATTIAENIRYG-RE--DVTMDEIEKAVkeanaydfIMKLphqfdTLVGERGA------QLSGGQKQR 534
Cdd:COG1127 83 rIGMLFQGGALFdSLTVFENVAFPlREhtDLSEAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 535 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 153791547 612 MR 613
Cdd:COG1127 230 LA 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1040-1251 |
4.53e-43 |
|
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: 156.90 E-value: 4.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1040 YPTRP-SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---RAQLGIVSQE 1115
Cdd:cd03257 11 FPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1116 PI-----LFdcSIAENIA-----YGDNSRvvsYEEIVRAAKEANIH-----QFIDSLPDkyntrvgdkgtQLSGGQKQRI 1180
Cdd:cd03257 91 PMsslnpRM--TIGEQIAeplriHGKLSK---KEARKEAVLLLLVGvglpeEVLNRYPH-----------ELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1181 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
50-361 |
6.51e-43 |
|
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: 158.87 E-value: 6.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 50 MLVGTLAAIIHGVALPLMMLIFGDMTDSFASVGNVSKnstnmseadkramfakleeeMTTYAYYYTGIGAGVLIVAYIQV 129
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL--------------------LLWIALLLLLLALLRALLSYLRR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 130 SFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWK 209
Cdd:cd07346 61 YLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 210 LTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAI 289
Cdd:cd07346 141 LTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAAR 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 290 TANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVFFSVLIGAFS-VGQASPNIEAFANARGAAYEV 361
Cdd:cd07346 221 LSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGE-LVAFLAYLGMLFGpIQRLANLYNQLQQALASLERI 292
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
388-614 |
1.69e-42 |
|
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: 158.29 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPL---DGMVSIDGQDIRTINVRYLR 463
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 464 EI----IGVVSQEPvlFA---------TTIAENIRYgREDVTMDEIEKAVKEA-------NAYDFIMKLPHQFdtlvger 523
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRI-HGGLSKAEARERAIELlervglpDPERRLDRYPHEL------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 524 gaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIAG 596
Cdd:COG0444 152 ----SGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAV 223
|
250
....*....|....*...
gi 153791547 597 FDGGVIVEQGNHDELMRE 614
Cdd:COG0444 224 MYAGRIVEEGPVEELFEN 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
388-614 |
2.42e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.22 E-value: 2.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYlREIIG 467
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRN 544
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1031-1249 |
2.52e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.82 E-value: 2.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPT-RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGKEIKQLN----V 1102
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1103 QWLRAQLGIVSQEPILFDC-SIAENIA----YGDNSRVVSYEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQK 1177
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1178 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIQNGKVKE 1249
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1042-1251 |
2.59e-42 |
|
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: 154.21 E-value: 2.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1042 TRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAQLGIVSQEPILFD- 1120
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLD 1196
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1197 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHG 1251
Cdd:cd03259 156 EPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
388-605 |
3.64e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 3.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN----VRYL 462
Cdd:COG1136 5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 463 REIIGVVSQEPVLFAT-TIAENI----RYGREDVtmDEIEKAVKEANAY----DFIMKLPHQfdtlvgergaqLSGGQKQ 533
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENValplLLAGVSR--KERRERARELLERvglgDRLDHRPSQ-----------LSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 534 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIA-HRLSTVRNADVIAGFDGGVIVEQ 605
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
388-617 |
3.71e-42 |
|
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: 155.67 E-value: 3.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI-NVRYLREII 466
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIA 538
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 539 RALVRNPKILLLDEATSALDTES-EAVVQAALD-KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG------NHDE 610
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*..
gi 153791547 611 LMREKGI 617
Cdd:TIGR04520 229 LLKEIGL 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
388-606 |
3.93e-42 |
|
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: 153.44 E-value: 3.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylREIIG 467
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFAT-TIAENIRYGREDVTM--DEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 544
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEGLLNRYP----HELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 606
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1049-1200 |
6.04e-42 |
|
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: 150.88 E-value: 6.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILF-DCSIAENI 1127
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1128 AYGDNSrvvsyEEIVRAAKEANIHQFID--SLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:pfam00005 81 RLGLLL-----KGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
388-614 |
6.05e-42 |
|
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: 154.43 E-value: 6.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVL-FATTIAENIRYGR------------EDvtMDEIEKAVKEANAYDFIMKLphqFDTlvgergaqLSGGQKQR 534
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrpsaED--REAVEEALERTGLEHLADRP---VDE--------LSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 535 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDEL 611
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
...
gi 153791547 612 MRE 614
Cdd:COG1120 226 LTP 228
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
105-361 |
7.44e-42 |
|
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: 155.39 E-value: 7.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 105 EEMTTYAYYYTGIGAGVLIVAYIQVsfWCLA-AGRQIHK-IRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGI 182
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRG--GCFSyAGTRLVRrLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 183 GDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIA 262
Cdd:cd18572 111 STNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 263 FGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFF--SVLIGAF- 339
Cdd:cd18572 191 FATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLyqQQLGEAFq 270
|
250 260
....*....|....*....|..
gi 153791547 340 SVGQaspNIEAFANARGAAYEV 361
Cdd:cd18572 271 SLGD---VFSSLMQAVGAAEKV 289
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
388-602 |
9.05e-42 |
|
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: 152.64 E-value: 9.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKE-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN----VRYL 462
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 463 REIIGVVSQEPVLFAT-TIAENIRYGredVTMDEIEKAVKEANAYDFI--MKLPHQFDTLVgergAQLSGGQKQRIAIAR 539
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 540 ALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIA-HRLSTVRNADVIAGFDGGVI 602
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
388-583 |
1.06e-41 |
|
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: 152.63 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylreiI 466
Cdd:cd03293 1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFA-TTIAENIRYGRE--DVTMDEIEKAVKEANA----YDFIMKLPHQfdtlvgergaqLSGGQKQRIAIAR 539
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERAEELLElvglSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 583
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
388-583 |
1.66e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.32 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylreiI 466
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFA-TTIAENIRYGREDVTMDEiEKAVKEANAY-------DFIMKLPHQfdtlvgergaqLSGGQKQRIAIA 538
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPK-AERRERARELlelvglaGFEDAYPHQ-----------LSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153791547 539 RALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 583
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
388-613 |
1.77e-41 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 152.84 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:cd03295 1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFA-TTIAENI-------RYGREdvtmdEIEKAVKEANAydfIMKLPHQfdTLVGERGAQLSGGQKQRIAIAR 539
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkllKWPKE-----KIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRL-STVRNADVIAGFDGGVIVEQGNHDELMR 613
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1026-1258 |
1.84e-41 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 153.03 E-value: 1.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1026 MLEGNvqfsGVVFNYPTRP-SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW 1104
Cdd:COG1124 1 MLEVR----NLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1105 LRAQLGIVSQEPIL-------FDCSIAE--NIAYGDNSRvvsyEEIVRAAKEANIH-QFIDSLPDkyntrvgdkgtQLSG 1174
Cdd:COG1124 77 FRRRVQMVFQDPYAslhprhtVDRILAEplRIHGLPDRE----ERIAELLEQVGLPpSFLDRYPH-----------QLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1175 GQKQRIAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
250
....*....|.
gi 153791547 1248 KEHGTHQQLLA 1258
Cdd:COG1124 218 VEELTVADLLA 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
388-613 |
2.71e-41 |
|
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: 151.89 E-value: 2.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-- 465
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 -IGVVSQEPVLF-ATTIAENIRYG-REDVTMDE--IEKAVKeanaydfiMKLphqfdTLVGERG------AQLSGGQKQR 534
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlREHTRLSEeeIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 535 IAIARALVRNPKILLLDEATSALD-TESEAVVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 153791547 612 MR 613
Cdd:cd03261 225 RA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1031-1249 |
3.31e-41 |
|
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: 151.09 E-value: 3.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPT-RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlrAQL 1109
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1110 GIVSQEPILFD-CSIAENIAYGDNSRVVSYEEIVRAAKEAnIHQ-----FIDSLPDkyntrvgdkgtQLSGGQKQRIAIA 1183
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-LELvglsgFENAYPH-----------QLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1184 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQN--GKVKE 1249
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1031-1246 |
3.94e-41 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 150.31 E-value: 3.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPSI--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPMAGSVFLDGKeikqlnvqwlr 1106
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1107 aqLGIVSQEPILFDCSIAENIAYG---DNSRvvsYEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIA 1183
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFGkpfDEER---YEKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1184 RALVRQPHILLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVIQNGK 1246
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1026-1252 |
3.98e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.26 E-value: 3.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1026 MLEGNVQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwl 1105
Cdd:COG3842 1 MAMPALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1106 RAQLGIVSQEPILF-DCSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRI 1180
Cdd:COG3842 76 KRNVGMVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1181 AIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVIQNGKVKEHGT 1252
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1031-1259 |
5.18e-41 |
|
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: 151.19 E-value: 5.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRP-SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVFLDGKEIKQLN---VQ 1103
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1104 WLRAQLGIVSQEPILFDC-SIAENIAYGDNSRVVSYEEIVRAAKE----ANIHQFIDSLPdkyntrvgdkgTQLSGGQKQ 1178
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1179 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQ 1255
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
....
gi 153791547 1256 LLAQ 1259
Cdd:cd03258 228 VFAN 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1031-1259 |
1.25e-40 |
|
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: 158.14 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVFLDGKEIKQLNVQWLRA 1107
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEPI--LFDCSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIA 1181
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELleavGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1182 IARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 153791547 1259 Q 1259
Cdd:COG1123 233 A 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1031-1259 |
2.07e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAQLG 1110
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILF-DCSIAENIAYGDNSRVVSYEEIVRAAKEAnIHQFidSLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQ 1189
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1190 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
388-600 |
2.57e-40 |
|
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: 146.95 E-value: 2.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRT--INVRYLREI 465
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFAT-TIAENIRYGredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRN 544
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFDGG 600
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
112-628 |
2.81e-40 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 163.19 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 112 YYYTGIGAGVLIVAY-IQVSFWCLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 190
Cdd:TIGR00957 1011 YGALGILQGFAVFGYsMAVSIGGIQASRVLH---QDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM 1087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 191 QAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKilSSFTDKELHAYAKAGAVAE--EVLAAIRTVIAFGGQKK 268
Cdd:TIGR00957 1088 GSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVA--SSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQER 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 269 ELERYNNNLEEAKR-----------LGIKKAITAN-ISMGAAFLLIYASYALAfwygTSLV-ISKEYSIgQVlTVFFSVL 335
Cdd:TIGR00957 1166 FIHQSDLKVDENQKayypsivanrwLAVRLECVGNcIVLFAALFAVISRHSLS----AGLVgLSVSYSL-QV-TFYLNWL 1239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 336 IGAFSvgQASPNIEAFANARgaayEVFKIIDNKPSI--DSFSKSGHKPdniQGNLEFKNIHFSYpsRKEVQ-ILKGLNLK 412
Cdd:TIGR00957 1240 VRMSS--EMETNIVAVERLK----EYSETEKEAPWQiqETAPPSGWPP---RGRVEFRNYCLRY--REDLDlVLRHINVT 1308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 413 VKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI----RYGR 488
Cdd:TIGR00957 1309 IHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSD 1388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 489 EDVTMdeiekAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAA 568
Cdd:TIGR00957 1389 EEVWW-----ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 569 LDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKlvMTQTAG 628
Cdd:TIGR00957 1464 IRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS--MAKDAG 1521
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
395-1268 |
3.41e-40 |
|
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: 162.77 E-value: 3.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 395 FSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQdirtinvrylreiIGVVSQEPV 474
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 475 LFATTIAENIRYGredVTMDEIE--KAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 552
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 553 ATSALD--TESEaVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIY------------ 618
Cdd:TIGR01271 575 PFTHLDvvTEKE-IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdn 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 619 -------------------------------------------------------------FKLV---MTQTAGNEIE-- 632
Cdd:TIGR01271 654 fsaerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVqmgPQKAQATTIEda 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 633 -------------------------------LGNEACKSKDEIDNLDMSSKDSGSSLIRRRSTRKSICGPHDQD------ 675
Cdd:TIGR01271 734 vrepserkfslvpedeqgeeslprgnqyhhgLQHQAQRRQSVLQLMTHSNRGENRREQLQTSFRKKSSITQQNElaseld 813
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 676 ---RKLSTKEALD------------------EDVPPASFWRI-LKLNSTEWPYFVVGIFCAIIngglqpaFSV-IFSKVV 732
Cdd:TIGR01271 814 iysRRLSKDSVYEiseeineedlkecfaderENVFETTTWNTyLRYITTNRNLVFVLIFCLVI-------FLAeVAASLL 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 733 GVFTNGGPPETQRQ--------------------NSNLFSLLFLILGII-SFITF-FLQGFTFGKAGEILTKRLRYMVFK 790
Cdd:TIGR01271 887 GLWLITDNPSAPNYvdqqhanasspdvqkpviitPTSAYYIFYIYVGTAdSVLALgFFRGLPLVHTLLTVSKRLHEQMLH 966
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 791 SMLRQDVSWFDDPKntTGALTTRLANDAAQVKGATGSRLAVIFQ-NIANLGTGIIISLIYGWqltlLLLAIVPIIAIAGV 869
Cdd:TIGR01271 967 SVLQAPMAVLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQlTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIM 1040
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 870 VEMKML-SGQALKdKKELEGSGKIATEAIENFR---TVVSLTREQKFETMYAQSLQIPYRN-----AMKKAHVFGITFSF 940
Cdd:TIGR01271 1041 LRAYFLrTSQQLK-QLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANwflylSTLRWFQMRIDIIF 1119
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 941 tqaMMYFSYAAcfrFGAYLVTQQLMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKATVSasHIIRIIEKTPEiDSYSTQ 1020
Cdd:TIGR01271 1120 ---VFFFIAVT---FIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVS--RVFKFIDLPQE-EPRPSG 1190
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1021 GLKPNML-----------------EGNVQFSGVVFNYpTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY 1083
Cdd:TIGR01271 1191 GGGKYQLstvlvienphaqkcwpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL 1269
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1084 DpMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNT 1163
Cdd:TIGR01271 1270 S-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDF 1345
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1164 RVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQ 1243
Cdd:TIGR01271 1346 VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIE 1425
|
1050 1060
....*....|....*....|....*
gi 153791547 1244 NGKVKEHGTHQQLLAQKGIYFSMVS 1268
Cdd:TIGR01271 1426 GSSVKQYDSIQKLLNETSLFKQAMS 1450
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1047-1259 |
4.61e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.60 E-value: 4.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPMAGSVFLDGKEI--KQLNVQWLRAQLGIVSQEPILF-D 1120
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFpH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYGdnSRVV---SYEEIVRAAKEAnihqfidsLpdkynTRVG--DKG----TQLSGGQKQRIAIARALVRQPH 1191
Cdd:COG1126 92 LTVLENVTLA--PIKVkkmSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1192 ILLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:COG1126 157 VMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1031-1257 |
5.55e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 149.04 E-value: 5.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPIL-FDCSIAENIAYG-----DNSRVVSYE--EIVRAA-KEANIHQFIDslpdkynTRVgdkgTQLSGGQKQRIA 1181
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlGLFGRPSAEdrEAVEEAlERTGLEHLAD-------RPV----DELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1182 IARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
388-602 |
5.72e-40 |
|
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: 147.29 E-value: 5.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI--RTINVRYLREI 465
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFA-TTIAENIRYGRedVTMDEIEKAVKEANAYDFIMK--LPHQFDtlvgERGAQLSGGQKQRIAIARALV 542
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 543 RNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVI 602
Cdd:cd03262 152 MNPKVMLFDEPTSALDPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1031-1249 |
1.28e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 147.93 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRP-SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLnvqwlRAQL 1109
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1110 GIVSQEPILFD-CSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 1184
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1185 ALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVIQN--GKVKE 1249
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
389-600 |
1.58e-39 |
|
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: 143.92 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 389 EFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGV 468
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 469 VSQepvlfattiaenirygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 548
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153791547 549 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFDGG 600
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
707-1004 |
1.71e-39 |
|
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: 148.85 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQPAFSVIFSKVVgvftNGGPPETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 786
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLI----DDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 787 MVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 866
Cdd:cd07346 77 DLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 867 AGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMY 946
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 947 FSYAACFRFGAYLVTQQLMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKATVSASHI 1004
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1031-1247 |
4.05e-39 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 145.33 E-value: 4.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPT-RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---- 1105
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1106 RAQLGIVSQE----PILfdcSIAENIAYGdnsrvVSYEEIVRAAKEANIHQFIDS--LPDKYNTRVGdkgtQLSGGQKQR 1179
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELP-----LLLAGVPKKERRERAEELLERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1180 IAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVIQNGKV 1247
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
388-606 |
4.32e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 149.48 E-value: 4.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVrYLREIiG 467
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKRNV-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 544
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAELLE---LVGLEGLADRYP----HQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFDGGVIVEQG 606
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
388-611 |
4.82e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 146.34 E-value: 4.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD--P---LDGMVSIDGQDI--RTINVR 460
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 YLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDEI-EKAVKEANAYDFImKlphqfDTLvGERGAQLSGGQKQ 533
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWDEV-K-----DRL-KKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 534 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREgRTTIVI-------AHRLStvrnaDVIAGFDGGVIVEQG 606
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFG 235
|
....*
gi 153791547 607 NHDEL 611
Cdd:COG1117 236 PTEQI 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
110-642 |
4.83e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 159.37 E-value: 4.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 110 YAYYYTGIGAGVLIVAYIQvSFW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDK 185
Cdd:PLN03232 952 YIVVYALLGFGQVAVTFTN-SFWlissSLHAAKRLH---DAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANL 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 186 IGMF----FQAMATFFggfIIGFTRgwklTLVILAISPVLGL--SAGIW-------AKILSSFTDKELhaYAKAGAvAEE 252
Cdd:PLN03232 1028 MNMFmnqlWQLLSTFA---LIGTVS----TISLWAIMPLLILfyAAYLYyqstsreVRRLDSVTRSPI--YAQFGE-ALN 1097
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 253 VLAAIRTVIAFGGQKKELERY--NN------NLEEAKRLGIKkaitaNISMGAAFLLIYASYAL----------AFWYGT 314
Cdd:PLN03232 1098 GLSSIRAYKAYDRMAKINGKSmdNNirftlaNTSSNRWLTIR-----LETLGGVMIWLTATFAVlrngnaenqaGFASTM 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 315 SLVISKEYSIGQVLTvffSVLIGAFSVGQASPNIEAFANARGAAYEVFKIIDNKPSIDSFSKSGhkpdniqgNLEFKNIH 394
Cdd:PLN03232 1173 GLLLSYTLNITTLLS---GVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG--------SIKFEDVH 1241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 395 FSYpsRKEVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEP 473
Cdd:PLN03232 1242 LRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP 1319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 474 VLFATTIAENIRYGREDVTMDeIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 553
Cdd:PLN03232 1320 VLFSGTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 554 TSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELM-REKGIYFKLVMTQTAGNEIE 632
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMVHSTGPANAQY 1478
|
570
....*....|
gi 153791547 633 LGNEACKSKD 642
Cdd:PLN03232 1479 LSNLVFERRE 1488
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1031-1252 |
4.97e-39 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.07 E-value: 4.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRP-SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVFLDGKEIKQLNVQWLR 1106
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1107 A---QLGIVSQEPILFD-CSIAENIAYGdnsrvvsyEEIVRAAKEAnIHQFIDSLPDkyntRVG--DKG----TQLSGGQ 1176
Cdd:COG1135 79 AarrKIGMIFQHFNLLSsRTVAENVALP--------LEIAGVPKAE-IRKRVAELLE----LVGlsDKAdaypSQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1177 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGT 1252
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
405-1267 |
9.03e-39 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 158.40 E-value: 9.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 405 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVsidgqdirtinvrYLREIIGVVSQEPVLFATTIAENI 484
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 485 RYGREDVTMDeIEKAVK----EANaydfIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 560
Cdd:PTZ00243 742 LFFDEEDAAR-LADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 561 -SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKgIYFKLVmTQTAGNEIELGNEACK 639
Cdd:PTZ00243 817 vGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLA-AELKENKDSKEGDADA 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 640 SKDEIDNLDMSSKDSGssliRRRSTRKSICGPHD------QDRKLSTKEaldEDVPPASFWrilklnSTEWPYFVvgiFC 713
Cdd:PTZ00243 895 EVAEVDAAPGGAVDHE----PPVAKQEGNAEGGDgaaldaAAGRLMTRE---EKASGSVPW------STYVAYLR---FC 958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 714 aiinGGLQPAFSVIFSKVV--------GVFTNGGPPETQRQNSNLFSLLFL---ILGIISFITFFLQGFTFGKAGeilTK 782
Cdd:PTZ00243 959 ----GGLHAAGFVLATFAVtelvtvssGVWLSMWSTRSFKLSAATYLYVYLgivLLGTFSVPLRFFLSYEAMRRG---SR 1031
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 783 RLRYMVFKSMLRQDVSWFDdpknTT--GALTTRLANDAaqvkGATGSRLAVIFQNIANLGTGIIIS-LIYGWQLTLLLLA 859
Cdd:PTZ00243 1032 NMHRDLLRSVSRGTMSFFD----TTplGRILNRFSRDI----DILDNTLPMSYLYLLQCLFSICSSiLVTSASQPFVLVA 1103
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 860 IVP------------------IIAIAGVVEMKMLS--GQALKDKKELEGSGK---IATEAIEnfrtvvsltreqKFETMY 916
Cdd:PTZ00243 1104 LVPcgylyyrlmqfynsanreIRRIKSVAKSPVFTllEEALQGSATITAYGKahlVMQEALR------------RLDVVY 1171
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 917 AQSLqipYRNAMKKAhvFGITFSFTQAMMYFSYAACFRFGAYL-VTQQLMTFENVLLVFSAIVFGAM--AVGQVSSFAPD 993
Cdd:PTZ00243 1172 SCSY---LENVANRW--LGVRVEFLSNIVVTVIALIGVIGTMLrATSQEIGLVSLSLTMAMQTTATLnwLVRQVATVEAD 1246
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 994 yAKATVSASHIIRIIEK--TPEIDSY---------------STQGLKP---------NMLEGNVQFSGVVFNYptRPSIP 1047
Cdd:PTZ00243 1247 -MNSVERLLYYTDEVPHedMPELDEEvdalerrtgmaadvtGTVVIEPasptsaaphPVQAGSLVFEGVQMRY--REGLP 1323
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 -VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAEN 1126
Cdd:PTZ00243 1324 lVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN 1403
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IaygDNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV-RQPHILLLDEATSALDTE 1205
Cdd:PTZ00243 1404 V---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPA 1480
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1206 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQL-LAQKGIYFSMV 1267
Cdd:PTZ00243 1481 LDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
388-616 |
1.45e-38 |
|
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: 144.62 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIiG 467
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKEanaYDFIMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRN 544
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEE---LIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 545 PKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKG 616
Cdd:COG4555 151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1031-1258 |
2.40e-38 |
|
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: 143.58 E-value: 2.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV---QWLRA 1107
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEPILFDC-SIAENIAYG-DNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIA 1181
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREHTDLSEAEIRELVLEKlelvGLPGAADKMPS-----------ELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1182 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
710-1002 |
3.00e-38 |
|
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: 145.01 E-value: 3.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 710 GIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPEtqrqNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVF 789
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLD----VLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 790 KSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGV 869
Cdd:cd18557 77 SSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 870 V---EMKMLSGQALkdkKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMY 946
Cdd:cd18557 155 IygrYIRKLSKEVQ---DALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 947 FSYAACFRFGAYLVTQ------QLMTFenvlLVFSAIVfgAMAVGQVSSFAPDYAKAtVSAS 1002
Cdd:cd18557 232 LSLLLVLWYGGYLVLSgqltvgELTSF----ILYTIMV--ASSVGGLSSLLADIMKA-LGAS 286
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
382-617 |
5.02e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 143.98 E-value: 5.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 382 DNIQGNLEFKNIHFSYPSrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRY 461
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQEP---VLFATT---IA---ENIRYGREDVTmDEIEKAVKEANAYDFIMKLPHqfdtlvgergaQLSGGQK 532
Cdd:PRK13632 81 IRKKIGIIFQNPdnqFIGATVeddIAfglENKKVPPKKMK-DIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 533 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDE 610
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
|
....*..
gi 153791547 611 LMREKGI 617
Cdd:PRK13632 229 ILNNKEI 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1026-1259 |
5.28e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.00 E-value: 5.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1026 MLEGNVQFSGVVFNYPTRpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL 1105
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1106 RAQLGIVSQEPilfD-----CSIAENIAYGDNSRVVSYEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQ 1176
Cdd:PRK13635 80 RRQVGMVFQNP---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1177 KQRIAIARALVRQPHILLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHG 1251
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
....*...
gi 153791547 1252 THQQLLAQ 1259
Cdd:PRK13635 223 TPEEIFKS 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1031-1258 |
5.29e-38 |
|
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: 142.64 E-value: 5.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV---QWLRA 1107
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEPILFDC-SIAENIAY-----GDNSRVVsYEEIVRAAKEA-NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRI 1180
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFplrehTRLSEEE-IREIVLEKLEAvGLRGAEDLYPA-----------ELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1181 AIARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELR 225
|
.
gi 153791547 1258 A 1258
Cdd:cd03261 226 A 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1031-1260 |
6.08e-38 |
|
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: 143.34 E-value: 6.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPtRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-QLNVQWLRAQL 1109
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1110 GIVSQEPilfD----CSIAEN-IAYGDNSRVVSYEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRI 1180
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1181 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 153791547 1259 QK 1260
Cdd:TIGR04520 226 QV 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1031-1246 |
8.09e-38 |
|
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: 140.01 E-value: 8.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPtrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN--VQWLRAQ 1108
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1109 LGIVSQEPILF-DCSIAENIAYGdnsrvvsyeeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALV 1187
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG-----------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1188 RQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGK 1246
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1032-1246 |
8.21e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 139.30 E-value: 8.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGI 1111
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQepilfdcsiaeniaygdnsrvvsyeeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPH 1191
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1192 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIQNGK 1246
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1031-1258 |
1.26e-37 |
|
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: 141.67 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILF-DCSIAENIAYGDNSRVVSYEEIVRAAKEanIHQFIDSLPDKYNTRVGDkgtQLSGGQKQRIAIARALVRQ 1189
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRERADE--LLALVGLDPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1190 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1048-1256 |
1.83e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 141.71 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--P---MAGSVFLDGKEI--KQLNVQWLRAQLGIVSQEPILFD 1120
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYG-----DNSRVVsYEEIVRAA-KEANihqfidsLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILL 1194
Cdd:COG1117 106 KSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1195 LDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVIQNGKVKEHGTHQQL 1256
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1032-1261 |
2.05e-37 |
|
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: 141.15 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYPtrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvQWLRAQLGI 1111
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQEPILFD-CSIAENIAYGDNSRVVSYEEIVRAAKEAnIHQFIdsLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQP 1190
Cdd:COG4555 79 LPDERGLYDrLTVRENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQKG 1261
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1031-1262 |
6.24e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.51 E-value: 6.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPilfD-----CSIAENIAYGDNSRVVSYEE----IVRAAKEANIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIA 1181
Cdd:PRK13632 87 IIFQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1182 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
...
gi 153791547 1260 KGI 1262
Cdd:PRK13632 233 KEI 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
388-604 |
6.46e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 139.03 E-value: 6.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN---VRYLRE 464
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 IIGVVSQE-PVLFATTIAENIRY-----GREDvtmDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQR 534
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREVldlvGLSDKAKALPHE-----------LSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 535 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTVRNAD--VIAgFDGGVIVE 604
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
389-606 |
8.67e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 142.63 E-value: 8.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 389 EFKNIHFSYP-SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-- 465
Cdd:PRK11153 3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 -IGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKE----------ANAYdfimklPhqfdtlvgergAQLSGGQ 531
Cdd:PRK11153 83 qIGMIFQHFNLLSSrTVFDNVALPLElaGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 532 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA-REGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQG 606
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1047-1267 |
9.64e-37 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 139.66 E-value: 9.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAEN 1126
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IaygDNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1206
Cdd:cd03288 115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1207 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQK-GIYFSMV 1267
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
134-345 |
1.66e-36 |
|
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: 140.34 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 134 LAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLV 213
Cdd:cd18573 67 IAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 214 ILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANI 293
Cdd:cd18573 147 MLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGL 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153791547 294 SMGAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVF--FSVLIGAfSVGQAS 345
Cdd:cd18573 227 FFGSTGFSGNLSLLSVLYYGGSLVASGELTVGD-LTSFlmYAVYVGS-SVSGLS 278
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
400-614 |
3.01e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 140.64 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 400 RKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI---IGVVSQEPvlF 476
Cdd:COG4608 28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 477 A---------TTIAENIRYgREDVTMDEIEKAVKEA------NAyDFIMKLPHQFdtlvgergaqlSGGQKQRIAIARAL 541
Cdd:COG4608 106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 542 VRNPKILLLDEATSALDteseaV-VQAA-----LD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 613
Cdd:COG4608 173 ALNPKLIVCDEPVSALD-----VsIQAQvlnllEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYA 247
|
.
gi 153791547 614 E 614
Cdd:COG4608 248 R 248
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1053-1259 |
3.65e-36 |
|
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: 138.55 E-value: 3.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA----QLGIVSQEPILF-DCSIAENI 1127
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 AYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1203
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1204 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
388-558 |
4.46e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 140.59 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYlREIiG 467
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLF-ATTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 544
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAAE---LLGLEDLLDRKP----KQLSGGQRQRVALGRALVRE 151
|
170
....*....|....
gi 153791547 545 PKILLLDEATSALD 558
Cdd:COG3839 152 PKVFLLDEPLSNLD 165
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
388-594 |
6.32e-36 |
|
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: 135.29 E-value: 6.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQ--ILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLyDPLDGMVSIDGQdirtinvrylre 464
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 iIGVVSQEPVLFATTIAENIRYGREdvtMDEIE-KAVKEANA--YDFIMkLPHQFDTLVGERGAQLSGGQKQRIAIARAL 541
Cdd:cd03250 68 -IAYVSQEPWIQNGTIRENILFGKP---FDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 542 VRNPKILLLDEATSALDTESEA-----VVQAALdkaREGRTTIVIAHRLSTVRNADVI 594
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRhifenCILGLL---LNNKTRILVTHQLQLLPHADQI 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
110-657 |
7.54e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 148.73 E-value: 7.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 110 YAYYYTGIGAGVLIVAYIQvSFW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDK 185
Cdd:PLN03130 955 YNLIYALLSFGQVLVTLLN-SYWlimsSLYAAKRLH---DAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVF 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 186 IGMF----FQAMATFFggfIIGFTRgwklTLVILAISPVLGLSAGIW---------AKILSSFTDKELhaYAKAGAvAEE 252
Cdd:PLN03130 1031 VNMFlgqiFQLLSTFV---LIGIVS----TISLWAIMPLLVLFYGAYlyyqstareVKRLDSITRSPV--YAQFGE-ALN 1100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 253 VLAAIRTVIAF------GGQKKEleryNN------NLEEAKRLGIKKAitaniSMGAAFLLIYASYAL----------AF 310
Cdd:PLN03130 1101 GLSTIRAYKAYdrmaeiNGRSMD----NNirftlvNMSSNRWLAIRLE-----TLGGLMIWLTASFAVmqngraenqaAF 1171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 311 WYGTSLVISKEYSIGQVLTvffSVLIGAfSVGQASPN-IEAFANARGAAYEVFKIIDNkpsidsfsksgHKPDN---IQG 386
Cdd:PLN03130 1172 ASTMGLLLSYALNITSLLT---AVLRLA-SLAENSLNaVERVGTYIDLPSEAPLVIEN-----------NRPPPgwpSSG 1236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 387 NLEFKNIHFSYpsRKEVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI 465
Cdd:PLN03130 1237 SIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV 1314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFATTIAENIRYGREDVTMDEIEkAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNP 545
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRFNLDPFNEHNDADLWE-SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 546 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDEL-MREKGIYFKLVMT 624
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQS 1473
|
570 580 590
....*....|....*....|....*....|....*....
gi 153791547 625 QTAGNEIEL------GNEACKSKDEIDNLDMSSKDSGSS 657
Cdd:PLN03130 1474 TGAANAQYLrslvfgGDEDRLAREESKALDGQRKWLASS 1512
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
388-602 |
8.54e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 134.06 E-value: 8.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTiNVRYLREIIG 467
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFAT-TIAENIRYgredvtmdeiekavkeanaydfimklphqfdtlvgergaqlSGGQKQRIAIARALVRNPK 546
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 547 ILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVI 602
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1031-1247 |
8.89e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 136.73 E-value: 8.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRA 1107
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEPILFD-CSIAENI---AYGDNS------RVVSYEEIVRAakeaniHQFIDS--LPDKYNTRVGdkgtQLSGG 1175
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERA------LEALERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1176 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
388-614 |
1.02e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.37 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylreiIG 467
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVL---FATTIAENI------------RYGREDVtmDEIEKAVKEANAYDFImklphqfDTLVGErgaqLSGGQK 532
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgrygrrglfrRPSRADR--EAVDEALERVGLEDLA-------DRPIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 533 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVR-NADVIAGFDGGVIVEqGNHDE 610
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEE 224
|
....
gi 153791547 611 LMRE 614
Cdd:COG1121 225 VLTP 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1048-1257 |
1.33e-35 |
|
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: 135.54 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYGDNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1206
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1207 EKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:cd03299 165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
405-624 |
7.88e-35 |
|
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: 134.27 E-value: 7.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 405 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI 484
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 485 RYGREdVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAV 564
Cdd:cd03288 116 DPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 565 VQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELM-REKGIYFKLVMT 624
Cdd:cd03288 195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRT 255
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1031-1251 |
9.84e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.87 E-value: 9.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPtrPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRA 1107
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQK 1177
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1178 QRIAIARALVRQPHILLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVIQNGKVKEHG 1251
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1047-1259 |
1.75e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.04 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGKEIK-QLNVQwlRAQLGIVSQEPILF-DC 1121
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR--ERRVGFVFQHYALFpHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYGDNSRVVSYEEIVRAAKE----ANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1197
Cdd:COG1118 91 TVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1198 ATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:COG1118 160 PFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
710-1003 |
2.26e-34 |
|
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: 133.91 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 710 GIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETQRQNSNLFSLLFLILGIISF--ITFFLQGFTFGKAGEILTKRLRYM 787
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIgsIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 788 VFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIA 867
Cdd:cd18780 81 LFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 868 GVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMYF 947
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 948 SYAACFRFGAYLVTQQLMT------FenVLLVFSAivfgAMAVGQVSSFAPDYAKAtVSASH 1003
Cdd:cd18780 239 AIVLVLWYGGRLVIDGELTtglltsF--LLYTLTV----AMSFAFLSSLYGDFMQA-VGASV 293
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
388-603 |
2.49e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.49 E-value: 2.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-- 465
Cdd:COG3638 3 LELRNLSKRYPGGTPA--LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 -IGVVSQEPVLFA-TTIAENI-----------RYGREDVTMDEIEKAvkeanaydfimklphqFDTL--VG------ERG 524
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVlagrlgrtstwRSLLGLFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 525 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGV 601
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKtARQVMDLLRRIAREdGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
..
