|
Name |
Accession |
Description |
Interval |
E-value |
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-1469 |
0e+00 |
|
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: 2624.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1 MQRSPLEKASVVSKLFFSWTRPILKKGYRQRLELSDIYHISSSDSADNLSEKLEREWDRELAS-KKNPKLINALRRCFFW 79
Cdd:TIGR01271 1 MQRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASaKKNPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 80 RFMFYGIILYLGEVTKAVQPLLLGRIIASYDPDNKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSL 159
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 160 IYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAFTFCGLAFLVVLALLQAG 239
Cdd:TIGR01271 161 IYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 240 LGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLNSSAFFFSGFFVVF 319
Cdd:TIGR01271 241 LGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 320 LSVLPYALLKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTDVVMENVTA 399
Cdd:TIGR01271 321 LSVVPYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 400 FWEEGFSKLFEKAKENNNNRKISNCDTSLFFSNL-LLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSE 478
Cdd:TIGR01271 401 SWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNFsLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 479 GKIKHSGRISFCSQYSWIMPGTIKDNIIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLA 558
Cdd:TIGR01271 481 GKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 559 RAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRPD 638
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 639 FSSKLMGCDTFDQFTAERRNSIITETLRRFSLEGD-TSVSWNETKKPSFKQTG-EFGEKRKNS-ILNSINSIRKFSVVQK 715
Cdd:TIGR01271 641 FSSLLLGLEAFDNFSAERRNSILTETLRRVSIDGDsTVFSGPETIKQSFKQPPpEFAEKRKQSiILNPIASARKFSFVQM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 716 TSLQMNG--IDGASDEPLERRLSLVPHSEPGEGILPRSNAVNSGPTFLGGRRQSVLNLMTCSsvNQGQSIHRKTATSTRK 793
Cdd:TIGR01271 721 GPQKAQAttIEDAVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHS--NRGENRREQLQTSFRK 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 794 MSLAPQAS--LAEIDIYSRRLSQDTGLEISEEINEEDLRDCFFDDVENIPAVTTWNTYLRYITVHKSLMFVLIWCLVVFL 871
Cdd:TIGR01271 799 KSSITQQNelASELDIYSRRLSKDSVYEISEEINEEDLKECFADERENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFL 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 872 VEVAASLVVLCLF---PKILLQDKGNSTKNAS--NSYAVIITSTSSYYIFYIYVGVADTLLALGLFRGLPLVHTLITVSK 946
Cdd:TIGR01271 879 AEVAASLLGLWLItdnPSAPNYVDQQHANASSpdVQKPVIITPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSK 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 947 TLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAF 1026
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIF 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1027 ILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMI 1106
Cdd:TIGR01271 1039 IMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1107 FVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEDGKPNNSFRPskdS 1186
Cdd:TIGR01271 1119 FVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGK---Y 1195
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1187 QPSKVMIIENQHVKKddIWPSGGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKG 1266
Cdd:TIGR01271 1196 QLSTVLVIENPHAQK--CWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG 1273
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1267 EIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCV 1346
Cdd:TIGR01271 1274 EIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYV 1353
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1347 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 1426
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*
gi 57526399 1427 SIQRMLSEKSLFRQAISPADRLKLLP--HRNSSRQRSRANIAALK 1469
Cdd:TIGR01271 1434 SIQKLLNETSLFKQAMSAADRLKLFPlhRRNSSKRKPQPKITALR 1478
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
844-1167 |
0e+00 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; 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: 350044 [Multi-domain] Cd Length: 324 Bit Score: 578.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 844 TTWNTYLRYITVHKSLMFVLIWCLVVFLVEVAASLVVLCLFPKILLQDKGNSTKNASNSYAVIITSTSSYYIFYIYVGVA 923
Cdd:cd18600 1 TTWNTYLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 924 DTLLALGLFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIG 1003
Cdd:cd18600 81 DSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1004 AVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALN 1083
Cdd:cd18600 161 AITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1084 LHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVSRV 1163
Cdd:cd18600 241 LHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
....
gi 57526399 1164 FKFI 1167
Cdd:cd18600 321 FKFI 324
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
389-669 |
0e+00 |
|
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: 563.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 389 TTDVVMENVTAFWEEGFSKLFEKAKENNNNRKISNCDTSLFFSNL-LLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLL 467
Cdd:cd03291 1 TTGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNLcLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 468 MMIMGELEPSEGKIKHSGRISFCSQYSWIMPGTIKDNIIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITL 547
Cdd:cd03291 81 MLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 548 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYG 627
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 57526399 628 TFSELQNQRPDFSSKLMGCDTFDQFTAERRNSIITETLRRFS 669
Cdd:cd03291 241 TFSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRRFS 282
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1209-1469 |
2.24e-166 |
|
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: 500.54 E-value: 2.24e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1209 GQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKGEIQIDGVSWDSITLQQWRKAFG 1288
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 1368
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1369 LLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQAISPADRL 1448
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
|
250 260
....*....|....*....|...
gi 57526399 1449 KLLPHRNSS--RQRSRANIAALK 1469
Cdd:cd03289 241 KLFPRRNSSksKRKPRPQIQALQ 263
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-1438 |
1.38e-152 |
|
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: 503.32 E-value: 1.38e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 5 PLEKASVVSKLFFSWTRPILKKGYRQRLELSDIYHISSSDSADNLSEKLEREWDRELAS--------------------- 63
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKtrkqpvsavygkkdpskpkgs 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 64 -------------------KKNPKLINALRRCFFWRFMFYGIILYLGEVTKAVQPLLLgRIIASYDPDNKVERSIAIYLG 124
Cdd:TIGR00957 283 sqldaneevealivksphkPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQIL-SLLIRFVNDPMAPDWQGYFYT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 125 IGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIA 204
Cdd:TIGR00957 362 GLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSA 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 205 PLQVTLLMGLLWDLLQAFTFCGLAFLVVLALLQAGLGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKI 284
Cdd:TIGR00957 442 PLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDK 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 285 IENLRQTELKLTRKAAYVRYLNSSAFFFS--GFFVVFLSVLPYALLKGII-LRKIFTTISFCIVLRMAVTrQFPWAVQTW 361
Cdd:TIGR00957 522 VEGIRQEELKVLKKSAYLHAVGTFTWVCTpfLVALITFAVYVTVDENNILdAEKAFVSLALFNILRFPLN-ILPMVISSI 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 362 YDSLGAINKIQDFLQKQEYKTLEYNLTTTD------VVMENVTAFWEEGFSklfekakennnnrkisncdtslffsnlll 435
Cdd:TIGR00957 601 VQASVSLKRLRIFLSHEELEPDSIERRTIKpgegnsITVHNATFTWARDLP----------------------------- 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 gtPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYSWIMPGTIKDNIIFGVSYDEYR 515
Cdd:TIGR00957 652 --PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKY 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 516 YRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCK--L 593
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegV 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 594 MANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRPDFSSKLmgcdtfdqftaerRNSIITETlrrfslEGD 673
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL-------------RTYAPDEQ------QGH 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 674 TSVSWNetkkpsfkqTGEFGEKRKNSILNsiNSIRKFSVVQKTslqmngidgasdepLERRLSlvPHSEPGEGIlprsna 753
Cdd:TIGR00957 871 LEDSWT---------ALVSGEGKEAKLIE--NGMLVTDVVGKQ--------------LQRQLS--ASSSDSGDQ------ 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 754 vnsgptflgGRRQSvlnlmtcsSVNQGQSIHRKTATStrKMSLAPQASLAEIDIysrrlsqdtgleiseeineedlrDCF 833
Cdd:TIGR00957 918 ---------SRHHG--------SSAELQKAEAKEETW--KLMEADKAQTGQVEL-----------------------SVY 955
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 834 FDDVENIPAVTTWNTYLRYITVHKSLMFVLIWcLVVFLVEVAAslvvlclfpkillqdkgNSTKNASNsyaviiTSTSSY 913
Cdd:TIGR00957 956 WDYMKAIGLFITFLSIFLFVCNHVSALASNYW-LSLWTDDPMV-----------------NGTQNNTS------LRLSVY 1011
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 914 YIFYIYVGVADTLLALGLFRGLplvhtlITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFD 993
Cdd:TIGR00957 1012 GALGILQGFAVFGYSMAVSIGG------IQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKM 1085
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 994 FIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPY 1073
Cdd:TIGR00957 1086 FMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQER 1165
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1074 FETLFHKALNLHTANWFLYLSTLRWFQMRIEMI--FVIFFIAVtFISILTTGEGEGRVGIILTLAMNIMGTLQWAVNSSI 1151
Cdd:TIGR00957 1166 FIHQSDLKVDENQKAYYPSIVANRWLAVRLECVgnCIVLFAAL-FAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSS 1244
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1152 DVDSLMRSVSRVFKFIDMPTEdgkpnnsfrpskdsQPSKVmiienQHVKKDDIWPSGGQMTVKDLTAKYIDGGNAILENI 1231
Cdd:TIGR00957 1245 EMETNIVAVERLKEYSETEKE--------------APWQI-----QETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHI 1305
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1232 SFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNT-KGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQ 1310
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ 1385
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1311 WSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLK 1390
Cdd:TIGR00957 1386 YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*...