gi 153791547 602 IV 603
Cdd:COG3638 225 VV 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
388-611 |
2.90e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 131.92 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-- 465
Cdd:cd03256 1 IEVENLSKTYPNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 -IGVVSQEPVLFA-TTIAENIRYGREDVT---------MDEIEKAvkeaNAYDFIMKLphQFDTLVGERGAQLSGGQKQR 534
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglFPKEEKQ----RALAALERV--GLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 535 IAIARALVRNPKILLLDEATSALDTE-SEAVVQAALDKARE-GRTTIVIAHRLSTVR-NADVIAGFDGGVIVEQGNHDEL 611
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
119-358 |
2.97e-34 |
|
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: 133.38 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 119 AGVLIV----AYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMA 194
Cdd:cd18576 43 LGLFLLqavfSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 195 TFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYN 274
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 275 NNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLT-VFFSVLIGAfSVGQASPNIEAFAN 353
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQK 281
|
....*
gi 153791547 354 ARGAA 358
Cdd:cd18576 282 ALGAS 286
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
410-614 |
3.42e-34 |
|
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: 132.77 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 410 NLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI----IGVVSQEPVLFA-TTIAENI 484
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 485 RYGREDVTMDEIEKAVKEANAY------DFIMKLPHqfdtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 558
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALelvgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 559 TESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
388-612 |
7.33e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 130.98 E-value: 7.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNI--HFSypsrkEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIR--TINVRYLR 463
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 464 EIIGVVSQEPVLFATTIA-ENIRYGREDVTmdEIEKAVKEANAYDFIMKlphqfdtlVG--ERG----AQLSGGQKQRIA 536
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFGPLRVR--GASKEEAEKQARELLAK--------VGlaERAhhypSELSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 537 IARALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELM 612
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1047-1256 |
8.90e-34 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 130.43 E-value: 8.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIkqLNVQWLRAQLGIVSQEPILF-DCSIAE 1125
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 NIAYGDNSRVVSYEEIVRAAKEAnIHQF-IDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1204
Cdd:cd03300 92 NIAFGLRLKKLPKAEIKERVAEA-LDLVqLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1205 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQL 1256
Cdd:cd03300 164 KLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
391-583 |
1.24e-33 |
|
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: 128.91 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 391 KNIHFSYPSRKEvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIrtiNVRYLREIIGVVS 470
Cdd:cd03226 3 ENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 471 QEP--VLFATTIAENIRYGREDVTMD--EIEKAVKEANAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIARALVRNPK 546
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 153791547 547 ILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAH 583
Cdd:cd03226 147 LLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITH 184
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1031-1259 |
1.37e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.21 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLnvqwlRAQLG 1110
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQE-------PIlfdcSIAENIAYGDNSRV--------VSYEEIVRAAKEANIHQFIDslpdkynTRVGdkgtQLSGG 1175
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMGRYGRRglfrrpsrADREAVDEALERVGLEDLAD-------RPIG----ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1176 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIqNGKVKEHGTH 1253
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*.
gi 153791547 1254 QQLLAQ 1259
Cdd:COG1121 223 EEVLTP 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1032-1247 |
2.00e-33 |
|
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: 129.61 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYPTrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---RAQ 1108
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1109 LGIVSQEPILFD-CSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLP-----DKYNTRVGdkgtQLSGGQKQRIAI 1182
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALErvgllDKAYQRAD----QLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1183 ARALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVIQNGKV 1247
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
388-613 |
2.34e-33 |
|
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: 136.74 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK--------EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLyDPLDGMVSIDGQDIRTIN- 458
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 459 --VRYLREIIGVVSQEPvlFAT-----TIAENIRYG----REDVTMDEIEKAVKEA-----------NAYdfimklPHQF 516
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRY------PHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 517 dtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN 590
Cdd:COG4172 427 -----------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....
gi 153791547 591 -ADVIAGFDGGVIVEQGNHDELMR 613
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1048-1247 |
2.94e-33 |
|
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: 128.03 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW--LRAQLGIVSQEPILF-DCSIA 1124
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIAYGD-NSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1199
Cdd:cd03262 95 ENITLAPiKVKGMSKAEAEERALELlekvGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1200 SALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:cd03262 164 SALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
388-582 |
4.40e-33 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 127.52 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI---RTINVRYLRE 464
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 IIGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLvgerGAQLSGGQKQRIAIARAL 541
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153791547 542 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA 582
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1031-1247 |
9.55e-33 |
|
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: 125.20 E-value: 9.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAQLG 1110
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILF-DCSIAENIaygdnsrvvsyeeivraakeanihqfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVRQ 1189
Cdd:cd03230 77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1190 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
389-602 |
9.59e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 126.49 E-value: 9.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 389 EFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQdirtiNVRYLREIIGV 468
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 469 VSQEPVL---FATTIAENI------------RYGREDvtMDEIEKAVKEANAYDFIMKlphQFDtlvgergaQLSGGQKQ 533
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmglyghkglfrRLSKAD--KAKVDEALERVGLSELADR---QIG--------ELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 534 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGGVI 602
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1031-1256 |
1.09e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.58 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPtrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlNVQWLRAQ-- 1108
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-----DVTDLPPKdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1109 -LGIVSQEPILFD-CSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAI 1182
Cdd:COG3839 76 nIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKPK-----------QLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1183 ARALVRQPHILLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVIQNGKVKEHGT 1252
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
....
gi 153791547 1253 HQQL 1256
Cdd:COG3839 218 PEEL 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
389-606 |
1.19e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 125.24 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 389 EFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGV 468
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 469 VSQepvlfattiaenirygredvtmdeiekAVKEANAYDFIMKlphQFDTlvgergaqLSGGQKQRIAIARALVRNPKIL 548
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 549 LLDEATSALDTESE-AVVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 606
Cdd:cd03214 120 LLDEPTSHLDIAHQiELLELLRRLARErGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
388-594 |
1.75e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 125.67 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYlREIIG 467
Cdd:COG4133 3 LEAENLSCRRGER---LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFAT-TIAENIR-----YGReDVTMDEIEKAVKEanaydfiMKLPHQFDTLVGergaQLSGGQKQRIAIARAL 541
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153791547 542 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTVRNADVI 594
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
723-991 |
1.86e-32 |
|
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: 128.40 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 723 AFSVIFSKVVGVFTNG-GPPETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFD 801
Cdd:cd18573 14 SVPFAIGKLIDVASKEsGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 802 dpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALK 881
Cdd:cd18573 94 --KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 882 DKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVT 961
Cdd:cd18573 172 VQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVA 251
|
250 260 270
....*....|....*....|....*....|
gi 153791547 962 QqlmtfenvllvfsaivfGAMAVGQVSSFA 991
Cdd:cd18573 252 S-----------------GELTVGDLTSFL 264
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1036-1259 |
1.87e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 127.93 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1036 VVFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQE 1115
Cdd:PRK13650 10 LTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1116 P--ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQ 1189
Cdd:PRK13650 90 PdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1190 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
388-611 |
2.46e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 126.81 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEvqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLDGMVSIDGQDI---RTINV 459
Cdd:PRK14239 6 LQVSDLSVYYNKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 460 RyLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDE-IEKAVKEANAYDFIMKLPHqfDTLVGergaqLSGGQK 532
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKDRLH--DSALG-----LSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 533 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1040-1259 |
3.20e-32 |
|
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: 128.63 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1040 YPTRP-SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVFLDGKEIKQLNVQWLRA----QLGI 1111
Cdd:COG0444 11 FPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQEP---------ILFdcSIAENI-AYGDNSRVVSYEEIVRAAKEANIH---QFIDSLPdkyntrvgdkgTQLSGGQKQ 1178
Cdd:COG0444 91 IFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPdpeRRLDRYP-----------HELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1179 RIAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHG 1251
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEG 233
|
....*...
gi 153791547 1252 THQQLLAQ 1259
Cdd:COG0444 234 PVEELFEN 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
388-615 |
3.81e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.12 E-value: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYL--REI 465
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEP--VLFATTIAENIRYGREDV--TMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAI 537
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPHH-----------LSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 538 ARALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 615
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1031-1252 |
4.10e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 129.68 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAQLG 1110
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILF-DCSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARA 1185
Cdd:PRK09452 90 TVFQSYALFpHMTVFENVAFGLRMQKTPAAEITPRVMEAlrmvQLEEFAQRKP-----------HQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1186 LVRQPHILLLDEATSALDTESEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVIQNGKVKEHGT 1252
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1044-1247 |
5.82e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 131.68 E-value: 5.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1044 PSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAQ-LGI--VSQEPILF- 1119
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR--DAQaAGIaiIHQELNLVp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1120 DCSIAENIAYGD---NSRVVSYEEIVRAAKEA----NIHqfIDslPDkynTRVGDkgtqLSGGQKQRIAIARALVRQPHI 1192
Cdd:COG1129 93 NLSVAENIFLGReprRGGLIDWRAMRRRARELlarlGLD--ID--PD---TPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1193 LLLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:COG1129 162 LILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1031-1256 |
7.92e-32 |
|
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: 124.76 E-value: 7.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPtrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAQLG 1110
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILF-DCSIAENIAYGDNSRVVSyEEIVRAAKEANIHQFI-----DSLPDKYNTrvgdkgtQLSGGQKQRIAIAR 1184
Cdd:cd03296 78 FVFQHYALFrHMTVFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1185 ALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQL 1256
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
388-613 |
9.50e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 9.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:PRK13635 6 IRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEP--VLFATTIAENIRYGRED--VTMDE----IEKAVKEANAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIAR 539
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMR 613
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1034-1251 |
9.86e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 122.54 E-value: 9.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1034 SGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVS 1113
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1114 QepilfdcsiaeniaygdnsrvvsyeeivrAAKEANIHQFIDSLpdkYNTrvgdkgtqLSGGQKQRIAIARALVRQPHIL 1193
Cdd:cd03214 80 Q-----------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1194 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHG 1251
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
388-613 |
1.02e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.96 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRT-INVRYLReiI 466
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERR--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKE----------ANAYdfimklPHQfdtlvgergaqLSGGQKQ 533
Cdd:COG1118 78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------PSQ-----------LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 534 RIAIARALVRNPKILLLDEATSALDT----ESEAVVQAALDkaREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNH 608
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTP 218
|
....*
gi 153791547 609 DELMR 613
Cdd:COG1118 219 DEVYD 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1032-1251 |
1.29e-31 |
|
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: 123.41 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLnvqwlRAQLGI 1111
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQEPIL---FDCSIAENIAYGDNSRVVSYEEIVRAAKEAnIHQFIDS--LPDKYNTRVGdkgtQLSGGQKQRIAIARAL 1186
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK-VDEALERvgLSELADRQIG----ELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1187 VRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIqNGKVKEHG 1251
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1035-1248 |
1.71e-31 |
|
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: 122.75 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1035 GVVFNYPTRPSIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlnvQWLRAQLGIVSQ 1114
Cdd:cd03226 4 NISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1115 EP--ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHI 1192
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1193 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVK 1248
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1046-1258 |
1.75e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 123.31 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1046 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAQLGI--VSQEPILF-DCS 1122
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 IAENIAYGDNSRVvsyeeivRAAKEANIHQFIDSLPDKYnTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1202
Cdd:cd03224 92 VEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1203 dteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVIQNGKVKEHGTHQQLLA 1258
Cdd:cd03224 164 ---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1031-1252 |
1.88e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.84 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGV--VFNYPTRPsIPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPMAGSVFLDGKEIKQLNVQWL 1105
Cdd:PRK11153 2 IELKNIskVFPQGGRT-IHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1106 RA---QLGIVSQE-PILFDCSIAENIAYGdnsrvvsyEEIVRAAKeANIHQFIDSLPDkyntRVG--DKG----TQLSGG 1175
Cdd:PRK11153 78 RKarrQIGMIFQHfNLLSSRTVFDNVALP--------LELAGTPK-AEIKARVTELLE----LVGlsDKAdrypAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1176 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGT 1252
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
388-606 |
2.40e-31 |
|
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: 122.75 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRtiNVRYLREIIG 467
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRN 544
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQIEH----LLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQG 606
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1042-1259 |
3.55e-31 |
|
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: 129.80 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1042 TRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPMAGSVFLDGKEIKQLN---VQWLRAQLGIVSQEPil 1118
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1119 fdcsiaeniaYGD-NSRVvSYEEIV------------RAAKEANIhqfIDSLpdkynTRVG-DKGT------QLSGGQKQ 1178
Cdd:COG4172 372 ----------FGSlSPRM-TVGQIIaeglrvhgpglsAAERRARV---AEAL-----EEVGlDPAArhryphEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1179 RIAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQG 508
|
....*...
gi 153791547 1252 THQQLLAQ 1259
Cdd:COG4172 509 PTEQVFDA 516
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
406-610 |
5.21e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 122.44 E-value: 5.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENI 484
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 485 RYGREDVTMD--EIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 562
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLEIAE---MLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791547 563 AVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 610
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1049-1256 |
5.88e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 125.23 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAQLGIVSQEPilFDC---- 1121
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YASlnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 -SIAENIAYG-DNSRVVSyeeivRAAKEANIHQFIDslpdkyntRVGDKGT-------QLSGGQKQRIAIARALVRQPHI 1192
Cdd:COG4608 112 mTVGDIIAEPlRIHGLAS-----KAERRERVAELLE--------LVGLRPEhadryphEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1193 LLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQL 1256
Cdd:COG4608 179 IVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1031-1252 |
9.20e-31 |
|
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: 121.78 E-value: 9.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVfnyptrpsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAQLG 1110
Cdd:cd03219 8 KRFGGLV----------ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVS--QEPILF-DCSIAENI----------AYGDNSRVVSYEEIVRAAKEAnIHQFidSLPDKYNTRVGDkgtqLSGGQK 1177
Cdd:cd03219 77 IGRtfQIPRLFpELTVLENVmvaaqartgsGLLLARARREEREARERAEEL-LERV--GLADLADRPAGE----LSYGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1178 QRIAIARALVRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGT 1252
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
388-606 |
1.03e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 122.45 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDpLDGMVSIDG------QDI--RTINV 459
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 460 RYLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDEI-EKAVKEANAYDFIMKLPHQfdtlvgeRGAQLSGGQK 532
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 533 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFDG-----GVIVE 604
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLVE 236
|
..
gi 153791547 605 QG 606
Cdd:PRK14258 237 FG 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1047-1241 |
1.03e-30 |
|
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: 120.66 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAQLGIVSQEPILF-DCSIAE 1125
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 NIA-----YGdnsRVVSYEEIVRAAKEANIHQFIDslpdkynTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:COG4133 95 NLRfwaalYG---LRADREAIDEALEAVGLAGLAD-------LPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153791547 1201 ALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1241
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
404-611 |
1.14e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 121.78 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 404 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMV-----SIDGQdiRTIN-----VRYLREIIGVVSQEP 473
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 474 VLFA-TTIAENIRYGreDVTMDEIEKAVKEANAYDFIMKLphqfdTLVGERGA---QLSGGQKQRIAIARALVRNPKILL 549
Cdd:PRK11264 95 NLFPhRTVLENIIEG--PVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 550 LDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1053-1259 |
1.20e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.40 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqwlrAQ--LGIVSQEPILFD-CSIAENIAY 1129
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErpVSMLFQENNLFPhLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1130 GDNSR----VVSYEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD-- 1203
Cdd:COG3840 95 GLRPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1204 --TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:COG3840 164 lrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1049-1268 |
2.70e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 121.77 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEP--ILFDCSIAEN 1126
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1202
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1203 DTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHG-----THQQLLAQKGIYFSMVS 1268
Cdd:PRK13647 170 DPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLVA 242
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
753-969 |
2.83e-30 |
|
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: 121.88 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 753 LLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVI 832
Cdd:cd18572 40 LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDPLSTNLNVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 833 FQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVE---MKMLSGQAlkdKKELEGSGKIATEAIENFRTVVSLTRE 909
Cdd:cd18572 118 LRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYgryYRKLSKEI---QDALAEANQVAEEALSNIRTVRSFATE 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 910 QKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFEN 969
Cdd:cd18572 195 EREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
388-558 |
3.02e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 124.29 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI-------RTINVr 460
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaenRHVNT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 ylreiigvVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEAnaydfiMKLPhQFDTLVGERGAQLSGGQKQRIAI 537
Cdd:PRK09452 91 --------VFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMV-QLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180
....*....|....*....|.
gi 153791547 538 ARALVRNPKILLLDEATSALD 558
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
388-614 |
3.04e-30 |
|
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: 119.85 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRY-LREII 466
Cdd:cd03224 1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAVKEAnaYDFIMKLphqfDTLVGERGAQLSGGQKQRIAIARALVRNP 545
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRL----KERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 546 KILLLDEATSALdteSEAVVQ---AALDKAREGRTTIVI----AHRLSTVrnADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:cd03224 152 KLLLLDEPSEGL---APKIVEeifEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
388-614 |
5.68e-30 |
|
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: 119.26 E-value: 5.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIrtINVRYLREIIG 467
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEAnaydfiMKLPhQFDTLVGERGAQLSGGQKQRIAIARALVRN 544
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrLKKLPKAEIKERVAEA------LDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
388-592 |
7.06e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.61 E-value: 7.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIAR 539
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRNAD 592
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSD 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
388-611 |
1.16e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.81 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIAR 539
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1049-1230 |
1.88e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 118.73 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA-----GSVFLDGKEI--KQLNVQWLRAQLGIVSQEPILFDC 1121
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYGdnSRVVSY----EEIV-RAAKEAnihqfidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1196
Cdd:PRK14243 106 SIYDNIAYG--ARINGYkgdmDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190
....*....|....*....|....*....|....
gi 153791547 1197 EATSALDTESEKVVQEALDKAREGRTCIVIAHRL 1230
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
382-615 |
2.45e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 118.68 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 382 DNIqgnLEFKNIHFSYpsRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRY 461
Cdd:PRK13647 2 DNI---IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHqfdtlvgergaQLSGGQKQ 533
Cdd:PRK13647 77 VRSKVGLVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 534 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLL 225
|
....
gi 153791547 612 MREK 615
Cdd:PRK13647 226 TDED 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
400-605 |
3.43e-29 |
|
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: 117.98 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 400 RKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN---VRYLREIIGVVSQE---P 473
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 474 VLFATTIAENIRYGREDVT-MDEIEKAVKEANAYDfIMKLPhqfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 552
Cdd:TIGR02769 101 VNPRMTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 553 ATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQ 605
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1031-1247 |
4.32e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 114.45 E-value: 4.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPtrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAQ-L 1109
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARrA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1110 GIvsqepilfdcsiaeniaygdnsrvvsyeeivraakeANIHQfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQ 1189
Cdd:cd03216 76 GI------------------------------------AMVYQ-------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1190 PHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:cd03216 101 ARLLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1031-1247 |
6.66e-29 |
|
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: 115.58 E-value: 6.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPtrPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRA 1107
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQE-PILFDCSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAI 1182
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1183 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA--DLIVVIQNGKV 1247
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1031-1256 |
8.91e-29 |
|
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: 115.29 E-value: 8.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPSiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAQLG 1110
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFD-CSIAENIAYgdNSRVVSY-EEIVRAAKEANIHQFidSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVR 1188
Cdd:cd03263 79 YCPQFDALFDeLTVREHLRF--YARLKGLpKSEIKEEVELLLRVL--GLTDKANKRART----LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1189 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQL 1256
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1049-1247 |
1.27e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 114.70 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAQLGIVSQEPILF-D 1120
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYG-----DNSRVVSYEEIVRAAKeanihqfIDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLL 1195
Cdd:cd03297 90 LNVRENLAFGlkrkrNREDRISVDELLDLLG-------LDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1196 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1048-1259 |
1.67e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 118.28 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1202
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEAlelvDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1203 DTESEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK11432 168 DANLRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
710-983 |
1.88e-28 |
|
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: 116.43 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 710 GIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETQRQNSNLFSLLFLILGIISFItfflQGFTFGKAGEILTKRLRYMVF 789
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFF----RIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 790 KSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGV 869
Cdd:cd18576 77 RHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 870 V---EMKMLSGQALkdkKELEGSGKIATEAIENFRTVVSLTREQkFETM-YAQSLQIPYRNAMKKAHVFGITFSFTQAMM 945
Cdd:cd18576 155 LfgrRIRKLSKKVQ---DELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 153791547 946 YFSYAACFRFGAYLVTQQLMTFENV--LLVFSAIVFGAMA 983
Cdd:cd18576 231 FGAIVAVLWYGGRLVLAGELTAGDLvaFLLYTLFIAGSIG 270
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1031-1257 |
1.93e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.19 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTrpsIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK--QLNVQWLRAQ 1108
Cdd:PRK09493 2 IEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1109 LGIVSQEPILFDCSIA-ENIAYGDNSrvvsyeeiVRAAKEANIHQFIDSLPDKYN--TRVGDKGTQLSGGQKQRIAIARA 1185
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGPLR--------VRGASKEEAEKQARELLAKVGlaERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1186 LVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
404-604 |
2.38e-28 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.55 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 404 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN---VRYLREIIGVVSQEP---VLFA 477
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 TTIAENIRYG-REDVTMDEIEKAVKEANAYDfIMKLPhqfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 556
Cdd:PRK10419 106 KTVREIIREPlRHLLSLDKAERLARASEMLR-AVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791547 557 LDTESEAVVQAALDKAREGRTT--IVIAHRLSTV-RNADVIAGFDGGVIVE 604
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1031-1256 |
2.62e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.62 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPSIpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPI-LFDCSIAE-NIAYGDNSRVVSYEEIVR----AAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 1184
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1185 ALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQL 1256
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
388-615 |
2.76e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 114.80 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGM-VSIDGQDIRTINVRYLREII 466
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVS---------QEPVL-------FATTiaeniryGR-EDVTMDEIEKAVKeanaydfIMKLPHqFDTLVGERGAQLSG 529
Cdd:COG1119 81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLyREPTDEQRERARE-------LLELLG-LAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 530 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV-IAHRLStvrnaDVIAGFD------GGV 601
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIThvlllkDGR 220
|
250
....*....|....
gi 153791547 602 IVEQGNHDELMREK 615
Cdd:COG1119 221 VVAAGPKEEVLTSE 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
388-648 |
3.46e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.57 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQ---ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI-NVRYLR 463
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 464 EIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRI 535
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPHL-----------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 536 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMR 613
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 153791547 614 E----KGIYFKL-VMTQTAgneIELGNEACKSKDEIDNLD 648
Cdd:PRK13633 234 EvemmKKIGLDVpQVTELA---YELKKEGVDIPSDILTID 270
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
388-581 |
4.15e-28 |
|
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: 114.07 E-value: 4.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSR-KEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN----VRYL 462
Cdd:COG4181 9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 463 REIIGVVSQEPVLFAT-TIAENI-----RYGREDVTmdeiEKAVKEANAYDfimklphqfdtlVGERG----AQLSGGQK 532
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVmlpleLAGRRDAR----ARARALLERVG------------LGHRLdhypAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153791547 533 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVI 581
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVL 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
843-1263 |
4.25e-28 |
|
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: 123.52 E-value: 4.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 843 IIISLIYGWQ-LTLLLLA----IVPIIAIAGVVEMKMLSGQaLKDKKELEGSGKIATEAIENFRTVV----SLTREQKFE 913
Cdd:TIGR00957 445 VILALYFLWLnLGPSVLAgvavMVLMVPLNAVMAMKTKTYQ-VAHMKSKDNRIKLMNEILNGIKVLKlyawELAFLDKVE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 914 TMYAQSLQIpyrnaMKKAHVFGITFSFTQAMMYFSYAAC-FRFGAYLVTQQLMTFENV---LLVFSAIVFGAMAVGQVSS 989
Cdd:TIGR00957 524 GIRQEELKV-----LKKSAYLHAVGTFTWVCTPFLVALItFAVYVTVDENNILDAEKAfvsLALFNILRFPLNILPMVIS 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 990 fapDYAKATVSASHI-IRIIEKTPEIDSYSTQGLKPNmlEGN-VQFSGVVFNYpTRPSIPVLQGLSLEVKKGQTLALVGS 1067
Cdd:TIGR00957 599 ---SIVQASVSLKRLrIFLSHEELEPDSIERRTIKPG--EGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQ 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1068 SGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlnvqwlraQLGIVSQEPILFDCSIAENIAYGDNSRVVSYEEIVRAAKe 1147
Cdd:TIGR00957 673 VGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA- 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1148 anIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL---DKAREGRTCI 1224
Cdd:TIGR00957 739 --LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRI 816
|
410 420 430
....*....|....*....|....*....|....*....
gi 153791547 1225 VIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIY 1263
Cdd:TIGR00957 817 LVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1031-1251 |
4.35e-28 |
|
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: 113.12 E-value: 4.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKqlNVQWLRAQLG 1110
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILF-DCSIAENIAYGDNSRVVSYEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARA 1185
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRKVPKDEIDErvreVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1186 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVIQNGKVKEHG 1251
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
388-607 |
4.89e-28 |
|
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: 112.26 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHF---SYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLM-----QRLYDPLDGMVSIDGQDIRTINV 459
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKST---LLnalagRRTGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 460 RYlreIIGVVSQEPVLFAT-TIAENIrygredvtmdeiekavkeanayDFIMKLphqfdtlvgeRGaqLSGGQKQRIAIA 538
Cdd:cd03213 81 RK---IIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 539 RALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQGN 607
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQGR 189
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
387-613 |
5.14e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 113.70 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 387 NLEFKNIHFSYpsrkEVQILKgLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVrYLREIi 466
Cdd:COG3840 1 MLRLDDLTYRY----GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFA-TTIAENI--------RYGREDVTmdEIEKAVKEANAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAI 537
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIglglrpglKLTAEQRA--QVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 538 ARALVRNPKILLLDEATSALD----TESEAVVQaalDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVD---ELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
..
gi 153791547 612 MR 613
Cdd:COG3840 218 LD 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
382-633 |
7.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.90 E-value: 7.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 382 DNIqgnLEFKNIHFSYPSRKEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLD---GMVSIDGQDIRTIN 458
Cdd:PRK13640 3 DNI---VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 459 VRYLREIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEANA----YDFIMKLPhqfdtlvgergAQLSGG 530
Cdd:PRK13640 79 VWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEP-----------ANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 531 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNH 608
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
250 260
....*....|....*....|....*
gi 153791547 609 DElmrekgIYFKLVMTQTAGNEIEL 633
Cdd:PRK13640 228 VE------IFSKVEMLKEIGLDIPF 246
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
402-614 |
1.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.37 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 402 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI--RTINVRYLREIIGVVSQEP--VLFA 477
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 TTIAENIRYGREDVTM--DEIEKAVKEANAydfIMKLPhqFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 555
Cdd:PRK13637 99 ETIEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 556 ALD--TESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:PRK13637 174 GLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
388-560 |
1.24e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 112.82 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylREIIG 467
Cdd:cd03296 3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFA-TTIAENIRYG------REDVTMDEIEKAVKEanaydfIMKLPhQFDTLVGERGAQLSGGQKQRIAIARA 540
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGlrvkprSERPPEAEIRAKVHE------LLKLV-QLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180
....*....|....*....|
gi 153791547 541 LVRNPKILLLDEATSALDTE 560
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAK 170
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
387-609 |
1.36e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.80 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 387 NLEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDG------QDIRTINVR 460
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 YLREIIGVVSQE----PVLfatTIAENIrygredvtmdeIEKAVK-----EANAYDFIMKLPH--QFDTLVGERGAQLSG 529
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENL-----------IEAPCKvlglsKEQAREKAMKLLArlRLTDKADRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 530 GQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGN 607
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAqVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
..
gi 153791547 608 HD 609
Cdd:COG4161 225 AS 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
406-606 |
1.46e-27 |
|
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: 111.62 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVK---SGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQ---DIR-TINVRYLREIIGVVSQEPVLFA- 477
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 TTIAENIRYGREDVTMDEIEKAVKEANAYdfiMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 557
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVDELLDL---LGLDH----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153791547 558 DTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQG 606
Cdd:cd03297 163 DRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1049-1239 |
1.48e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 112.95 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEI---KQLNVQwLRAQLGIVSQEPILFD 1120
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYGDNSRVVSYEEIVRAAKEANIHQfiDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 153791547 1201 ALDTESEKVVQEALDKAREGRTCIVIAHrlsTIQNADLI 1239
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
388-603 |
1.64e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 109.83 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-I 466
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQepvlfattiaenirygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPK 546
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 547 ILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIV 603
Cdd:cd03216 103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1047-1260 |
1.89e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 112.98 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA---QLGIVSQepilfDC-- 1121
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ-----DSps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 ------SIAENIAygdnSRVVSYEEIVRAAKEANIHQFID--SLPDKYNTRVgdkGTQLSGGQKQRIAIARALVRQPHIL 1193
Cdd:TIGR02769 100 avnprmTVRQIIG----EPLRHLTSLDESEQKARIAELLDmvGLRSEDADKL---PRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1194 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQK 1260
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1044-1245 |
1.99e-27 |
|
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: 111.65 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1044 PSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQ----LGIVSQEPILF 1119
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1120 DCSIAENIAYGDNSRVVSYEEIVRAAkeaNIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1199
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153791547 1200 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIQNG 1245
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1042-1205 |
2.10e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.03 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1042 TRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVFLDGKEIKQLNVQwlRAQLGIVSQEPIL 1118
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1119 FD-CSIAENIAYGDNSRvvsyeeIVRAAKEANIHQFIDS--LPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLL 1195
Cdd:COG4136 88 FPhLSVGENLAFALPPT------IGRAQRRARVEQALEEagLAGFADRDPA----TLSGGQRARVALLRALLAEPRALLL 157
|
170
....*....|
gi 153791547 1196 DEATSALDTE 1205
Cdd:COG4136 158 DEPFSKLDAA 167
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1031-1258 |
2.61e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG 1110
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEP--ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANIHqfIDSLpdKYNTRvgdKGTQLSGGQKQRIAIARALVR 1188
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLA--VNML--DFKTR---EPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1189 QPHILLLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:PRK13642 158 RPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
388-611 |
2.93e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.43 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-I 466
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFAT-TIAENIRYGREDVT---MD--EIEKAVKEANAYdfiMKLPHQFDTLVGErgaqLSGGQKQRIAIARA 540
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRgglIDwrAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 541 LVRNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:COG1129 155 LSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
388-606 |
4.06e-27 |
|
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: 117.48 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPS-RKEVQILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLMQRLYDPLDGMVSIDGQDIRTINVRYL 462
Cdd:COG4172 7 LSVEDLSVAFGQgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 463 REI----IGVVSQEPV-----LFatTI----AENIR----YGREDVT------MDE--IEKAVKEANAYdfimklPHQfd 517
Cdd:COG4172 87 RRIrgnrIAMIFQEPMtslnpLH--TIgkqiAEVLRlhrgLSGAAARaralelLERvgIPDPERRLDAY------PHQ-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 518 tlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN- 590
Cdd:COG4172 157 ---------LSGGQRQRVMIAMALANEPDLLIADEPTTALD----VTVQAQiLDllkdlQRELGMALLLITHDLGVVRRf 223
|
250
....*....|....*.
gi 153791547 591 ADVIAGFDGGVIVEQG 606
Cdd:COG4172 224 ADRVAVMRQGEIVEQG 239
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1031-1252 |
5.87e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.20 E-value: 5.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPSiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS---VFLDGKEIKQLNVQWLRA 1107
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEP--ILFDCSIAENIAYGDNSRVVSYEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIA 1181
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1182 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGT 1252
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1049-1252 |
6.02e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.06 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--KQLNVQWLRAQLGIVSQEP--ILFDCSIA 1124
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIAYGDNSRVVSYEEIVRAAKEAnihqfIDSLPDKYNTrVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDEATSALD 1203
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1204 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGT 1252
Cdd:PRK13637 177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
382-630 |
9.24e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 9.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 382 DNIqgnLEFKNIHFSYPSrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRY 461
Cdd:PRK13648 5 NSI---IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQ 533
Cdd:PRK13648 81 LRKHIGIVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPNA-----------LSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 534 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQG----- 606
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGtptei 229
|
250 260
....*....|....*....|....*..
gi 153791547 607 -NHDELMREKG--IYFKLVMTQTAGNE 630
Cdd:PRK13648 230 fDHAEELTRIGldLPFPIKINQMLGHQ 256
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
381-615 |
9.42e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.48 E-value: 9.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 381 PDNIqgnLEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQ--DIRTIN 458
Cdd:PRK13636 2 EDYI---LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 459 VRYLREIIGVVSQEP--VLFATTIAENIRYGREDVTM--DEIEKAVKEANAYDFIMKLPHQfdtlvgeRGAQLSGGQKQR 534
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 535 IAIARALVRNPKILLLDEATSALDTE--SEaVVQAALDKAREGRTTIVIA-HRLSTVR-NADVIAGFDGGVIVEQGNHDE 610
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
....*
gi 153791547 611 LMREK 615
Cdd:PRK13636 229 VFAEK 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
388-613 |
1.15e-26 |
|
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: 109.69 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPsrkEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINV-RYLREII 466
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFAT-TIAENIR---YGREDVtmDEIEKAVKEAnaYDFimklphqFDTLvGER----GAQLSGGQKQRIAIA 538
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLlgaYARRDR--AEVRADLERV--YEL-------FPRL-KERrrqrAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 539 RALVRNPKILLLDEATSALdteSEAVVQ---AALDKAREGRTTIVI----AHRLSTVrnADVIAGFDGGVIVEQGNHDEL 611
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGL---APLIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAEL 223
|
..