gi 57526399 1391 QAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLF 1438
Cdd:TIGR00957 1466 TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-1446 |
1.26e-145 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 483.71 E-value: 1.26e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 5 PLEKASVVSKLFFSWTRPILKKGYRQRLELSDIYHISSSDSADNLSEKLEREWDRElASKKNPKLINALRRCFFWRFMFY 84
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE-SRRPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 85 GIILYLGEVTKAVQPLLLGRIIASY---DPD-NKVERSIAIYLGIGLCLLFIVRTLLlhpaifGLHHIGMQMRIAMFSLI 160
Cdd:PLN03232 307 GIFKIGHDLSQFVGPVILSHLLQSMqegDPAwVGYVYAFLIFFGVTFGVLCESQYFQ------NVGRVGFRLRSTLVAAI 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAFTFCGLAFLVVLALLQAGL 240
Cdd:PLN03232 381 FHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 241 GKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLNSSAFFFSGFFVVFL 320
Cdd:PLN03232 461 VRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLV 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 321 SVLPYALLKG-IILRKIFTTISFCIVLRMAVTrQFPWAVQTWYDSLGAINKIQDFLQKQEyKTLEYNLT----TTDVVME 395
Cdd:PLN03232 541 SFGVFVLLGGdLTPARAFTSLSLFAVLRSPLN-MLPNLLSQVVNANVSLQRIEELLLSEE-RILAQNPPlqpgAPAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 396 NVTAFWEEGFSKlfekakennnnrkisncdtslffsnlllgtPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELE 475
Cdd:PLN03232 619 NGYFSWDSKTSK------------------------------PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 476 PSE-GKIKHSGRISFCSQYSWIMPGTIKDNIIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRAR 554
Cdd:PLN03232 669 HAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQR 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 555 ISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQN 634
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 635 QRPDFSSKLMGCDTFDQFTAERRNSiitETLRRFSleGDTSVSWNETKKPSFKQtgefgekrknsilnsinsirkfsvvq 714
Cdd:PLN03232 829 SGSLFKKLMENAGKMDATQEVNTND---ENILKLG--PTVTIDVSERNLGSTKQ-------------------------- 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 715 ktslqmngidgasdeplerrlslvphsepgegilprsnavnsgptflGGRRQSVLnlmtcssvnqgqsihrktatstrkm 794
Cdd:PLN03232 878 -----------------------------------------------GKRGRSVL------------------------- 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 795 slapqaslaeidiysrrlsqdtgleISEEINEEdlrdcffddvenipAVTTWNTYLRYITVHKSLMFVLIWCLVVFLVEV 874
Cdd:PLN03232 886 -------------------------VKQEERET--------------GIISWNVLMRYNKAVGGLWVVMILLVCYLTTEV 926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 875 --AASLVVLCLFpkillqdkgnSTKNASNSYaviitsTSSYYIFyIYVGVADTLLALGLFRGLPLVHTLITVSKTLHHKM 952
Cdd:PLN03232 927 lrVSSSTWLSIW----------TDQSTPKSY------SPGFYIV-VYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAM 989
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 953 LQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAFILLRGY 1032
Cdd:PLN03232 990 LNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLY 1069
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1033 FLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIF-VIFF 1111
Cdd:PLN03232 1070 YQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGgVMIW 1149
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1112 IAVTFiSILTTGEGEGRV------GIILTLAMNIMGTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEdgkpnnsfrpskd 1185
Cdd:PLN03232 1150 LTATF-AVLRNGNAENQAgfastmGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSE------------- 1215
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1186 sqpsKVMIIENQhvKKDDIWPSGGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNT- 1264
Cdd:PLN03232 1216 ----ATAIIENN--RPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELe 1289
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1265 KGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGG 1344
Cdd:PLN03232 1290 KGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGG 1369
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1345 CVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 1424
Cdd:PLN03232 1370 ENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
1450 1460
....*....|....*....|....*.
gi 57526399 1425 YDSIQRMLSEK--SLFR--QAISPAD 1446
Cdd:PLN03232 1450 YDSPQELLSRDtsAFFRmvHSTGPAN 1475
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-1438 |
1.62e-134 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 454.97 E-value: 1.62e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 5 PLEKASVVSKLFFSWTRPILKKGYRQRLELSDIYHISSSDSADNLSEKLEREWDRELaSKKNPKLINALRRCFFWRFMFY 84
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEEL-KKPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 85 GIILYLGEVTKAVQPLLLGRIIASYDPDNKVER----SIAIYLGIGLCLLF-------IVRTlllhpaifglhhiGMQMR 153
Cdd:PLN03130 307 GFFKIGNDLSQFVGPLLLNLLLESMQNGEPAWIgyiyAFSIFVGVVLGVLCeaqyfqnVMRV-------------GFRLR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 154 IAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAFTFCGLAFLVVL 233
Cdd:PLN03130 374 STLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLM 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 234 ALLQAGLGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLNSSAFFFS 313
Cdd:PLN03130 454 FPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSI 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 314 GFFVVFLSVLPYALLKGIIL-RKIFTTISFCIVLRMAVTrQFPWAVQTWYDSLGAINKIQDFLQKQEY-----KTLEYNL 387
Cdd:PLN03130 534 PVLVTVVSFGVFTLLGGDLTpARAFTSLSLFAVLRFPLF-MLPNLITQAVNANVSLKRLEELLLAEERvllpnPPLEPGL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 388 TTtdVVMENVTAFWEegfSKLfEKakennnnrkisncdtslffsnlllgtPVLKDISFKIERGQLLAVAGSTGAGKTSLL 467
Cdd:PLN03130 613 PA--ISIKNGYFSWD---SKA-ER--------------------------PTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 468 MMIMGELEP-SEGKIKHSGRISFCSQYSWIMPGTIKDNIIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGIT 546
Cdd:PLN03130 661 SAMLGELPPrSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVN 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 547 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFY 626
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 627 GTFSELQNQRPDFSsKLMgcdtfdqftaERRNSiitetLRRFSLEGDTSVSWNETKKPsfKQTGEFGEKRKNSILNSiNS 706
Cdd:PLN03130 821 GTYEELSNNGPLFQ-KLM----------ENAGK-----MEEYVEENGEEEDDQTSSKP--VANGNANNLKKDSSSKK-KS 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 707 IRKFSVVQKTSLQMNGIdgASDEPLERRlslvphsepgegilprSNAvnsgptfLGGRrQSVLNLMTCSSvnqgqsihrk 786
Cdd:PLN03130 882 KEGKSVLIKQEERETGV--VSWKVLERY----------------KNA-------LGGA-WVVMILFLCYV---------- 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 787 tatstrkmslapqasLAEIdiysRRLSQDTGLeiSEEINEEDLRDcffddvenipavttwntylryitvHKSLMFVLIWC 866
Cdd:PLN03130 926 ---------------LTEV----FRVSSSTWL--SEWTDQGTPKT------------------------HGPLFYNLIYA 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 867 LVVFlvevaaslvvlclfpkillqdkGNSTKNASNSYAVIITSTSSyyifyiyvgvadtllalglfrglplvhtlitvSK 946
Cdd:PLN03130 961 LLSF----------------------GQVLVTLLNSYWLIMSSLYA--------------------------------AK 986
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 947 TLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFI----QLL--LIVIGAVVVVSvlqpyiFLATV 1020
Cdd:PLN03130 987 RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqifQLLstFVLIGIVSTIS------LWAIM 1060
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1021 PVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQ 1100
Cdd:PLN03130 1061 PLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLA 1140
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1101 MRIEMI--FVIFFIAvTFiSILTTGEGEGRV------GIILTLAMNIMGTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTE 1172
Cdd:PLN03130 1141 IRLETLggLMIWLTA-SF-AVMQNGRAENQAafastmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSE 1218
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1173 dgKPnnsfrpskdsqpskvMIIENQhvKKDDIWPSGGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKS 1252
Cdd:PLN03130 1219 --AP---------------LVIENN--RPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKS 1279
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1253 TLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQ 1331
Cdd:PLN03130 1280 SMLNALFRIVElERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRR 1359
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1332 FPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLEC 1411
Cdd:PLN03130 1360 NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDC 1439
|
1450 1460
....*....|....*....|....*...
gi 57526399 1412 QRFLVIEENKVRQYDSIQRMLS-EKSLF 1438
Cdd:PLN03130 1440 DRILVLDAGRVVEFDTPENLLSnEGSAF 1467
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
83-372 |
1.34e-119 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 375.82 E-value: 1.34e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 83 FYGIILYLGEVTKAVQPLLLGRIIASYDPDNKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYK 162
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 163 KTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAFTFCGLAFLVVLALLQAGLGK 242
Cdd:cd18594 81 KTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 243 MMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLNSSAFFFSGFFVVFLSV 322
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 323 LPYALLKGII-LRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQ 372
Cdd:cd18594 241 VPYVLTGNTLtARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
69-1439 |
9.97e-117 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 403.01 E-value: 9.97e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 69 LINALRRCFFWRFMFygiiLYLGEVTKAVQPLLLGRIIASYDPDNKVERSiaiylGIGLCLLFIVRTLLLHPAIFGLHHI 148
Cdd:PTZ00243 238 LFAALPYYVWWQIPF----KLLSDVCTLTLPVLLKYFVKFLDADNATWGR-----GLGLVLTLFLTQLIQSVCLHRFYYI 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 149 ----GMQMRIAMFSLIYKKTLKLSSRVLDK--ISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAF 222
Cdd:PTZ00243 309 sircGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWC 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 223 TFCGLAFLVVLALLQAGLGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYV 302
Cdd:PTZ00243 389 ALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 303 RYLNSSAFFFSGFFVVFLSVLPYALLkGIILRK--IFTTISFCIVLRMAVtRQFPWAVQTWYDSLGAINKIQDFLQ---- 376
Cdd:PTZ00243 469 RVATSFVNNATPTLMIAVVFTVYYLL-GHELTPevVFPTIALLGVLRMPF-FMIPWVFTTVLQFLVSIKRISTFLEcdna 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 377 -------KQEYKTLEYNLTTT---DVVMEN--VTAFW------------------------------------------- 401
Cdd:PTZ00243 547 tcstvqdMEEYWREQREHSTAcqlAAVLENvdVTAFVpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedt 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 402 -------------EEGFSKLFEKAKENNNNRKISNCDTSLFFSnlLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLM 468
Cdd:PTZ00243 627 dygspssasrhivEGGTGGGHEATPTSERSAKTPKMKTDDFFE--LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQ 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 469 MIMGELEPSEGKIKHSGRISFCSQYSWIMPGTIKDNIIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLS 548
Cdd:PTZ00243 705 SLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLS 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 549 GGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGT 628
Cdd:PTZ00243 785 GGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGS 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 629 FSelqnqrpDFssklMGCDTFDQFTAERRNSiitetlrrfslegdtsvswnetkkpsfkqtgefgEKRKNSILNsinsir 708
Cdd:PTZ00243 865 SA-------DF----MRTSLYATLAAELKEN----------------------------------KDSKEGDAD------ 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 709 kfsvvqktslqmngidgASDEPLERRLSLVPHSEPGEGiLPRSNAVNSGPTflggrrqsvlnlmtcssvnqgqsihRKTA 788
Cdd:PTZ00243 894 -----------------AEVAEVDAAPGGAVDHEPPVA-KQEGNAEGGDGA-------------------------ALDA 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 789 TSTRKMSLAPQASlaeidiysrrlsqdtgleiseeineedlrdcffddvENIPavttWNTYLRYITVHKSLMFVLIWCLV 868
Cdd:PTZ00243 931 AAGRLMTREEKAS------------------------------------GSVP----WSTYVAYLRFCGGLHAAGFVLAT 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 869 VFLVEV--AASLVVLCLFpkillqdkgnSTKNASnsyaviiTSTSSYYIFYIYVGVADTLlalglfrGLPL-----VHTL 941
Cdd:PTZ00243 971 FAVTELvtVSSGVWLSMW----------STRSFK-------LSAATYLYVYLGIVLLGTF-------SVPLrfflsYEAM 1026
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 942 ITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVP 1021
Cdd:PTZ00243 1027 RRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVP 1106
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1022 VIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQpyfETLFHKALN----LHTANwFLYLSTLR 1097
Cdd:PTZ00243 1107 CGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKA---HLVMQEALRrldvVYSCS-YLENVANR 1182
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1098 WFQMRIEMIFVIFFIAVTFISILTTGEGEGR--VGII---LTLAMNIMGTLQWAVNSSIDVDSLMRSVSRVFKFID---- 1168
Cdd:PTZ00243 1183 WLGVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVslsLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDevph 1262
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1169 --MPTEDGKPNNSFRPSKDSQP-SKVMIIENQHVKKDDIWP-SGGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLL 1244
Cdd:PTZ00243 1263 edMPELDEEVDALERRTGMAADvTGTVVIEPASPTSAAPHPvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIV 1342
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1245 GRTGSGKSTLLLAFLRLLNT-KGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEV 1323
Cdd:PTZ00243 1343 GRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELV 1422
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1324 GLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK-AKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSE 1402
Cdd:PTZ00243 1423 GLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIA 1502
|
1450 1460 1470
....*....|....*....|....*....|....*...
gi 57526399 1403 HRIEAMLECQRFLVIEENKVRQYDSIQRM-LSEKSLFR 1439
Cdd:PTZ00243 1503 HRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFH 1540
|
|
| CFTR_R |
pfam14396 |
Cystic fibrosis TM conductance regulator (CFTR), regulator domain; |
638-849 |
3.34e-115 |
|
Cystic fibrosis TM conductance regulator (CFTR), regulator domain;
Pssm-ID: 464164 Cd Length: 213 Bit Score: 360.59 E-value: 3.34e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 638 DFSSKLMGCDTFDQFTAERRNSIITETLRRFSLEGDTSVSWNETKKPSFKQTGEFGEKRKNS-ILNSINSIRKFSVVQKT 716
Cdd:pfam14396 1 DFSSLLMGLEAFDNFSAERRNSILTETLRRFSVDEDAGGSRNEPKKQSFKQTDDFNEKRKNSvILNPLAASRKFSIIQKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 717 SLQMNGIDGASDEPLERRLSLVPHSEPGEGILPRSNAVNSGPTFLGGRRQSVLNLMTcSSVNQGQSIHRKTATSTRKMSL 796
Cdd:pfam14396 81 QLQMNGIEEGLSELPERRLSLVPESEQGEAALPRSNVLNTGPTLQGQRRQSVLALMT-NTVAQGQGRREKGQSSFRKMSV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 797 APQASLA-EIDIYSRRLSQDTGLEISEEINEEDLRDCFFDDVENIPAVTTWNTY 849
Cdd:pfam14396 160 VPQSNLAsELDIYARRLSKDSVLDITEEINEEDLKECFADDIENVFETTTWNTY 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
392-622 |
3.25e-94 |
|
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: 302.08 E-value: 3.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 392 VVMENVTAFWEEGFSKlfekakennnnrkisncdtslffsnlllGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIM 471
Cdd:cd03250 1 ISVEDASFTWDSGEQE----------------------------TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 472 GELEPSEGKIKHSGRISFCSQYSWIMPGTIKDNIIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQ 551
Cdd:cd03250 53 GELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 552 RARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCK-LMANKTRILVTSKMEHLKKADKILILHEGS 622
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGlLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1209-1427 |
1.58e-86 |
|
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: 281.30 E-value: 1.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1209 GQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKAF 1287
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFrLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 1367
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1368 LLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDS 1427
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
895-1163 |
7.99e-80 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 266.11 E-value: 7.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 895 STKNASNSYAVIITSTSSYYIFYIYVGVADTLLALGLFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILN 974
Cdd:cd18601 41 DRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 975 RFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTH 1054
Cdd:cd18601 121 RFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSH 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1055 LVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISI-LTTGEGEGRVGIIL 1133
Cdd:cd18601 201 LSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLATSRWLAVRLDALCALFVTVVAFGSLfLAESLDAGLVGLSL 280
|
250 260 270
....*....|....*....|....*....|
gi 57526399 1134 TLAMNIMGTLQWAVNSSIDVDSLMRSVSRV 1163
Cdd:cd18601 281 SYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
865-1167 |
5.94e-74 |
|
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: 248.19 E-value: 5.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 865 WCLVVFLVevaASLVVLCLFPKILLqdkgnstKNASNSYAVIITSTSSYYIFYIYVGVADTLLALGLFRGLPLVHTLITV 944
Cdd:cd18580 1 VLLLLLLL---LLLAFLSQFSNIWL-------DWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 945 SKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIA 1024
Cdd:cd18580 71 SRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1025 AFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIE 1104
Cdd:cd18580 151 VYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1105 MIFVIFFIAVTFISILTTGE-GEGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVSRVFKFI 1167
Cdd:cd18580 231 LLGALLALVVALLAVLLRSSiSAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
845-1422 |
2.04e-73 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 256.63 E-value: 2.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 845 TWNTYLRYITVHKSLMFVLIwclVVFLVEVAASLVVLCLFPKILlqDKGNSTKNASNSYAVIItstssyyifyIYVGVAD 924
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILAL---LLLLLSALLELLLPLLLGRII--DALLAGGDLSALLLLLL----------LLLGLAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 925 TLLALGLFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGA 1004
Cdd:COG1132 73 LRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1005 VVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNL 1084
Cdd:COG1132 153 LVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1085 HTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGE---GRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVS 1161
Cdd:COG1132 233 LRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSltvGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1162 RVFKFIDMPTEdgkpnnsfrpskdsqpskvmIIENQHVKKDDiwPSGGQMTVKDLTAKYiDGGNAILENISFSISPGQRV 1241
Cdd:COG1132 313 RIFELLDEPPE--------------------IPDPPGAVPLP--PVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1242 GLLGRTGSGKSTlllaflrLLN--------TKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL---DPYEq 1310
Cdd:COG1132 370 ALVGPSGSGKST-------LVNlllrfydpTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPDA- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1311 wSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLK 1390
Cdd:COG1132 442 -TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALE 520
|
570 580 590
....*....|....*....|....*....|..
gi 57526399 1391 QAFADCTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:COG1132 521 RLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
927-1440 |
2.57e-62 |
|
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: 227.41 E-value: 2.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 927 LALGLFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSkDIAVLDDLLP----LTIFDFIQLL--LI 1000
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgsllTALLDLLFVLifLI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1001 VIGAVVVVSVLqpyIFLATVPVIAAFILLRGYFLHtSQQLKQLESEGRspIFTHLVTSLKGLWTLRAFGRQPYF----ET 1076
Cdd:COG2274 289 VLFFYSPPLAL---VVLLLIPLYVLLGLLFQPRLR-RLSREESEASAK--RQSLLVETLRGIETIKALGAESRFrrrwEN 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1077 LFHKALNL-----HTANWFLYLSTLrwfqmriemIFVIFFIAVTFISILTTGEGEGRVG------IILTLAMNIMGTLqw 1145
Cdd:COG2274 363 LLAKYLNArfklrRLSNLLSTLSGL---------LQQLATVALLWLGAYLVIDGQLTLGqliafnILSGRFLAPVAQL-- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1146 aVNSSIDVDSLMRSVSRVFKFIDMPTE-DGKPNNSFRPSKDsqpskvmiienqhvkkddiwpsgGQMTVKDLTAKYIDGG 1224
Cdd:COG2274 432 -IGLLQRFQDAKIALERLDDILDLPPErEEGRSKLSLPRLK-----------------------GDIELENVSFRYPGDS 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1225 NAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRK 1303
Cdd:COG2274 488 PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLgLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1304 NL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 1380
Cdd:COG2274 568 NItlgDPDA--TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAE 645
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1381 TYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQ 1440
Cdd:COG2274 646 TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAE 705
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
964-1441 |
8.27e-59 |
|
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: 213.47 E-value: 8.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 964 LNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYI-FLATVPVIAAFILLRGYFLHTSQQLKQ 1042
Cdd:COG4987 106 LARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALaLVLALGLLLAGLLLPLLAARLGRRAGR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1043 LESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFEtlfhKALNLHTANWFLYLSTLRWFQMRIE--MIFVIFFIAVTFISIL 1120
Cdd:COG4987 186 RLAAARAALRARLTDLLQGAAELAAYGALDRAL----ARLDAAEARLAAAQRRLARLSALAQalLQLAAGLAVVAVLWLA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1121 TTGEGEGRVGIILtLAMNIMGTLqwavnSSIDV-----------DSLMRSVSRVFKFIDMPTEDGKPNNSFRPskdsqps 1189
Cdd:COG4987 262 APLVAAGALSGPL-LALLVLAAL-----ALFEAlaplpaaaqhlGRVRAAARRLNELLDAPPAVTEPAEPAPA------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1190 kvmiienqhvkkddiwPSGGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEI 1268
Cdd:COG4987 329 ----------------PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpQSGSI 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1269 QIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGC 1345
Cdd:COG4987 393 TLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGR 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1346 VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQY 1425
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
490
....*....|....*.