gi 153791547 612 MR 613
Cdd:COG0410 224 LA 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1048-1268 |
1.25e-26 |
|
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: 111.10 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENI 1127
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 -AYGDNSRvvsyEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1206
Cdd:cd03289 98 dPYGKWSD----EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1207 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVS 1268
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
385-606 |
1.43e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.00 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 385 QGNLEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLDGMVSIDGQDIRTINV 459
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 460 RYLREIIGVVSQEPVLFAT-TIAENIRYG----REDVTMDEIEKAVKEANAYdfiMKLPHQFDTLVGERGAQLSGGQKQR 534
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 535 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQG 606
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1031-1258 |
1.51e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.85 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN-VQWLRAQL 1109
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1110 GIVSQEP--ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEAnihqFIDSLPDKYNTRvgdKGTQLSGGQKQRIAIARALV 1187
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1188 RQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1036-1260 |
1.61e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.55 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1036 VVFNYPTRPSipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL--RAQLGIVS 1113
Cdd:PRK13639 7 LKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1114 QEP--ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEAnihqfidslpdkyNTRVGDKGTQ------LSGGQKQRIAIARA 1185
Cdd:PRK13639 85 QNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEA-------------LKAVGMEGFEnkpphhLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1186 LVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVIQNGKVKEHGTHQQLLAQK 1260
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1046-1258 |
1.92e-26 |
|
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: 109.30 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1046 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRAQLGI--VSQEPILF-DCS 1122
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 IAENIaygdnsRVVSYEEIVRAAKEANIHQFIDSLPD-KynTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1201
Cdd:COG0410 95 VEENL------LLGAYARRDRAEVRADLERVYELFPRlK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1202 LdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:COG0410 167 L---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
388-558 |
2.05e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.12 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI--RTINVRYlrei 465
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHQFDTLVGergaQLSGGQKQRIAIARALV 542
Cdd:PRK11432 80 ICMVFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALI 152
|
170
....*....|....*.
gi 153791547 543 RNPKILLLDEATSALD 558
Cdd:PRK11432 153 LKPKVLLFDEPLSNLD 168
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
388-583 |
3.60e-26 |
|
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: 107.98 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTiNVRYLREIIG 467
Cdd:cd03263 1 LQIRNLTKTYKK-GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFAT-TIAENIRY-----GREDVTMDEiekavkEANAYDFIMKLPHQFDTLVGergaQLSGGQKQRIAIARAL 541
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153791547 542 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH 583
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
388-609 |
3.76e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.56 E-value: 3.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDG------QDIRTINVRY 461
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQEPVLFA-TTIAENIrygredvtmdeIEKAVK-----EANAYDFIMKLphqFDTLVGERGA-----QLSGG 530
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNL-----------IEAPCRvlglsKDQALARAEKL---LERLRLKPYAdrfplHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 531 QKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNH 608
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAqIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
.
gi 153791547 609 D 609
Cdd:PRK11124 226 S 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1031-1247 |
4.33e-26 |
|
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: 108.97 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVfnyptrpsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRAQLG 1110
Cdd:COG0411 12 KRFGGLV----------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVS--QEPILF-DCSIAENIAYG--------------DNSRVVSYEEIVRAAKEANIHQFidSLPDKYNTRVGDkgtqLS 1173
Cdd:COG0411 81 IARtfQNPRLFpELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERV--GLADRADEPAGN----LS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1174 GGQKQRIAIARALVRQPHILLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1047-1245 |
4.43e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 114.90 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFL-DGKEIkqlnvqwlraqLgIVSQEPILFDCSIAE 1125
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 NIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLpdkynTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1205
Cdd:COG4178 445 ALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153791547 1206 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNG 1245
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1049-1245 |
4.72e-26 |
|
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: 107.94 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLraqlgIVSQEPILFD-CSIAENI 1127
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 AygdnsrvVSYEEIVRAAKEANIHQFIDSLPDKYN-TRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1205
Cdd:TIGR01184 76 A-------LAVDRVLPDLSKSERRAIVEEHIALVGlTEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153791547 1206 SEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIQNG 1245
Cdd:TIGR01184 149 TRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
388-606 |
5.47e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 107.28 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTvALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRtINVRYLREIIG 467
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFAT-TIAENIRY-----GREDVTMD-EIEKAVKEANAYDFimklphqfdtlVGERGAQLSGGQKQRIAIARA 540
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 541 LVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 606
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
402-612 |
5.71e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.52 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 402 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI-------------NVRYLREIIGV 468
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 469 VSQEPVLFA-TTIAENIRygREDVTMDEIEKAVKEANAYDFIMKLPHQfDTLVGERGAQLSGGQKQRIAIARALVRNPKI 547
Cdd:PRK10619 97 VFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 548 LLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNADVIAGF-DGGVIVEQGNHDELM 612
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1047-1259 |
6.34e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 114.01 E-value: 6.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA----QLGIVSQEPI- 1117
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1118 ----LFdcSIAENIAygdnsrvvsyeEIV-------RAAKEANIHQFIDS--LPDKyNTRVGDKGTQLSGGQKQRIAIAR 1184
Cdd:COG4172 104 slnpLH--TIGKQIA-----------EVLrlhrglsGAAARARALELLERvgIPDP-ERRLDAYPHQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1185 ALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:COG4172 170 ALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELF 245
|
..
gi 153791547 1258 AQ 1259
Cdd:COG4172 246 AA 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1031-1233 |
7.51e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.20 E-value: 7.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVFLDGK-EI-------KQLNV 1102
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFfnqniyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1103 QWLRAQLGIVSQEPILFDCSIAENIAYGdnSRVVSY------EEIVRAAKEANihqfidSLPDKYNTRVGDKGTQLSGGQ 1176
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYG--VKIVGWrpkleiDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1177 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTI 1233
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
400-606 |
9.76e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 106.97 E-value: 9.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 400 RKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQL-MQRLYDP--LDGMVSIDGQDIRtinvRYL-REIIGVVSQEPVL 475
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAiSGRVEGGgtTSGQILFNGQPRK----PDQfQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 476 FAT-TIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHqfDTLVG-ERGAQLSGGQKQRIAIARALVRNPKILLLDEA 553
Cdd:cd03234 93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 554 TSALDTESE-AVVQAALDKAREGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQG 606
Cdd:cd03234 171 TSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
143-358 |
1.13e-25 |
|
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: 108.34 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 143 IRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVL- 221
Cdd:cd18575 71 LRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVv 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 222 --GLSAGIWAKILSSFTDKELhayAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEA-----KRLGIKKAITAnis 294
Cdd:cd18575 151 lpIILFGRRVRRLSRASQDRL---ADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAfaaalRRIRARALLTA--- 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 295 mgAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVF-FSVLIGAFSVGQASPNIEAFANARGAA 358
Cdd:cd18575 225 --LVIFLVFGAIVFVLWLGAHDVLAGRMSAGE-LSQFvFYAVLAAGSVGALSEVWGDLQRAAGAA 286
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1048-1258 |
1.14e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.53 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--------KQLNVQWLRAQLGIVSQEPILF 1119
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1120 DC-SIAENIAYGDnsrvVSYEEIVRAAKEANIHQFIdslpdkynTRVGDKGTQ------LSGGQKQRIAIARALVRQPHI 1192
Cdd:PRK11264 98 PHrTVLENIIEGP----VIVKGEPKEEATARARELL--------AKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1193 LLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:PRK11264 166 ILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
388-615 |
1.16e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.33 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYP--SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI----RTINVRY 461
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDeIEKAvkEANAYDFIMKLPHQFDTLvGERGAQLSGGQKQRIAIAR 539
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALDKAR--EGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 615
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
707-1004 |
1.29e-25 |
|
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: 108.29 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGglqpAFSVIFSKVVGVFTNGGPPETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 786
Cdd:cd18542 1 YLLAILALLLAT----ALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 787 MVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 866
Cdd:cd18542 77 DLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 867 AGVVEMKMLsGQALKDKKELEGS-GKIATEAIENFRTVVSLTRE----QKFETMYAQslqipYRNA-MKKAHVFGITFSF 940
Cdd:cd18542 155 FSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFAREdyeiEKFDKENEE-----YRDLnIKLAKLLAKYWPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 941 TQAMMYFSYAACFRFGAYLVTQQLMTFENvLLVFSAIVFG-AMAVGQVSSFAPDYAKATVSASHI 1004
Cdd:cd18542 229 MDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFISYLWMlIWPVRQLGRLINDMSRASASAERI 292
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
406-598 |
1.62e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.56 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPL-----DGMVSIDGQDI--RTINVRYLREIIGVVSQEPVLFAT 478
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 479 TIAENIRYGRE----DVTMDE-IEKAVKEANAYDFIMklphqfDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 553
Cdd:PRK14243 106 SIYDNIAYGARingyKGDMDElVERSLRQAALWDEVK------DKL-KQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153791547 554 TSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFD 598
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFN 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
140-341 |
1.62e-25 |
|
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: 108.28 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 140 IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISP 219
Cdd:cd18552 71 VRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 220 VLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAF 299
Cdd:cd18552 151 LAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153791547 300 LLIYASYALAFWYGTSLVISKEYSIGQvltvFFSVLIGAFSV 341
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1045-1259 |
2.30e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.48 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1045 SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW-LRAQLGIVSQEPilfDCSI 1123
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNP---DNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 A-----ENIAYGDNSRVVSYEEIVR----AAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILL 1194
Cdd:PRK13633 99 VativeEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1195 LDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1052-1251 |
2.43e-25 |
|
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: 105.27 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1052 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAQLGIVSQEPILF-DCSIAENIAYG 1130
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1131 DNSRV----VSYEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1206
Cdd:cd03298 95 LSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 153791547 1207 EKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1047-1257 |
2.45e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.78 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPIL-FDCSIAE 1125
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 NIAYGdnsrvvsyeeivRAAKEANIHQFiDSLPDKYNTRVGDKG------TQLSGGQKQRIAIARALVR------QPHIL 1193
Cdd:PRK13548 96 VVAMG------------RAPHGLSRAED-DALVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1194 LLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:PRK13548 163 LLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
388-611 |
2.95e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 108.26 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKN--IHFSYPSRKEV-----QILK---GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI 457
Cdd:PRK15079 9 LEVADlkVHFDIKDGKQWfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 458 NVRYLREI---IGVVSQEPV-------LFATTIAENIRYGREDVTMDEIEKAVKEANAY-----DFIMKLPHQFdtlvge 522
Cdd:PRK15079 89 KDDEWRAVrsdIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPHEF------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 523 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDG 599
Cdd:PRK15079 163 -----SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAqVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYL 237
|
250
....*....|..
gi 153791547 600 GVIVEQGNHDEL 611
Cdd:PRK15079 238 GHAVELGTYDEV 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
388-611 |
3.16e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.13 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK-------EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN-- 458
Cdd:PRK11308 6 LQAIDLKKHYPVKRglfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 459 -VRYLREIIGVVSQ-----------------EPVLFATTIAENIRygREDVtMDEIEKAVKEANAYDfimKLPHQFdtlv 520
Cdd:PRK11308 86 aQKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSLSAAER--REKA-LAMMAKVGLRPEHYD---RYPHMF---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 521 gergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIV-IAHRLSTVRNA--DVIAG 596
Cdd:PRK11308 156 -------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEHIadEVMVM 228
|
250
....*....|....*
gi 153791547 597 FDGGViVEQGNHDEL 611
Cdd:PRK11308 229 YLGRC-VEKGTKEQI 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1045-1251 |
3.27e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1045 SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEP-IL 1118
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1119 FDCSIAENIAYGD--NSRVVSYEEIVRAAKEA-NIHQFIDSLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLL 1195
Cdd:PRK14247 95 PNLSIFENVALGLklNRLVKSKKELQERVRWAlEKAQLWDEVKDRLDAPAG----KLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1196 DEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVIQNGKVKEHG 1251
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
388-608 |
3.48e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.51 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKE-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN----VRYL 462
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 463 REIIGVVSQEPVLFA-TTIAENIRYgreDVTMDEIEKAVKEANAYDFIMKLphQFDTLVGERGAQLSGGQKQRIAIARAL 541
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 542 VRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNAD-VIAGFDGGVIVEQGNH 608
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAErVIEIRDGEIVRNPPAQ 228
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
140-333 |
3.79e-25 |
|
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: 107.13 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 140 IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISP 219
Cdd:cd18542 71 AYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 220 VLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAF 299
Cdd:cd18542 151 FIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMD 230
|
170 180 190
....*....|....*....|....*....|....
gi 153791547 300 LLIYASYALAFWYGTSLVISKEYSIGQvLTVFFS 333
Cdd:cd18542 231 FLSGLQIVLVLWVGGYLVINGEITLGE-LVAFIS 263
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1052-1260 |
4.25e-25 |
|
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: 108.28 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1052 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYG-----DNSRVVSYEEIVRAAkeaNIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1201
Cdd:TIGR02142 96 LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1202 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQK 1260
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1048-1259 |
4.39e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.82 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-------QLNV------QWLRAQLGIVSQ 1114
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVadknqlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1115 EPILFD-CSIAENIAYGDN-----SRVVSYEEIVRAAKEANIHqfiDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVR 1188
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPIqvlglSKQEARERAVKYLAKVGID---ERAQGKYPV-------HLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1189 QPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1048-1249 |
4.39e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.21 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGKEIKQLN----VQWLRAQLGIVSQE----P 1116
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 ILfdcSIAEN------IAYGDNSRVvsyeeivRAAKEanihqfidsLpdkynTRVGDKG------TQLSGGQKQRIAIAR 1184
Cdd:COG4181 104 TL---TALENvmlpleLAGRRDARA-------RARAL---------L-----ERVGLGHrldhypAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1185 ALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVIQNGKVKE 1249
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
371-622 |
7.72e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 112.95 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 371 IDSFSKSGHKPDNIQ-GNLEFKNIHFSYpsRKEVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVS 448
Cdd:PTZ00243 1291 IEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 449 IDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREdVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLS 528
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYS 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 529 GGQKQRIAIARALV-RNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 607
Cdd:PTZ00243 1448 VGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
250
....*....|....*.
gi 153791547 608 HDEL-MREKGIYFKLV 622
Cdd:PTZ00243 1528 PRELvMNRQSIFHSMV 1543
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
406-613 |
7.76e-25 |
|
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: 104.44 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylrEI----IGVVSQEPVLFAT-TI 480
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIarlgIGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 481 AENIRYG-----REDVTMDEIEKAVKEANAYDF----IMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLD 551
Cdd:cd03219 93 LENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 552 EATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 613
Cdd:cd03219 169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
388-558 |
8.24e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.03 E-value: 8.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIRYGRedvtmdEIEKAVKEANAY-DFIMK--LPhqfDTLVGERGAQLSGGQKQRIAIARALVRN 544
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 153791547 545 PKILLLDEATSALD 558
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
388-606 |
9.48e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 103.60 E-value: 9.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSY-PSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTiNVRYLREII 466
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFA-TTIAENIRY--GREDVTMDEIEKAVKEanaydFIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVR 543
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYfaGLYGLKGDELTARLEE-----LADRL--GMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 544 NPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFDGGVIVEQG 606
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1047-1252 |
9.93e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.60 E-value: 9.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAQLGIVSQ--EPILFD 1120
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQIRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYGDNSRVVSYEEIVRAAKEA-NIHQFIDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1199
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1200 SALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGT 1252
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1031-1257 |
1.07e-24 |
|
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: 104.40 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-SVFLDGKEIKQLNVQWLRAQL 1109
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1110 GIVS---QEPILFDCSIAENIAYGDNSRVVSYEEI----VRAAKEAnIHQF-IDSLPDK-YNTrvgdkgtqLSGGQKQRI 1180
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFDSIGLYREPtdeqRERAREL-LELLgLAHLADRpFGT--------LSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1181 AIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVIQNGKVKEHGTHQ 1254
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAGPKE 228
|
...
gi 153791547 1255 QLL 1257
Cdd:COG1119 229 EVL 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
404-560 |
1.07e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.09 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 404 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLReiIGVVSQEPVLFA-TTIAE 482
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 483 NIRYG------REDVTMDEIEKAVkeanaydfiMKLPH--QFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 554
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
....*.
gi 153791547 555 SALDTE 560
Cdd:PRK10851 165 GALDAQ 170
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
102-361 |
1.47e-24 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 105.09 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 102 KLEEEMTTYAYYYTGIGAGVLIVAYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEG 181
Cdd:cd18784 30 KSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 182 IGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVI 261
Cdd:cd18784 110 VSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 262 AFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQvltvFFSVLIGAFSV 341
Cdd:cd18784 190 SFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLEL 265
|
250 260
....*....|....*....|....
gi 153791547 342 GQASPNIEA----FANARGAAYEV 361
Cdd:cd18784 266 GSCLESVGSvytgLMQAVGAAEKV 289
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1049-1259 |
1.48e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 106.20 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAQLGIVSQEPilfdcsiae 1125
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 niaYGD-NSR-VVSY--EE-------IVRAAKEANIHQFIdslpdkynTRVGDKGTQ-------LSGGQKQRIAIARALV 1187
Cdd:PRK11308 102 ---YGSlNPRkKVGQilEEpllintsLSAAERREKALAMM--------AKVGLRPEHydryphmFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1188 RQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1047-1251 |
1.64e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 102.24 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVFLDGKEIKQlnvQWLRAQLGIVSQEPILFDC-SI 1123
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 AENIAYgdnsrvvsyeeivrAAKeanihqfidsLpdkyntrvgdKGtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1203
Cdd:cd03213 100 RETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1204 TESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVIQNGKVKEHG 1251
Cdd:cd03213 144 SSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1047-1260 |
2.33e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.94 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPIL-FDCSIAE 1125
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 NIAYGdNSRVVSY--------EEIVRAAKEANihqFIDSLPDKyntRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1197
Cdd:PRK11231 96 LVAYG-RSPWLSLwgrlsaedNARVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1198 ATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLLAQK 1260
Cdd:PRK11231 165 PTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
388-558 |
2.88e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.79 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKE-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylReii 466
Cdd:COG4525 4 LTVRHVSVRYPGGGQpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFA-TTIAENIRYGredVTMDEIEKAVKEANAydfimklpHQFDTLVGERGA------QLSGGQKQRIAIAR 539
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARA--------EELLALVGLADFarrriwQLSGGMRQRVGIAR 147
|
170
....*....|....*....
gi 153791547 540 ALVRNPKILLLDEATSALD 558
Cdd:COG4525 148 ALAADPRFLLMDEPFGALD 166
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1031-1260 |
3.82e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.77 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--KQLNVQWLRAQ 1108
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1109 LGIVSQEP--ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLPDKyntrvgdKGTQLSGGQKQRIAIARAL 1186
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1187 VRQPHILLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVIQNGKVKEHGTHQQLLAQK 1260
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1048-1257 |
4.37e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.20 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---MAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILF-D 1120
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1201 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1046-1251 |
4.38e-24 |
|
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: 101.52 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1046 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlrAQLGIVSQEPILFD-CSIA 1124
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYPnLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIAYGDNSRVVSYEEIVRAAKEANIHQfidslpdkyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1204
Cdd:cd03268 91 ENLRLLARLLGIRKKRIDEVLDVVGLKD-----------SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153791547 1205 ESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:cd03268 160 DGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
392-599 |
4.78e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 101.64 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 392 NIHFSYPSrkEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMV----SIDGQDIRTINVRYLREIIG 467
Cdd:cd03290 5 NGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIRYGREdvTMDEIEKAVKEANAYD-FIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPK 546
Cdd:cd03290 83 YAAQKPWLLNATVEENITFGSP--FNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 547 ILLLDEATSALDTE-SEAVVQAALDK--AREGRTTIVIAHRLSTVRNAD-VIAGFDG 599
Cdd:cd03290 161 IVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADwIIAMKDG 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1031-1251 |
5.09e-24 |
|
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: 101.50 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAQLG 1110
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFD-CSIAENIAY-----GDNSRVVSyEEIVRAAKEANihqfidsLPDKYNTRVGdkgtQLSGGQKQRIAIAR 1184
Cdd:cd03264 76 YLPQEFGVYPnFTVREFLDYiawlkGIPSKEVK-ARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1185 ALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
388-614 |
5.31e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.14 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN-VRYLREII 466
Cdd:PRK13644 2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEP--VLFATTIAENIRYGREDVTMD--EIEKAVKEANAYDFIMKLPHQfdtlvgeRGAQLSGGQKQRIAIARALV 542
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 543 RNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
387-611 |
5.58e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 105.50 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 387 NLEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQdiRTINVRYLREII 466
Cdd:PRK11000 3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFA-TTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVR 543
Cdd:PRK11000 78 GMVFQSYALYPhLSVAENMSFGLKlaGAKKEEINQRVNQVAE---VLQLAH----LLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 544 NPKILLLDEATSALDTESEavVQ-----AALDKaREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALR--VQmrieiSRLHK-RLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1032-1228 |
5.77e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.63 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYP-TRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlrAQLG 1110
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFD-CSIAENIAYGDNSRVVSyeeivRAAKEANIHQFIdslpdkynTRVGDKGT------QLSGGQKQRIAIA 1183
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRLRGVP-----KAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153791547 1184 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1228
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
388-615 |
5.98e-24 |
|
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: 101.83 E-value: 5.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI-RTINVRYLREII 466
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFAT-TIAENIRYGREdvTMDEIEKAVKeanayDFIMKL-PHQFDTLvGERGAQLSGGQKQRIAIARALVRN 544
Cdd:TIGR03410 78 AYVPQGREIFPRlTVEENLLTGLA--ALPRRSRKIP-----DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREK 615
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1049-1259 |
6.22e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 105.18 E-value: 6.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGK----EIKQLNVQWLRAQLGIVSQEP 1116
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 ILFD-CSIAENIAYG-----DNSRVVSYEEIVRAAkeaNIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQP 1190
Cdd:COG4148 87 RLFPhLSVRGNLLYGrkrapRAERRISFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1191 HILLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:COG4148 153 RLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
388-615 |
6.50e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.40 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:PRK11231 3 LRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVL-FATTIAENIRYGR------------EDVTMdeIEKAVKEAnaydfimklphQFDTLVGERGAQLSGGQKQR 534
Cdd:PRK11231 80 LLPQHHLTpEGITVRELVAYGRspwlslwgrlsaEDNAR--VNQAMEQT-----------RINHLADRRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 535 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELM 612
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
...
gi 153791547 613 REK 615
Cdd:PRK11231 227 TPG 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1046-1228 |
6.53e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.30 E-value: 6.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1046 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlnVQWLRAQLGIVSQEPILF-DCSIA 1124
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIAYGDNSRVVSYEEIVRAAKE----ANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190
....*....|....*....|....*....|
gi 153791547 1201 ALDTESEKVVQ-EALD-KAREGRTCIVIAH 1228
Cdd:PRK11607 179 ALDKKLRDRMQlEVVDiLERVGVTCVMVTH 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1031-1260 |
7.14e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.37 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVvfNYPTRPSIPV----LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK----QLNV 1102
Cdd:PRK13641 3 IKFENV--DYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1103 QWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSYEEivraAKEANIhqfidslpdKYNTRVG------DKGT-QLS 1173
Cdd:PRK13641 81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1174 GGQKQRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHG 1251
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHA 227
|
....*....
gi 153791547 1252 THQQLLAQK 1260
Cdd:PRK13641 228 SPKEIFSDK 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1041-1251 |
7.45e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 101.29 E-value: 7.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1041 PTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAQLGIVSQEPILFD 1120
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 -CSIAENIAY-GDnsrvvsyeeiVRAAKEANIHQFIDSLPDKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPHI 1192
Cdd:cd03266 92 rLTARENLEYfAG----------LYGLKGDELTARLEELADRLgmeellDRRVGG----FSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1193 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
138-358 |
7.70e-24 |
|
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: 103.28 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 138 RQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAI 217
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 218 SPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGA 297
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 298 AFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAA 358
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGAL 286
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1049-1258 |
8.52e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.18 E-value: 8.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAQLGIVSQ--EPILFDCS 1122
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 IAENIAYGDNSRVVSYEEIVRAAKEAnihqfID--SLPDKYNTRvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PRK13634 103 VEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLAR---SPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1201 ALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:PRK13634 175 GLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1263 |
8.72e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.78 E-value: 8.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1037 VFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ-------------LLERFY-----DPMAGSVFLDGKEIK 1098
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigdkkNNHELITNPYSKKIK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1099 qlNVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSYEEivrAAKEANIHQFIDSLPDKYNTRvgdKGTQLSGGQ 1176
Cdd:PRK13631 110 --NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSYLER---SPFGLSGGQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1177 KQRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGTHQ 1254
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPY 261
|
....*....
gi 153791547 1255 QLLAQKGIY 1263
Cdd:PRK13631 262 EIFTDQHII 270
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
409-606 |
8.83e-24 |
|
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: 100.65 E-value: 8.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 409 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENIRYG 487
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 488 R------EDVTMDEIEKAVKEANAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 561
Cdd:cd03298 95 LspglklTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 153791547 562 EAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 606
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
385-584 |
1.02e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.20 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 385 QGNLEFKNIHFSYPSRKEvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSI-DGQDIrtinvryLr 463
Cdd:COG4178 360 DGALALEDLTLRTPDGRP--LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 464 eiigVVSQEPVLFATTIAENIRY--GREDVTMDEIEKAVKEANaydfimkLPH---QFDTlVGERGAQLSGGQKQRIAIA 538
Cdd:COG4178 430 ----FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGHlaeRLDE-EADWDQVLSLGEQQRLAFA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153791547 539 RALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHR 584
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1048-1251 |
1.18e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.84 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEIKQLNVQWL--RAQLGIVSQEPILF- 1119
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1120 DCSIAENIAYGdnsrvVSYEEIVRAAKEanIHQFID------SLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHIL 1193
Cdd:PRK14267 99 HLTIYDNVAIG-----VKLNGLVKSKKE--LDERVEwalkkaALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1194 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlSTIQNA---DLIVVIQNGKVKEHG 1251
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
401-583 |
1.39e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 100.59 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 401 KEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQ----DI-----RTI-NVRylREIIGVVS 470
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLaqaspREIlALR--RRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 471 QepvlFATTIAeniRYGREDVTMDE-IEKAVKEANAYDFIMKLPHQFDtlVGERGAQL-----SGGQKQRIAIARALVRN 544
Cdd:COG4778 100 Q----FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIAD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIV-IAH 583
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
390-615 |
1.40e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 390 FKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGqdirtiNVRylreiIGVV 469
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 470 SQEPVLFAT-TIAENIRYGREDVT-----MDEIEKAVK-----------------EANAYDF-------IMKL---PHQF 516
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELRaleaeLEELEAKLAepdedlerlaelqeefeALGGWEAearaeeiLSGLgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 517 DTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqaaldKAREGrTTIVIAH-R--LSTVr 589
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSHdRyfLDRV- 215
|
250 260
....*....|....*....|....*..
gi 153791547 590 nADVIAGFDGGVIVE-QGNHDELMREK 615
Cdd:COG0488 216 -ATRILELDRGKLTLyPGNYSAYLEQR 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
392-611 |
1.59e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.28 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 392 NIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQ------DIRTINVRYLREI 465
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFA-TTIAENIRYGREDVTMD---EIEKAVKEANAYDFIMKLPHqfDTLvGERGAQLSGGQKQRIAIARAL 541
Cdd:PRK14246 92 VGMVFQQPNPFPhLSIYDNIAYPLKSHGIKekrEIKKIVEECLRKVGLWKEVY--DRL-NSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 542 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1047-1258 |
1.95e-23 |
|
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: 100.31 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRAQLGI--VSQEPILF-DCSI 1123
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 AENIAYGDNSRVVSYEEIVRAAkEANIHQF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1202
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1203 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
388-606 |
2.12e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.74 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI----NVRY 461
Cdd:PRK13649 3 INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQ--EPVLFATTIAENIRYGRED--VTMDEIEKAVKEANAYDFIMklphqfDTLVGERGAQLSGGQKQRIAI 537
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 538 ARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQG 606
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1048-1251 |
2.13e-23 |
|
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: 99.66 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYGDNSRVVSYEEIVRAAKEAnIHQFidSLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1206
Cdd:cd03269 91 LVYLAQLKGLKKEEARRRIDEW-LERL--ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153791547 1207 EKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:cd03269 164 VELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1042-1249 |
2.15e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 101.30 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1042 TRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN----------VQWL------ 1105
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1106 ----RAQLGIVSQEPI--LFDCSIAENIAygdnsRVvsyEEIVRAAKEANIHqfIDSLPdkyntrvgdkgTQLSGGQKQR 1179
Cdd:PRK10419 101 avnpRKTVREIIREPLrhLLSLDKAERLA-----RA---SEMLRAVDLDDSV--LDKRP-----------PQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1180 IAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKE 1249
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1032-1228 |
2.37e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.93 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlrAQLGI 1111
Cdd:PRK11248 3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQ-EPILFDCSIAENIAYGDNSRVVSyeeivRAAKEANIHQFIdslpdkynTRVGDKGT------QLSGGQKQRIAIAR 1184
Cdd:PRK11248 75 VFQnEGLLPWRNVQDNVAFGLQLAGVE-----KMQRLEIAHQML--------KKVGLEGAekryiwQLSGGQRQRVGIAR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153791547 1185 ALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1228
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
388-606 |
2.71e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYP--SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIR----TINVRY 461
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPhqfDTLVGERGAQLSGGQKQRIAIAR 539
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLS---EDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 540 ALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHrlstvrNADVIAGFDGGVIV-EQG 606
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVlEHG 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
388-606 |
2.84e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.69 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLDGMVSIDGQDIRTINVR-- 460
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 YLREIIGVVSQEPVLFA-TTIAENIRYG-------REDVTMDE-IEKAVKEANAYDfimklphQFDTLVGERGAQLSGGQ 531
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWD-------EVKDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 532 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHR-LSTVRNADVIAGFDGGVIVEQG 606
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1047-1260 |
2.98e-23 |
|
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: 101.47 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwlraqLGIVSQEPILFDCSIAEN 1126
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYGDNSRVVSYEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1206
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1207 EKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQK 1260
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
707-1004 |
3.33e-23 |
|
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: 101.36 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPpetqrqNSNLFSLLFLILgIISFITFFLQGFTFGKAGEILTKRLRY 786
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGS------SGGLLALLVALF-LLQAVLSALSSYLLGRTGERVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 787 MVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 866
Cdd:cd18551 74 RLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 867 AGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMY 946
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 947 FSYAACFRFGAYLVTQ------QLMTFenVLLVFSAIvfgaMAVGQVSSFAPDYAKATVSASHI 1004
Cdd:cd18551 232 LALLVVLGVGGARVASgaltvgTLVAF--LLYLFQLI----TPLSQLSSFFTQLQKALGALERI 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
704-1260 |
3.86e-23 |
|
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: 107.30 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 704 WPYFVVGIFCAI--INGGLQPafsVIFSKVVGVFTNGGPPEtqRQNSNLFSLLFLILGIISFItfFLQGFTFG--KAGEI 779
Cdd:TIGR01271 80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASYDPFNAPE--REIAYYLALGLCLLFIVRTL--LLHPAIFGlhHLGMQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 780 LTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGsrLAViFQNIANLGTGIIISLIygWQLT----- 854
Cdd:TIGR01271 153 MRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLA--LAH-FVWIAPLQVILLMGLI--WELLevngf 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 855 -----LLLLAIVPiiAIAGVVEMKMLSGQALKDKKELegsgKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMK 929
Cdd:TIGR01271 226 cglgfLILLALFQ--ACLGQKMMPYRDKRAGKISERL----AITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 930 KAHVfgitfsftqamMYFSYAACFRFGAYLVTQQLMTF---ENVLL--VFSAIVFGAMAVGQVSSFAPDYAKATVSASHI 1004
Cdd:TIGR01271 300 IAYL-----------RYFYSSAFFFSGFFVVFLSVVPYaliKGIILrrIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1005 IRIIEKTPEIDSYSTqgLKPNMLEGNVQF-------------------------------SGVVFNYPTRPSIPVLQGLS 1053
Cdd:TIGR01271 369 ITKIQDFLCKEEYKT--LEYNLTTTEVEMvnvtaswdegigelfekikqnnkarkqpngdDGLFFSNFSLYVTPVLKNIS 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1054 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwlraqLGIVSQEPILFDCSIAENIAYGDNS 1133
Cdd:TIGR01271 447 FKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGLSY 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1134 RVVSYEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEA 1213
Cdd:TIGR01271 514 DEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 153791547 1214 -LDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQK 1260
Cdd:TIGR01271 591 cLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
401-606 |
3.99e-23 |
|
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: 98.83 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 401 KEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI-RTINVRylrEIIGVVSQEPVLFAT- 478
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqKNIEAL---RRIGALIEAPGFYPNl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 479 TIAENIR-----YGREDVTMDEIEKAVKEANAYDfimklphqfdtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEA 553
Cdd:cd03268 88 TARENLRllarlLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 554 TSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 606
Cdd:cd03268 154 TNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
707-977 |
4.23e-23 |
|
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: 100.96 E-value: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETQRqnsnLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 786
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 787 MVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 866
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 867 AGVV---EMKMLSgqalkdKKELEGSGKIAT---EAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSF 940
Cdd:cd18552 155 PIRRigkRLRKIS------RRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPL 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 153791547 941 TQAMMYFSYAACFRFGAYLVTQQLMTFENVLLVFSAI 977
Cdd:cd18552 229 MELLGAIAIALVLWYGGYQVISGELTPGEFISFITAL 265
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1047-1243 |
4.42e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAEN 1126
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYGDNSRVVSYEEivrAAKEANIHQFidSLPDKyntrVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1205
Cdd:PRK10247 101 LIFPWQIRNQQPDP---AIFLDDLERF--ALPDT----ILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153791547 1206 SEKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIVVIQ 1243
Cdd:PRK10247 172 NKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
420-561 |
4.86e-23 |
|
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: 102.49 E-value: 4.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 420 ALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDG---QDIRT-INV-RYLREIiGVVSQEPVLFAT-TIAENIRYGRedvtm 493
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLpPHRRRI-GYVFQEARLFPHlSVRGNLLYGR----- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 494 deieKAVKEANAYDfimklphQFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 561
Cdd:COG4148 103 ----KRAPRAERRI-------SFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
406-583 |
5.01e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 99.08 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLreiigVVSQEPVLFA-TTIAENI 484
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 485 RYG----REDVTMDEIEKAVKEANAydfIMKLPHQFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 560
Cdd:TIGR01184 76 ALAvdrvLPDLSKSERRAIVEEHIA---LVGLTEAAD----KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180
....*....|....*....|....*
gi 153791547 561 SEAVVQAALDKARE--GRTTIVIAH 583
Cdd:TIGR01184 149 TRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1044-1246 |
5.32e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 104.63 E-value: 5.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1044 PSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA---GSVFLDGKEIKQLNVQWL-RAQLGIVSQEPILF 1119
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1120 -DCSIAENIAYGD---NSRVVSYEEIVRAAKE--ANIHQFIDSlpdkyNTRVGDkgtqLSGGQKQRIAIARALVRQPHIL 1193
Cdd:PRK13549 95 kELSVLENIFLGNeitPGGIMDYDAMYLRAQKllAQLKLDINP-----ATPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1194 LLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGK 1246
Cdd:PRK13549 166 ILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
388-615 |
5.68e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.85 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVL-FATTIAENIRYGREDVT--MDEIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVR- 543
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRAPHGlsRAEDDALVAAALA---QVDLAH----LAGRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 544 -----NPKILLLDEATSALD-TESEAVVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMREK 615
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTPE 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1048-1256 |
5.91e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.08 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYGdnSRVV-SYEEIVRAAKEANIHQFID-----SLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PRK10851 95 IAFG--LTVLpRRERPNAAAIKAKVTQLLEmvqlaHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1201 ALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVIQNGKVKEHGTHQQL 1256
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
381-618 |
6.14e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 381 PDNIQGN--LEFKNIH--FSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSID----GQ 452
Cdd:PRK13631 13 PNPLSDDiiLRVKNLYcvFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 453 DIRTI------------NVRYLREIIGVVSQEP--VLFATTIAENIRYGREDVTMDEIEkAVKEANAYDFIMKLPHQFDt 518
Cdd:PRK13631 93 KKNNHelitnpyskkikNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLDDSYL- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 519 lvgERGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIA 595
Cdd:PRK13631 171 ---ERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVI 247
|
250 260
....*....|....*....|...
gi 153791547 596 GFDGGVIVEQGNHDELMREKGIY 618
Cdd:PRK13631 248 VMDKGKILKTGTPYEIFTDQHII 270
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1053-1260 |
6.80e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEikQLNVQWLRAQLGIVSQEPILFD-CSIAENIAYGD 1131
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1132 NS--RVVSY--EEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1203
Cdd:PRK10771 97 NPglKLNAAqrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1204 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLLAQK 1260
Cdd:PRK10771 166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1047-1252 |
6.94e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.99 E-value: 6.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPMAGSVFLDGKEIKQLNVQwLRAQLGI-VS-QEPIlfdc 1121
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPV---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 siaeniaygdnsRV--VSYEEIVRAAKEAN------IHQFID---------SLPDKYNTR---VGdkgtqLSGGQKQRIA 1181
Cdd:COG0396 88 ------------EIpgVSVSNFLRTALNARrgeelsAREFLKllkekmkelGLDEDFLDRyvnEG-----FSGGEKKRNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1182 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIQNGKVKEHGT 1252
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
388-611 |
7.20e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 7.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:PRK13652 4 IETRDLCYSYSGSKEA--LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEP--VLFATTIAENIRYGREDVTMDE------IEKAVKEANAYDFIMKLPHqfdtlvgergaQLSGGQKQRIAIAR 539
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
406-612 |
7.26e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.80 E-value: 7.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI----IGVVSQEPVLFA-TTI 480
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 481 AENIRYGREdvtMDEIEKAVKEANAYDFIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 560
Cdd:PRK10070 124 LDNTAFGME---LAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 561 SEAVVQAALDK--AREGRTTIVIAHRL-STVRNADVIAGFDGGVIVEQGNHDELM 612
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
388-606 |
8.06e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.02 E-value: 8.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK--------EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYdPLDGMVSIDGQDIRTINV 459
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 460 RYL---REIIGVVSQEP---------VLfaTTIAENIRYGREDVTMDEIEKAVKEAnaydfiMKlphqfdtlvgERG--- 524
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------ME----------EVGldp 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 525 -------AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNA--DV 593
Cdd:PRK15134 417 etrhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQV 496
|
250
....*....|...
gi 153791547 594 IAGFDGGViVEQG 606
Cdd:PRK15134 497 IVLRQGEV-VEQG 508
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
406-611 |
9.34e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 98.21 E-value: 9.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTiNVRYLREIIGVVSQEPvlfattIAENIR 485
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 486 YGREDVTM---------DEIEKAVKEANAYdfiMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSA 556
Cdd:cd03265 89 TGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 557 LDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
409-615 |
9.82e-23 |
|
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: 101.34 E-value: 9.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 409 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDG---QDIRT-INVRYLREIIGVVSQEPVLFA-TTIAEN 483
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 484 IRYGREDVTMDEieKAVKEANAYDfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 563
Cdd:TIGR02142 96 LRYGMKRARPSE--RRISFERVIE-LLGIGH----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 564 VVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 615
Cdd:TIGR02142 169 EILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1044-1247 |
9.99e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.57 E-value: 9.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1044 PSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN-VQWLRAQLGIVSQEPILFDC- 1121
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYGDNSRVVSYEEIVRAAKEanihqfIDSLPDKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLL 1195
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1196 DEATSAL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIQNGKV 1247
Cdd:COG3845 166 DEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
387-558 |
1.21e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.07 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 387 NLEFKNIHFSYPSRkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRyLREIi 466
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRDI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFA-TTIAENIRYGREDVTM--DEIEKAVKEANAydfIMKLphqfDTLVGERGAQLSGGQKQRIAIARALVR 543
Cdd:PRK11650 79 AMVFQNYALYPhMSVRENMAYGLKIRGMpkAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 153791547 544 NPKILLLDEATSALD 558
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
388-611 |
1.25e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.45 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQilkGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINvRYLREIiG 467
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPI-N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKE----ANAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIARA 540
Cdd:PRK11607 95 MMFQSYALFPhMTVEQNIAFGlkQDKLPKAEIASRVNEmlglVHMQEFAKRKPHQ-----------LSGGQRQRVALARS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 541 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1053-1257 |
1.80e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.65 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL----RAQLGIVSQE-PILFDCSIAENI 1127
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 AYGDNSRVVSYEE----IVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1203
Cdd:PRK10070 128 AFGMELAGINAEErrekALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1204 TESEKVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1042-1257 |
2.42e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.07 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1042 TRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPIL-FD 1120
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYGDN---SRVVSYEEIVRAAKE-----ANIHQFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARALVRQPHI 1192
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVEramerTGVAQFADR-----------PVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1193 LLLDEATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:PRK09536 161 LLLDEPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
399-560 |
3.03e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.40 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 399 SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP---LDGMVSIDGQDIRTINVrYLREIiGVVSQEPVL 475
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA-EQRRI-GILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 476 FA-TTIAENIRYG-REDVTM----DEIEKAVKEANaydfimkLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILL 549
Cdd:COG4136 88 FPhLSVGENLAFAlPPTIGRaqrrARVEQALEEAG-------LAGFADRDP----ATLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 153791547 550 LDEATSALDTE 560
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1026-1247 |
3.41e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.46 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1026 MLE-GNVQfsgVVFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqW 1104
Cdd:COG1101 1 MLElKNLS---KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1105 LRAQL-GIVSQEPILFDC---SIAEN--IAYGDNSRvvsyEEIVRAAKEANIHQFIDS-------LPDKYNTRVGdkgtQ 1171
Cdd:COG1101 77 KRAKYiGRVFQDPMMGTApsmTIEENlaLAYRRGKR----RGLRRGLTKKRRELFRELlatlglgLENRLDTKVG----L 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1172 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGKV 1247
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
388-589 |
3.89e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.64 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL---YDPLDGMVSIDGQDIRtinvrylre 464
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKST---LMKILyglYQPDSGEILIDGKPVR--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 I----------IGVVSQEPVLFAT-TIAENIRYGREDVT-----MDEIEKAVKE-ANAYDFIMKLphqfDTLVGergaQL 527
Cdd:COG3845 71 IrsprdaialgIGMVHQHFMLVPNlTVAENIVLGLEPTKggrldRKAARARIRElSERYGLDVDP----DAKVE----DL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 528 SGGQKQRIAIARALVRNPKILLLDEATSALdTESEAV-VQAALDK-AREGRTTIVIAHRLSTVR 589
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVL-TPQEADeLFEILRRlAAEGKSIIFITHKLREVM 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1044-1242 |
4.11e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1044 PSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlraqlgiVSQEPILFDCSI 1123
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 AENIAYGDNSRVVSYEEIVRAAKEAnihqFIDSLpdkynTRVGDKG------TQLSGGQKQRIAIARALVRQPHILLLDE 1197
Cdd:NF040873 75 RDLVAMGRWARRGLWRRLTRDDRAA----VDDAL-----ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153791547 1198 ATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVI 1242
Cdd:NF040873 146 PTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1048-1254 |
4.23e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP------MAGSVFLDGKEIKQLNVQWLRAQLGIVSQE----PI 1117
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPrsgtlnIAGNHFDFSKTPSDKAIRELRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1118 LfdcSIAENIAYGDnSRV--VSYEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPH 1191
Cdd:PRK11124 97 L---TVQQNLIEAP-CRVlgLSKDQALARAEKLlerlRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1192 ILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQ 1254
Cdd:PRK11124 162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
48-585 |
5.07e-22 |
|
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: 103.45 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 48 LYMLVGTLAAIIHGVALPLMMLIFgdMTDSFASVGNVSKNSTNMSEADkrAMFAKLEEEMTTYA--YYYTGIGAGVLIVA 125
Cdd:TIGR01271 867 VFVLIFCLVIFLAEVAASLLGLWL--ITDNPSAPNYVDQQHANASSPD--VQKPVIITPTSAYYifYIYVGTADSVLALG 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 126 YIQ---VSFWCLAAGRQIHKirqKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGG-FI 201
Cdd:TIGR01271 943 FFRglpLVHTLLTVSKRLHE---QMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAiFV 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 202 IGFTRGWkltlVILAISPVLGLSAGIWAKIL-SSFTDKELHAYAKAGAVAEEV--LAAIRTVIAFGGQKkelerYNNNLE 278
Cdd:TIGR01271 1020 VSVLQPY----IFIAAIPVAVIFIMLRAYFLrTSQQLKQLESEARSPIFSHLItsLKGLWTIRAFGRQS-----YFETLF 1090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 279 EaKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVIS------KEYSIGQVLTVFFSVLiGAFSVGQASpNIEAFA 352
Cdd:TIGR01271 1091 H-KALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAigtnqdGEGEVGIILTLAMNIL-STLQWAVNS-SIDVDG 1167
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 353 NARGAAyEVFKIIDnKPSIDSFSKSGHKPDNIQGNLEFKNIHFS--YPSRKEVQ--------------ILKGLNLKVKSG 416
Cdd:TIGR01271 1168 LMRSVS-RVFKFID-LPQEEPRPSGGGGKYQLSTVLVIENPHAQkcWPSGGQMDvqgltakyteagraVLQDLSFSVEGG 1245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 417 QTVALVGNSGCGKSTTVQLMQRLYDPlDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI----RYGREdvt 492
Cdd:TIGR01271 1246 QRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdpyeQWSDE--- 1321
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 493 mdEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA 572
Cdd:TIGR01271 1322 --EIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS 1399
|
570
....*....|...
gi 153791547 573 REGRTTIVIAHRL 585
Cdd:TIGR01271 1400 FSNCTVILSEHRV 1412
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1034-1258 |
5.68e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.39 E-value: 5.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1034 SGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--KQLNVQWLRAQLGI 1111
Cdd:PRK13638 5 SDLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQEP--ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANihqfidSLPDKYNTRvgDKGTQ-LSGGQKQRIAIARALVR 1188
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAL------TLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1189 QPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1040-1274 |
8.44e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.93 E-value: 8.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1040 YPTRPSIpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVfldgkeikqlnvqWLRAQLGIVSQEPILF 1119
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1120 DCSIAENIAYGDNSRVVSYEEIVRAAK-EANIHQfidsLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1198
Cdd:PTZ00243 734 NATVRGNILFFDEEDAARLADAVRVSQlEADLAQ----LGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1199 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQlLAQKGIYFSMVSVQAGAK 1274
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAELKENK 885
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1030-1203 |
9.14e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 98.38 E-value: 9.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1030 NVQFSGVVFNYPTRpsIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpMAGSVFLDGKEIKQLnvqwlr 1106
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1107 aqlgivsqEPILFDC-------------SIAENIAYGDNSRVVSYEEIVR----AAKEANIHQFIDSLPdkyntrvgdkg 1169
Cdd:PRK11650 72 --------EPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKP----------- 132
|
170 180 190
....*....|....*....|....*....|....
gi 153791547 1170 TQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1203
Cdd:PRK11650 133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1031-1252 |
1.07e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.73 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVvfNYPTRPSIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNV 1102
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1103 QWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSYEEIVRAAKE-----ANIHQFIDSLPdkyntrvgdkgTQLSGG 1175
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1176 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGT 1252
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1038-1272 |
1.09e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 102.36 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1038 FNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdgkeikqlnvqwLRAQLGIVSQEPI 1117
Cdd:PLN03232 622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1118 LFDCSIAENIAYGDNSRVVSYEeivRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1197
Cdd:PLN03232 690 IFNATVRENILFGSDFESERYW---RAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1198 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQlLAQKGIYFSMVSVQAG 1272
Cdd:PLN03232 767 PLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
388-612 |
1.31e-21 |
|
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: 94.92 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINV-RYLREII 466
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAVK-EANAYDF-IMKLPHQFdtlvgerGAQLSGGQKQRIAIARALVR 543
Cdd:cd03218 78 GYLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKlEELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 544 NPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HR----LSTVRNADVIagFDGGVIVEqGNHDELM 612
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYII--YEGKVLAE-GTPEEIA 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1030-1253 |
1.37e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.46 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1030 NVQFSGVVFNYPtrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG------KEIKQLNVQ 1103
Cdd:COG4161 2 SIQLKNINCFYG---SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1104 WLRAQLGIVSQE----PILfdcSIAENIAYG-----DNSRVVSYEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSG 1174
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1175 GQKQRIAIARALVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGT 1252
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
.
gi 153791547 1253 H 1253
Cdd:COG4161 225 A 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
388-614 |
1.62e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.13 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSypsRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQR-LYDPLDGMVSIDGQDI--RTINVR--- 460
Cdd:COG0396 1 LEIKNLHVS---VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHpKYEVTSGSILLDGEDIleLSPDERara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 -------YLREIIGV-VSQepvlFATTIAENIRygREDVTMDEIEKAVKEANAydfIMKLPHQFdtlvGERG--AQLSGG 530
Cdd:COG0396 78 giflafqYPVEIPGVsVSN----FLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 531 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQGN 607
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
....*..
gi 153791547 608 HdELMRE 614
Cdd:COG0396 225 K-ELALE 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1046-1245 |
1.64e-21 |
|
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: 94.81 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1046 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEiKQLNV------QWL---RAQLGIVSQ-- 1114
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-GWVDLaqasprEILalrRRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1115 -------------EPILfdcsiaeniaygdnSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyNTrvgdkgtqLSGGQK 1177
Cdd:COG4778 103 rviprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLPERLWDLPP--AT--------FSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1178 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIQNG 1245
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
389-618 |
1.80e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.15 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 389 EFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGV 468
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 469 VSQEPVlFAT--TIAENIRYGR----------EDvtmdeiEKAVKEANAYDFIMKLPHQF-DtlvgergaQLSGGQKQRI 535
Cdd:COG4604 80 LRQENH-INSrlTVRELVAFGRfpyskgrltaED------REIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 536 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK-ARE-GRTTIVIAHRLstvrN-----ADVIAGFDGGVIVEQGNH 608
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTP 220
|
250
....*....|...
gi 153791547 609 DELMRE---KGIY 618
Cdd:COG4604 221 EEIITPevlSDIY 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1048-1247 |
1.88e-21 |
|
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: 94.65 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVFLDGKEIKQlnVQWLRaQLGIVSQEPILFDC-SI 1123
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 AENIAYGDNSRV-VSYEEIVRAAKEAnihqfIDSLPDKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSA 1201
Cdd:cd03234 99 RETLTYTAILRLpRKSSDAIRKKRVE-----DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153791547 1202 LDTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVIQNGKV 1247
Cdd:cd03234 174 LDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
388-605 |
1.91e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 99.69 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-I 466
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFAT-TIAENIRYGREDVT-MDEIE--KAVKEANAYDFIMKLPHQFDTLVGErgaqLSGGQKQRIAIARALV 542
Cdd:PRK10762 82 GIIHQELNLIPQlTIAENIFLGREFVNrFGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 543 RNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRNA--DVIAGFDGGVIVEQ 605
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIFEIcdDVTVFRDGQFIAER 223
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1048-1252 |
1.94e-21 |
|
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: 94.51 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAQLGI--VSQEPILF-DCSIA 1124
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIAYGdnsrvvsYEeiVRAAKEANIHQFIDSL-P---DKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:TIGR03410 94 ENLLTG-------LA--ALPRRSRKIPDEIYELfPvlkEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1201 ALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGT 1252
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
388-615 |
2.29e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI----RTINVRY 461
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPHQ------FDtlvgergaqLSGGQKQ 533
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEEllarspFE---------LSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 534 RIAIARALVRNPKILLLDEATSALDTESEAVVQ---AALDKaREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHD 609
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*.
gi 153791547 610 ELMREK 615
Cdd:PRK13634 232 EIFADP 237
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
386-585 |
2.55e-21 |
|
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: 95.31 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 386 GNLEFKNIHFSYPSRKEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDpLDGMVSIDGQDIRTINVRYLREI 465
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFATTIAENIR-YGREdvTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRN 544
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 585
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
396-592 |
3.25e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 396 SYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGqdirTINVRYLREIIGVVSQEPVl 475
Cdd:NF040873 1 GYGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 476 fatTIAENI------------RYGREDvtmdeiEKAVKEAnaydfIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVR 543
Cdd:NF040873 73 ---TVRDLVamgrwarrglwrRLTRDD------RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153791547 544 NPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRNAD 592
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1031-1250 |
3.65e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdGKEIKqlnvqwlraqLG 1110
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFDcsiaeniaygDNSRVvsYEEIVRAA---KEANIHQFIDSL---PDKYNTRVGDkgtqLSGGQKQRIAIAR 1184
Cdd:COG0488 382 YFDQHQEELD----------PDKTV--LDELRDGApggTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1185 ALVRQPHILLLDEATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVIQNGKVKEH 1250
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
388-585 |
3.75e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.77 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIH--FSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVrYLR-E 464
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 IIGVVSQEPVL---FATTIAEN------------IRYGREDVTMDEIEKAVKEANaydfiMKLPHQFDTLVGergaQLSG 529
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDTKVG----LLSG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 530 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRL 585
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1045-1246 |
5.19e-21 |
|
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: 98.36 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1045 SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGSVFLDGKEIKQLNVQWL-RAQLGIVSQEPILF-D 1120
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYGD----NSRVVSYEEIVRAAKEAnIHQFidSLPDKYNTR-VGDKGtqlsGGQKQRIAIARALVRQPHILLL 1195
Cdd:TIGR02633 93 LSVAENIFLGNeitlPGGRMAYNAMYLRAKNL-LREL--QLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1196 DEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGK 1246
Cdd:TIGR02633 166 DEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1049-1253 |
5.48e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.02 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAQLGIVSQEP-ILFDCSIA 1124
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIAYgdnsrvvsyEEIVRAAKEANIHQFIDSLPDKyntrVG--DKG----TQLSGGQKQRIAIARALVRQPHILLLDEA 1198
Cdd:PRK10908 98 DNVAI---------PLIIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1199 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVIQNGKVkeHGTH 1253
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1040-1259 |
5.74e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.48 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1040 YPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEP--I 1117
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1118 LFDCSIAENIAYGDNSRVVSYEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHIL 1193
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSAlhmlGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1194 LLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
142-331 |
6.24e-21 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 94.71 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 142 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVL 221
Cdd:cd18590 70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 222 GLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLL 301
Cdd:cd18590 150 AIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVL 229
|
170 180 190
....*....|....*....|....*....|
gi 153791547 302 IYASYALAFWYGTSLVISKEYSIGQVLTVF 331
Cdd:cd18590 230 QLGVQVLMLYCGRQLIQSGHLTTGSLVSFI 259
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1256 |
7.38e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.77 E-value: 7.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1037 VFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV---FLDGKEIKQL------------- 1100
Cdd:PRK13651 11 IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTkekekvleklviq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1101 --------NVQWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSYEEIVRAAKEanihqFID--SLPDKYNTRvgdK 1168
Cdd:PRK13651 91 ktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIElvGLDESYLQR---S 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1169 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVIQNGK 1246
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
250
....*....|.
gi 153791547 1247 -VKEHGTHQQL 1256
Cdd:PRK13651 243 iIKDGDTYDIL 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1046-1249 |
8.13e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.53 E-value: 8.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1046 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW---LRAQ-LGIVSQEPILFDC 1121
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIA-ENIAY-----GDNSRvVSYEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLL 1195
Cdd:PRK10584 103 LNAlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1196 DEATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIQNGKVKE 1249
Cdd:PRK10584 171 DEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
388-594 |
1.06e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.31 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLDGMVSIDGQDIRTINVRYL 462
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKST---LMKVLsgvypHGTYEGEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 463 REI-IGVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLphQFDTLVGERGAQLSGGQKQRIAIARA 540
Cdd:PRK13549 80 ERAgIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 541 LVRNPKILLLDEATSALdTESEAVVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVI 594
Cdd:PRK13549 158 LNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTI 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1048-1258 |
1.63e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVFLDGKEIKQLNVQWL---RAQLGIVSQEP---ILFDC 1121
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYGDNsrvVSYEEIVRAAKEAnihQFIDSLpdkynTRVG-DKGT------QLSGGQKQRIAIARALVRQPHILL 1194
Cdd:PRK15134 380 NVLQIIEEGLR---VHQPTLSAAQREQ---QVIAVM-----EEVGlDPETrhrypaEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1195 LDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:PRK15134 449 LDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1048-1258 |
2.28e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.85 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-----SVFLDGKEI-KQLNVQWLRAQLGIVSQEPILFDC 1121
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYGDNSRVVSYEEIVRAAKEANIHQFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1201
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1202 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLA 1258
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
388-584 |
2.72e-20 |
|
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: 89.14 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDirtiNVRYLreiig 467
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLLFL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 vvSQEPVLFATTIAENIRYGREDVtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKI 547
Cdd:cd03223 70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 153791547 548 LLLDEATSALDTESEAvvqAALDKAREGRTTIV-IAHR 584
Cdd:cd03223 113 VFLDEATSALDEESED---RLYQLLKELGITVIsVGHR 147
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
707-967 |
2.99e-20 |
|
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: 92.84 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETQrqNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 786
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQ--GLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 787 MVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLgTGIIISLIY-GWQLTLLLLAIVPIIA 865
Cdd:cd18544 79 DLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLL-IGILIAMFLlNWRLALISLLVLPLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 866 IAGVVeMKMLSGQALKDKKEL--EGSGKIAtEAIENFRTVVSLTREQKFETMYAQsLQIPYRNAMKKA-HVFGITFSFTQ 942
Cdd:cd18544 156 LATYL-FRKKSRKAYREVREKlsRLNAFLQ-ESISGMSVIQLFNREKREFEEFDE-INQEYRKANLKSiKLFALFRPLVE 232
|
250 260
....*....|....*....|....*
gi 153791547 943 AMMYFSYAACFRFGAYLVTQQLMTF 967
Cdd:cd18544 233 LLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1047-1197 |
4.26e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.86 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPMAGSVFLDGKEIKQLNVqWLRAQLGI--VSQEPIL 1118
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1119 F-DCSIAENIaygdnsRVVSyeEIVRAAKEAnIHQFIDSLPDKYN-TRVGD-KGTQLSGGQKQRIAIARALVRQPHILLL 1195
Cdd:COG1137 90 FrKLTVEDNI------LAVL--ELRKLSKKE-REERLEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFILL 160
|
..
gi 153791547 1196 DE 1197
Cdd:COG1137 161 DE 162
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
403-613 |
6.05e-20 |
|
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: 90.87 E-value: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 403 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI--------------RTI-NVRYLRE--- 464
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriarlgiaRTFqNPRLFPEltv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 ----IIGVVSQEPVLFATTIAENIRYGREDvtmDEIEKAVKEANAydfIMKLPHQFDTLVGErgaqLSGGQKQRIAIARA 540
Cdd:COG0411 97 lenvLVAAHARLGRGLLAALLRLPRARREE---REARERAEELLE---RVGLADRADEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 541 LVRNPKILLLDEATSAL-DTESEAVVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 613
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1033-1228 |
8.04e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 8.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1033 FSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlnvqwlRAQLGIV 1112
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1113 SQEPILFD-CSIAENIAYGDNSRV--------------VSYEEIVRAAK-------------EANIHQFIDSL---PDKY 1161
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRaleaeleeleaklaEPDEDLERLAElqeefealggweaEARAEEILSGLgfpEEDL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1162 NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH 1228
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
105-333 |
8.42e-20 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 91.32 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 105 EEMTTYAYYYTGIGAGVLIVAYIQVSFWcLAAGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIG 183
Cdd:cd18541 37 SQLLRYALLILLLALLIGIFRFLWRYLI-FGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 184 DKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAF 263
Cdd:cd18541 116 PGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAF 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 264 GGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVFFS 333
Cdd:cd18541 196 VQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGD-LVAFNS 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1035-1259 |
8.47e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.59 E-value: 8.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1035 GVVFnyptrPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQ-WLRAQLGIVS 1113
Cdd:PRK11288 11 GKTF-----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1114 QEPILF-DCSIAENIAYGD--NSR-VVSYEEIVRAAKEANIHQFIDSLPDkynTRVGDkgtqLSGGQKQRIAIARALVRQ 1189
Cdd:PRK11288 86 QELHLVpEMTVAENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1190 PHILLLDEATSALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIQNG-KVKEHG-----THQQLLA 1258
Cdd:PRK11288 159 ARVIAFDEPTSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGrYVATFDdmaqvDRDQLVQ 235
|
.
gi 153791547 1259 Q 1259
Cdd:PRK11288 236 A 236
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1038-1259 |
9.21e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.67 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1038 FNYPT----RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAQLgI-- 1111
Cdd:COG4167 14 FKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKH-Irm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQEPilfdcsiaeNIAYgdNSRVvsyeeivraakeaNIHQFIDsLPDKYNT----------------RVG-------DK 1168
Cdd:COG4167 92 IFQDP---------NTSL--NPRL-------------NIGQILE-EPLRLNTdltaeereerifatlrLVGllpehanFY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1169 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIV 1240
Cdd:COG4167 147 PHMLSSGQKQRVALARALILQPKIIIADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVL 221
|
250
....*....|....*....
gi 153791547 1241 VIQNGKVKEHGTHQQLLAQ 1259
Cdd:COG4167 222 VMHQGEVVEYGKTAEVFAN 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1047-1259 |
9.62e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 9.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----MAGSVFLDGKEIKQLNVQWLRA----QLGIVSQEPI 1117
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1118 L-------FDCSIAENIA-YGDNSRVVSYEEIVRAAKEANIHQfidslpdkYNTRVGDKGTQLSGGQKQRIAIARALVRQ 1189
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIRQ--------AAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1190 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
707-990 |
9.69e-20 |
|
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: 91.31 E-value: 9.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETQRQNSNLFSLLFLILGI--ISFITFFLQGFTFGKAGEILTKRL 784
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLylLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 785 RYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPII 864
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 865 AIAgvveMKMLSGQALKD-KKELEGSGKI---ATEAIENFRTVVSLTRE----QKFETMYAQslqipYRNAMKKAHVF-G 935
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREeeaiEEFDEINEE-----LYKASFKAQFYsG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 936 ITFSFTQAMMYFSYAACFRFGAYLVtqqlmtfenvllvfsaiVFGAMAVGQVSSF 990
Cdd:cd18547 230 LLMPIMNFINNLGYVLVAVVGGLLV-----------------INGALTVGVIQAF 267
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1026-1258 |
1.01e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1026 MLEGNVQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWL 1105
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1106 RAQLGIVSQ----EPilfDCSIAENIaygdnsRVVS-YEEIVRAAKEANIHQFID--SLPDKYNTRVGDkgtqLSGGQKQ 1178
Cdd:PRK13537 79 RQRVGVVPQfdnlDP---DFTVRENL------LVFGrYFGLSAAAARALVPPLLEfaKLENKADAKVGE----LSGGMKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1179 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQ 1255
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHA 224
|
...
gi 153791547 1256 LLA 1258
Cdd:PRK13537 225 LIE 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
388-612 |
1.05e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.28 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSY------PSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRY 461
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 ----LREI-------------IGVVSQEPVLFATTIAENIRYGRedvtmdeIEKAVKE-------ANAYdfimklPHQfd 517
Cdd:COG4167 85 rckhIRMIfqdpntslnprlnIGQILEEPLRLNTDLTAEEREER-------IFATLRLvgllpehANFY------PHM-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 518 tlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTVRN-ADVI 594
Cdd:COG4167 150 ---------LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSDKV 220
|
250
....*....|....*...
gi 153791547 595 AGFDGGVIVEQGNHDELM 612
Cdd:COG4167 221 LVMHQGEVVEYGKTAEVF 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1031-1260 |
1.70e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.22 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYP--TRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQW 1104
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1105 LRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSYEEIVRAAkeaniHQFIDSLPDKYNTrVGDKGTQLSGGQKQRIAI 1182
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDLGFSRDV-MSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1183 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 153791547 1260 K 1260
Cdd:PRK13646 237 K 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
388-614 |
2.01e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEV--QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN----VRY 461
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKE-----ANAYDFIMKLPHQfdtlvgergaqLSGGQK 532
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSPFE-----------LSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 533 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 610
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
....
gi 153791547 611 LMRE 614
Cdd:PRK13643 231 VFQE 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
402-583 |
2.06e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.68 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 402 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVR---YLR-EIIGVVSQEPVLFA 477
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 TTIAenirygREDVTMDEIEKAVKEANAYDFIMKLPHQFDtlVGER----GAQLSGGQKQRIAIARALVRNPKILLLDEA 553
Cdd:PRK10584 102 TLNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|..
gi 153791547 554 TSALDTES-EAVVQAALDKAREGRTT-IVIAH 583
Cdd:PRK10584 174 TGNLDRQTgDKIADLLFSLNREHGTTlILVTH 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1048-1259 |
2.07e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlRAQLGIVSQEPILF-DCSIAEN 1126
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAY-----GdnsrvVSYEEIVRAAKEanihqFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1199
Cdd:COG4152 92 LVYlarlkG-----LSKAEAKRRADE-----WLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1200 SALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:COG4152 158 SGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1032-1247 |
2.13e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYPT-RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL----R 1106
Cdd:PRK10535 6 ELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1107 AQLGIVSQE-PILFDCSIAENIAYGdnsrvVSYEEIVRAAKEANIHQFIDSLpdKYNTRVGDKGTQLSGGQKQRIAIARA 1185
Cdd:PRK10535 86 EHFGFIFQRyHLLSHLTAAQNVEVP-----AVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1186 LVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIQNGKV 1247
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1049-1256 |
2.35e-19 |
|
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: 88.20 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAQLGIVSQEPILFDCSIA-ENI 1127
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 AYgdNSRVVSYEEIVRAAKEANIHQFIDsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1207
Cdd:cd03265 95 YI--HARLYGVPGAERRERIDELLDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1208 KVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGTHQQL 1256
Cdd:cd03265 168 AHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1054-1251 |
2.46e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.63 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1054 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKqlNVQWLRAQLGIVSQEPILF-DCSIAENIAYGDN 1132
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMVFQSYALYpHLSVAENMSFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1133 SRVVSYEEIVRAAKE-ANIHQfIDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEkvVQ 1211
Cdd:PRK11000 102 LAGAKKEEINQRVNQvAEVLQ-LAHLLDR-------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153791547 1212 EALDKA----REGRTCIVIAH-RLSTIQNADLIVVIQNGKVKEHG 1251
Cdd:PRK11000 172 MRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
399-606 |
3.03e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.83 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 399 SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVL-FA 477
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 TTIAENIRYGRED-----VTMDE-----IEKAVKEANAYDFIMKlphQFDTlvgergaqLSGGQKQRIAIARALVRNPKI 547
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFADR---PVTS--------LSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 548 LLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 606
Cdd:PRK09536 161 LLLDEPTASLDINHQVrTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1048-1247 |
3.30e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.97 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----MAGSVFL-DGKEIKQLNVQWLRaqlgivsqepILFDC 1121
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLaEAREDTRLMFQDAR----------LLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYGdnsrvvsyeeiVRAAKEANIHQFIDS--LPDkyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1199
Cdd:PRK11247 97 KVIDNVGLG-----------LKGQWRDAALQALAAvgLAD----RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1200 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGKV 1247
Cdd:PRK11247 162 GALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
380-613 |
3.64e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.69 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 380 KPDNIQGNLEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINV 459
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 460 R-YLREIIGVVSQEPVLFATTIAENI------------RYGREDvtmdeiEKAVKEANAYDFIMKLPHQfdtLVGergaQ 526
Cdd:PRK10575 81 KaFARKVAYLPQQLPAAEGMTVRELVaigrypwhgalgRFGAAD------REKVEEAISLVGLKPLAHR---LVD----S 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 527 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-ARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIV 603
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMI 227
|
250
....*....|
gi 153791547 604 EQGNHDELMR 613
Cdd:PRK10575 228 AQGTPAELMR 237
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
753-1197 |
4.22e-19 |
|
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: 92.55 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 753 LLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATgSRLAVI 832
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLE--RIGAARLLAALTEDVRTISQAF-VRLPEL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 833 FQNIANlgtgIIISLIY-GWQLTLLLLAIVPIIAIAGVVEMKMLSgqalKDKKELEGSGKIATEAIENFRTVVSLTREQK 911
Cdd:COG4615 129 LQSVAL----VLGCLAYlAWLSPPLFLLTLVLLGLGVAGYRLLVR----RARRHLRRAREAEDRLFKHFRALLEGFKELK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 912 F-----ETMYAQSLQIP---YRNAMKKAHV-FGITFSFTQAMMYFSYAACFrfgaYLVTQQLMTFENVLLVFS-AIVFGA 981
Cdd:COG4615 201 LnrrrrRAFFDEDLQPTaerYRDLRIRADTiFALANNWGNLLFFALIGLIL----FLLPALGWADPAVLSGFVlVLLFLR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 982 MAVGQVSSFAPDYAKATVSASHIIRIIEKTPEIDSYSTQGLKPNMLEG--NVQFSGVVFNYPTRPSIP--VLQGLSLEVK 1057
Cdd:COG4615 277 GPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEgfTLGPIDLTIR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1058 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDcsiaeniaygdnsRVVS 1137
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-------------RLLG 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1138 YEEIVRAAKeanIHQFIDSL--PDKynTRVGDKG---TQLSGGQKQRIAIARALVRQPHILLLDE 1197
Cdd:COG4615 424 LDGEADPAR---ARELLERLelDHK--VSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1031-1253 |
4.32e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAQLG 1110
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQepilFD-----CSIAEN-IAYGDNSRVvSYEEIvraakEANIHQFID--SLPDKYNTRVGDkgtqLSGGQKQRIAI 1182
Cdd:PRK13536 118 VVPQ----FDnldleFTVRENlLVFGRYFGM-STREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1183 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIQNG-KVKEHGTH 1253
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
395-643 |
5.01e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 5.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 395 FSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQ--DIRTINVRYLREIIGVVSQE 472
Cdd:PRK13638 9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 473 P--VLFATTIAENIRYGRED--VTMDEIEKAVKEANaydfimklphqfdTLVGERGAQ------LSGGQKQRIAIARALV 542
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 543 RNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV----------RNADVIAGFDGGVIVEQGnhdEL 611
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyeisdavyvlRQGQILTHGAPGEVFACT---EA 229
|
250 260 270
....*....|....*....|....*....|..