gi 57526399 1426 DSIQRMLSEKSLFRQA 1441
Cdd:COG4987 551 GTHEELLAQNGRYRQL 566
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
83-371 |
6.53e-57 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 199.37 E-value: 6.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 83 FYGIILYLGEVTKAVQPLLLGRIIASYDPDNK-VERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIY 161
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSsISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 162 KKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAFTFCGLAFLVVLALLQAGLG 241
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 242 KMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLNSSAFFFSGFFVVFLS 321
Cdd:cd18593 161 KLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 322 VLPYALLKGIIL-RKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKI 371
Cdd:cd18593 241 FLAYILLGNILTaERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
85-371 |
9.27e-54 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 190.00 E-value: 9.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 85 GIILYLGEVTKAVQPLLLGRIIASYDPDNKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKT 164
Cdd:cd18579 3 GLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 165 LKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAFTFCGLAFLVVLALLQAGLGKMM 244
Cdd:cd18579 83 LRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 245 MKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLNSSAFFFSGFFVVFLSVLP 324
Cdd:cd18579 163 SKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFAT 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 57526399 325 YALLKGII-LRKIFTTISFCIVLRMaVTRQFPWAVQTWYDSLGAINKI 371
Cdd:cd18579 243 YVLLGNPLtAAKVFTALSLFNLLRF-PLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1205-1427 |
2.80e-53 |
|
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: 185.69 E-value: 2.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1205 WPSGGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQW 1283
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1284 RKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVadevgLRsvieqfpgkldfvLVDGGCVLSHGHKQLMCLARSVLS 1363
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGA-----LR-------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1364 KAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDS 1427
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
63-632 |
6.92e-53 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 196.54 E-value: 6.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 63 SKKNPKLINALRRCF--FWRFMFYGIILYLGE-VTKAVQPLLLGRIIASYDpdNKVERSIAIYLGIGLCLLFIVRTLLLH 139
Cdd:COG1132 2 SKSPRKLLRRLLRYLrpYRGLLILALLLLLLSaLLELLLPLLLGRIIDALL--AGGDLSALLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 140 PAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNkfdeglALAHFVWIAPLQVTLLmgllwdll 219
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVD------AVEQFLAHGLPQLVRS-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 220 qAFTFCGLAFLVVLALLQAGL----------------GKMMMK-YRDQRA--GKINERLVitsEMIENIQSVKAYCWEEA 280
Cdd:COG1132 146 -VVTLIGALVVLFVIDWRLALivllvlpllllvlrlfGRRLRKlFRRVQEalAELNGRLQ---ESLSGIRVVKAFGREER 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 281 M----EKIIENLRQTELKLTRKAAYVRYLNSSafffsgffvvfLSVLPYALLKGIILRKIF-------TTISFCIVLRMA 349
Cdd:COG1132 222 ElerfREANEELRRANLRAARLSALFFPLMEL-----------LGNLGLALVLLVGGLLVLsgsltvgDLVAFILYLLRL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 350 VT--RQFPWAVQTWYDSLGAINKIQDFLQ-----KQEYKTLEYNLTTTDVVMENVTafweegFSklFEKakennnnrkis 422
Cdd:COG1132 291 FGplRQLANVLNQLQRALASAERIFELLDeppeiPDPPGAVPLPPVRGEIEFENVS------FS--YPG----------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 423 ncdtslffsnlllGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISF 489
Cdd:COG1132 352 -------------DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGV 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 490 CSQYSWIMPGTIKDNIIFGV-SYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLY 568
Cdd:COG1132 419 VPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPIL 498
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 569 LLDSPFGYLDVLTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:COG1132 499 ILDEATSALDTETEALIQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
944-1424 |
7.81e-52 |
|
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: 193.05 E-value: 7.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 944 VSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDD-------------LLPLTIFDFIQLLLIVIGAvvvvsv 1010
Cdd:COG4988 89 VKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfarylpqlflaaLVPLLILVAVFPLDWLSGL------ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1011 lqpyIFLATVPVIAAFILLRGYFLHTSQQlKQLESEGR-SpifTHLVTSLKGLWTLRAFGRQP-YFETLFHKALNLHTAn 1088
Cdd:COG4988 163 ----ILLVTAPLIPLFMILVGKGAAKASR-RQWRALARlS---GHFLDRLRGLTTLKLFGRAKaEAERIAEASEDFRKR- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1089 wflylsTLRwfQMRIEM--IFVI-FF-------IAVTFISILTTGEGEGRVGI-ILTLA------MNIMGTlQW-----A 1146
Cdd:COG4988 234 ------TMK--VLRVAFlsSAVLeFFaslsialVAVYIGFRLLGGSLTLFAALfVLLLApefflpLRDLGS-FYharanG 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1147 VNSSidvdslmrsvSRVFKFIDMPTEDGKPNNSFRPskdsqpskvmiienqhvkkddiWPSGGQMTVKDLTAKYiDGGNA 1226
Cdd:COG4988 305 IAAA----------EKIFALLDAPEPAAPAGTAPLP----------------------AAGPPSIELEDVSFSY-PGGRP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1227 ILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL 1305
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLgFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1306 DPYE-QWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQI 1384
Cdd:COG4988 432 RLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 57526399 1385 IRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 1424
Cdd:COG4988 512 ILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVE 551
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
900-1163 |
7.30e-49 |
|
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: 176.12 E-value: 7.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 900 SNSYAVIITSTSS-----YYIfYIYVGVADTLLALGLFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILN 974
Cdd:cd18604 26 ASAYETSSALPPSevsvlYYL-GIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 975 RFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTH 1054
Cdd:cd18604 105 RFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSH 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1055 LVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILT 1134
Cdd:cd18604 185 FGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPGIDAGLAGFSLS 264
|
250 260
....*....|....*....|....*....
gi 57526399 1135 LAMNIMGTLQWAVNSSIDVDSLMRSVSRV 1163
Cdd:cd18604 265 FALGFSSAILWLVRSYNELELDMNSVERI 293
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
909-1163 |
5.43e-48 |
|
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: 173.43 E-value: 5.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 909 STSSYYIFYIYVGVADTLLALGLFrgLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLP 988
Cdd:cd18606 33 SQGFYIGIYAGLGVLQAIFLFLFG--LLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 989 LTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAF 1068
Cdd:cd18606 111 DSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1069 GRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMI--FVIFFIAVtFISILTTGEGEGRVGIILTLAMNIMGTLQWA 1146
Cdd:cd18606 191 GAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLgsLLVLIVAL-LCVTRRFSISPSSTGLVLSYVLQITQVLSWL 269
|
250
....*....|....*..
gi 57526399 1147 VNSSIDVDSLMRSVSRV 1163
Cdd:cd18606 270 VRQFAEVENNMNSVERL 286
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1211-1421 |
9.36e-48 |
|
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: 168.33 E-value: 9.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKAFGV 1289
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLrLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFSGTFRKNLdpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1369
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1370 LDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENK 1421
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
893-1167 |
1.73e-46 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 170.05 E-value: 1.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 893 GNSTKNASNSyAVIITSTSSY--YIFY--IYVGVADTLLALGLFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLK 968
Cdd:cd18599 35 GNTTNNVDNS-TVDSGNISDNpdLNFYqlVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 969 TGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGR 1048
Cdd:cd18599 114 TGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1049 SPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGE-GEG 1127
Cdd:cd18599 194 SPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLKGSiSPA 273
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 57526399 1128 RVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVSRVFKFI 1167
Cdd:cd18599 274 FAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
862-1147 |
2.91e-46 |
|
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: 167.82 E-value: 2.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 862 VLIWCLVVFLVEVAASLVVLCLfpKILLQDkgNSTKNASNSYAVIItstssYYIFYIYVGVADTLLALGLFRGLplVHTL 941
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVL--GRILDV--LLPDGDPETQALNV-----YSLALLLLGLAQFILSFLQSYLL--NHTG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 942 ITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVP 1021
Cdd:pfam00664 70 ERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1022 VIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQM 1101
Cdd:pfam00664 150 VLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 57526399 1102 RIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMnIMGTLQWAV 1147
Cdd:pfam00664 230 ITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLS-LFAQLFGPL 274
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
928-1163 |
1.71e-45 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 166.50 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 928 ALGLFRGL-----PLVHTLITV--SKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLI 1000
Cdd:cd18603 49 ALGLGQAIfvflgSLALALGCVraSRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1001 VIGAVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHK 1080
Cdd:cd18603 129 VISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1081 ALNLHTANWFLYLSTLRWFQMRIEMI--FVIFF---IAVTFISILTTGEgegrVGIILTLAMNIMGTLQWAVNSSIDVDS 1155
Cdd:cd18603 209 RVDENQRAYYPSIVSNRWLAVRLEFLgnLIVLFaalFAVLSRDSLSPGL----VGLSISYALQITQTLNWLVRMTSELET 284
|
....*...