gi 153791547 612 MREKGIYFKLVMTQTAgneiELGNEACKSKDE 643
Cdd:PRK13638 230 MEQAGLTQPWLVKLHT----QLGLPLCKTETE 257
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
392-594 |
5.38e-19 |
|
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: 88.76 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 392 NIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQdirtinvrylreiIGVVSQ 471
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 472 EPVLFATTIAENIRYGredVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 549
Cdd:cd03291 106 FSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153791547 550 LDEATSALD--TESEaVVQAALDKAREGRTTIVIAHRLSTVRNADVI 594
Cdd:cd03291 183 LDSPFGYLDvfTEKE-IFESCVCKLMANKTRILVTSKMEHLKKADKI 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1048-1251 |
5.46e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 86.43 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVFLDGKEIKQLNVQwLRAQLGI--VSQEPILFDcsi 1123
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 aeniayGdnsrvVSYEEIVRaakeanihqfidslpdkyNTRVGdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1203
Cdd:cd03217 91 ------G-----VKNADFLR------------------YVNEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1204 TESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIQNGKVKEHG 1251
Cdd:cd03217 137 IDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1049-1274 |
5.91e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.15 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGS-VFLDGKEIKQL-----NVQWLRAQLGIVSQEPILFD 1120
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 -CSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLpdkynTRVG------DKGTQLSGGQKQRIAIARALVRQPHIL 1193
Cdd:PRK09984 100 rLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1194 LLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLLAQK--GIYFSMVS 1268
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfdHLYRSINR 254
|
....*.
gi 153791547 1269 VQAGAK 1274
Cdd:PRK09984 255 VEENAK 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
388-610 |
6.17e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIdGQdirtiNVRylreiIG 467
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFAT--TIAENIRYGREDVTmdeiekavkEANAYDFIMKL---PHQFDTLVGErgaqLSGGQKQRIAIARALV 542
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 543 RNPKILLLDEATSALDTESEAVVQAALDkAREGrTTIVIAH-R--LSTVrnADVIAGFDGGVIVE-QGNHDE 610
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDD 516
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
400-582 |
6.70e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 400 RKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVR----YLREIIGVvsqEPVL 475
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAM---KPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 476 fatTIAENIR-----YGREDVTMDEiekavkeanAYDFiMKLPHQFDTlvgeRGAQLSGGQKQRIAIARALVRNPKILLL 550
Cdd:PRK13539 89 ---TVAENLEfwaafLGGEELDIAA---------ALEA-VGLAPLAHL----PFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|..
gi 153791547 551 DEATSALDTESEAVVqAALDKAREGRTTIVIA 582
Cdd:PRK13539 152 DEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
410-558 |
8.72e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 8.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 410 NLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENIRYG- 487
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 488 --------REDVTMDEIEKAVkeaNAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 558
Cdd:PRK10771 97 npglklnaAQREKLHAIARQM---GIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
388-606 |
9.99e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 9.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSR--------KEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN- 458
Cdd:PRK10261 314 LQVRNLVTRFPLRsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 459 --VRYLREIIGVVSQEPvlFAT---------TIAENIRY--------GREDVTMDEIEKAVKEANAYDFimklPHQFdtl 519
Cdd:PRK10261 394 gkLQALRRDIQFIFQDP--YASldprqtvgdSIMEPLRVhgllpgkaAAARVAWLLERVGLLPEHAWRY----PHEF--- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 520 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKARE-GRTTIVIAHRLSTV-RNADVIAG 596
Cdd:PRK10261 465 --------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGqIINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAV 536
|
250
....*....|
gi 153791547 597 FDGGVIVEQG 606
Cdd:PRK10261 537 MYLGQIVEIG 546
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1048-1252 |
1.04e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.79 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW---LRAQ-LGIVSQ-EPILFDCS 1122
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 IAENIAY----GDNSRVVSYEEIVRAAKEANIHQfidslpdkyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1198
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLAAVGLEH-----------RANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1199 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGT 1252
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
388-583 |
1.06e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.06 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYlreiiG 467
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQ-EPVLFATTIAENIRYGREdvtMDEIEKAVKEANAYDFIMKlphqfdtlVGERGA------QLSGGQKQRIAIARA 540
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153791547 541 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 583
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
388-615 |
1.33e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.22 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRK--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI-------- 457
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 458 ----------------NVRYLREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPHQFDtl 519
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 520 vgERGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA-REGRTTIVIAHRLSTV--RNADVIA 595
Cdd:PRK13651 160 --QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIF 237
|
250 260
....*....|....*....|
gi 153791547 596 GFDGGVIVEQGNHDELMREK 615
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSDNK 257
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1048-1247 |
1.62e-18 |
|
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: 84.79 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAQLGIVSQEP----ILFDCS 1122
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 IAENIAYGDnsrvvsyeeivraakeanihqfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1202
Cdd:cd03215 95 VAENIALSS---------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1203 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVIQNGKV 1247
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
388-552 |
2.14e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.85 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVrYLREI-- 465
Cdd:COG1137 4 LEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM-HKRARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IGVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAvKEANAY--DF-IMKLPHQfdtlvgeRGAQLSGGQKQRIAIARAL 541
Cdd:COG1137 80 IGYLPQEASIFRKlTVEDNILAVLELRKLSKKERE-ERLEELleEFgITHLRKS-------KAYSLSGGERRRVEIARAL 151
|
170
....*....|.
gi 153791547 542 VRNPKILLLDE 552
Cdd:COG1137 152 ATNPKFILLDE 162
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
388-606 |
2.55e-18 |
|
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: 85.02 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINvrylREIIG 467
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLF-ATTIAENIRY-GR-EDVTMDEIEKAVKEanaydFIMKL---PHQfdtlvGERGAQLSGGQKQRIAIARAL 541
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQlKGLKKEEARRRIDE-----WLERLelsEYA-----NKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 542 VRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQG 606
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNvELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
388-558 |
2.77e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.88 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTInvrylREIIG 467
Cdd:PRK11247 13 LLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFA-TTIAENIRYGREDVTMDEIEKAVKEANAYDfimklphqfdtLVGERGAQLSGGQKQRIAIARALVRNPK 546
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPG 153
|
170
....*....|..
gi 153791547 547 ILLLDEATSALD 558
Cdd:PRK11247 154 LLLLDEPLGALD 165
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1048-1257 |
2.99e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.19 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPIL-FDCSIAEN 1126
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 IAYG--------DNSRVVSYEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEA 1198
Cdd:PRK10253 102 VARGryphqplfTRWRKEDEEAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1199 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:PRK10253 171 TTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
105-333 |
3.24e-18 |
|
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: 86.67 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 105 EEMTTYAYYYTGIGAGVLIVAYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGD 184
Cdd:cd18544 38 QGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 185 KIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFG 264
Cdd:cd18544 118 GLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFN 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 265 GQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGqVLTVFFS 333
Cdd:cd18544 198 REKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG-VLYAFIQ 265
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1051-1256 |
4.40e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.43 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1051 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLrAQLGIVS--QEPILF-DCSIAENI 1127
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 AYGD----NSRVVS-------YEeivRAAKEA--NIHQFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHI 1192
Cdd:PRK11300 102 LVAQhqqlKTGLFSgllktpaFR---RAESEAldRAATWLErvGLLEHANRQAGN----LAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1193 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQL 1256
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
388-614 |
4.49e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.32 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVR---YLRE 464
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 iigvvsqEPVLFAT-TIAENIRY-GR-EDVTMDEIEKAVKEAnaydfimklphqFDTL-VGERGA----QLSGGQKQRIA 536
Cdd:COG4152 79 -------ERGLYPKmKVGEQLVYlARlKGLSKAEAKRRADEW------------LERLgLGDRANkkveELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 537 IARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1048-1252 |
4.78e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnVQWLraqLGI-VSQEPILfdcSIAEN 1126
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LELgAGFHPEL---TGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 I-----AYGdnsrvVSYEEIVRAAKE----ANIHQFIDsLPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1197
Cdd:COG1134 109 IylngrLLG-----LSRKEIDEKFDEivefAELGDFID-QPVKT----------YSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1198 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGT 1252
Cdd:COG1134 173 VLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
388-614 |
6.64e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVR-YLREII 466
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQE----PVLfatTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFD--TLVGErgaqLSGGQKQRIAIARA 540
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 541 LVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGF-DGGVI-----VEQGNHDELM 612
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRaEGRVILYVSHRMEEIfALCDAITVFkDGRYVatfddMAQVDRDQLV 234
|
..
gi 153791547 613 RE 614
Cdd:PRK11288 235 QA 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
409-606 |
7.02e-18 |
|
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: 90.07 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 409 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTiNVRYLREIIGVVSQEPVLFA-TTIAENIRYG 487
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 488 REdVTMDEIEKAVKEANAYDFIMKLPHQFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQA 567
Cdd:TIGR01257 1028 AQ-LKGRSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*....
gi 153791547 568 ALDKAREGRTTIVIAHRLStvrNADVIAgfDGGVIVEQG 606
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQG 1136
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1047-1252 |
1.08e-17 |
|
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: 89.69 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIkQLNVQWLRAQLGIVSQEPILFD-CSIAE 1125
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 NIAYGDNSRVVSYEEiVRAAKEANIHQfiDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1205
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-AQLEMEAMLED--TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1206 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVIQNGKVKEHGT 1252
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
143-333 |
1.13e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 85.25 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 143 IRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLG 222
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 223 -LSAGIWAKILSSFTdKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLL 301
Cdd:cd18563 158 wGSYFFWKKIRRLFH-RQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFL 236
|
170 180 190
....*....|....*....|....*....|..
gi 153791547 302 IYASYALAFWYGTSLVISKEYSIGqVLTVFFS 333
Cdd:cd18563 237 TSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLS 267
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1046-1251 |
1.14e-17 |
|
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: 83.35 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1046 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnVQW-LRAQLGIVSQ----EPILFD 1120
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPEltgrENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIaeniaYGdnsrvVSYEEIvrAAKEANIHQFIDsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:cd03220 109 GRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1201 ALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHG 1251
Cdd:cd03220 172 VGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1029-1259 |
1.31e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1029 GNVQFSGVVFNYPTRP--SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG-------KEIKQ 1099
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1100 lnVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSYEEIVRaakeaNIHQFID--SLPDKYNTRvgdKGTQLSGG 1175
Cdd:PRK13645 85 --VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYK-----KVPELLKlvQLPEDYVKR---SPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1176 QKQRIAIARALVRQPHILLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHG 1251
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233
|
250
....*....|....
gi 153791547 1252 ------THQQLLAQ 1259
Cdd:PRK13645 234 spfeifSNQELLTK 247
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1042-1249 |
1.43e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 87.54 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1042 TRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---MAGSVFLDGKE-----IKQlnvqwlRAQLGIV- 1112
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVcrfkdIRD------SEALGIVi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1113 -SQE----PILfdcSIAENIAYGdNSR----VVSYEEIVRAAKE--ANIhqfidSLPDKYNTRVGDKGTqlsgGQKQRIA 1181
Cdd:NF040905 83 iHQElaliPYL---SIAENIFLG-NERakrgVIDWNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1182 IARALVRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKE 1249
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
388-614 |
1.46e-17 |
|
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: 82.57 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSypsRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLDGMVSIDGQDIR--TINVR 460
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITdlPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 yLREIIGVVSQEPVLFA-TTIAENIRYgredvtmdeiekavkeanaydfimklphqfdtlVGErgaQLSGGQKQRIAIAR 539
Cdd:cd03217 75 -ARLGIFLAFQYPPEIPgVKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQGNhDELMRE 614
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1051-1256 |
1.49e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.53 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1051 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI-KQLNVQWL--RAQLGIVSQEPILF---DCSIA 1124
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDDEWRavRSDIQMIFQDPLASlnpRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIA------YGDNSRVvSYEEIVRA--AKEANIHQFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLD 1196
Cdd:PRK15079 119 EIIAeplrtyHPKLSRQ-EVKDRVKAmmLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1197 EATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQL 1256
Cdd:PRK15079 187 EPVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1032-1247 |
1.66e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVvfnyptrpsiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAQLGI 1111
Cdd:PRK15439 20 QYSGV----------EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 --VSQEPILF-DCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARALVR 1188
Cdd:PRK15439 89 ylVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1189 QPHILLLDEATSALD-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVIQNGKV 1247
Cdd:PRK15439 158 DSRILILDEPTASLTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
394-581 |
1.89e-17 |
|
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: 83.15 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 394 HFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIiGVV--SQ 471
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRI-GVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 472 EPVLFATTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILL 549
Cdd:cd03267 104 TQLWWDLPVIDSFYLLAAiyDLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190
....*....|....*....|....*....|...
gi 153791547 550 LDEATSALDTESEAVVQAALDKA-REGRTTIVI 581
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL 209
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
750-990 |
2.14e-17 |
|
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: 84.07 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 750 LFSLLFLILGIISFITFFLqgftFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRL 829
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 830 AVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlKDKkeLEGSGKIATEAIENFRTVVSL 906
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRAS-QDR--LADLSAFAEETLSAIKTVQAF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 907 TREQKFETMYAQSLQIPYRNAMKKAHVfgitfsftqammyfsyaacfrfgaylvtQQLMTFENVLLVFSAIVF------- 979
Cdd:cd18575 192 TREDAERQRFATAVEAAFAAALRRIRA----------------------------RALLTALVIFLVFGAIVFvlwlgah 243
|
250
....*....|....*
gi 153791547 980 ----GAMAVGQVSSF 990
Cdd:cd18575 244 dvlaGRMSAGELSQF 258
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1031-1229 |
2.19e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 81.05 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTrpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEikqlnvqwlraQLG 1110
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 IVSQEPILFDCSIAENIAYgdnsrvvsyeeivraakeanihqfidslPdkyntrvgdKGTQLSGGQKQRIAIARALVRQP 1190
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY----------------------------P---------WDDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHR 1229
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
383-643 |
2.23e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.29 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 383 NIQGNLEFKNIHFSYPSRK--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLydpldgMVSIDGQDI------ 454
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL------IISETGQTIvgdyai 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 455 -----RTINVRYLREIIGVVSQEP--VLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPHQFdtlVGERGAQL 527
Cdd:PRK13645 76 panlkKIKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 528 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVE 604
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 153791547 605 QGNHDELMREKGIYFKL---------VMTQTAGNEIELGNEACKSKDE 643
Cdd:PRK13645 232 IGSPFEIFSNQELLTKIeidppklyqLMYKLKNKGIDLLNKNIRTIEE 279
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
388-583 |
3.07e-17 |
|
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: 79.80 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDgqdiRTINVRYLreiig 467
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 vvsqepvlfattiaenirygredvtmdeiekavkeanaydfimklphqfdtlvgergAQLSGGQKQRIAIARALVRNPKI 547
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 153791547 548 LLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 583
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1043-1259 |
3.98e-17 |
|
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: 86.39 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1043 RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-------FLDGKEIKQLNVQWLRAQLGIVSQE 1115
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1116 PILF-DCSIAENIaygdnSRVVSYEEIVRAAKEANIHQF-IDSLPDKYNTRVGDKGT-QLSGGQKQRIAIARALVRQPHI 1192
Cdd:TIGR03269 374 YDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLkMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1193 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
388-615 |
4.00e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTiNVRYLREIIG 467
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVL-FATTIAEN-IRYGRE-DVTMDEIEKAVkeANAYDFiMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 544
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRYfGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 615
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1047-1252 |
4.11e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.44 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILfdcsiaen 1126
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 iaygdNSRV-----VSY--------------EEIVRAAkeanIHQF-IDSLPDKYNTrvgdkgtQLSGGQKQRIAIARAL 1186
Cdd:COG4604 87 -----NSRLtvrelVAFgrfpyskgrltaedREIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1187 VRQPHILLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVIQNGKVKEHGT 1252
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
388-614 |
4.34e-17 |
|
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: 86.01 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPS--RKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVS-------IDGQDIRTIN 458
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 459 VRYLREIIGVVSQEPVLFA-TTIAENIRygrEDVTM---DEI--EKAV--------KEANAYDFIMKLPHQfdtlvgerg 524
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLT---EAIGLelpDELarMKAVitlkmvgfDEEKAEEILDKYPDE--------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 525 aqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGV 601
Cdd:TIGR03269 428 --LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGK 505
|
250
....*....|...
gi 153791547 602 IVEQGNHDELMRE 614
Cdd:TIGR03269 506 IVKIGDPEEIVEE 518
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
399-582 |
4.71e-17 |
|
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: 80.87 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 399 SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFAT 478
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 479 TIAENIRYGREDV--TMDEIEKAVKEANaydfimkLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 556
Cdd:TIGR01189 89 SALENLHFWAAIHggAQRTIEDALAAVG-------LTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 153791547 557 LDTESEAVVQAALDkAREGRTTIVIA 582
Cdd:TIGR01189 158 LDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
751-969 |
5.37e-17 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 751 FSLLFLILGIISFITFFLQG-----FTFGKAGeiLTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAT 825
Cdd:cd18784 35 FSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 826 GSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVS 905
Cdd:cd18784 111 SLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 906 LTREQKFETMYAQSLQIPYRNAMKKAHVFGiTFSFTQAMMYFS-YAACFRFGAYLVTQQLMTFEN 969
Cdd:cd18784 191 FANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELAlTVSTLYYGGHLVITGQISGGN 254
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
116-340 |
5.51e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 83.33 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 116 GIGAGVLIVAYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMAT 195
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 196 FFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNN 275
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 276 NLEEAKRLGIK-KAITANISmGAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVFFSVLIGAFS 340
Cdd:cd18564 222 ENRKSLRAGLRaARLQALLS-PVVDVLVAVGTALVLWFGAWLVLAGRLTPGD-LLVFLAYLKNLYK 285
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
388-612 |
6.37e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTiNVRYLREIIG 467
Cdd:PRK13537 8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQ----EPVLfatTIAENIR-YGRE-DVTMDEIEKAVkeANAYDFiMKLPHQFDTLVGErgaqLSGGQKQRIAIARAL 541
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 542 VRNPKILLLDEATSALDTESEAVVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELM 612
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
142-326 |
7.27e-17 |
|
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: 82.59 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 142 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSK--------INEGIgdkigmffQAMATFFGGFIIGFTRGWKLTLV 213
Cdd:cd18574 76 RLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------RSVTQTVGCVVSLYLISPKLTLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 214 ILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRL--------GI 285
Cdd:cd18574 148 LLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLneklglgiGI 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153791547 286 KKAITaNISMGAAFLLIYasyalafWYGTSLVISKEYSIGQ 326
Cdd:cd18574 228 FQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGD 260
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
50-333 |
7.72e-17 |
|
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: 82.84 E-value: 7.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 50 MLVGTLAAIIHGVALPLMMLIFGDMTDSFASvGNVSKNSTNMSEadkramfakleeeMTTYAYYYTGIGAGVLIVAYIQv 129
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIE-GLGGGGGVDFSG-------------LLRILLLLLGLYLLSALFSYLQ- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 130 SFWCLAAGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGW 208
Cdd:cd18547 66 NRLMARVSQRTvYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 209 KLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELER---YNNNLEEAkrlGI 285
Cdd:cd18547 146 LLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEfdeINEELYKA---SF 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 153791547 286 KKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGqVLTVFFS 333
Cdd:cd18547 223 KAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVG-VIQAFLQ 269
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
399-563 |
8.23e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.23 E-value: 8.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 399 SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFAT 478
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 479 TIAENIRYGREDVTMDEIEKAVKEANAYDFimklphqFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 558
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
....*
gi 153791547 559 TESEA 563
Cdd:cd03231 158 KAGVA 162
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
388-611 |
8.44e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.14 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEV-QILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLMQRLYDP----LDGMVSIDGQDIRTINVRY 461
Cdd:PRK15134 6 LAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREI----IGVVSQEPVLFAT---TIAENI-------RYGREDVTMDE---------IEKAVKEANAYdfimklPHQfdt 518
Cdd:PRK15134 86 LRGVrgnkIAMIFQEPMVSLNplhTLEKQLyevlslhRGMRREAARGEilncldrvgIRQAAKRLTDY------PHQ--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 519 lvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIA 595
Cdd:PRK15134 157 --------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVA 228
|
250
....*....|....*.
gi 153791547 596 GFDGGVIVEQGNHDEL 611
Cdd:PRK15134 229 VMQNGRCVEQNRAATL 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1047-1247 |
1.02e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAQLGIVS----QEPILFDC 1121
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENI---AYGDNSR--VVSYEEIVRAAKEanihqFIDSLpdkyNTRVGDKGT---QLSGGQKQRIAIARALVRQPHIL 1193
Cdd:COG1129 346 SIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRL----RIKTPSPEQpvgNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1194 LLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVIQNGKV 1247
Cdd:COG1129 417 ILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
400-611 |
1.24e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 400 RKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLYDPL--DGMVSIDGqdiRTINVRYLREIIGVVSQEPVLF 476
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNaLAFRSPKGVkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 477 AT-TIAENI------RYGReDVTMDEIEKAVKEanaydFI--MKLPHQFDTLVGERGAQ--LSGGQKQRIAIARALVRNP 545
Cdd:TIGR00955 112 PTlTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 546 KILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLST--VRNADVIAGFDGGVIVEQGNHDEL 611
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
388-611 |
1.32e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-I 466
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFAT-TIAENIRYG--REDVTMDEIEKAVKEANAYdfiMKLPHQFDTL-VGERgaqlsggqkQRIAIARALV 542
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 543 RNPKILLLDEATSALD-TESEAV---VQAALDKareGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK15439 157 RDSRILILDEPTASLTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1031-1246 |
1.39e-16 |
|
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: 77.87 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmagsvfldgkeikqlnvqwlraqlg 1110
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1111 ivsqepilfdcsiaeniaygdNSRVVSYEEIVRAAKEANIHQFidslpdkyntrvgdkgTQLSGGQKQRIAIARALVRQP 1190
Cdd:cd03221 47 ---------------------AGELEPDEGIVTWGSTVKIGYF----------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1191 HILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIQNGK 1246
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
405-612 |
1.41e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 405 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFA-TTIAEN 483
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 484 IRYGREDVT------MDEIEKAVKEANAYDFIMKLPHQ-FDTlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSA 556
Cdd:PRK10253 102 VARGRYPHQplftrwRKEDEEAVTKAMQATGITHLADQsVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 557 LDTESEA-VVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELM 612
Cdd:PRK10253 174 LDISHQIdLLELLSELNREkGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
404-599 |
2.44e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.53 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 404 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI---RTINVRYLREIIGVVSQE-------- 472
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDhhllmdrt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 473 -------PVLFATTIAENIRYgREDVTMDEIEKAVKEANaydfimkLPhqfdtlvgergAQLSGGQKQRIAIARALVRNP 545
Cdd:PRK10908 96 vydnvaiPLIIAGASGDDIRR-RVSAALDKVGLLDKAKN-------FP-----------IQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 546 KILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTV--RNADVIAGFDG 599
Cdd:PRK10908 157 AVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsrRSYRMLTLSDG 213
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
707-966 |
2.45e-16 |
|
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: 80.92 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQpafsVIFSKVVGVFTNGGPPETQRQNS-NLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLR 785
Cdd:cd18541 1 YLLGILFLILVDLLQ----LLIPRIIGRAIDALTAGTLTASQlLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 786 YMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIA 865
Cdd:cd18541 77 NDLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 866 IAGVVEMKMLSGQALKDKKELegsGKIATEAIENF---RTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQ 942
Cdd:cd18541 155 LLVYRLGKKIHKRFRKVQEAF---SDLSDRVQESFsgiRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
|
250 260
....*....|....*....|....
gi 153791547 943 AMMYFSYAACFRFGAYLVTQQLMT 966
Cdd:cd18541 232 LLIGLSFLIVLWYGGRLVIRGTIT 255
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1043-1257 |
2.59e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1043 RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----MAGSVFLDGKEIkqlNVQWLRAQLGIVSQEPIL 1118
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1119 FDCSIAEN----IAYGDNSRVVSYEEivraaKEANIHQFID--SLPDKYNTRVGDKGTQ--LSGGQKQRIAIARALVRQP 1190
Cdd:TIGR00955 111 IPTLTVREhlmfQAHLRMPRRVTKKE-----KRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1191 HILLLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
405-586 |
3.36e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.47 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 405 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI----IGVVSQEPVLFATTI 480
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 481 AenirygREDVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 558
Cdd:PRK11629 104 A------LENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 153791547 559 TESEAVVQAALDK--AREGRTTIVIAHRLS 586
Cdd:PRK11629 178 ARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1031-1256 |
4.05e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.81 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFnypTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---RA 1107
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEPILF-DCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQfidslpdkyntrVGDKG------TQLSGGQKQRI 1180
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEA------------VGLRGaaklmpSELSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1181 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQL 1256
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
388-589 |
4.18e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-I 466
Cdd:PRK09700 6 ISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQE-PVLFATTIAENIRYGRE------DVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGErgaqLSGGQKQRIAIAR 539
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153791547 540 ALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVR 589
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIR 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1049-1257 |
4.25e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---------RAQLGIVSQEP--- 1116
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 ILFDCSIAENI-----AYGDNSrvvsYEEIVRAAKEANIHQFIDSlpdkynTRVGDKGTQLSGGQKQRIAIARALVRQPH 1191
Cdd:PRK11701 102 LRMQVSAGGNIgerlmAVGARH----YGDIRATAGDWLERVEIDA------ARIDDLPTTFSGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1192 ILLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:PRK11701 172 LVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
388-607 |
5.33e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.17 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQilkGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVR-YLREII 466
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFAT-TIAENIRYG---REDVTMDEIEKAVKEANAyDFimKLPHQFDTLvgerGAQLSGGQKQRIAIARALV 542
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMAVlqiRDDLSAEQREDRANELME-EF--HIEHLRDSM----GQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 543 RNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRlsTVRnaDVIAGFDGGVIVEQGN 607
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH--NVR--ETLAVCERAYIVSQGH 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
392-613 |
5.58e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.98 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 392 NIHFSYpSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN--VRYLREI---- 465
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 --------IGVVSQEPV-----LFAT--TIAENIR----YGREDvtmdeiekAVKEANAYDFIMKLPhQFDTLVGERGAQ 526
Cdd:PRK10261 98 mrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREE--------AMVEAKRMLDQVRIP-EAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 527 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------VVQAALDKAregrtTIVIAHRLSTVRN-ADVIAGFD 598
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilqlikVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMY 243
|
250
....*....|....*
gi 153791547 599 GGVIVEQGNHDELMR 613
Cdd:PRK10261 244 QGEAVETGSVEQIFH 258
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1048-1214 |
6.18e-16 |
|
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: 77.92 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENI 1127
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 AY--GDNSRvvsyEEIVRAAKEANIHQFIDsLPdkyntrvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1205
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGFED-RP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 153791547 1206 SEKVVQEAL 1214
Cdd:cd03231 160 GVARFAEAM 168
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1044-1246 |
7.98e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 7.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1044 PSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-------QlnvqwlRAQLGIVSQEP 1116
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssQ------EAGIGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 ILFD-CSIAENIAYGdnsrvvsyEEIVRAAKEAN---IHQFIDSLPDKYN------TRVGDkgtqLSGGQKQRIAIARAL 1186
Cdd:PRK10762 89 NLIPqLTIAENIFLG--------REFVNRFGRIDwkkMYAEADKLLARLNlrfssdKLVGE----LSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1187 VRQPHILLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIQNGK 1246
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
389-598 |
8.13e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 83.23 E-value: 8.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 389 EFKNIHFSYPSRKEV-QILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRLYDPLDGMVSIDGqdIRTINVRYLRE--- 464
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGG--DRLVNGRPLDSsfq 835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 -IIGVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKavKEANAY-DFIMKL---PHQFDTLVGERGAQLSGGQKQRIAIA 538
Cdd:TIGR00956 836 rSIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIG 913
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 539 RALVRNPKILL-LDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFD 598
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFD 971
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
388-594 |
9.06e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 81.76 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLDGMVSIDGQ-----DIRTi 457
Cdd:NF040905 2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvypHGSYEGEILFDGEvcrfkDIRD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 458 nvrylREIIGVV--SQE----PVLfatTIAENIRYGREDVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAqlsg 529
Cdd:NF040905 75 -----SEALGIViiHQElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV---- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 530 GQKQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVI 594
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSI 209
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1046-1262 |
9.31e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.38 E-value: 9.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1046 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerFYDPMA--GSVFLDGKEIKQL-NVQWLRAQLGIVSQEPILFD-C 1121
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDITDWqTAKIMREAVAIVPEGRRVFSrM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYGDnsrvvSYEEivRAAKEANIHQFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARALVRQPHILLLDEATSA 1201
Cdd:PRK11614 96 TVEENLAMGG-----FFAE--RDQFQERIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1202 LdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLLAQKGI 1262
Cdd:PRK11614 168 L---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1043-1227 |
9.67e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 77.01 E-value: 9.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1043 RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCS 1122
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 IAENIAYgdnsrvvsyeeivraakEANIHQFIDSLPDKYNTRVGDKG------TQLSGGQKQRIAIARALVRQPHILLLD 1196
Cdd:TIGR01189 90 ALENLHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|.
gi 153791547 1197 EATSALDTESEKVVQEALDkAREGRTCIVIA 1227
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
388-644 |
1.24e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.41 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLY--DPLDGMVSIDGQDIRTINVRYL-RE 464
Cdd:TIGR02633 2 LEMKGIVKTFGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 IIGVVSQEPVLFAT-TIAENIRYGRE----DVTMDEIEkAVKEANAYDFIMKLPHQFDTL-VGERGaqlsGGQKQRIAIA 538
Cdd:TIGR02633 79 GIVIIHQELTLVPElSVAENIFLGNEitlpGGRMAYNA-MYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 539 RALVRNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRnadviAGFDGGVIVEQGNHDELMREKGI 617
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQHVATKDMSTM 228
|
250 260
....*....|....*....|....*....
gi 153791547 618 YFKLVMTQTAGNEIE--LGNEACKSKDEI 644
Cdd:TIGR02633 229 SEDDIITMMVGREITslYPHEPHEIGDVI 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1043-1256 |
1.25e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1043 RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG-------------KEIKQLNVQWLR-AQ 1108
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1109 LGIVSQEPI-----LFDC--SIAENIAYGDNsrvVSYEEIVRAAKeanihQFIDS--LPDKyNTRVGDKGTQLSGGQKQR 1179
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAK-----RMLDQvrIPEA-QTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1180 IAIARALVRQPHILLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVETG 251
|
....*
gi 153791547 1252 THQQL 1256
Cdd:PRK10261 252 SVEQI 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1037-1251 |
1.37e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1037 VFNYPTRpSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAQLGIVS 1113
Cdd:PRK10261 329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1114 QEPilfdcsiaenIAYGDNSRVVSYE--EIVRaakeanIHQFIDSLPDKYNT-----RVGDKGT-------QLSGGQKQR 1179
Cdd:PRK10261 408 QDP----------YASLDPRQTVGDSimEPLR------VHGLLPGKAAAARVawlleRVGLLPEhawryphEFSGGQRQR 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1180 IAIARALVRQPHILLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:PRK10261 472 ICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1044-1245 |
1.92e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1044 PSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAQLG--IVSQEPILFD- 1120
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENIAYGD-------NSRVVSYEEIvraAKEANIHQFIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHIL 1193
Cdd:PRK09700 95 LTVLENLYIGRhltkkvcGVNIIDWREM---RVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1194 LLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNG 1245
Cdd:PRK09700 168 IMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
401-642 |
2.32e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 80.62 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 401 KEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRL--YDPLDGMV----------------SIDGQ---------- 452
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 453 ----DIRTINVRYLREIIGVVSqepVLFATTIAeniRYGREDV------TMDEIEKAVKEA--NAYDFI--MKLPHQFDT 518
Cdd:TIGR03269 91 peevDFWNLSDKLRRRIRKRIA---IMLQRTFA---LYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 519 LVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA--REGRTTIVIAHRLSTVRN-ADVIA 595
Cdd:TIGR03269 165 IARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 153791547 596 GFDGGVIVEQGNHDELMrekGIYFKLVMTQTAGNEIELGNEACKSKD 642
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVV---AVFMEGVSEVEKECEVEVGEPIIKVRN 284
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
132-329 |
2.59e-15 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 77.90 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 132 WCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLT 211
Cdd:cd18589 60 YNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 212 LVILAISPVLGL---SAGIWAKILSSFTDKELhayAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKA 288
Cdd:cd18589 140 LLTALGLPLLLLvpkFVGKFQQSLAVQVQKSL---ARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEA 216
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153791547 289 ITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLT 329
Cdd:cd18589 217 AAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVT 257
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
388-606 |
2.97e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 75.36 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPS-RKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLYDPL-DGMVSIDGQDIRtinvRYLRE 464
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 IIGVVSQEPVLFAT-TIAENIRygredvtmdeiekavkeanaydFIMKLphqfdtlvgeRGaqLSGGQKQRIAIARALVR 543
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 544 NPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFDGGVIVEQG 606
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKFDRLLLLKRG 185
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
388-612 |
4.00e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIH--FSYPS----RKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRY 461
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 462 LREIIGVVSQEPvlfATTIAENIRYGR---------EDVTMDEIEKAVKE-----------ANAYdfimklPHQfdtlvg 521
Cdd:PRK15112 85 RSQRIRMIFQDP---STSLNPRQRISQildfplrlnTDLEPEQREKQIIEtlrqvgllpdhASYY------PHM------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 522 ergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFD 598
Cdd:PRK15112 150 -----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMH 224
|
250
....*....|....