gi 57526399 1156 LMRSVSRV 1163
Cdd:cd18603 285 NIVSVERI 292
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
865-1163 |
5.61e-45 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 165.47 E-value: 5.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 865 WCLVVFLVEVAASLVVLCLFPKILLQDKGNSTKNASNSYAVIITSTSSY-YIFYIYVGVADTLLALGLFRGLPLVHTLIT 943
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVsYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 944 VSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVI 1023
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1024 AAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRI 1103
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1104 EMI-FVIFFIAvTFISILTTGEGE---GRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVSRV 1163
Cdd:cd18602 241 DYLgAVIVFLA-ALSSLTAALAGYispSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERV 303
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1208-1438 |
8.82e-45 |
|
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: 163.16 E-value: 8.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1208 GGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNT-KGEIQIDGVSWDSITLQQWRKA 1286
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 FGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 1366
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1367 ILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEK-SLF 1438
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
436-639 |
1.53e-43 |
|
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: 170.79 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIK 502
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG---VSYDEyryrsVIKACQ---LEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:COG2274 567 ENITLGdpdATDEE-----IIEAARlagLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 577 LDVLTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRPDF 639
Cdd:COG2274 642 LDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
436-635 |
2.42e-43 |
|
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: 167.63 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIK 502
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG-VSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 581
Cdd:COG4988 429 ENLRLGrPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 582 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQ 635
Cdd:COG4988 509 EAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
436-621 |
4.63e-43 |
|
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: 154.85 E-value: 4.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIK 502
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIifgvsydeyryrsvikacqleediskfsekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 582
Cdd:cd03228 94 ENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 57526399 583 KEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 621
Cdd:cd03228 133 ALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
436-622 |
9.98e-43 |
|
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: 155.95 E-value: 9.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI-----------------KHSGRISFCSQYSWIMP 498
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 GTIKDNIIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 57526399 579 VLTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGS 622
Cdd:cd03290 173 IHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1222-1422 |
1.77e-39 |
|
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: 146.99 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1222 DGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRL-LNTKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGT 1300
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1301 FRKNL---DPYEQwsDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 1377
Cdd:cd03254 93 IMENIrlgRPNAT--DEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 57526399 1378 DPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:cd03254 171 DTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
436-639 |
5.70e-39 |
|
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: 154.54 E-value: 5.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIK 502
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG---VSyDEyRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:COG4987 427 ENLRLArpdAT-DE-ELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDA 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 580 LTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRPDF 639
Cdd:COG4987 505 ATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
895-1167 |
9.54e-39 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 147.29 E-value: 9.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 895 STKNASNSYAVIITSTSSYYIFYIYVGVADTLLALglFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILN 974
Cdd:cd18605 26 VSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTL--LRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 975 RFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTH 1054
Cdd:cd18605 104 RFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1055 LVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGE----GRVG 1130
Cdd:cd18605 184 FSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQHFFGLsidaGLIG 263
|
250 260 270
....*....|....*....|....*....|....*..
gi 57526399 1131 IILTLAMNIMGTLQWAVNSSIDVDSLMRSVSRVFKFI 1167
Cdd:cd18605 264 LALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
436-636 |
2.27e-38 |
|
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: 143.52 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIK 502
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFGVSY--DEyryrSVIKACQLE--EDISKFSEKD-NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 577
Cdd:cd03254 95 ENIRLGRPNatDE----EVIEAAKEAgaHDFIMKLPNGyDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 578 DVLTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQR 636
Cdd:cd03254 171 DTETEKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
436-632 |
1.02e-36 |
|
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: 138.90 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-------------ISFCSQYSWIMPGTIK 502
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFGVS-YDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 581
Cdd:cd03251 94 ENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 582 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:cd03251 174 ERLVQAA-LERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
904-1404 |
1.69e-36 |
|
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: 146.35 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 904 AVIITSTSSYYI-------FYIYVGVADTLL-ALGLFRGL-----PLV--HTLITVSKTLHHKMLQSVLQAPMSTLNTLK 968
Cdd:TIGR02868 29 AVALLGVSAWLIsraaempPVLYLSVAAVAVrAFGIGRAVfryleRLVghDAALRSLGALRVRVYERLARQALAGRRRLR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 969 TGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQP--YIFLATVPVIAAFiLLRGYFLHTSQQLKQLESE 1046
Cdd:TIGR02868 109 RGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVpaALILAAGLLLAGF-VAPLVSLRAARAAEQALAR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1047 GRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKA-LNLHTAN----WFLYLSTlrwfqmriemIFVIFFIAVTFISILT 1121
Cdd:TIGR02868 188 LRGELAAQLTDALDGAAELVASGALPAALAQVEEAdRELTRAErraaAATALGA----------ALTLLAAGLAVLGALW 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1122 TGEG---EGRVG-------IILTLAM-NIMGTLQWAVNSsidVDSLMRSVSRVFKFIDmpTEDGKPNNSFRPSKDSQPSK 1190
Cdd:TIGR02868 258 AGGPavaDGRLApvtlavlVLLPLAAfEAFAALPAAAQQ---LTRVRAAAERIVEVLD--AAGPVAEGSAPAAGAVGLGK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1191 VmiienqhvkkddiwpsggQMTVKDLTAKYiDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNT-KGEIQ 1269
Cdd:TIGR02868 333 P------------------TLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPlQGEVT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1270 IDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLS 1348
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLS 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1349 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHR 1404
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1209-1422 |
2.05e-36 |
|
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: 137.72 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1209 GQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKAF 1287
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAgLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQKVFIFSGTFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK 1364
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1365 AKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIeAMLE-CQRFLVIEENKV 1422
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDlVDRIIVMDSGRI 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1206-1440 |
5.70e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 142.27 E-value: 5.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1206 PSGGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWR 1284
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDpQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1285 KAFGVIPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGkLDFVLVDGGCVLSHGHKQLMCLARSV 1361
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLEDDKG-LNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1362 LSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQ 1440
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1198-1417 |
2.52e-34 |
|
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: 139.73 E-value: 2.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1198 HVKKDDIWPSGGQMTVKDLTAKYIDGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWD 1276
Cdd:TIGR02857 309 AGKAPVTAAPASSLEFSGVSVAYPGRRPA-LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLgFVDPTEGSIAVNGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1277 SITLQQWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQ 1353
Cdd:TIGR02857 388 DADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1354 LMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVI 1417
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1212-1440 |
3.11e-34 |
|
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: 131.97 E-value: 3.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVI 1290
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDvDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQKVFIFSGTFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 1367
Cdd:cd03251 82 SQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1368 LLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQ 1440
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
436-632 |
9.47e-34 |
|
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: 130.43 E-value: 9.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK-----------HSGR--ISFCSQYSWIMPGTIK 502
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRraIGVVPQDTVLFNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG-VSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 581
Cdd:cd03253 93 YNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 582 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:cd03253 173 EREIQAA-LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1214-1440 |
1.19e-33 |
|
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: 130.43 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1214 KDLTAKYiDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQ 1292
Cdd:cd03253 4 ENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDvSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1293 KVFIFSGTFRKNLDpYEQW--SDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:cd03253 83 DTVLFNDTIGYNIR-YGRPdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1371 DEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQ 1440
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
427-618 |
2.92e-33 |
|
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: 136.65 E-value: 2.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 427 SLFFSNLLL----GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISF 489
Cdd:TIGR02857 321 SLEFSGVSVaypgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 490 CSQYSWIMPGTIKDNIIFGVSY-DEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLY 568
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 569 LLDSPFGYLDVLTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILIL 618
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1228-1375 |
5.52e-33 |
|
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: 125.07 E-value: 5.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKST-LLLAFLRLLNTKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSG-TFRKNL 1305
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTlLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1306 -------DPYEQWSDQEIWKVADEVGLrsvieqfPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 1375
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGL-------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
440-574 |
1.19e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 124.30 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK-------------HSGRISFCSQYSWIMPG-TIKDNI 505
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 506 IFGVsyDEYRYRSVIKACQLEEDISKFSEKD--NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
436-640 |
1.88e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 128.81 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELePSEGKIKHSG-------------RISFCSQYSWIMPGTIK 502
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG-VSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 581
Cdd:PRK11174 441 DNVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 582 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRPDFS 640
Cdd:PRK11174 521 EQLVMQA-LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA 578
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
85-371 |
4.50e-30 |
|
Six-transmembrane helical domain 1 (TMD1) 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: 350041 [Multi-domain] Cd Length: 293 Bit Score: 121.79 E-value: 4.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 85 GIILYLGEVTKAVQPLLLGRII------ASYDPDNKVERSIAiyLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFS 158
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLInfvedaYLGGPPPSIGYGIG--YAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 159 LIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAFTFCGLAFLVVLALLQA 238
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 239 GLGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLNSSAFFFSGFFVV 318
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 319 FLSVLPYALLKGiILR--KIFTTISFCIVLRMAVTrQFPWAVQTWYDSLGAINKI 371
Cdd:cd18597 241 MLSFITYYATGH-TLDpaNIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1227-1440 |
5.21e-30 |
|
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: 119.95 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1227 ILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL 1305
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1306 ---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 1382
Cdd:cd03249 98 rygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1383 QIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQ 1440
Cdd:cd03249 176 KLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAK 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1211-1440 |
5.75e-30 |
|
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: 119.51 E-value: 5.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRL-LNTKGEIQIDGVSWDSITLQQWRKAFGV 1289
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 1366
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1367 ILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQ 1440
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
438-628 |
8.97e-30 |
|
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: 118.36 E-value: 8.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKDN 504
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 I-IFGVSYDEYRYRsVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEK 583
Cdd:cd03244 98 LdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 57526399 584 EIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGT 628
Cdd:cd03244 177 LIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1213-1421 |
1.42e-29 |
|
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: 117.57 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKST-LLLAFLRLLNTKGEIQIDGVSWDSITLQQWRKAFGVIP 1291
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTlLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 Q--KVFIFSGTFR-------KNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLArSVL 1362
Cdd:cd03225 82 QnpDDQFFGPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRSPFT-----------LSGGQKQRVAIA-GVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1363 S-KAKILLLDEPSAHLDPITYQIIRRTLKQaFADC--TVILSEHRIEAMLE-CQRFLVIEENK 1421
Cdd:cd03225 150 AmDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
438-623 |
1.70e-29 |
|
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: 116.16 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFcsqyswimpgtikdniifgvSYDEYRYR 517
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--------------------QWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 518 SVIKAcqLEEDISKF--SEKDNIvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMA 595
Cdd:cd03246 76 DHVGY--LPQDDELFsgSIAENI--------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA 145
|
170 180
....*....|....*....|....*...
gi 57526399 596 NKTRILVTSKMEHLKKADKILILHEGSV 623
Cdd:cd03246 146 GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
81-306 |
2.15e-29 |
|
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: 119.28 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 81 FMFYGIILYLGEVTKAVQPLLLGRIIASYDPDNKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLI 160
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQ-AFTFCGLAFLVVLALLQAG 239
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGwKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 240 LGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLN 306
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLS 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
437-621 |
4.27e-29 |
|
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: 116.53 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKD 503
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFGVSY-DEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 582
Cdd:cd03245 97 NITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 57526399 583 KEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 621
Cdd:cd03245 177 ERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1224-1458 |
5.71e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 124.19 E-value: 5.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1224 GNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRK 1303
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1304 NL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 1380
Cdd:PRK11174 442 NVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1381 TYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQaispadrlkLLPHRNSSR 1458
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT---------LLAHRQEEI 588
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
438-632 |
6.61e-29 |
|
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: 116.48 E-value: 6.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI-------------KHSGRISFCSQYSWIMPGTIKDN 504
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFG-----VSYDEyryrSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:cd03249 97 IRYGkpdatDEEVE----EAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57526399 580 LTEKEIFESCVcKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:cd03249 173 ESEKLVQEALD-RAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1213-1422 |
8.28e-29 |
|
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: 114.24 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKAFGVIP 1291
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILgLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 QKVFIFSGTFRKNldpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLD 1371
Cdd:cd03246 83 QDDELFSGSIAEN-----------------------------------------ILSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1372 EPSAHLDPITYQIIRRTLKQA-FADCTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1213-1440 |
1.09e-28 |
|
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: 115.51 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYiDGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaFLRLLN-----TKGEIQIDGVSWDSITLQQWRKAF 1287
Cdd:COG1122 3 LENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKST----LLRLLNgllkpTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVipqkVF------IFSGTFR-------KNLdpyeQWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHG 1350
Cdd:COG1122 78 GL----VFqnpddqLFAPTVEedvafgpENL----GLPREEIRERVEEalelVGLEHLADRPPHE-----------LSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1351 HKQLMCLArSVLS-KAKILLLDEPSAHLDPITYQIIRRTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDS 1427
Cdd:COG1122 139 QKQRVAIA-GVLAmEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
250
....*....|...
gi 57526399 1428 IQRMLSEKSLFRQ 1440
Cdd:COG1122 218 PREVFSDYELLEE 230
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
956-1442 |
2.14e-28 |
|
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: 123.31 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 956 VLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQL-LLIVIGAVVVVSVLQpyIFLATVPVIAAFILLRGYFL 1034
Cdd:TIGR01193 239 LFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMwILVIVGLFLVRQNML--LFLLSLLSIPVYAVIIILFK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1035 HTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPY--------FETLFHKALNLHTAnwflylstlRWFQMRI--- 1103
Cdd:TIGR01193 317 RTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAEryskidseFGDYLNKSFKYQKA---------DQGQQAIkav 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1104 -EMIFVIFFIAVTFISILTTGEGEGR-------VGIILTLAMNIMgTLQWAVNSSIDVDSLMRSVSRVfkfidmpteDGK 1175
Cdd:TIGR01193 388 tKLILNVVILWTGAYLVMRGKLTLGQlitfnalLSYFLTPLENII-NLQPKLQAARVANNRLNEVYLV---------DSE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1176 PNNSFRPSKDSQPSkvmiienqhvkkddiwpsgGQMTVKDLTAKYIDGGNaILENISFSISPGQRVGLLGRTGSGKSTLL 1255
Cdd:TIGR01193 458 FINKKKRTELNNLN-------------------GDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1256 LAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL--DPYEQWSDQEIWKVADEVGLRSVIEQF 1332
Cdd:TIGR01193 518 KLLVGFFQaRSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENM 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1333 PGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ-IIRRTLKqaFADCTVILSEHRIEAMLEC 1411
Cdd:TIGR01193 598 PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKkIVNNLLN--LQDKTIIFVAHRLSVAKQS 675
|
490 500 510
....*....|....*....|....*....|.
gi 57526399 1412 QRFLVIEENKVRQYDSIQRMLSEKSLFRQAI 1442
Cdd:TIGR01193 676 DKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
436-635 |
4.99e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.01 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQYSWIMPG-TIK 502
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNI-----IFGVSYDEY--RYRSVIKACQLEEDISKFSEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:COG1131 92 ENLrffarLYGLPRKEAreRIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 576 YLDVLTEKEIFEsCVCKLMANKTRILVTSkmeHL-----KKADKILILHEGSVYFYGTFSELQNQ 635
Cdd:COG1131 161 GLDPEARRELWE-LLRELAAEGKTVLLST---HYleeaeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1212-1421 |
5.50e-28 |
|
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: 111.18 E-value: 5.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVI 1290
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQkvfifsgtfrknldpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1371 DEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRIE-AMLECQRFLVIEENK 1421
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPElAELAADRVIVLKDGK 157
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1211-1422 |
7.12e-28 |
|
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: 111.64 E-value: 7.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSwDSITLQQWRKAFGV 1289
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKpQQGEITLDGVP-VSDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFSGTFRKNLdpyeqwsdqeiwkvadevGLRsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1369
Cdd:cd03247 80 LNQRPYLFDTTLRNNL------------------GRR--------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1370 LDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
436-627 |
2.25e-27 |
|
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: 111.47 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG--------RISFCSQ---YSWIMPGTIKD- 503
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQrrsIDRDFPISVRDv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 -------NIIFGVSYDEYRYRSVIKAcqLEE-DISKFSEKDnivLGEggitLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:cd03235 91 vlmglygHKGLFRRLSKADKAKVDEA--LERvGLSELADRQ---IGE----LSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 576 YLDVLTEKEIFEsCVCKL-MANKTRILVTSKMEH-LKKADKILILhEGSVYFYG 627
Cdd:cd03235 162 GVDPKTQEDIYE-LLRELrREGMTILVVTHDLGLvLEYFDRVLLL-NRTVVASG 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
436-603 |
4.20e-27 |
|
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: 117.85 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIK 502
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG---VSYDEYRyrSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:TIGR02868 427 ENLRLArpdATDEELW--AALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....
gi 57526399 580 LTEKEIFEScVCKLMANKTRILVT 603
Cdd:TIGR02868 505 ETADELLED-LLAALSGRTVVLIT 527
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
436-638 |
7.03e-27 |
|
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: 117.54 E-value: 7.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIkhsgRISFCSQYSW-----------------IMP 498
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV----RLDGADLSQWdreelgrhigylpqdveLFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 GTIKDNII-FGVSYDEyryrSVIKACQL---EEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:COG4618 420 GTIAENIArFGDADPE----KVVAAAKLagvHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 575 GYLDVLTEKeifescvcKLMA--------NKTRILVTSKMEHLKKADKILILHEGSVYFYGT----FSELQNQRPD 638
Cdd:COG4618 496 SNLDDEGEA--------ALAAairalkarGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPrdevLARLARPAAA 563
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
436-647 |
8.01e-27 |
|
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: 110.85 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPG-TI 501
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 502 KDNI-----IFGVSYDEYRYRsvikACQLEEDISkfsekdnivLGEGGIT------LSGGQRARISLARAVYKDADLYLL 570
Cdd:cd03295 93 EENIalvpkLLKWPKEKIRER----ADELLALVG---------LDPAEFAdrypheLSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 571 DSPFGYLDVLTEKEIFESCV-CKLMANKTRILVTSKM-EHLKKADKILILHEGSVYFYGTFSE-LQNQRPDFSSKLMGCD 647
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEiLRSPANDFVAEFVGAD 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1212-1434 |
1.18e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.15 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSiTLQQWRKAFGVI 1290
Cdd:COG1131 2 EVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQKVFIFSG-TFRKNLD--------PYEQwSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSV 1361
Cdd:COG1131 79 PQEPALYPDlTVRENLRffarlyglPRKE-ARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 1362 LSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQRMLSE 1434
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLeEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1212-1436 |
1.24e-26 |
|
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: 110.33 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLA-FLRLLNTKGEIQIDGVSWDSITLQqWRKAFGVI 1290
Cdd:COG4555 3 EVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMlAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQKVFIFSG-TFRKNLDPY-EQW--SDQEIWKVADEV----GLRSVIEQfpgkldfvLVDGgcvLSHGHKQLMCLARSVL 1362
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFaELYglFDEELKKRIEELiellGLEEFLDR--------RVGE---LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1363 SKAKILLLDEPSAHLDPITYQIIRRTLKQAFA-DCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQRMLSEKS 1436
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
436-647 |
1.55e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.79 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG--------RISFCSQYS---WIMPGTIKDN 504
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRAevdWDFPITVRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGvsydeyRY-------------RSVIKACqLEE-DISKFSEKDnivLGEggitLSGGQRARISLARAVYKDADLYLL 570
Cdd:COG1121 98 VLMG------RYgrrglfrrpsradREAVDEA-LERvGLEDLADRP---IGE----LSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 571 DSPFGYLDVLTEKEIFEscvckLMA-----NKTRILVTskmeH-----LKKADKILILHEGsVYFYGTFSELQNqrPDFS 640
Cdd:COG1121 164 DEPFAGVDAATEEALYE-----LLRelrreGKTILVVT----HdlgavREYFDRVLLLNRG-LVAHGPPEEVLT--PENL 231
|
....*..
gi 57526399 641 SKLMGCD 647
Cdd:COG1121 232 SRAYGGP 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
436-621 |
5.29e-26 |
|
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: 105.40 E-value: 5.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIkhsgrisfcsqyswimpgTIKDNIIFGVSYDEYR 515
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------LIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 516 YRSVIKACqleediskfsekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMA 595
Cdd:cd00267 73 RRIGYVPQ-----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE 129
|
170 180
....*....|....*....|....*..