gi 153791547 599 GGVIVEQGNHDELM 612
Cdd:PRK15112 225 QGEVVERGSTADVL 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1048-1258 |
4.16e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.85 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVFLDGKEIKQLNVQWLRAQLG---------IVSQEP 1116
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYVERPSKVGepcpvcggtLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 ILFDCS------IAENIA---------YGDNSRVV----SYEEIVRAAKEAnIHQFIDSLPD-KYNTRVGDKGTQLSGGQ 1176
Cdd:TIGR03269 95 DFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEA-VGRAVDLIEMvQLSHRITHIARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1177 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTH 1253
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTP 253
|
....*
gi 153791547 1254 QQLLA 1258
Cdd:TIGR03269 254 DEVVA 258
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1038-1258 |
4.23e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.75 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1038 FNYPT----RPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVS 1113
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1114 QEPI-----------LFDCSIAENIaygdnsrvvsyeEIVRAAKEANIHQFIDS---LPDKYNTRvgdkGTQLSGGQKQR 1179
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLNT------------DLEPEQREKQIIETLRQvglLPDHASYY----PHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1180 IAIARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQL 1256
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADV 237
|
..
gi 153791547 1257 LA 1258
Cdd:PRK15112 238 LA 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
375-606 |
5.34e-15 |
|
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: 75.65 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 375 SKSGHKPDNIQGNLEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQdi 454
Cdd:cd03220 7 SKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 455 rtinVRYLREI-IGVvsqEPVLfatTIAENIR-----YGREDVTMDEIEKAVKE-ANAYDFImklphqfDTLVGErgaqL 527
Cdd:cd03220 85 ----VSSLLGLgGGF---NPEL---TGRENIYlngrlLGLSRKEIDEKIDEIIEfSELGDFI-------DLPVKT----Y 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 528 SGGQKQRIAIARALVRNPKILLLDEATSALDtesEAVVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFDGGVI 602
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGD---AAFQEKCQRRLREllkqGKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
....
gi 153791547 603 VEQG 606
Cdd:cd03220 221 RFDG 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1047-1227 |
5.35e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQ-EPILfdcSIAE 1125
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL---TVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 NIA-----YGDNSRvvsyeEIVRAAKEANIHQFIDsLPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PRK13539 93 NLEfwaafLGGEEL-----DIAAALEAVGLAPLAH-LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*..
gi 153791547 1201 ALDTESEKVVQEALdKAREGRTCIVIA 1227
Cdd:PRK13539 157 ALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
143-339 |
5.98e-15 |
|
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: 77.05 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 143 IRQKFFHAIMNqeigwFDVHDVGE-----LNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAI 217
Cdd:cd18548 74 LRKDLFEKIQS-----FSFAEIDKfgtssLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 218 SPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGA 297
Cdd:cd18548 149 IPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153791547 298 AFLLIYASYALAFWYGTSLVISKEYSIGQV-------LTVFFSVLIGAF 339
Cdd:cd18548 229 MMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1013-1259 |
6.16e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.25 E-value: 6.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1013 EIDSYSTQGLKPNMLEG--NVQFSGVVFNYPTR-----PsipvlqgLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP 1085
Cdd:PRK10522 303 ALAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNgfsvgP-------INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1086 MAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDcsiaeniaygdnsRVVSYEEivRAAKEANIHQFIDSLPDKYNTRV 1165
Cdd:PRK10522 376 QSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLEL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1166 GD---KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIV 1240
Cdd:PRK10522 441 EDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLL 520
|
250 260
....*....|....*....|
gi 153791547 1241 VIQNGKVKE-HGTHQQLLAQ 1259
Cdd:PRK10522 521 EMRNGQLSElTGEERDAASR 540
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-611 |
7.45e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 405 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGM-----VSIDGQDIRTI-NVRYLREIIGVVSQEPVLFAT 478
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 479 TIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 558
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153791547 559 TESEAVVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
388-603 |
7.96e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.07 E-value: 7.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIH--FSYPSrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTV-QLMQRLYDP--LDGMVSIDGQDIRTINVRYL 462
Cdd:PRK09473 13 LDVKDLRvtFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAfALMGLLAANgrIGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 463 REI----IGVVSQEPVlfaTTIAENIRYG-------------------REDVTMDEiekAVKEANAYDFIMKLPHQFdtl 519
Cdd:PRK09473 92 NKLraeqISMIFQDPM---TSLNPYMRVGeqlmevlmlhkgmskaeafEESVRMLD---AVKMPEARKRMKMYPHEF--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 520 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV-IAHRLStvrnadVIAGF 597
Cdd:PRK09473 163 --------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGI 228
|
....*.
gi 153791547 598 DGGVIV 603
Cdd:PRK09473 229 CDKVLV 234
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
142-339 |
1.15e-14 |
|
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: 75.95 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 142 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVL 221
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 222 GLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLL 301
Cdd:cd18570 155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 153791547 302 IYASYALAFWYGTSLVISKEYSIGQVLTvfFSVLIGAF 339
Cdd:cd18570 235 SLIGSLLILWIGSYLVIKGQLSLGQLIA--FNALLGYF 270
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1041-1247 |
1.21e-14 |
|
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: 75.06 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1041 PTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlNVQW-----LRAQLGIV--S 1113
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1114 QEPILFDCSIAENIAYgdNSRVVSYEEiVRAAKEanihqfIDSLPDKYN-TRVGDKGT-QLSGGQKQRIAIARALVRQPH 1191
Cdd:cd03267 103 KTQLWWDLPVIDSFYL--LAAIYDLPP-ARFKKR------LDELSELLDlEELLDTPVrQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1192 ILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1047-1247 |
1.85e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPMAGSVFLDGKEIKQLNV-QWLRAQLGIVSQEP-----IL 1118
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPEDRlgrglVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1119 fDCSIAENIAYGDNSR-------VVSYEEIVRAAKEanihqfidsLPDKYNTRVGDKGT---QLSGGQKQRIAIARALVR 1188
Cdd:COG3845 350 -DMSVAENLILGRYRRppfsrggFLDRKAIRAFAEE---------LIEEFDVRTPGPDTparSLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1189 QPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
744-1003 |
2.07e-14 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 75.45 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 744 QRQNSNLFSLLFLILGIISFITFFLQG-----FTFgkAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDA 818
Cdd:cd18590 28 GEYQHNAFTSAIGLMCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 819 AQVKGATGSRLAVIFQN-IANLGT-GIIISLiyGWQLTLLLLAIVPIIAIAgvveMKMLSGQALKDKKELEGS----GKI 892
Cdd:cd18590 104 TLMSRSVALNANVLLRSlVKTLGMlGFMLSL--SWQLTLLTLIEMPLTAIA----QKVYNTYHQKLSQAVQDSiakaGEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 893 ATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFENVLl 972
Cdd:cd18590 178 AREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLV- 256
|
250 260 270
....*....|....*....|....*....|...
gi 153791547 973 vfSAIVFGAMAVGQVSSFAPDYAK--ATVSASH 1003
Cdd:cd18590 257 --SFILYQKNLGSYVRTLVYIYGDmlSNVGAAA 287
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
370-614 |
2.76e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 370 SIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSI 449
Cdd:COG1134 6 EVENVSKSYRLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 450 DGqdirtiNVRYLREIIGVVSQEpvlfaTTIAENIR-----YGredVTMDEIEKAVKEANAY----DFImklphqfDTLV 520
Cdd:COG1134 86 NG------RVSALLELGAGFHPE-----LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 521 GergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE----SEAVVQaalDKAREGRTTIVIAHRLSTVRN-ADVIA 595
Cdd:COG1134 145 K----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAI 217
|
250
....*....|....*....
gi 153791547 596 GFDGGVIVEQGNHDELMRE 614
Cdd:COG1134 218 WLEKGRLVMDGDPEEVIAA 236
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
111-552 |
3.25e-14 |
|
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: 77.15 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 111 AYYYTGIGAGVLIVAYIQvsfwclaagRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDkIGMFF 190
Cdd:COG4615 60 LLLLSRLASQLLLTRLGQ---------HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 191 QAMATFFGGFIIGFTRGWKLTLVILAIspvlgLSAGIWAKILssFTDKELHAYAKAGAVAEEVLAAIRTVIafGGQKkEL 270
Cdd:COG4615 130 QSVALVLGCLAYLAWLSPPLFLLTLVL-----LGLGVAGYRL--LVRRARRHLRRAREAEDRLFKHFRALL--EGFK-EL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 271 ------------ERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLV-ISKEYSIGQVLTVFF----- 332
Cdd:COG4615 200 klnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGwADPAVLSGFVLVLLFlrgpl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 333 SVLIGAF-SVGQAS---PNIEAFANARGAAYEVFKIIDNKPSIDSFSKsghkpdniqgnLEFKNIHFSYPSRKEVQ--IL 406
Cdd:COG4615 280 SQLVGALpTLSRANvalRKIEELELALAAAEPAAADAAAPPAPADFQT-----------LELRGVTYRYPGEDGDEgfTL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 407 KGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTiaenirY 486
Cdd:COG4615 349 GPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------L 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 487 GREDVTMDEiekavkEANAYDFIMKLPH-------QFDTLvgergaQLSGGQKQRIAIARALVRNPKILLLDE 552
Cdd:COG4615 423 GLDGEADPA------RARELLERLELDHkvsvedgRFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
388-557 |
4.30e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI-NVRYLREII 466
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFA-TTIAENIRYGREDVTMDEIEKAVKEAnaYDFimkLPHQFDTLVgERGAQLSGGQKQRIAIARALVRNP 545
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQP 156
|
170
....*....|..
gi 153791547 546 KILLLDEATSAL 557
Cdd:PRK11614 157 RLLLLDEPSLGL 168
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
404-558 |
4.99e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.91 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 404 QILKGLNLKVK-----SGQTvALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQ---DI-RTINVRYLREIIGVVSQEPV 474
Cdd:PRK11144 8 QQLGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 475 LFA-TTIAENIRYGredvtMDEIEKAvkeanaydfimklphQFDTLVGERG---------AQLSGGQKQRIAIARALVRN 544
Cdd:PRK11144 87 LFPhYKVRGNLRYG-----MAKSMVA---------------QFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTA 146
|
170
....*....|....
gi 153791547 545 PKILLLDEATSALD 558
Cdd:PRK11144 147 PELLLMDEPLASLD 160
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
406-600 |
5.24e-14 |
|
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: 71.69 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-IGVVSQEPV---LFAT-TI 480
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 481 AENIrygredvtmdeiekavkeanaydfimklphqfdTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 560
Cdd:cd03215 96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153791547 561 SEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGG 600
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
114-331 |
6.31e-14 |
|
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: 74.04 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 114 YTGIGAGVLIVAYIQVSFWCLAAGRQ----------IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIG 183
Cdd:cd18545 36 LSGLLIIALLFLALNLVNWVASRLRIylmakvgqriLYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 184 DKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAF 263
Cdd:cd18545 116 NGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSF 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 264 GGQKKELERY---NNNLEEAKRlgikKAITANISMGAAFLLIYA-SYALAFWYGTSLVISKEYSIGqVLTVF 331
Cdd:cd18545 196 AREDENEEIFdelNRENRKANM----RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG-VLVAF 262
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
399-584 |
7.53e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 7.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 399 SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLY--DPLDGMVSIDGQDIrtinvrylreiigvvSQEpvlf 476
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 477 aTTIAENIryGREDVTMDEIE--KAVKEANAYDFIMKLPHqfdtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEAT 554
Cdd:COG2401 100 -ASLIDAI--GRKGDFKDAVEllNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|..
gi 153791547 555 SALDTESEAVVQAALDK-AREGRTTIVIA-HR 584
Cdd:COG2401 165 SHLDRQTAKRVARNLQKlARRAGITLVVAtHH 196
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
763-943 |
9.84e-14 |
|
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: 73.35 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 763 FITFFLQG-FTF------GKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSrlaVIFQN 835
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQ---CVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 836 IANLG--TGIIISLIY-GWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlkdKKELEGSGKIATEAIENFRTVVSLTRE 909
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLygsFLRKLSRRA---QAQVAKATGVADEALGNIRTVRAFAME 200
|
170 180 190
....*....|....*....|....*....|....
gi 153791547 910 QKFETMYAQSLQipyrNAMKKAHVFGITFSFTQA 943
Cdd:cd18574 201 DRELELYEEEVE----KAAKLNEKLGLGIGIFQG 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
399-613 |
1.09e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 399 SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLYDP-------LDGMVSIDGQDIRTINVRYLREIIGVVS 470
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 471 Q--EPVlFATTIAENIRYGR----------EDVTMDEIEKAVKEANAydfimklphqfDTLVGERGAQLSGGQKQRIAIA 538
Cdd:PRK13547 90 QaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 539 RAL---------VRNPKILLLDEATSALDTESE----AVVQAALDKAREGRTTIVIAHRLSTvRNADVIAGFDGGVIVEQ 605
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAH 236
|
....*...
gi 153791547 606 GNHDELMR 613
Cdd:PRK13547 237 GAPADVLT 244
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
388-608 |
1.12e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 72.13 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKST-TVQLMQRL-YDPLDGMVSIDGQDIRTIN------- 458
Cdd:PRK09580 2 LSIKDLHVSV---EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSpedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 459 -----VRYLREIIGVVSQepvLFATTIAENIRYGREDVTMDEIEKAvkeanayDFI------MKLPHqfDTLVGERGAQL 527
Cdd:PRK09580 79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 528 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREG-RTTIVIAH--RLSTVRNADVIAGFDGGVIVE 604
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
....
gi 153791547 605 QGNH 608
Cdd:PRK09580 227 SGDF 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1047-1247 |
1.68e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.77 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN-----------VQWLRAQLGIVSQE 1115
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1116 PILFDCSIAENIAYGDNSRVVSYEEIvraakEANIHQFIDSLPDK---YNTRVGdkgtQLSGGQKQRIAIARALVRQPHI 1192
Cdd:PRK10982 342 DIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1193 LLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:PRK10982 413 LMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1032-1257 |
1.69e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1032 QFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGI 1111
Cdd:PRK10575 13 ALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 VSQE-PILFDCSIAENIA------------YGDNSRVVSYEEIVRAAKEANIHQFIDSlpdkyntrvgdkgtqLSGGQKQ 1178
Cdd:PRK10575 90 LPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDS---------------LSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1179 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVIQNGKVKEHGTHQ 1254
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPA 233
|
...
gi 153791547 1255 QLL 1257
Cdd:PRK10575 234 ELM 236
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
415-607 |
1.91e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 68.94 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 415 SGQTVALVGNSGCGKSTTVQLMQRLYDPLD-GMVSIDGQDIRTINVRYLREIIgvvsqepvlfattiaenirygredvtm 493
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 494 deiekavkeanaydfimklphqfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD--- 570
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153791547 571 ----KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 607
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1045-1252 |
1.93e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1045 SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVFLDGKEIKQLNVQwLRAQLGI----------- 1111
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1112 -VSQEPILfdcsiaeNIAYgdNSRVVSYEEivraaKEANIHQFIDSLPDKYNTrVGDKGTQL--------SGGQKQRIAI 1182
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSKRKFQGL-----PELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1183 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVIQNGKVKEHGT 1252
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
405-613 |
2.08e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 405 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP----LDGMVSIDGQDIRTINVRylREIIGVVSQEP------- 473
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQNPrsafnpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 474 VLFATTIAENIR-YGRE--DVTMDEIEKAVKEANAyDFIMKLpHQFdtlvgergaQLSGGQKQRIAIARALVRNPKILLL 550
Cdd:PRK10418 96 HTMHTHARETCLaLGKPadDATLTAALEAVGLENA-ARVLKL-YPF---------EMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 551 DEATSALDteseAVVQA-ALD-----KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMR 613
Cdd:PRK10418 165 DEPTTDLD----VVAQArILDllesiVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1048-1262 |
2.94e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.08 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAQLGI--VSQEPILFD-CSIA 1124
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIA-----YGDNSRVVSYEEIVRAAKEANIHQFIDSLpdkyntrvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1199
Cdd:PRK10895 97 DNLMavlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1200 SALDTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVIQNGKVKEHGTHQQLLAQKGI 1262
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
409-614 |
3.58e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 409 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYdPLDGMVSIDGQDIRTINVRYLREIIGVVSQE-PVLFATTIAENI-RY 486
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLtLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 487 GREDVTMDEIEKAVKE-ANAYDFIMKLPhqfdTLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSALD 558
Cdd:PRK03695 94 QPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 559 TESeavvQAALDK-----AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:PRK03695 166 VAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
388-615 |
4.64e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIhfSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREI-I 466
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVSQEPVLFAT----TIAENI---RYGREDVT------MDEIEKAVKEA-NAYDfiMKLPHQfDTLVGergaQLSGGQK 532
Cdd:COG3845 336 AYIPEDRLGRGLvpdmSVAENLilgRYRRPPFSrggfldRKAIRAFAEELiEEFD--VRTPGP-DTPAR----SLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 533 QRIAIARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 610
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVGEVPAAE 488
|
....*
gi 153791547 611 LMREK 615
Cdd:COG3845 489 ATREE 493
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
753-1004 |
5.13e-13 |
|
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: 71.28 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 753 LLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVI 832
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFVMMLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 833 FQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTRE--- 909
Cdd:cd18548 121 VRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREdye 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 910 -QKFETMYAQslqipYRNAMKKA-HVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFENvLLVFSA----IVFGAMA 983
Cdd:cd18548 201 eERFDKANDD-----LTDTSLKAgRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGD-LVAFINylmqILMSLMM 274
|
250 260
....*....|....*....|.
gi 153791547 984 VGQVSSFAPdyaKATVSASHI 1004
Cdd:cd18548 275 LSMVFVMLP---RASASAKRI 292
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1012-1231 |
5.57e-13 |
|
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: 73.63 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1012 PEIDSYSTQGLKPNMLEGN----VQFSGVVF-NYP--TRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD 1084
Cdd:TIGR00954 424 EEIESGREGGRNSNLVPGRgiveYQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1085 PMAGSVFLDGKeikqlnvqwlrAQLGIVSQEPILFDCSIAENIAYGDNSrvvsYEEIVRAAKEANIHQFIDSLP-DKYNT 1163
Cdd:TIGR00954 504 VYGGRLTKPAK-----------GKLFYVPQRPYMTLGTLRDQIIYPDSS----EDMKRRGLSDKDLEQILDNVQlTHILE 568
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1164 R------VGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAreGRTCIVIAHRLS 1231
Cdd:TIGR00954 569 ReggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1052-1251 |
5.59e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1052 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAQLGIVSQEPILF-DC 1121
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYG-DNSRVVSYEEIVRAAKeanihqfIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PRK11144 92 KVRGNLRYGmAKSMVAQFDKIVALLG-------IEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1201 ALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVIQNGKVKEHG 1251
Cdd:PRK11144 158 SLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1052-1259 |
5.81e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.68 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1052 LSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--MAGSVFLDGKEI-----KQLNVqwLRA-QLGIVSQEPIlfdCS 1122
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREIlnlpeKELNK--LRAeQISMIFQDPM---TS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 IAENIAYGDN-----------SRVVSYEEIVR---AAKEANIHQFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVR 1188
Cdd:PRK09473 110 LNPYMRVGEQlmevlmlhkgmSKAEAFEESVRmldAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1189 QPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
390-582 |
6.08e-13 |
|
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: 69.21 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 390 FKNIHF-SYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL------YDPLDGMVSIDGQDIRTINVRYL 462
Cdd:cd03233 6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 463 REIIgVVSQEPVLFAT-TIAEnirygredvTMDeiekAVKEANAYDFImklphqfdtlvgeRGaqLSGGQKQRIAIARAL 541
Cdd:cd03233 83 GEII-YVSEEDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEAL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 153791547 542 VRNPKILLLDEATSALDTESeavvqaALD-------KAREGRTTIVIA 582
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSST------ALEilkcirtMADVLKTTTFVS 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1041-1258 |
6.76e-13 |
|
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: 72.55 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1041 PTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PMAGSVFLDGKEIKQLN-VQWLRAQLGIVSQEP-- 1116
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 --ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLpdKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHIL 1193
Cdd:TIGR02633 348 hgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1194 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVK----EHG-THQQLLA 1258
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
396-583 |
1.08e-12 |
|
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: 72.28 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 396 SYPSRKEvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDgqdiRTINVRYLreiigvvSQEPVL 475
Cdd:TIGR03719 13 VVPPKKE--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIKVGYL-------PQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 476 FAT-TIAENI-------------------RYGREDVTMD-------EIEKAVKEANAYDFIMKLPHQFDTLVGERG---- 524
Cdd:TIGR03719 80 DPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLEIAMDALRCPPWdadv 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 525 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 583
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1047-1229 |
1.17e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGSVFLDGKEIKQlnvqwlraqlgivsqepilfDCSIA 1124
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIA-YGDNSRVVsyeEIVRAAKeanihqfidsLPDKYNTRVgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1203
Cdd:COG2401 104 DAIGrKGDFKDAV---ELLNAVG----------LSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*...
gi 153791547 1204 TESEKVVQEALDKA--REGRTCIVIAHR 1229
Cdd:COG2401 169 RQTAKRVARNLQKLarRAGITLVVATHH 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
404-600 |
2.12e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.89 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 404 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRL----------YDPLDGMVSIDGQDIRtiNVRYLREIIGVVSQEP 473
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLAR--DIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 474 VLF-ATTIAENIRYGREDVT------MDEIEKAVKEaNAYDFIMK--LPHqfdtLVGERGAQLSGGQKQRIAIARALVRN 544
Cdd:PRK09984 96 NLVnRLSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRvgMVH----FAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 545 PKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAH----------RLSTVRNADVIagFDGG 600
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHqvdyalryceRIVALRQGHVF--YDGS 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
378-611 |
2.46e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 378 GHKPDNIqgnLEFKNIHFSypsRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTI 457
Cdd:PRK11831 1 EQSVANL---VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 458 NVRYL---REIIGVVSQEPVLFA-TTIAENIRYG-REDVTMDE--IEKAVkeanaydfIMKLphqfdTLVGERGA----- 525
Cdd:PRK11831 75 SRSRLytvRKRMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKL-----EAVGLRGAaklmp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 526 -QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHR----LSTVRNADVIAgfd 598
Cdd:PRK11831 142 sELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVA--- 218
|
250
....*....|...
gi 153791547 599 GGVIVEQGNHDEL 611
Cdd:PRK11831 219 DKKIVAHGSAQAL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1041-1258 |
2.61e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1041 PTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM-AGSVFLDGKEIKQLN-VQWLRAQLGIVSQEP-- 1116
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDRkr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 --ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNT---RVGdkgtQLSGGQKQRIAIARALVRQPH 1191
Cdd:PRK13549 350 dgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1192 ILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVK-----EHGTHQQLLA 1258
Cdd:PRK13549 426 ILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdlinHNLTQEQVME 499
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
140-337 |
3.56e-12 |
|
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: 68.66 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 140 IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISP 219
Cdd:cd18550 71 MYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 220 VLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAA--IRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGA 297
Cdd:cd18550 151 LFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153791547 298 AFLLIYASYALAFWYGTSLVISKEYSIGQVltVFFSVLIG 337
Cdd:cd18550 231 LGLFTAIGPALVYWVGGLLVIGGGLTIGTL--VAFTALLG 268
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1049-1245 |
3.69e-12 |
|
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: 66.50 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-ERFYD-PMAGSVFLDGKEIKQLnvqwLRAQLGIVSQEPILFDCSIaen 1126
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN----FQRSTGYVEQQDVHSPNLT--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1127 iaygdnsrvvsyeeiVRAAKE--ANIhqfidslpdkyntrvgdKGtqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1204
Cdd:cd03232 96 ---------------VREALRfsALL-----------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 153791547 1205 ESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVIQNG 1245
Cdd:cd03232 142 QAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
412-614 |
4.08e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.00 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 412 KVKSGQTVALVGNSGCGKSTTVQLMQRLYDpLDGMVS-----IDGQDIRTINVRYLREIIG----VVSQEPVlfaTTIAE 482
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRISEKERRNLVGaevaMIFQDPM---TSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 483 NIRYGREdvTMDEIE------KAVKEANAYDFImklphqfdTLVG-----ER----GAQLSGGQKQRIAIARALVRNPKI 547
Cdd:PRK11022 105 CYTVGFQ--IMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSRldvyPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 548 LLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:PRK11022 175 LIADEPTTALDVTIQAqIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
408-583 |
4.35e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 408 GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREII------GVvsqEPVLfatTIA 481
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGI---KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 482 ENIRY-------GREDVTMDEIEKavkeanaydfimklphqfdtlVGERG------AQLSGGQKQRIAIARALVRNPKIL 548
Cdd:PRK13538 93 ENLRFyqrlhgpGDDEALWEALAQ---------------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 153791547 549 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIAH 583
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
391-588 |
4.63e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 391 KNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQdirtinvryLReiIGVVS 470
Cdd:PRK09544 8 ENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 471 QEPVLFAT---TIAENIRYgREDVTMDEIEKAVKEANAYDFImKLPHQfdtlvgergaQLSGGQKQRIAIARALVRNPKI 547
Cdd:PRK09544 74 QKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153791547 548 LLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTV 588
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
406-588 |
5.39e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRtinvRYLRE-IIGVVSQE-------PVLFA 477
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 TTIAENiRYG-----REDVTMDEieKAVKEANAYDFIMKLPHQfdtLVGErgaqLSGGQKQRIAIARALVRNPKILLLDE 552
Cdd:PRK15056 99 DVVMMG-RYGhmgwlRRAKKRDR--QIVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 153791547 553 ATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV 588
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
117-339 |
6.63e-12 |
|
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: 67.86 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 117 IGAGVLIVAYI-------QVSFWCLAAGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINE----GIGD 184
Cdd:cd18549 43 IIGAILLALYIlrtllnyFVTYWGHVMGARIeTDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 185 kigmFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGlsagiwakILSSFTDKELHA-----YAKAG---AVAEEVLAA 256
Cdd:cd18549 123 ----LFISIITIIGSFIILLTINVPLTLIVFALLPLMI--------IFTIYFNKKMKKafrrvREKIGeinAQLEDSLSG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 257 IRTVIAFGGQKKELERY---NNNLEEAKRLGIKkaITANISMGAAFL--LIYASyALAFwyGTSLVISKEYSIGQVLTvf 331
Cdd:cd18549 191 IRVVKAFANEEYEIEKFdegNDRFLESKKKAYK--AMAYFFSGMNFFtnLLNLV-VLVA--GGYFIIKGEITLGDLVA-- 263
|
....*...
gi 153791547 332 FSVLIGAF 339
Cdd:cd18549 264 FLLYVNVF 271
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1052-1257 |
7.85e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1052 LSLEVKKGQTLALVGSSGCGKSTvvqLLERfydpMAG------SVFLDGKEIKQLNVQWL---RAQLgiVSQEPILF--- 1119
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLAR----MAGllpgsgSIQFAGQPLEAWSAAELarhRAYL--SQQQTPPFamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1120 -----DCSIAENIAYGDNSRVVsyEEIVRAAKeanihqfidsLPDKYNTRVGdkgtQLSGGQKQRIAIArALVRQ----- 1189
Cdd:PRK03695 86 vfqylTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLA-AVVLQvwpdi 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1190 -PH--ILLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVIQNGKVKEHGTHQQLL 1257
Cdd:PRK03695 149 nPAgqLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1047-1251 |
8.88e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.65 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVFLDGKEIKQlnvQWLRAQL-GIVSQEP----- 1116
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRGRKiATIMQNPrsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 ---ILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHIL 1193
Cdd:PRK10418 94 plhTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1194 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHG 1251
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1050-1228 |
1.07e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1050 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQL------NVQWLRAQLGIVSqepilfDCSI 1123
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKT------ELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 AENIAYgdnsrvvsYEEIVRAAKEANIHQFIDslpdkyntRVGDKGT------QLSGGQKQRIAIARALVRQPHILLLDE 1197
Cdd:PRK13538 92 LENLRF--------YQRLHGPGDDEALWEALA--------QVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|..
gi 153791547 1198 ATSALDTESEKVVQEALDK-AREGRTCIVIAH 1228
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
416-606 |
1.43e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 416 GQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINV---------RYLREIIGVVSQEP-------VLFATT 479
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrRLLRTEWGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 480 IAE-----------NIRYGREDvTMDEIEKAVkeanayDFIMKLPHQFdtlvgergaqlSGGQKQRIAIARALVRNPKIL 548
Cdd:PRK11701 112 IGErlmavgarhygDIRATAGD-WLERVEIDA------ARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 549 LLDEATSALDTEseavVQAA-LDKARE-----GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 606
Cdd:PRK11701 174 FMDEPTGGLDVS----VQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1058-1239 |
1.49e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.55 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1058 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVfldgkeikqlnvqwlraqlgivsqepILFDCSIAENIAYGDNSrvvs 1137
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDILEEVLDQLL---- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1138 yeeivraakeanihqfidslpdkyNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-- 1215
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....*....
gi 153791547 1216 -----KAREGRTCIVIAHRLSTIQNADLI 1239
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
398-580 |
3.06e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.26 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 398 PSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIiGVV----SQ-- 471
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 472 --EPVLfattiaENIRYGRE--DVTMDEIEKAVKEanaYDFIMKLPHQFDTLVgeRgaQLSGGQKQRIAIARALVRNPKI 547
Cdd:COG4586 109 wdLPAI------DSFRLLKAiyRIPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
|
170 180 190
....*....|....*....|....*....|....
gi 153791547 548 LLLDEATSALDTESEAVVQAALDK-AREGRTTIV 580
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEyNRERGTTIL 209
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1052-1252 |
4.34e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 65.92 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1052 LSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLR----AQLGIVSQEPIlfdcsI 1123
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPM-----T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 AENIAYgdnsrVVSYEeIVRAAKeanIHQ----------FIDSL-----PDKyNTRVGDKGTQLSGGQKQRIAIARALVR 1188
Cdd:PRK11022 101 SLNPCY-----TVGFQ-IMEAIK---VHQggnkktrrqrAIDLLnqvgiPDP-ASRLDVYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1189 QPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIQNGKVKEHGT 1252
Cdd:PRK11022 171 RPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
119-341 |
4.94e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 65.28 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 119 AGVLIVA--------YIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 190
Cdd:cd18565 57 GGLTVAAflleslfqYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSII 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 191 QAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKEL 270
Cdd:cd18565 137 RVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFER 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 271 ERynnnLEEAKRLGIKKAITAnISMGAAF-----LLIYASYALAFWYGTSLVISKEYSIGQVLTVffsvliGAFSV 341
Cdd:cd18565 217 ER----VADASEEYRDANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
390-599 |
5.30e-11 |
|
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: 67.08 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 390 FKNIHFSYPSrKEVQILKgLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDgqdiRTINVRYlreiigvV 469
Cdd:TIGR00954 454 FENIPLVTPN-GDVLIES-LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----AKGKLFY-------V 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 470 SQEPVLFATTIAENIRYgrEDVTMDEIEKAVKEANAYDFIMKLphQFDTLVGERGA---------QLSGGQKQRIAIARA 540
Cdd:TIGR00954 521 PQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDKDLEQILDNV--QLTHILEREGGwsavqdwmdVLSGGEKQRIAMARL 596
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 541 LVRNPKILLLDEATSALDTESEavvQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDG 599
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVE---GYMYRLCREfGITLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
388-604 |
5.35e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFattiaenirygreDVTMDEIEKAVKEANAYDFI--MKLPHQFdTLVGERGA--QLSGGQKQRIAIARALVR 543
Cdd:PRK10522 401 AVFTDFHLF-------------DQLLGPEGKPANPALVEKWLerLKMAHKL-ELEDGRISnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 544 NPKILLLDEATSALDTESEAVV-QAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDGGVIVE 604
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1047-1247 |
6.95e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSVFLDGKEI---KQLNVQWL-----RAQLGIVsqepil 1118
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIiyeQDLIVARLqqdppRNVEGTV------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1119 FDcSIAENIA--------YGDNSRVVSYEE----IVRAAK-------------EANIHQFIDSL---PDKyntrvgdKGT 1170
Cdd:PRK11147 84 YD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLgldPDA-------ALS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1171 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
737-1004 |
7.11e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 64.80 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 737 NGGPPETQRQNSNLFSLLflilGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLAN 816
Cdd:cd18589 28 NKDAPEAFTAAITVMSLL----TIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 817 DAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEA 896
Cdd:cd18589 102 DTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVET 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 897 IENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITfSFTQAMMYFSYAAC-FRFGAYLVTQ------QLMTFEN 969
Cdd:cd18589 182 FSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVS-MWTSSFSGLALKVGiLYYGGQLVTAgtvssgDLVTFVL 260
|
250 260 270
....*....|....*....|....*....|....*
gi 153791547 970 VLLVFSAivfgamAVGQVSSFAPDYAKATVSASHI 1004
Cdd:cd18589 261 YELQFTS------AVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
750-1004 |
7.27e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 64.82 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 750 LFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRL 829
Cdd:cd18546 40 LAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 830 AVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKmLSGQALKDKKElegsgKIAT------EAIENFRTV 903
Cdd:cd18546 118 VQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRARE-----RIAAvnadlqETLAGIRVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 904 VSLTREQKFETMYAQsLQIPYRNAMKKAH-VFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFeNVLLVF---SAIVF 979
Cdd:cd18546 192 QAFRRERRNAERFAE-LSDDYRDARLRAQrLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTV-GVLVAFllyLRRFF 269
|
250 260
....*....|....*....|....*
gi 153791547 980 GAMavGQVSSFAPDYAKATVSASHI 1004
Cdd:cd18546 270 API--QQLSQVFDSYQQARAALEKI 292
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1047-1237 |
1.03e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAQLGIVSQEP-ILFDCSIAE 1125
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGHRSgINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 NIAYG--DNSRVVSYEEIVRAAKEANIHQFIDSLpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1203
Cdd:PRK13540 94 NCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|....*
gi 153791547 1204 TESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1237
Cdd:PRK13540 160 ELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
413-586 |
1.07e-10 |
|
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: 63.54 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 413 VKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSiDGQDIRTInVRYLReiiGVVSQEpvLFATTIAENIRYGREDVT 492
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEI-LDEFR---GSELQN--YFTKLLEGDVKVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 493 MDEIEKAVKeANAYDFIMKLP--HQFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 561
Cdd:cd03236 96 VDLIPKAVK-GKVGELLKKKDerGKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|....*.