gi 57526399 596 NKTRILVTSKMEHLKKA-DKILILHEG 621
Cdd:cd00267 130 GRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
438-637 |
5.68e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 114.54 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-------------ISFCSQYSWIMPGTIKDN 504
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGV--SYDEyRYRSVIKACQLEedisKFSEKD---NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:PRK11160 434 LLLAApnASDE-ALIEVLQQVGLE----KLLEDDkglNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 580 LTEKEIFESCVcKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRP 637
Cdd:PRK11160 509 ETERQILELLA-EHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1197-1440 |
6.84e-26 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 114.82 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1197 QHVKKDDIWPSGGQMTVKDLTAKYIDGgNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSW 1275
Cdd:PRK10790 327 QQYGNDDRPLQSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPlTEGEIRLDGRPL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1276 DSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLM 1355
Cdd:PRK10790 406 SSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1356 CLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEK 1435
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
....*
gi 57526399 1436 SLFRQ 1440
Cdd:PRK10790 566 GRYWQ 570
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1213-1422 |
1.07e-25 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 105.17 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLqQWRKAFGVIP 1291
Cdd:cd03230 3 VRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILgLLKPDSGEIKVLGKDIKKEPE-EVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 QKVFIFSG-TFRKNLDpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:cd03230 80 EEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1371 DEPSAHLDPITYQIIRRTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKV 1422
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
439-632 |
1.61e-25 |
|
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: 106.80 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKDNI 505
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 506 IFGvsyDE-YRYRSVIKACQL---EEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 581
Cdd:cd03252 97 ALA---DPgMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 582 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:cd03252 174 EHAIMRN-MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
438-636 |
1.75e-25 |
|
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: 106.87 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQ----YSWImpgTI 501
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDerglYDRL---TV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 502 KDNI-----IFGVSYDEYRYR--SVIKACQLEEDI-SKFSEkdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:COG4555 92 RENIryfaeLYGLFDEELKKRieELIELLGLEEFLdRRVGE------------LSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 574 FGYLDVLTeKEIFESCVCKLMANKTRILVTSK-MEHLKK-ADKILILHEGSVYFYGTFSELQNQR 636
Cdd:COG4555 160 TNGLDVMA-RRLLREILRALKKEGKTVLFSSHiMQEVEAlCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
437-627 |
3.14e-25 |
|
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: 103.93 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQYSWIMPGTIKDN 504
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IifgvsydeyryrsvikacqleediskfsekdnivlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKE 584
Cdd:cd03247 95 L--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 57526399 585 IFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYG 627
Cdd:cd03247 137 LLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
436-632 |
3.64e-25 |
|
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: 105.49 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSW---IMPg 499
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPDdqlFAP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 TIKDNIIFG-----VSYDEYRYRsVIKAcqLEE-DISKFSEKDnivlgeggI-TLSGGQRARISLARAVYKDADLYLLDS 572
Cdd:COG1122 92 TVEEDVAFGpenlgLPREEIRER-VEEA--LELvGLEHLADRP--------PhELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 573 PFGYLDVLTEKEIFEsCVCKL-MANKTRILVTSKMEHL-KKADKILILHEGSVYFYGTFSEL 632
Cdd:COG1122 161 PTAGLDPRGRRELLE-LLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1209-1440 |
1.08e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.88 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1209 GQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAF 1287
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQKVFIFSGTFRKNLdPY---EQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK 1364
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNI-AYartEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1365 AKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQ 1440
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
432-645 |
1.43e-24 |
|
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: 103.95 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 432 NLLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-----------RISFCSQYSWIMPG- 499
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 TIKDNIIFGVsydeyRYRSVIKAcQLEEDISKFSEKDNI--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 577
Cdd:cd03299 87 TVYKNIAYGL-----KKRKVDKK-EIERKVLEIAEMLGIdhLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 578 DVLT-EKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSE-LQNQRPDFSSKLMG 645
Cdd:cd03299 161 DVRTkEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEvFKKPKNEFVAEFLG 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
436-623 |
2.27e-24 |
|
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: 102.60 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI-----------KHSGRISFCSQ----YSWImpgT 500
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgvpPERRNIGMVFQdyalFPHL---T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFG-----VSYDEYRYR--SVIKACQLEEDISKFSEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:cd03259 89 VAENIAFGlklrgVPKAEIRARvrELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 574 FGYLDV-LTE------KEIFESCvcklmaNKTRILVTSKM-EHLKKADKILILHEGSV 623
Cdd:cd03259 158 LSALDAkLREelreelKELQREL------GITTIYVTHDQeEALALADRIAVMNEGRI 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
436-623 |
2.54e-24 |
|
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: 101.32 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKhsgrisfcsqyswimpgtikdniIFGVSYDEYR 515
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-----------------------VLGKDIKKEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 516 YRSVIKACQLEEDISKFSE---KDNivlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVcK 592
Cdd:cd03230 69 EEVKRRIGYLPEEPSLYENltvREN-------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR-E 140
|
170 180 190
....*....|....*....|....*....|...
gi 57526399 593 LMANKTRILVTS-KMEHLKK-ADKILILHEGSV 623
Cdd:cd03230 141 LKKEGKTILLSShILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
97-303 |
4.37e-24 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 104.09 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 97 VQPLLLGRIIaSYDPDNKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKIS 176
Cdd:cd18595 15 ASPQLLKLLI-NFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLSNSARKKST 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 177 IGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAFTFcglaflvvlallqAGLGKM------------- 243
Cdd:cd18595 94 VGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVL-------------AGLGVMilliplnavlark 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 244 -------MMKYRDqragkinERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVR 303
Cdd:cd18595 161 ikklqvkQMKLKD-------ERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLN 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
436-627 |
4.44e-24 |
|
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: 100.59 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKhsgrisfcsqyswimpgtikdniIFGVSYDEYR 515
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-----------------------LDGKDLASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 516 YRSVIKAC----Q-LEE-DISKFSEKD-NivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFES 588
Cdd:cd03214 68 PKELARKIayvpQaLELlGLAHLADRPfN--------ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLEL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 57526399 589 cVCKLMA--NKTRILVTSKMEH-LKKADKILILHEGSVYFYG 627
Cdd:cd03214 140 -LRRLARerGKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1209-1425 |
6.46e-24 |
|
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: 108.30 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1209 GQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaf-lrllnTKGEIQIDGVswdsiTLQQWRKA- 1286
Cdd:COG4618 329 GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTlarllvgvwppTAGSVRLDGA-----DLSQWDREe 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 ----FGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVL 1362
Cdd:COG4618 404 lgrhIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1363 SKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRIEAMLECQRFLVIEENKVRQY 1425
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
929-1440 |
8.62e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 108.66 E-value: 8.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 929 LGLFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVV 1008
Cdd:TIGR00958 217 SAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFM 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1009 SVLQPYI----FLATVPVIAAFILLRGYFLHTSQQLKqlESEGRSpifTHLV-TSLKGLWTLRAFGRQPYFETLFHKALN 1083
Cdd:TIGR00958 297 LWLSPRLtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKA---NQVAeEALSGMRTVRSFAAEEGEASRFKEALE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1084 -LHTANW------FLYLSTLRWFQMRIEMIfvIFFIAVTFIsilTTGEGEGrvGIILTLAMNIMGTLQWAVNSSIDVDSL 1156
Cdd:TIGR00958 372 eTLQLNKrkalayAGYLWTTSVLGMLIQVL--VLYYGGQLV---LTGKVSS--GNLVSFLLYQEQLGEAVRVLSYVYSGM 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1157 MRSV---SRVFKFIDMptedgKPNnsFRPSKDSQPSKVMiienqhvkkddiwpsgGQMTVKDLTAKY-IDGGNAILENIS 1232
Cdd:TIGR00958 445 MQAVgasEKVFEYLDR-----KPN--IPLTGTLAPLNLE----------------GLIEFQDVSFSYpNRPDVPVLKGLT 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1233 FSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKN----LDP 1307
Cdd:TIGR00958 502 FTLHPGEVVALVGPSGSGKSTVAALLQNLYQpTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENiaygLTD 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1308 YEqwsDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpityQIIRR 1387
Cdd:TIGR00958 582 TP---DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQ 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 1388 TLKQ--AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQ 1440
Cdd:TIGR00958 655 LLQEsrSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
436-621 |
1.26e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 100.28 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIK 502
Cdd:COG4619 12 GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFGVSYDEYRYrsviKACQLEEDISKFsEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTe 582
Cdd:COG4619 92 DNLPFPFQLRERKF----DRERALELLERL-GLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 57526399 583 KEIFESCVCKLMANKTR--ILVTSKMEHLKK-ADKILILHEG 621
Cdd:COG4619 166 TRRVEELLREYLAEEGRavLWVSHDPEQIERvADRVLTLEAG 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
438-635 |
1.80e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.50 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKDN 504
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGVSY-DEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEK 583
Cdd:TIGR00958 575 IAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 584 EIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQ 635
Cdd:TIGR00958 655 LLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1212-1422 |
2.13e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 99.89 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTL-LLAFLRLLNTKGEIQIDGVSWDSITLQQWRKAFGVI 1290
Cdd:COG4619 2 ELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLlRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQKVFIFSGTFRKNLDPYEQWSDQEIwkvaDEVGLRSVIEQFpgKLDFVLVDGGCV-LSHGHKQLMCLARSVLSKAKILL 1369
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKF----DRERALELLERL--GLPPDILDKPVErLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1370 LDEPSAHLDP----ITYQIIRRTLKQafADCTVILSEH-RIEAMLECQRFLVIEENKV 1422
Cdd:COG4619 154 LDEPTSALDPentrRVEELLREYLAE--EGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
437-632 |
2.48e-23 |
|
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: 99.89 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQYSWIMPG-TIKD 503
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIF-----GVSYDEYRYRS--VIKACQLEEDISKFSekdnivlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:cd03263 95 HLRFyarlkGLPKSEIKEEVelLLRVLGLTDKANKRA-----------RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 577 LDVLTEKEIFEsCVCKLMANKTRILVTSKM---EHLkkADKILILHEGSVYFYGTFSEL 632
Cdd:cd03263 164 LDPASRRAIWD-LILEVRKGRSIILTTHSMdeaEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
436-621 |
2.76e-23 |
|
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: 98.41 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRisfcsqyswimpgTIKDNIIFGVSYDEyR 515
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE-------------DLTDLEDELPPLRR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 516 YRSVIKACQLeedISKFSEKDNIVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIfESCVCKLMA 595
Cdd:cd03229 78 IGMVFQDFAL---FPHLTVLENIALG-----LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV-RALLKSLQA 148
|
170 180
....*....|....*....|....*....