gi 153791547 562 EAVVQAALDK-AREGRTTIVIAHRLS 586
Cdd:cd03236 175 RLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
388-607 |
1.09e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.51 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLM--QRLYDPLDGMVSIDGQDIRTIN------- 458
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEpeerahl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 459 -----VRYLREIIGVVSQEpvlFATTIAENIRYGREDVTMDEIEkavkeanAYDFIM-KLPhqfdtLVGERGAQL----- 527
Cdd:CHL00131 85 giflaFQYPIEIPGVSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeKLK-----LVGMDPSFLsrnvn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 528 ---SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAH--RLSTVRNADVIAGFDGGV 601
Cdd:CHL00131 150 egfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGK 229
|
....*.
gi 153791547 602 IVEQGN 607
Cdd:CHL00131 230 IIKTGD 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1048-1230 |
1.20e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwLRaqLGIVSQEpILFDCSIAENI 1127
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQK-LYLDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 aygdnSRV------VSYEEIVRAAKEANIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1201
Cdd:PRK09544 87 -----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|.
gi 153791547 1202 LDTESEKVVQEALDKAREGRTCIV--IAHRL 1230
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
388-592 |
1.24e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYpsrKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIG 467
Cdd:PRK13540 2 LDVIELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIRYG-REDVTMDEIEKAVKeanaydfIMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRNPK 546
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDiHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153791547 547 ILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNAD 592
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1048-1270 |
1.26e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPMAGSVFLDGKEIKQlnvQWLRaQLGIVSQEPILF-DCSIA 1124
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIAYGDNSRV---VSYEEIVRAAkEANIHQFidSLPDKYNTRVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PLN03211 159 ETLVFCSLLRLpksLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1201 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIQNGKVKEHGTHQQLLAqkgiYFSMVSVQ 1270
Cdd:PLN03211 236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1047-1259 |
1.34e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.27 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVFLDGKEIKQLNVQwLRAQLGI--VSQEPI----- 1117
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1118 ----LFDCSIAENIAYGDNSRV--VSYEEIVraakEANIHQFidSLPDKYNTRVGDKGtqLSGGQKQRIAIARALVRQPH 1191
Cdd:PRK09580 94 snqfFLQTALNAVRSYRGQEPLdrFDFQDLM----EEKIALL--KMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1192 ILLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVIQNGKVKEHGTH---QQLLAQ 1259
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
119-358 |
2.65e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 62.94 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 119 AGVLIVAYI-QVSFWCL-------AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 190
Cdd:cd18778 43 ALLLLGAYLlRALLNFLriylnhvAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 191 QAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKEL 270
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 271 ERYNnnlEEAKRLGiKKAITANISMGAAFLLIY----ASYALAFWYGTSLVISKEYSIGQVltVFFSVLIGAF--SVGQA 344
Cdd:cd18778 203 KRFE---ALSRRYR-KAQLRAMKLWAIFHPLMEfltsLGTVLVLGFGGRLVLAGELTIGDL--VAFLLYLGLFyePITSL 276
|
250
....*....|....
gi 153791547 345 SPNIEAFANARGAA 358
Cdd:cd18778 277 HGLNEMLQRALAGA 290
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1048-1252 |
2.75e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPMA-------GSVFLDGKEIKQLNVQWL---RAQLGIVSQEP 1116
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 ILFdcSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFidSLPDKyNTRVGDKGTQLSGGQKQRIAIARAL---------V 1187
Cdd:PRK13547 96 FAF--SAREIVLLGRYPHARRAGALTHRDGEIAWQAL--ALAGA-TALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1188 RQPHILLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVIQNGKVKEHGT 1252
Cdd:PRK13547 171 QPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1044-1246 |
3.36e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1044 PSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-QLNVQWLRAQLGIVSQE-PILFDC 1121
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYGDNSR---VVSYEEIVRAAKeanihQFIDSLPDKYNTRvgDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1198
Cdd:PRK10982 89 SVMDNMWLGRYPTkgmFVDQDKMYRDTK-----AIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1199 TSALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVIQNGK 1246
Cdd:PRK10982 162 TSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
747-966 |
3.98e-10 |
|
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: 62.60 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 747 NSNLFSLLFLILGIISFITF-----FLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLaNDAAQV 821
Cdd:cd18566 35 NESIPTLQVLVIGVVIAILLesllrLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERL-NSLEQI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 822 KGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSgQALKDKKELEGS-GKIATEAIENF 900
Cdd:cd18566 112 REFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR-RALKERSRADERrQNFLIETLTGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 901 RTVVSLTREQ----KFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMyfsyAACFRFGAYLVTQQLMT 966
Cdd:cd18566 191 HTIKAMAMEPqmlrRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSM----VAVVAFGALLVINGDLT 256
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
406-607 |
4.03e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 61.86 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQ------LMQRL---------YDPLDGMVSIDgqdiRTINV------RYLRE 464
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLhlkkeqpgnHDRIEGLEHID----KVIVIdqspigRTPRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 I----IGVVSQEPVLFATtIAENIRYGRE--DVTM------DEIEKAVKEAnaYDF---IMKLPHQFDTLV--------- 520
Cdd:cd03271 87 NpatyTGVFDEIRELFCE-VCKGKRYNREtlEVRYkgksiaDVLDMTVEEA--LEFfenIPKIARKLQTLCdvglgyikl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 521 GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVI-- 594
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWIid 243
|
250
....*....|....*..
gi 153791547 595 ----AGFDGGVIVEQGN 607
Cdd:cd03271 244 lgpeGGDGGGQVVASGT 260
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
767-1001 |
4.09e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 62.53 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 767 FLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLG--TGII 844
Cdd:cd18564 72 YAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVgmLGVM 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 845 ISLiyGWQLTLLLLAIVPIIAIAGVV---EMKmlsgQALKDKKELEGS-GKIATEAIENFRTVVSLTREQ----KFETMY 916
Cdd:cd18564 150 FWL--DWQLALIALAVAPLLLLAARRfsrRIK----EASREQRRREGAlASVAQESLSAIRVVQAFGREEheerRFAREN 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 917 AQSLQIPYRNAMKKA---HVFGITFSFTQAMMYFsyaacfrFGAYLVTQQLMTFeNVLLVFSAIVFGAMA-VGQVSSFAP 992
Cdd:cd18564 224 RKSLRAGLRAARLQAllsPVVDVLVAVGTALVLW-------FGAWLVLAGRLTP-GDLLVFLAYLKNLYKpVRDLAKLTG 295
|
....*....
gi 153791547 993 DYAKATVSA 1001
Cdd:cd18564 296 RIAKASASA 304
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
403-608 |
9.31e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.33 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 403 VQILKGLNLKVKSGQTVALVGNSGCGKSTtvqlmqrLYDPLDGMVS---IDGqDIRTINVRYLREIIGVVS--------- 470
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTT-------LMDVLAGRKTggyIEG-DIRISGFPKKQETFARISgyceqndih 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 471 ------QEPVLFATTIAENIRYGREDVTM--DEIEKAVKEANAYDFIMKLPhqfdtlvGERGaqLSGGQKQRIAIARALV 542
Cdd:PLN03140 965 spqvtvRESLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELV 1035
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 543 RNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQGNH 608
Cdd:PLN03140 1036 ANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
392-615 |
9.87e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 392 NIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRLYD--PLDgmvsiDGQDIRTINVrylreiigVV 469
Cdd:PRK11147 5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKST---LMKILNGevLLD-----DGRIIYEQDL--------IV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 470 S---QEPVLFATT-----IAENI--------RYGR--EDVTMDEIEKAVKE-ANAYDfimKLPH----QFDTLVGERGAQ 526
Cdd:PRK11147 69 ArlqQDPPRNVEGtvydfVAEGIeeqaeylkRYHDisHLVETDPSEKNLNElAKLQE---QLDHhnlwQLENRINEVLAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 527 -----------LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAHRLSTVRN-ADVI 594
Cdd:PRK11147 146 lgldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRI 223
|
250 260
....*....|....*....|..
gi 153791547 595 AGFDGGVIVE-QGNHDELMREK 615
Cdd:PRK11147 224 VDLDRGKLVSyPGNYDQYLLEK 245
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1025-1233 |
1.08e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.05 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1025 NMLEGNVQFSGVVFNYptRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW 1104
Cdd:PRK15056 1 MMQQAGIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1105 LRAQLGIVSQEPILFDCSIAENIAYGDnsrvVSYEEIVRAAKEANiHQFIDS------LPDKYNTRVGdkgtQLSGGQKQ 1178
Cdd:PRK15056 79 LVAYVPQSEEVDWSFPVLVEDVVMMGR----YGHMGWLRRAKKRD-RQIVTAalarvdMVEFRHRQIG----ELSGGQKK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1179 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1233
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
397-583 |
1.42e-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: 60.11 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 397 YPSRKEVQILKGLNLKVKSG-----QTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI----RTINVRYlreiig 467
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKADY------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 vvsqepvlfattiaenirYGREDVTMDEIEKAVKEANAYDF-IMKlPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPK 546
Cdd:cd03237 75 ------------------EGTVRDLLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDAD 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 153791547 547 ILLLDEATSALDTESEAVVQAALDKAREG--RTTIVIAH 583
Cdd:cd03237 136 IYLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
391-562 |
1.58e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 391 KNIHFSYPSrkeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRY-LREIIGVV 469
Cdd:PRK10982 2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 470 SQE-PVLFATTIAENI---RYGREDVTMDEiEKAVKEANAYdfimklphqFDTL-----VGERGAQLSGGQKQRIAIARA 540
Cdd:PRK10982 79 HQElNLVLQRSVMDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAKA 148
|
170 180
....*....|....*....|..
gi 153791547 541 LVRNPKILLLDEATSALdTESE 562
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSL-TEKE 169
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
115-332 |
1.68e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 60.58 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 115 TGIGAGVLIVAYIQVSFWCLAAGRQ----IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 190
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 191 QAMATFFGGFIIGFTRGWKLTLVILAISPVLGLsAGIWAKILSSftdkelHAYAKA-GAVAE------EVLAAIRTVIAF 263
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-ATRWFRRRSS------RAYRRArERIAAvnadlqETLAGIRVVQAF 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 264 GGQKKELERYnNNLEEAKRLGIKKAITAN-ISMGAAFLLIYASYALAFWYGTSLVISKEYSIGqVLTVFF 332
Cdd:cd18546 195 RRERRNAERF-AELSDDYRDARLRAQRLVaIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVG-VLVAFL 262
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1046-1247 |
1.68e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.87 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1046 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRaQLGIV----SQepILFDC 1121
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ--LWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAEniaygdnsrvvSYE------EIVRAAKEANIHQFID--SLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHIL 1193
Cdd:COG4586 112 PAID-----------SFRllkaiyRIPDAEYKKRLDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1194 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV 1247
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
397-561 |
1.78e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 397 YPSRKevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSI-DGqdirtINVRYLreiigvvSQEPVL 475
Cdd:PRK11819 16 VPPKK--QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPG-----IKVGYL-------PQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 476 FAT-TIAENI-------------------RYGREDVTMD-------EIEKAVKEANAYDfimkLPHQF------------ 516
Cdd:PRK11819 82 DPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFDalaaeqgELQEIIDAADAWD----LDSQLeiamdalrcppw 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153791547 517 DTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 561
Cdd:PRK11819 158 DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
408-606 |
1.78e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.00 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 408 GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDI--------------RTI-NVRYLREIIGV---- 468
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 469 VSQE--------PVLFATTiaeniRYGREDvtMDEIEKAvkeANAYDFIMKLPhqfdtLVGERGAQLSGGQKQRIAIARA 540
Cdd:PRK11300 103 VAQHqqlktglfSGLLKTP-----AFRRAE--SEALDRA---ATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 541 LVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIagfdggVIVEQG 606
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRI------YVVNQG 230
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
707-979 |
2.07e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 60.66 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIING--GLQP------AFSVIFSK---VVGVFTNGGPPETQRQnsnlfslLFLILGIISFITF-------FL 768
Cdd:cd18565 1 LVLGLLASILNRlfDLAPplligvAIDAVFNGeasFLPLVPASLGPADPRG-------QLWLLGGLTVAAFlleslfqYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 769 QGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDDpkNTTGALTTRLANDAAQV-----KGATGS-RLAVIFqnianLGTG 842
Cdd:cd18565 74 SGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLerfldDGANSIiRVVVTV-----LGIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 843 IIIsLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELegsGKIAT---EAIENFRTVVSLTREQkFET--MYA 917
Cdd:cd18565 147 AIL-FYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAV---GDLNArleNNLSGIAVIKAFTAED-FERerVAD 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 918 QSLQipYRNAMKKAHVFGITFSFT-QAMMYFSYAACFRFGAYLVTQQLMTFENVLLV--FSAIVF 979
Cdd:cd18565 222 ASEE--YRDANWRAIRLRAAFFPViRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTVgtLVTFLF 284
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
707-991 |
2.09e-09 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 60.19 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQpafsVIFSKVVGVFTNGGPPETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRY 786
Cdd:cd18543 1 LILALLAALLATLAG----LAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 787 MVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATgSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 866
Cdd:cd18543 77 DLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFL-AFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 867 AGVVEMKMLSGQALKDKkelEGSGKIATEAIEN---FRTVVSLTRE----QKFETMyAQSLqipYRNAMKKAHVFGITFS 939
Cdd:cd18543 154 VARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRErrelDRFEAA-ARRL---RATRLRAARLRARFWP 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 153791547 940 FTQAMMYFSYAACFRFGAYLVTQQLMTFeNVLLVFSAIVfgAMAVGQVSSFA 991
Cdd:cd18543 227 LLEALPELGLAAVLALGGWLVANGSLTL-GTLVAFSAYL--TMLVWPVRMLG 275
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
401-588 |
2.29e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 401 KEVQILKGLNLKVKSGQTVALVGNSGCGKST-----TVQLMQRLYDpLDGMVSIDGQDIRTINVRYLREIIGVVSQE--- 472
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGITPEEIKKHYRGDVVYNAETDvhf 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 473 PVLfatTIAENIRYGREDVT-------MDEIEKAVKEANAYDFIMKLPHQFDTLVGE---RGaqLSGGQKQRIAIARALV 542
Cdd:TIGR00956 151 PHL---TVGETLDFAARCKTpqnrpdgVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASL 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153791547 543 RNPKILLLDEATSALDTESeavvqaALDKAREGRTTIVIAHRLSTV 588
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1037-1257 |
2.33e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1037 VFNYPTRPSIPV---LQGL---------SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-Q 1103
Cdd:PRK11288 245 IYGYRPRPLGEVrlrLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1104 WLRAqlGIV------SQEPILFDCSIAENIAYGDNSRVVSYEEIVRAAKEA-NIHQFIDSLPDKynTRVGD-KGTQLSGG 1175
Cdd:PRK11288 325 AIRA--GIMlcpedrKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGG 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1176 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKV-----K 1248
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaR 480
|
....*....
gi 153791547 1249 EHGTHQQLL 1257
Cdd:PRK11288 481 EQATERQAL 489
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
401-606 |
2.88e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 401 KEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLY-DPLDGMVSIDGqdiRTINVRYLREIiGVVSQEPVLFA- 477
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNaLAGRIQgNNFTGTILANN---RKPTKQILKRT-GFVTQDDILYPh 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 TTIAENIRYGREDVTMDEIEKAVKEANAYDFI--MKLPHQFDTLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDE 552
Cdd:PLN03211 155 LTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 553 ATSALD-TESEAVVQAALDKAREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQG 606
Cdd:PLN03211 233 PTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS----RVYQMFDSVLVLSEG 283
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
741-1001 |
3.01e-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: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 741 PETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLaNDAAQ 820
Cdd:cd18570 34 PSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFE--TRKTGEIISRF-NDANK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 821 VKGA-TGSRLAVIFQNIANLGTGIIIsLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGqalKDKKELEGSGKIATEAIEN 899
Cdd:cd18570 111 IREAiSSTTISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYILIILLFNKPFKK---KNREVMESNAELNSYLIES 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 900 FR---TVVSLTREQKFetmyAQSLQIPYRNAMKKAHVFGITF----SFTQAMMYFSYAACFRFGAYLVTQ------QLMT 966
Cdd:cd18570 187 LKgieTIKSLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSnlqsSIKGLISLIGSLLILWIGSYLVIKgqlslgQLIA 262
|
250 260 270
....*....|....*....|....*....|....*
gi 153791547 967 FeNVLLVFsaivFGAmAVGQVSSFAPDYAKATVSA 1001
Cdd:cd18570 263 F-NALLGY----FLG-PIENLINLQPKIQEAKVAA 291
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1055-1239 |
3.83e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1055 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDgkeikqLNV----QWLRA-QLGIVSQepilFDCSIAENIay 1129
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIsykpQYIKPdYDGTVED----LLRSITDDL-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1130 gDNSRVvsYEEIVraaKEANIHQFIDSlpdkyntRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1209
Cdd:PRK13409 429 -GSSYY--KSEII---KPLQLERLLDK-------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|..
gi 153791547 1210 VQEALDKAREGR--TCIVIAHRLSTIqnaDLI 1239
Cdd:PRK13409 492 VAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1031-1254 |
3.83e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1031 VQFSGVVFNYPTRPSIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKE----IKQLNVQWLR 1106
Cdd:PLN03073 509 ISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmavFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1107 aqlgiVSQEPILFdcsiaeniaygdnsrvvsYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARAL 1186
Cdd:PLN03073 587 -----LSSNPLLY------------------MMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYT-LSGGQKSRVAFAKIT 642
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1187 VRQPHILLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVIQNGKVKE-HGTHQ 1254
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1048-1231 |
4.39e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgkeikqlnvqwLRAQLGIVSQEPilfdcSIAENI 1127
Cdd:cd03236 16 KLHRLPV-PREGQVLGLVGPNGIGKSTALKIL-------AGK---------------LKPNLGKFDDPP-----DWDEIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1128 AYGDNSRVVSYEEIVRAAKEANIH--QFIDSLPDKYNTRVG-------DKGT-------------------QLSGGQKQR 1179
Cdd:cd03236 68 DEFRGSELQNYFTKLLEGDVKVIVkpQYVDLIPKAVKGKVGellkkkdERGKldelvdqlelrhvldrnidQLSGGELQR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1180 IAIARALVRQPHILLLDEATSALDTESE----KVVQEAldkAREGRTCIVIAHRLS 1231
Cdd:cd03236 148 VAIAAALARDADFYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1052-1203 |
7.14e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1052 LSLEVKKGQTLALVGSSGCGKStvvQLLERFY---DPMAGSVFLDGKEIKQLNVQwLRAQLGIV-----SQEPILF-DCS 1122
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 IAENI---AYGDNSRvvsyeeIVRAAKEANI-HQFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARALVRQPHILLLDEA 1198
Cdd:PRK15439 358 LAWNVcalTHNRRGF------WIKPARENAVlERYRRALNIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
....*
gi 153791547 1199 TSALD 1203
Cdd:PRK15439 431 TRGVD 435
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
740-867 |
7.80e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 58.68 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 740 PPETQRQNSNLFSLLFLILGIISFITFFLQ---GFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLAN 816
Cdd:cd18563 31 IQLGPGGNTSLLLLLVLGLAGAYVLSALLGilrGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTS 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 153791547 817 DAAQVKGATGSRLAVIFQNIANLgTGIIISLIY-GWQLTLLLLAIVPIIAIA 867
Cdd:cd18563 109 DTDRLQDFLSDGLPDFLTNILMI-IGIGVVLFSlNWKLALLVLIPVPLVVWG 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1057-1242 |
8.59e-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: 59.80 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1057 KKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgkeikqlnvqwLRAQLGIVSQEPilfdcSIAENIAYGDNSRVV 1136
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIL-------SGE---------------LKPNLGDYDEEP-----SWDEVLKRFRGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1137 SYEEIVRAAKEANIH--QFIDSLPDKYNTRVGD-------KG-------------------TQLSGGQKQRIAIARALVR 1188
Cdd:COG1245 150 DYFKKLANGEIKVAHkpQYVDLIPKVFKGTVREllekvdeRGkldelaeklglenildrdiSELSGGELQRVAIAAALLR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 1189 QPHILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVI 1242
Cdd:COG1245 230 DADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
388-581 |
8.76e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIhfsypSRKEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRY-LREII 466
Cdd:COG1129 257 LEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVVS----QEPVLFATTIAENI------RYGREDVtMDEiEKAVKEANAY--DFIMKLPHQfDTLVGergaQLSGGQKQR 534
Cdd:COG1129 330 AYVPedrkGEGLVLDLSIRENItlasldRLSRGGL-LDR-RRERALAEEYikRLRIKTPSP-EQPVG----NLSGGNQQK 402
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 153791547 535 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVI 581
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVI 450
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1049-1240 |
1.09e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 57.62 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVqlLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLG---IVSQEPI-------- 1117
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIgrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1118 -----LFD------CSIAENIAYGDNSRVVSY---------EEIVRAAKE-----ANIHQFIDSLPD---KYnTRVGDKG 1169
Cdd:cd03271 89 atytgVFDeirelfCEVCKGKRYNRETLEVRYkgksiadvlDMTVEEALEffeniPKIARKLQTLCDvglGY-IKLGQPA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1170 TQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1240
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWII 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1045-1261 |
1.16e-08 |
|
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: 60.03 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1045 SIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAQLGIVSQEPILFDCSIA 1124
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTG 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 -ENIAYGDNSRVVSYEEIVRAA----KEANIHQFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEAT 1199
Cdd:TIGR01257 2030 rEHLYLYARLRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 1200 SALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQKG 1261
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
707-869 |
1.50e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 57.55 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGgppetQRQNSNLFSLLFLILG--IISFITFFLQGFTFGKAGEILTKRL 784
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIG-----SKSLGLLLGLALLLLGayLLRALLNFLRIYLNHVAEQKVVADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 785 RYMVFKSMLRQDVSWFDDPKntTGALTTRLANDAAQVKgatgsRLAV--IFQNIANLGT--GIIISLIY-GWQLTLLLLA 859
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQ--TGDLMSRVINDVANVE-----RLIAdgIPQGITNVLTlvGVAIILFSiNPKLALLTLI 148
|
170
....*....|
gi 153791547 860 IVPIIAIAGV 869
Cdd:cd18778 149 PIPFLALGAW 158
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
389-560 |
1.79e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 389 EFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQdirtINVRYL---REI 465
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqhRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 466 IgvvsqEPvlfATTIAENIRYGREDVTMDEIEKAVKeanAY--DFIMKlPHQFDTLVgergAQLSGGQKQRIAIARALVR 543
Cdd:PRK11147 394 L-----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLK 457
|
170
....*....|....*..
gi 153791547 544 NPKILLLDEATSALDTE 560
Cdd:PRK11147 458 PSNLLILDEPTNDLDVE 474
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1055-1252 |
3.16e-08 |
|
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: 57.87 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1055 EVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSVFLDGKEI-KQLNV----QWLRAQLGIVSQEpILFDcSIAENIay 1129
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVdEDLKIsykpQYISPDYDGTVEE-FLRS-ANTDDF-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1130 gDNSRVvsYEEIVRAAKeanihqfIDSLPDKYntrVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1209
Cdd:COG1245 431 -GSSYY--KTEIIKPLG-------LEKLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 153791547 1210 VQEALDKAREGR--TCIVIAHRLSTIqnaDLI---VVIQNGKVKEHGT 1252
Cdd:COG1245 494 VAKAIRRFAENRgkTAMVVDHDIYLI---DYIsdrLMVFEGEPGVHGH 538
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
707-967 |
3.30e-08 |
|
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: 56.69 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 707 FVVGIFCAIINGGLqpafSVIFSKVVGVFTNGGPPEtqrQNSNLFSLLFLILGIISFITFFLQgFTFGKAGEILTKR--- 783
Cdd:cd18549 4 FFLDLFCAVLIAAL----DLVFPLIVRYIIDDLLPS---KNLRLILIIGAILLALYILRTLLN-YFVTYWGHVMGARiet 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 784 -LRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVkgatgSRLA-----VIFQNIANLGTGIIISLIYGWQLTLLL 857
Cdd:cd18549 76 dMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDI-----SELAhhgpeDLFISIITIIGSFIILLTINVPLTLIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 858 LAIVPIIAIAGVVEMKMLSGQALKDKKELegsGKIATEAIENF---RTVVSLTRE----QKFETMYAQslqipYRNAMKK 930
Cdd:cd18549 149 FALLPLMIIFTIYFNKKMKKAFRRVREKI---GEINAQLEDSLsgiRVVKAFANEeyeiEKFDEGNDR-----FLESKKK 220
|
250 260 270
....*....|....*....|....*....|....*...
gi 153791547 931 AH-VFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTF 967
Cdd:cd18549 221 AYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITL 258
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
108-345 |
3.39e-08 |
|
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: 56.36 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 108 TTYAYYYTGIGAGVLIVAYIQVSFW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIG 183
Cdd:cd18580 38 GYYLGVYAALLVLASVLLVLLRWLLfvlaGLRASRRLH---DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 184 DKIGMFFQAMATFFGGFI-IGFTRGWkltlVILAISPVLGLSAGIW----------------AK--ILSSFTdkelhaya 244
Cdd:cd18580 115 LALLDFLQSLFSVLGSLIvIAIVSPY----FLIVLPPLLVVYYLLQryylrtsrqlrrleseSRspLYSHFS-------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 245 kagavaeEVLAAIRTVIAFGGQKKELERYNNNLeeakrlgikkaitaNISMGAAFLLIYASYALAFWYgtslviskeysi 324
Cdd:cd18580 183 -------ETLSGLSTIRAFGWQERFIEENLRLL--------------DASQRAFYLLLAVQRWLGLRL------------ 229
|
250 260
....*....|....*....|.
gi 153791547 325 gQVLTVFFSVLIGAFSVGQAS 345
Cdd:cd18580 230 -DLLGALLALVVALLAVLLRS 249
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
112-333 |
3.77e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 56.33 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 112 YYYTGIGAGVLIVAYIQVSFWCLAAGRQ----IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINE----GIG 183
Cdd:cd18540 42 TGFILLYLGLILIQALSVFLFIRLAGKIemgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 184 DkigmFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIwakilssFTDKELHAYAKAGAVAEEVLAA------- 256
Cdd:cd18540 122 D----LVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY-------FQKKILKAYRKVRKINSRITGAfnegitg 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 257 IRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVFFS 333
Cdd:cd18540 191 AKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGT-LVAFIS 266
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
116-339 |
3.87e-08 |
|
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: 56.36 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 116 GIGAGVLIVAYIQVSFwclAAGRQIHKIRQKFFHAIMNQEIG--------WFDVHDVGELNTRLtDDVSKINEGIGDKIG 187
Cdd:cd18555 45 GIGILILFLLYGLFSF---LRGYIIIKLQTKLDKSLMSDFFEhllklpysFFENRSSGDLLFRA-NSNVYIRQILSNQVI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 188 MFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQK 267
Cdd:cd18555 121 SLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEK 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 268 KELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTvfFSVLIGAF 339
Cdd:cd18555 201 NIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIA--FSSLAGSF 270
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
406-611 |
4.10e-08 |
|
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: 57.72 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQ------LMQRLY---------------DPLDGMVSID----GQDIRTINVR 460
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypaLANRLNgaktvpgrytsieglEHLDKVIHIDqspiGRTPRSNPAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 YlreiIGVVSQEPVLFATT------------IAENIRYGRED---------VTM-------------------------- 493
Cdd:TIGR00630 704 Y----TGVFDEIRELFAETpeakvrgytpgrFSFNVKGGRCEacqgdgvikIEMhflpdvyvpcevckgkrynretlevk 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 494 -------DEIEKAVKEAnaYDFIMKLP---HQFDTLV---------GERGAQLSGGQKQRIAIARALVR---NPKILLLD 551
Cdd:TIGR00630 780 ykgkniaDVLDMTVEEA--YEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILD 857
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 552 EATSALDTESEA----VVQAALDKareGRTTIVIAHRLSTVRNADVI------AGFDGGVIVEQGNHDEL 611
Cdd:TIGR00630 858 EPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1056-1242 |
4.36e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1056 VKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgkeikqlnvqwLRAQLGIVSQEPilfdcSIAENIAYGDNSRV 1135
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIL-------SGE---------------LIPNLGDYEEEP-----SWDEVLKRFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1136 VSYEEIVRAAKEANIH--QFIDSLPDKYNTRVGD--KGT------------------------QLSGGQKQRIAIARALV 1187
Cdd:PRK13409 149 QNYFKKLYNGEIKVVHkpQYVDLIPKVFKGKVREllKKVdergkldevverlglenildrdisELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153791547 1188 RQPHILLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVVI 1242
Cdd:PRK13409 229 RDADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
115-335 |
4.57e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 55.95 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 115 TGIGAGVLIVAYIQvsfWCLAAGRQI----------HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGd 184
Cdd:cd18543 39 WPLVLLLLALGVAE---AVLSFLRRYlagrlslgveHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 185 KIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTdkeLHAYAKAGAVA---EEVLAAIRTVI 261
Cdd:cd18543 115 FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVK 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 262 AFGGQKKELERYNNNLEEAKRLGIKKA-ITANISMgAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVFFSVL 335
Cdd:cd18543 192 AFGRERRELDRFEAAARRLRATRLRAArLRARFWP-LLEALPELGLAAVLALGGWLVANGSLTLGT-LVAFSAYL 264
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1053-1259 |
4.87e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS--------VFLDGKEIKQL-NVQWLRAQLGIVSQEPILFDCSI 1123
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1124 AENIAYG--DNSRVVSYEEivraakeanihQF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PRK10938 103 AEIIQDEvkDPARCEQLAQ-----------QFgITALLDR-------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1201 ALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIQNGKVKEHGTHQQLLAQ 1259
Cdd:PRK10938 165 GLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
399-583 |
5.54e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 399 SRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTIN-VRYlreiIGVVSQEPVLFA 477
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRF----MAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 TTIA-ENIRY-----GREDVTMdeiekavkEANAYDfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLD 551
Cdd:PRK13543 96 DLSTlENLHFlcglhGRRAKQM--------PGSALA-IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 153791547 552 EATSALDTESEAVVQAALD-KAREGRTTIVIAH 583
Cdd:PRK13543 163 EPYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1056-1228 |
8.59e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1056 VKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlnvQWlraQLGIVSQEPILFDCSIAENIAYGDNsrv 1135
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQETPALPQPALEYVIDGDR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1136 vSYEEIVRAAKEAN----------IHQFIDSLpDKYNTR---------VGDKGTQL-------SGGQKQRIAIARALVRQ 1189
Cdd:PRK10636 90 -EYRQLEAQLHDANerndghaiatIHGKLDAI-DAWTIRsraasllhgLGFSNEQLerpvsdfSGGWRMRLNLAQALICR 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 153791547 1190 PHILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAH 1228
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1145-1240 |
8.64e-08 |
|
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: 56.95 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1145 AKEANIHQFIDSLPD---KYnTRVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEK----VVQEAL 1214
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90 100
....*....|....*....|....*.
gi 153791547 1215 DKareGRTCIVIAHRLSTIQNADLIV 1240
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYII 902
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1044-1206 |
8.85e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1044 PSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLlerfydpMAGsvfLD----GKEIKQLNVQwlraqLGIVSQEPILf 1119
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI-------MAG---VDkdfnGEARPQPGIK-----VGYLPQEPQL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1120 DCS--IAENI--AYGDNSRVVS-YEEI------------VRAAKEANIHQFIDS------------------LPDkyntr 1164
Cdd:TIGR03719 80 DPTktVRENVeeGVAEIKDALDrFNEIsakyaepdadfdKLAAEQAELQEIIDAadawdldsqleiamdalrCPP----- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153791547 1165 vGD-KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1206
Cdd:TIGR03719 155 -WDaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1012-1237 |
8.90e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1012 PEIDSYSTQ-GLKPNmlEGNVQFSGVVFNYPTRPsipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGS- 1089
Cdd:PRK10938 243 PEPDEPSARhALPAN--EPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGYSn 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1090 -VFLDGKeikqlnvqwlraQLGivSQEPIlFDcsIAENIAYGDNSRVVSYEeIVRAAKEANIHQFIDSL------PDK-- 1160
Cdd:PRK10938 317 dLTLFGR------------RRG--SGETI-WD--IKKHIGYVSSSLHLDYR-VSTSVRNVILSGFFDSIgiyqavSDRqq 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1161 -----------YNTRVGDKGTQ-LSGGQkQRIA-IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRT---- 1222
Cdd:PRK10938 379 klaqqwldilgIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllf 457
|
250 260
....*....|....*....|....*
gi 153791547 1223 ----------CivIAHRLSTIQNAD 1237
Cdd:PRK10938 458 vshhaedapaC--ITHRLEFVPDGD 480
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
704-967 |
1.29e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 54.79 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 704 WPYFVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETqrqnSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKR 783
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDG----LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 784 LRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPI 863
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 864 IAIAGVV-EMKMLSGQALKDKKELEGSGKIaTEAIENFRTVVSLTREQK----F----ETMYAQSlqipyrnaMKKAHVF 934
Cdd:cd18540 155 LAVVSIYfQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVREEKnlreFkeltEEMRRAS--------VRAARLS 225
|
250 260 270
....*....|....*....|....*....|...
gi 153791547 935 GITFSFTQAMMYFSYAACFRFGAYLVTQQLMTF 967
Cdd:cd18540 226 ALFLPIVLFLGSIATALVLWYGGILVLAGAITI 258
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1053-1215 |
1.80e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1053 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqLNVQWL---RAQLgivsqEPilfDCSIAENIAY 1129
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqhRAEL-----DP---EKTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1130 GD-----NSR---VVSYeeivraakeanIHQFIDSlPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1201
Cdd:PRK11147 407 GKqevmvNGRprhVLGY-----------LQDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170
....*....|....
gi 153791547 1202 LDTESEKVVQEALD 1215
Cdd:PRK11147 471 LDVETLELLEELLD 484
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
409-585 |
1.97e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.79 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 409 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTiNVRYLREIIGVVSQEPVLfattiaENIRYGR 488
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 489 ED---------VTMDEIEKAvkeANAYDFIMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 559
Cdd:TIGR01257 2031 EHlylyarlrgVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180
....*....|....*....|....*..
gi 153791547 560 ESEAVV-QAALDKAREGRTTIVIAHRL 585
Cdd:TIGR01257 2104 QARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1049-1252 |
2.44e-07 |
|
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: 53.18 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLerfydpmAGSVFLDGKEIKqlnvqwlrAQLGIVSQEP----ILF 1119
Cdd:cd03237 10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIE--------IELDTVSYKPqyikADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1120 DCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDS-LPDkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1198
Cdd:cd03237 75 EGTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDReVPE------------LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 1199 TSALDTESE----KVVQEALDKARegRTCIVIAHrlsTIQNADLI---VVIQNGKVKEHGT 1252
Cdd:cd03237 143 SAYLDVEQRlmasKVIRRFAENNE--KTAFVVEH---DIIMIDYLadrLIVFEGEPSVNGV 198
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
749-976 |
2.53e-07 |
|
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: 54.01 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 749 NLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGATGSR 828
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 829 LAVIFQNIANLgTGIIISLIY-GWQLTLLLLAIVPIIAIAgvveMKMLSGQALKDKKELegSGKIAT------EAIENFR 901
Cdd:cd18545 118 LINLIPDLLTL-VGIVIIMFSlNVRLALVTLAVLPLLVLV----VFLLRRRARKAWQRV--RKKISNlnaylhESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 902 TVVSLTREQK-FETMyaQSLQIPYRNA-MKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFeNVLLVFSA 976
Cdd:cd18545 191 VIQSFAREDEnEEIF--DELNRENRKAnMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITV-GVLVAFIG 264
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1048-1214 |
2.82e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdGKEIK-----QLNVQWLRAqlgivSQEPIlfdcs 1122
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKlgyfaQHQLEFLRA-----DESPL----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1123 iaeniaygdnsrvvsyEEIVRAAKEANIHQFIDSLP------DKyntrVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1196
Cdd:PRK10636 396 ----------------QHLARLAPQELEQKLRDYLGgfgfqgDK----VTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170
....*....|....*...
gi 153791547 1197 EATSALDTESEKVVQEAL 1214
Cdd:PRK10636 456 EPTNHLDLDMRQALTEAL 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1170-1206 |
3.01e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 3.01e-07
10 20 30
....*....|....*....|....*....|....*..
gi 153791547 1170 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1206
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
388-617 |
3.02e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIdgqdirTINVRylreiIG 467
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SENAN-----IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVL-FATTIA---------------ENIR--YGREDVTMDEIEKAVKeanaydfimklphqfdtlvgergaQLSG 529
Cdd:PRK15064 386 YYAQDHAYdFENDLTlfdwmsqwrqegddeQAVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 530 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKArEGrTTIVIAH------RLSTvrnaDVIAGFDGGVIV 603
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
|
250
....*....|....
gi 153791547 604 EQGNHDELMREKGI 617
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1047-1258 |
3.72e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQlGIV------SQEPILFD 1120
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1121 CSIAENI---AYGDNSRvvSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGtQLSGGQKQRIAIARALVRQPHILLLDE 1197
Cdd:PRK10762 345 MSVKENMsltALRYFSR--AGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1198 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIQNGKV-----KEHGTHQQLLA 1258
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
388-588 |
6.14e-07 |
|
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: 53.68 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-PLDGMVSIDGQ--DIRT-------- 456
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRNpaqairag 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 457 -INVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLvgergAQLSGGQKQRI 535
Cdd:TIGR02633 338 iAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI-----GRLSGGNQQKA 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153791547 536 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV 588
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEV 466
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
749-866 |
8.19e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 52.10 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 749 NLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGATGSR 828
Cdd:cd18550 39 VLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGT 116
|
90 100 110
....*....|....*....|....*....|....*...
gi 153791547 829 LAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAI 866
Cdd:cd18550 117 LTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
200-340 |
8.70e-07 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 52.12 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 200 FIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEE 279
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 280 AKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVltVFFSVLIGAFS 340
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQL--IAFNMLAGQVS 271
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1066-1239 |
8.76e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1066 GSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAQLGIVSqepilfDCSIAENIAYGdnSRVVSYEEIV 1142
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKL------EMTVFENLKFW--SEIYNSAETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1143 RAAkeanIHQF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-KAREG 1220
Cdd:PRK13541 105 YAA----IHYFkLHDLLDE-------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSG 173
|
170
....*....|....*....
gi 153791547 1221 RTCIVIAHRLSTIQNADLI 1239
Cdd:PRK13541 174 GIVLLSSHLESSIKSAQIL 192
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1041-1203 |
9.45e-07 |
|
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: 50.72 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1041 PTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPmAGSVFLDGKEIKQLNVQWlRAQLGIVSQEp 1116
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVSEE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1117 ilfDCSIAEniaygdnsrvVSYEEIVRAAKEANIHQFIdslpdkyntrvgdKGtqLSGGQKQRIAIARALVRQPHILLLD 1196
Cdd:cd03233 92 ---DVHFPT----------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWD 143
|
....*..
gi 153791547 1197 EATSALD 1203
Cdd:cd03233 144 NSTRGLD 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
388-566 |
1.34e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVsidgqdIRTINVRylreiIG 467
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 VVSQEPVLFATTIAENIRYgredvtMDEIEKAVKEanaydfiMKLPHQFDT--LVGERGAQ----LSGGQKQRIAIARAL 541
Cdd:PLN03073 576 VFSQHHVDGLDLSSNPLLY------MMRCFPGVPE-------QKLRAHLGSfgVTGNLALQpmytLSGGQKSRVAFAKIT 642
|
170 180
....*....|....*....|....*.
gi 153791547 542 VRNPKILLLDEATSALDTES-EAVVQ 566
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1047-1262 |
1.49e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1047 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVfldgkeikqlnvQWL-RAQLGIVSQEP--------I 1117
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYYAQDHaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1118 LFDCsIAENIAYGDNSRVV---------SYEEIVRAAKeanihqfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVR 1188
Cdd:PRK15064 401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1189 QPHILLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH-R--LSTIqnADLIVVIQNGKVKE-HGTHQQLLAQKGI 1262
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdRefVSSL--ATRIIEITPDGVVDfSGTYEEYLRSQGI 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
526-587 |
1.54e-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: 52.48 E-value: 1.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153791547 526 QLSGGQKQRIAIARALVRNPKILLLDEATSALD-TESEAVVQAALDKAREGRTTIVIAHRLST 587
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
147-337 |
1.63e-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: 51.41 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 147 FFHAIMNQEIGWFDVHDVGELNTRLTDdvskiNEGI-----GDKIGMFFQAMATFFGGFIIgFTRGWKLTLVILAISPVL 221
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRFQE-----NQKIrrfltRSALTTILDLLMVFIYLGLM-FYYNLQLTLIVLAFIPLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 222 GLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLL 301
Cdd:cd18568 155 VLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLI 234
|
170 180 190
....*....|....*....|....*....|....*.
gi 153791547 302 IYASYALAFWYGTSLVISKEYSIGQVltVFFSVLIG 337
Cdd:cd18568 235 NHLGTIAVLWYGAYLVISGQLTIGQL--VAFNMLFG 268
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
117-337 |
1.94e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 51.05 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 117 IGAGVLIVAYIQVSFWCL-------AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLtDDVSKINEGIGDKIGMF 189
Cdd:cd18782 44 IGVVMLVAALLEAVLTALrtylftdTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 190 FQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAfggQKKE 269
Cdd:cd18782 123 LLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA---QNAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 270 L-------ERYNNNLEEAKRLGIKKAITANISmgaaFLLIYASYALAFWYGTSLVISKEYSIGQVLTvfFSVLIG 337
Cdd:cd18782 200 LkarwrwqNRYARSLGEGFKLTVLGTTSGSLS----QFLNKLSSLLVLWVGAYLVLRGELTLGQLIA--FRILSG 268
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
388-610 |
3.10e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.47 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRkevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIdGQDIRTINVRYLREIIg 467
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 468 vvsqEPvlfATTIAENIRYGredvtMDEIEKAVKEAN--AY--DFIMKLPHQfDTLVGergaQLSGGQKQRIAIARALVR 543
Cdd:TIGR03719 398 ----DP---NKTVWEEISGG-----LDIIKLGKREIPsrAYvgRFNFKGSDQ-QKKVG----QLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153791547 544 NPKILLLDEATSALDTES-EAVVQAALDKAreGrTTIVIAH-RLSTVRNADVIAGFDGGVIVE--QGNHDE 610
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETlRALEEALLNFA--G-CAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1049-1240 |
3.54e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1049 LQGLSLEVKKGQTLALVGSSGCGKSTVVQllERFYDpmagsvfldgkeikqlnvqwlRAQLGIVSQEPilfdcsiaeniA 1128
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA---------------------SGKARLISFLP-----------K 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1129 YGDNSRVvsyeeivraakeanihqFIDSLPDKYNT-----RVGDKGTQLSGGQKQRIAIARALVRQPH--ILLLDEATSA 1201
Cdd:cd03238 57 FSRNKLI-----------------FIDQLQFLIDVglgylTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153791547 1202 LDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1240
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
527-606 |
4.12e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 527 LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNADVI------AGF 597
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGK 167
|
....*....
gi 153791547 598 DGGVIVEQG 606
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1132-1246 |
5.32e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1132 NSRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGD---KGtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESek 1208
Cdd:TIGR00956 169 QNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT-- 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 153791547 1209 vvqeALDKAREGRTCIVIAHRLSTI------QNA----DLIVVIQNGK 1246
Cdd:TIGR00956 245 ----ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1050-1249 |
7.41e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1050 QGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPMA-GSVFLDGKEIKQLN-VQWLRAQLGIVSQ---EPILF-DC 1121
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFpNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1122 SIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNTR---VGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1198
Cdd:PRK09700 357 SIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153791547 1199 TSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIQNGKVKE 1249
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
398-630 |
8.91e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 398 PSRKEVQILKG------LNLKVKSGQTVALVGNSGCGKSttvQLMQRLY--DPLD-GMVSIDGQdirTINVRYLREII-- 466
Cdd:PRK11288 255 EVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRS---ELMKLLYgaTRRTaGQVYLDGK---PIDIRSPRDAIra 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 467 GVV------SQEPVLFATTIAENIRYG--REDVTMDEIEKAVKEA-NAYDFIMKL----PHQfDTLVGergaQLSGGQKQ 533
Cdd:PRK11288 329 GIMlcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 534 RIAIARALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 611
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQA 483
|
250
....*....|....*....
gi 153791547 612 MREKGIyfKLVMTQTAGNE 630
Cdd:PRK11288 484 TERQAL--SLALPRTSAAV 500
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
723-977 |
1.20e-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: 48.66 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 723 AFSVIFSKVVGVFTNGGPPETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDd 802
Cdd:cd18555 16 LLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 803 pKNTTGALTTRlANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGqalKD 882
Cdd:cd18555 95 -NRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKK---LN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 883 KKELEGSGK---IATEAIENFRTVVSLTREQKFetmYAQSLQIpYRNAM----KKAHVFGITFSFTQAMMYFSYAACFRF 955
Cdd:cd18555 170 QEEIVAQTKvqsYLTETLYGIETIKSLGSEKNI---YKKWENL-FKKQLkafkKKERLSNILNSISSSIQFIAPLLILWI 245
|
250 260
....*....|....*....|..
gi 153791547 956 GAYLVTQQLMTFeNVLLVFSAI 977
Cdd:cd18555 246 GAYLVINGELTL-GELIAFSSL 266
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
406-583 |
1.28e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDgqdirtINVRYLREIIGVVSQEPV-LFATT 479
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKISYKPQYIKPDYDGTVeDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 480 IAENIR--YGREDVtmdeIEKavkeanaydfiMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 557
Cdd:PRK13409 424 ITDDLGssYYKSEI----IKP-----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
170 180
....*....|....*....|....*...
gi 153791547 558 DTESEAVVQAALDKAREGR--TTIVIAH 583
Cdd:PRK13409 485 DVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
711-967 |
1.37e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 48.36 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 711 IFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETqrqnsnLFSLLFLILGIISFITFF--LQGFTFGKAGEILTKRLRYMV 788
Cdd:cd18782 8 LALSFVVQLLGLANPLLFQVIIDKVLVQQDLAT------LYVIGVVMLVAALLEAVLtaLRTYLFTDTANRIDLELGGTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 789 FKSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKG-----ATGSRLAVIFQNIAnlgtgIIISLIYGWQLTLLLLAIVPI 863
Cdd:cd18782 82 IDHLLRLPLGFFD--KRPVGELSTRI-SELDTIRGfltgtALTTLLDVLFSVIY-----IAVLFSYSPLLTLVVLATVPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 864 IAIAGVVEMKMLSGQaLKDKKELEGSGKIA-TEAIENFRTVVSLTRE----QKFETMYAQSLQIPYRNAMKKAHVFGITF 938
Cdd:cd18782 154 QLLLTFLFGPILRRQ-IRRRAEASAKTQSYlVESLTGIQTVKAQNAElkarWRWQNRYARSLGEGFKLTVLGTTSGSLSQ 232
|
250 260
....*....|....*....|....*....
gi 153791547 939 SFTQammyFSYAACFRFGAYLVTQQLMTF 967
Cdd:cd18782 233 FLNK----LSSLLVLWVGAYLVLRGELTL 257
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
141-326 |
1.61e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 48.35 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 141 HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINEgigdkigmFF--QAMAT---------FFGgfIIGFTrGWK 209
Cdd:cd18566 75 HRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLAlldlpfvliFLG--LIWYL-GGK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 210 LTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAI 289
Cdd:cd18566 143 LVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAK 222
|
170 180 190
....*....|....*....|....*....|....*..
gi 153791547 290 TANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQ 326
Cdd:cd18566 223 INAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGA 259
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1048-1232 |
1.83e-05 |
|
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: 48.78 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdGKEIKqlnvqwlraqLGIVSQ--EPILFDCSIAE 1125
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1126 NIAYG-DNSRVVSYEEIVRAakeanihqfidslpdkYNTRVGDKGT-------QLSGGQKQRIAIARALVRQPHILLLDE 1197
Cdd:TIGR03719 406 EISGGlDIIKLGKREIPSRA----------------YVGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153791547 1198 ATSALDTESEKVVQEALDKAreGRTCIVIAH------RLST 1232
Cdd:TIGR03719 470 PTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
400-558 |
1.86e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 400 RKEVQILKG-----LNLKVKSGQTVALVGNSGCGKSttvQLMQRLYDPL---DGMVSIDGQDIRTIN--------VRYLR 463
Cdd:PRK10762 257 RLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRT---ELMKVLYGALprtSGYVTLDGHEVVTRSpqdglangIVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 464 E-------IIGV-VSQEPVLFA----TTIAENIRYGREDVTMDeiekavkeanayDFIM----KLPHQfDTLVGErgaqL 527
Cdd:PRK10762 334 EdrkrdglVLGMsVKENMSLTAlryfSRAGGSLKHADEQQAVS------------DFIRlfniKTPSM-EQAIGL----L 396
|
170 180 190
....*....|....*....|....*....|.
gi 153791547 528 SGGQKQRIAIARALVRNPKILLLDEATSALD 558
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
369-592 |
1.86e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 369 PSIDSFSKSGHKPDNiQGNLEFKNIHFSYPSRKevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLM-----QRLYDPL 443
Cdd:PRK10938 243 PEPDEPSARHALPAN-EPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGYSNDL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 444 D--GMVSIDGQDIRTInvrylREIIGVVSQEPVL---FATTIAENIRYGREDVTmdEIEKAVKEANaydfiMKLPHQFDT 518
Cdd:PRK10938 319 TlfGRRRGSGETIWDI-----KKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSI--GIYQAVSDRQ-----QKLAQQWLD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 519 LVGERGAQ-------LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV--------- 580
Cdd:PRK10938 387 ILGIDKRTadapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaeda 465
|
250
....*....|....*
gi 153791547 581 ---IAHRLSTVRNAD 592
Cdd:PRK10938 466 pacITHRLEFVPDGD 480
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
526-585 |
2.12e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 2.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 526 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 585
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
527-599 |
3.05e-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: 46.03 E-value: 3.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 527 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDG 599
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
406-583 |
4.85e-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: 47.47 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLmqrlydpLDGMVSIDGQDIR-TINVRYLREIIGVVSQEPVlfatt 479
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKI-------LAGVLKPDEGEVDeDLKISYKPQYISPDYDGTV----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 480 iaenirygrEDVTMDEIEKAVKEANAYDFIMK---LPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSA 556
Cdd:COG1245 419 ---------EEFLRSANTDDFGSSYYKTEIIKplgLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180
....*....|....*....|....*....
gi 153791547 557 LDTESEAVVQAALDKAREGR--TTIVIAH 583
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
111-227 |
5.15e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 46.69 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 111 AYY---YTGIGAGVLIVAYIQVSFWC---LAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGD 184
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFfgsLRASRKLH---ERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELAD 119
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 153791547 185 KIGMFFQAMATFFGGFIigftrgwkltlVILAISPVLGLSAGI 227
Cdd:cd18604 120 SLSSLLESTLSLLVILI-----------AIVVVSPAFLLPAVV 151
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
723-866 |
5.85e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 46.31 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 723 AFSVIFSKVVGVFTN--------GGPPETQRQnsnlFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLR 794
Cdd:cd18606 5 LLLLILSQFAQVFTNlwlsfwteDFFGLSQGF----YIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153791547 795 QDVSWFDdpknTT--GALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYgwqLTLLLLAIVPIIAI 866
Cdd:cd18606 81 APMSFFD----TTplGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIY---LPWFAIALPPLLVL 147
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
843-966 |
6.50e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 46.40 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 843 IIISLIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGSgkiATEAIENFRTVVSLTREQKF----ETM 915
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPLYVLLTLLsspKLKRNSREIFQANAEQQSF---LVEALTGIATIKALAAERPIrwrwENK 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 153791547 916 YAQSLQIPYRNAmKKAHVFGITFSFtqaMMYFSYAACFRFGAYLVTQQLMT 966
Cdd:cd18568 210 FAKALNTRFRGQ-KLSIVLQLISSL---INHLGTIAVLWYGAYLVISGQLT 256
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
526-597 |
6.55e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 6.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 526 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGF 597
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
423-594 |
7.69e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 423 GNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTInvrylreiigvvsQEPvlFATTIAENIRYGREDVTMDEIEKAVKE 502
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKP--YCTYIGHNLGLKLEMTVFENLKFWSEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 503 ANAYDFIMKLPHQF--DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD-KAREGRTTI 579
Cdd:PRK13541 98 YNSAETLYAAIHYFklHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVL 177
|
170
....*....|....*
gi 153791547 580 VIAHRLSTVRNADVI 594
Cdd:PRK13541 178 LSSHLESSIKSAQIL 192
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
410-614 |
8.03e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 410 NLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIigvVSQEpvlFATTIAENIRYGRE 489
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDE---WQRNNTDMLSPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 490 DV---TMDEIEKAVKEANAydfIMKLPHQF--DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAV 564
Cdd:PRK10938 97 DTgrtTAEIIQDEVKDPAR---CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153791547 565 VQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:PRK10938 174 LAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1164-1240 |
8.76e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1164 RVGDKGTQLSGGQKQRIAIARALVRQPH---ILLLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1236
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....
gi 153791547 1237 DLIV 1240
Cdd:PRK00349 900 DWII 903
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
402-616 |
9.05e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 402 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVqLMQRLYDPLDGMVSIDGQdIRTINVRYLREIIGVvsQEPVLFATTIA 481
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*-TWCANRRALRRTIG*--HRPVR*GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 482 ENiryGREDVTM--DEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 559
Cdd:NF000106 101 FS---GRENLYMigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 560 ESE-AVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKG 616
Cdd:NF000106 178 RTRnEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1172-1243 |
9.25e-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: 44.49 E-value: 9.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1172 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIQ 1243
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1171-1228 |
9.72e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 9.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 1171 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARegRTCIVIAH 1228
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
372-615 |
1.29e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 372 DSFSKSGHKPDNIQGN--LEFKNIhfsypSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSttvQLMQRLY--DPL-DGM 446
Cdd:PRK09700 248 NRFNAMKENVSNLAHEtvFEVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRaGGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 447 VSIDGQDIrTINVRY--LREIIGVVSQ---EPVLFAT-TIAENI------RYGREDVTM----DEIEKAVKEANAYDFIM 510
Cdd:PRK09700 320 IRLNGKDI-SPRSPLdaVKKGMAYITEsrrDNGFFPNfSIAQNMaisrslKDGGYKGAMglfhEVDEQRTAENQRELLAL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 511 KLpHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVR 589
Cdd:PRK09700 399 KC-HSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEII 473
|
250 260
....*....|....*....|....*...
gi 153791547 590 NA-DVIAGFDGGVIVEQ-GNHDELMREK 615
Cdd:PRK09700 474 TVcDRIAVFCEGRLTQIlTNRDDMSEEE 501
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
526-583 |
1.35e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 153791547 526 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARegRTTIVIAH 583
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
208-333 |
1.40e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 45.53 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 208 WKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKK 287
Cdd:cd18567 141 PKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRL 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 153791547 288 AITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGqVLTVFFS 333
Cdd:cd18567 221 QRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVG-MLFAFLA 265
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1166-1252 |
1.55e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1166 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIV----------IAHRLSTIQ 1234
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLttqymeeaeqLAHELTVID 218
|
90
....*....|....*...
gi 153791547 1235 NADlivVIQNGKVKEHGT 1252
Cdd:NF000106 219 RGR---VIADGKVDELKT 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
388-558 |
1.78e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSttvQLMQRLYDPLDGM----VSIDGQDIRTINVR-YL 462
Cdd:PRK13549 260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRT---ELVQCLFGAYPGRwegeIFIDGKPVKIRNPQqAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 463 REIIGVVSQE-------PVLfatTIAENI------RYGREDVtmdeIEKAVKEANAYDFIMKL----PHQFdtlvgERGA 525
Cdd:PRK13549 337 AQGIAMVPEDrkrdgivPVM---GVGKNItlaaldRFTGGSR----IDDAAELKTILESIQRLkvktASPE-----LAIA 404
|
170 180 190
....*....|....*....|....*....|...
gi 153791547 526 QLSGGQKQRIAIARALVRNPKILLLDEATSALD 558
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1048-1231 |
1.81e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1048 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVFLDGKEIKQLNVQWLRaqlGIVSQEPILF-DCSIA 1124
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQETFARIS---GYCEQNDIHSpQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1125 ENIAYGDNSRV---VSYEEIVRAAKEANIHQFIDSLPDKYntrVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATS 1200
Cdd:PLN03140 972 ESLIYSAFLRLpkeVSKEEKMMFVDEVMELVELDNLKDAI---VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190
....*....|....*....|....*....|..
gi 153791547 1201 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLS 1231
Cdd:PLN03140 1049 GLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
484-600 |
2.25e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 484 IRYGREDVTmDEIEKAVKEANayDFIMKLPH-----------QFDTL-VGERGAQLSGGQKQRIAIARAL---VRNPKIL 548
Cdd:PRK00635 758 VRYKGKNIA-DILEMTAYEAE--KFFLDEPSihekihalcslGLDYLpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLY 834
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 549 LLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIA--GFDGG 600
Cdd:PRK00635 835 VLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLelGPEGG 889
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
191-339 |
2.48e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of 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: 350052 [Multi-domain] Cd Length: 294 Bit Score: 44.46 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 191 QAMATFF-GGFIIGFTrgwkltLVILAISP-----VLGLSAGIWAKILSSF------TDKELHAYAKAGAVAEEVLAAIR 258
Cdd:cd18779 118 QTLSALLdGTLVLGYL------ALLFAQSPllglvVLGLAALQVALLLATRrrvrelMARELAAQAEAQSYLVEALSGIE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 259 TVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTvfFSVLIGA 338
Cdd:cd18779 192 TLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLA--LNALAGA 269
|
.
gi 153791547 339 F 339
Cdd:cd18779 270 F 270
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
406-614 |
2.51e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 406 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQ-DIRTINVRYLREIIGVvsqepvlfattiaENI 484
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGI-------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 485 RYgrEDVTMDEIEKAVKEanaydfIMKLPHQFDTLvGERGAQ----LSGGQKQRIAIARALVRNPKILLLDEATSALDte 560
Cdd:PRK13546 107 EF--KMLCMGFKRKEIKA------MTPKIIEFSEL-GEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGD-- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153791547 561 sEAVVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 614
Cdd:PRK13546 176 -QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
527-618 |
2.70e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 527 LSGGQKQRIAIARALVR--NPKIL-LLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNAD-VI-----AG 596
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADwIIdlgpeGG 906
|
90 100
....*....|....*....|..
gi 153791547 597 FDGGVIVEQGNHDELMREKGIY 618
Cdd:COG0178 907 DGGGEIVAEGTPEEVAKVKASY 928
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1171-1258 |
2.74e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1171 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIQNGKV 1247
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 153791547 1248 KEHGTHQQLLA 1258
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
527-606 |
3.89e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 527 LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVI------AGF 597
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidigpgAGV 217
|
....*....
gi 153791547 598 DGGVIVEQG 606
Cdd:cd03270 218 HGGEIVAQG 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
527-582 |
5.83e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 5.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 527 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESE-AVVQAALDKAREGRTTIVIA 582
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIIS 448
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
409-613 |
7.44e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.50 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 409 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVR--------YL---REIIGVVSQEPVLFA 477
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglvYLpedRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 478 T-TIAEN-----IRYGREDVTMDEIEKAVKeanaydfiMKLPHqfdtlvGERGAQ-LSGGQKQRIAIARALVRNPKILLL 550
Cdd:PRK15439 362 VcALTHNrrgfwIKPARENAVLERYRRALN--------IKFNH------AEQAARtLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 551 DEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIV-----EQGNHDELMR 613
Cdd:PRK15439 428 DEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEISgaltgAAINVDTIMR 497
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
485-618 |
9.00e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 485 RYGRE---------------DVTMDEiekavkeanAYDF---IMKLPHQFDTLV---------GERGAQLSGGQKQRIAI 537
Cdd:PRK00349 771 RYNREtlevkykgkniadvlDMTVEE---------ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKL 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 538 ARALVRNP--KIL-LLDEATSALDTESEA----VVQAALDKareGRTTIVIAHRLSTVRNADVI------AGFDGGVIVE 604
Cdd:PRK00349 842 AKELSKRStgKTLyILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLDVIKTADWIidlgpeGGDGGGEIVA 918
|
170
....*....|....
gi 153791547 605 QGNHDELMREKGIY 618
Cdd:PRK00349 919 TGTPEEVAKVEASY 932
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
387-594 |
9.84e-04 |
|
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: 41.82 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 387 NLEFKNIHfSYPSRKEVQILKGLNLkvksgqtvaLVGNSGCGKSTTvqlmqrlydpLDGM-VSIDGQ-DIRTINVRYLRE 464
Cdd:cd03240 3 KLSIRNIR-SFHERSEIEFFSPLTL---------IVGQNGAGKTTI----------IEALkYALTGElPPNSKGGAHDPK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 465 IIGVvsqepvlfATTIAEnIRYGREDVTMDEIeKAVKEANAYDFIMKLPH-QFDTLVGERGAQLSGGQKQ------RIAI 537
Cdd:cd03240 63 LIRE--------GEVRAQ-VKLAFENANGKKY-TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLAL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 538 ARALVRNPKILLLDEATSALDTESEAVVQAALDKAREG---RTTIVIAHRLSTVRNADVI 594
Cdd:cd03240 133 AETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVDAADHI 192
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1170-1240 |
1.06e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1170 TQLSGGQKQRIAIARALVR---QPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1240
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1171-1240 |
1.19e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 1.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153791547 1171 QLSGGQKQRIAIARALVRQPH----ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1240
Cdd:cd03227 77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
135-332 |
1.24e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 42.27 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 135 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVI 214
Cdd:cd18561 63 AAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALIL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 215 LAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANIS 294
Cdd:cd18561 143 LVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLS 222
|
170 180 190
....*....|....*....|....*....|....*...
gi 153791547 295 MGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFF 332
Cdd:cd18561 223 SGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILF 260
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
526-612 |
1.80e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.10 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 526 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVI 602
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 153791547 603 VEQGNHDELM 612
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1044-1079 |
2.14e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 2.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 153791547 1044 PSIPV-----LQGLSLEV-----KKGQTLALVGSSGCGKSTVV-QLL 1079
Cdd:PRK01889 170 PGVPVlavsaLDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
388-581 |
2.56e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 388 LEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLMQRLYDP-LDGMVSIDGQDIRTINVR----- 460
Cdd:NF040905 258 FEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSdaida 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 461 ---YL---REIIGVVSQEPVLFATTIAENIRYGREDVtMDEIEKaVKEANAY--DFIMKLPHqfdtlVGERGAQLSGGQK 532
Cdd:NF040905 338 glaYVtedRKGYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPS-----VFQKVGNLSGGNQ 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153791547 533 QRIAIARALVRNPKILLLDEATSALDT----ESEAVVQaalDKAREGRTTIVI 581
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIIN---ELAAEGKGVIVI 460
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1041-1226 |
2.69e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1041 PTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-MAGSVFLDGKEIKQLNVQWL-----------RA 1107
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1108 QLGIVSQEPILFDCSIA--ENIAygdNSRVVSYEEIVRAAKEanihqFIDSLpdkyNTR---VGDKGTQLSGGQKQRIAI 1182
Cdd:NF040905 348 GYGLNLIDDIKRNITLAnlGKVS---RRGVIDENEEIKVAEE-----YRKKM----NIKtpsVFQKVGNLSGGNQQKVVL 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 153791547 1183 ARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1226
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1165-1269 |
3.66e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 1165 VGDKGTQLSGGQKQRIAIARALV---RQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1240
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
90 100 110
....*....|....*....|....*....|..
gi 153791547 1241 VIQNGKVKEHGthqQLL---AQKGIYFSMVSV 1269
Cdd:PRK00635 1773 EMGPGSGKTGG---KILfsgPPKDISASKDSL 1801
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
750-870 |
5.47e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 40.53 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 750 LFSLLFLILGIISFITFFLQGFtfgKAGEILTKRLRYMVFKSMLRqdvsWFDdpKNTTGALTTRLANDAAQVkgatGSRL 829
Cdd:cd18604 51 LISLLSVLLGTLRYLLFFFGSL---RASRKLHERLLHSVLRAPLR----WLD--TTPVGRILNRFSKDIETI----DSEL 117
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 153791547 830 AVIFQNIANLGTGIIISLIygwqltlLLLAIVPIIAIAGVV 870
Cdd:cd18604 118 ADSLSSLLESTLSLLVILI-------AIVVVSPAFLLPAVV 151
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
747-885 |
5.63e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 40.48 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 747 NSNLFSLLFLILGIISFITFFL--------QGFTFGKAGEILtKRLRYMVFKSMLRQDVSWFDDpkNTTGALTTRLANDA 818
Cdd:cd18554 37 LDEKVYKLFTIIGIMFFIFLILrppveyyrQYFAQWIANKIL-YDIRKDLFDHLQKLSLRYYAN--NRSGEIISRVINDV 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 819 AQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAgvveMKMLSGQALKDKKE 885
Cdd:cd18554 114 EQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILA----VKYFFGRLRKLTKE 176
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
745-966 |
6.31e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 40.14 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 745 RQNSNLFSLL---FLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDdpKNTTGALTTRLaNDAAQV 821
Cdd:cd18567 35 SGDRDLLTVLaigFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFE--KRHLGDIVSRF-GSLDEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 822 KGA-TGSRLAVIFQNIANLGTGIIIsLIYGWQLTLLLLAIVPIIAIagvveMKMLSGQALKDKKE--LEGSGKIATEAIE 898
Cdd:cd18567 112 QQTlTTGFVEALLDGLMAILTLVMM-FLYSPKLALIVLAAVALYAL-----LRLALYPPLRRATEeqIVASAKEQSHFLE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 899 NFRTVVSL-------TREQKFETMYAQSLqipyrNAMKKAHVFGITFSFTQAM-MYFSYAACFRFGAYLVTQQLMT 966
Cdd:cd18567 186 TIRGIQTIklfgreaEREARWLNLLVDAI-----NADIRLQRLQILFSAANGLlFGLENILVIYLGALLVLDGEFT 256
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1172-1240 |
7.17e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 7.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153791547 1172 LSGGQKQRIAIARAL------VrqphILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1240
Cdd:cd03270 138 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
124-332 |
7.19e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 40.10 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 124 VAYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIG 203
Cdd:cd18554 62 VEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIM 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 204 FTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRL 283
Cdd:cd18554 142 LVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTR 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153791547 284 GIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQvLTVFF 332
Cdd:cd18554 222 ALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGT-LVAFV 269
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1170-1240 |
8.74e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 8.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153791547 1170 TQLSGGQKQRIAIarALV-----RQPH-ILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIV 1240
Cdd:pfam02463 1076 DLLSGGEKTLVAL--ALIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
530-612 |
9.12e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153791547 530 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH-R--LSTV--RNADViagfDGGVI-V 603
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL-NERNS-TMIIISHdRhfLNSVctHMADL----DYGELrV 232
|
....*....
gi 153791547 604 EQGNHDELM 612
Cdd:PRK15064 233 YPGNYDEYM 241
|
|
| |