gi 57526399 596 N--KTRILVTSKMEHLKK-ADKILILHEG 621
Cdd:cd03229 149 QlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1212-1422 |
6.55e-23 |
|
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: 97.51 E-value: 6.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVI 1290
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQkvfifsgtfrknldpyeqwsdqeiwkVADEVGLRSVIEQFpgkldfvlVDggcVLSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:cd03214 79 PQ--------------------------ALELLGLAHLADRP--------FN---ELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1371 DEPSAHLDpITYQI----IRRTLKQAFaDCTVILSEHRIE-AMLECQRFLVIEENKV 1422
Cdd:cd03214 122 DEPTSHLD-IAHQIelleLLRRLARER-GKTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
396-636 |
1.97e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.56 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 396 NVTAFWEEG-------FSKLFEKAKENNNNRKISNCDTSLFFSNLLLG-----TPVLKDISFKIERGQLLAVAGSTGAGK 463
Cdd:PRK11176 303 NVNAQFQRGmaacqtlFAILDLEQEKDEGKRVIERAKGDIEFRNVTFTypgkeVPALRNINFKIPAGKTVALVGRSGSGK 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 464 TSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKDNIIFGVSyDEYRYRSVIKACQLE---E 527
Cdd:PRK11176 383 STIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDTIANNIAYART-EQYSREQIEEAARMAyamD 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 528 DISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIfESCVCKLMANKTRILVTSKME 607
Cdd:PRK11176 462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLS 540
|
250 260
....*....|....*....|....*....
gi 57526399 608 HLKKADKILILHEGSVYFYGTFSELQNQR 636
Cdd:PRK11176 541 TIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1209-1439 |
2.26e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 103.25 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1209 GQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAF 1287
Cdd:PRK10789 312 GELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK 1364
Cdd:PRK10789 392 AVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 1365 AKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFR 1439
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYR 544
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
438-635 |
2.67e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 103.25 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK-HS------------GRISFCSQYSWIMPGTIKDN 504
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDipltklqldswrSRLAVVSQTPFLFSDTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFG---VSYDEYRYrsVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 581
Cdd:PRK10789 409 IALGrpdATQQEIEH--VARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRT 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 582 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQ 635
Cdd:PRK10789 487 EHQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
437-621 |
3.16e-22 |
|
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: 96.38 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI-------------KHSGRISFCSQYS---WIMPgT 500
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkELRRKVGLVFQNPddqFFGP-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFGVsydEYRYRSvikacqlEEDISKfseKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLD 571
Cdd:cd03225 93 VEEEVAFGL---ENLGLP-------EEEIEE---RVEEALELVGLeglrdrspfTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 572 SPFGYLDVLTEKEIFEScVCKLMA-NKTRILVTSKMEHLKK-ADKILILHEG 621
Cdd:cd03225 160 EPTAGLDPAGRRELLEL-LKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1213-1422 |
3.33e-22 |
|
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: 97.19 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSIT---LQQWRKAFG 1288
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVgLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VIPQKVFIFSG-TFRKN----LDPYEQWSDQEIWKVA----DEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1359
Cdd:cd03261 81 MLFQSGALFDSlTVFENvafpLREHTRLSEEEIREIVleklEAVGLRGAEDLYPAE-----------LSGGMKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1360 SVLSKAKILLLDEPSAHLDPIT-YQIIR--RTLKQAFaDCTVILSEHRIEAMLE-CQRFLVIEENKV 1422
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIAsGVIDDliRSLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKI 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1211-1426 |
5.12e-22 |
|
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: 96.05 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaflrLLN--------TKGEIQIDGVSWDSITLQq 1282
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTT-------LLRliaglerpDSGEILIDGRDVTGVPPE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1283 wRKAFGVIPQK--------VF--IFSGtFRKNLDPYEQWSDQEIWkVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHK 1352
Cdd:cd03259 71 -RRNIGMVFQDyalfphltVAenIAFG-LKLRGVPKAEIRARVRE-LLELVGLEGLLNRYPHE-----------LSGGQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1353 QLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQYD 1426
Cdd:cd03259 137 QRVALARALAREPSLLLLDEPLSALDAKLREELREELKelQRELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1211-1437 |
1.02e-21 |
|
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: 96.27 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKST-------LLLAflrllnTKGEIQIDGVSWDSITLQQW 1283
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTllralagLLKP------SSGEVLLDGRDLASLSRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1284 RKAFGVIPQKVFI-FSGTFRK--------NLDPYEQWSDQE---IWKVADEVGL-----RSVIEqfpgkldfvlvdggcv 1346
Cdd:COG1120 74 ARRIAYVPQEPPApFGLTVRElvalgrypHLGLFGRPSAEDreaVEEALERTGLehladRPVDE---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1347 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQI-IRRTLKQ--AFADCTVILSEHRIE-AMLECQRFLVIEENKV 1422
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLD-LAHQLeVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRI 216
|
250
....*....|....*
gi 57526399 1423 RQYDSIQRMLSEKSL 1437
Cdd:COG1120 217 VAQGPPEEVLTPELL 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1212-1467 |
1.27e-21 |
|
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: 100.75 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL----RLLNTKGEIQIDGVSWDSITLQQWRKAF 1287
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMgllpHGGRISGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQ---------KVF--IFSGTFRKNLDPYEQWsdQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMC 1356
Cdd:COG1123 86 GMVFQdpmtqlnpvTVGdqIAEALENLGLSRAEAR--ARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1357 LARSVLSKAKILLLDEPSAHLDPITYQIIRRTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRqydsiqrmls 1433
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIV---------- 222
|
250 260 270
....*....|....*....|....*....|....
gi 57526399 1434 EKSLFRQAISPADRLKLLPHRNSSRQRSRANIAA 1467
Cdd:COG1123 223 EDGPPEEILAAPQALAAVPRLGAARGRAAPAAAA 256
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
438-641 |
1.79e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.81 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKDN 504
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGV--SYDEYRYRSViKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 582
Cdd:PRK13657 429 IRVGRpdATDEEMRAAA-ERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 583 KEIFESCVCkLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRPDFSS 641
Cdd:PRK13657 508 AKVKAALDE-LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAA 565
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
436-618 |
2.23e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 95.54 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG--------RISFCSQ-YS---WImpgTIKD 503
Cdd:COG1116 23 GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQePAllpWL---TVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFG-----VSYDEYRYR--SVIKACQLEEDISKF-SEkdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:COG1116 100 NVALGlelrgVPKAERRERarELLELVGLAGFEDAYpHQ------------LSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 576 YLDVLTeKEIFESCVCKLMA--NKTRILVTskmeH-------LkkADKILIL 618
Cdd:COG1116 168 ALDALT-RERLQDELLRLWQetGKTVLFVT----HdvdeavfL--ADRVVVL 212
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1222-1422 |
2.44e-21 |
|
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: 100.28 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1222 DGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGT 1300
Cdd:COG5265 368 DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDvTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1301 FRKNLdPYEQW--SDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1378
Cdd:COG5265 448 IAYNI-AYGRPdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 57526399 1379 PITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:COG5265 527 SRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1213-1421 |
3.21e-21 |
|
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: 93.30 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDG---GNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLrllntkGEIQ-IDGVSwdsitlqQWRKAFG 1288
Cdd:cd03250 3 VEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL------GELEkLSGSV-------SVPGSIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VIPQKVFIFSGTFRKNL---DPYEQwsdQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 1365
Cdd:cd03250 70 YVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1366 KILLLDEPSAHLDPITYQ-IIRRTLKQAFADC-TVILSEHRIEAMLECQRFLVIEENK 1421
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRhIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
427-618 |
4.09e-21 |
|
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: 93.31 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 427 SLFFSNLLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI--------KHSGRISFCSQYSWIMP 498
Cdd:cd03293 7 SKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepvtGPGPDRGYVFQQDALLP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 -GTIKDNIIFG-----VSYDEYRYR--SVIKACQLEEDISKF-SEkdnivlgeggitLSGGQRARISLARAVYKDADLYL 569
Cdd:cd03293 87 wLTVLDNVALGlelqgVPKAEARERaeELLELVGLSGFENAYpHQ------------LSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 570 LDSPFGYLDVLTEKEIFEScvckLMA-----NKTRILVT-SKMEHLKKADKILIL 618
Cdd:cd03293 155 LDEPFSALDALTREQLQEE----LLDiwretGKTVLLVThDIDEAVFLADRVVVL 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
437-621 |
5.76e-21 |
|
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: 92.94 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------------ISFCSQYSWIMPG 499
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 -TIKDNI-----IFGVSYDEY--RYRSVIKACQLEEDISKF-SEkdnivlgeggitLSGGQRARISLARAVYKDADLYLL 570
Cdd:cd03255 97 lTALENVelpllLAGVPKKERreRAEELLERVGLGDRLNHYpSE------------LSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 571 DSPFGYLDVLTEKEIFEscvckLM------ANKTRILVTSKMEHLKKADKILILHEG 621
Cdd:cd03255 165 DEPTGNLDSETGKEVME-----LLrelnkeAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
438-635 |
1.31e-20 |
|
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: 92.79 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------ISFCSQ-YSWIMPGTIKDNI 505
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQhYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 506 IFGV---------SYDEYRYR--SVIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:cd03296 96 AFGLrvkprserpPEAEIRAKvhELLKLVQLDWLADRYPAQ-----------LSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 575 GYLDVLTEKEIfESCVCKLM--ANKTRILVT-SKMEHLKKADKILILHEGSVYFYGTFSELQNQ 635
Cdd:cd03296 165 GALDAKVRKEL-RRWLRRLHdeLHVTTVFVThDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
436-604 |
1.66e-20 |
|
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: 91.39 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQYSWIMPG-TIK 502
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIF-----GVSYDEYRYRSVIKACQLEEDISKFSEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 577
Cdd:COG4133 94 ENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*..
gi 57526399 578 DVLTeKEIFESCVCKLMANKTRILVTS 604
Cdd:COG4133 163 DAAG-VALLAELIAAHLARGGAVLLTT 188
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
121-371 |
1.75e-20 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 93.39 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 121 IYLGIGLCLLF----IVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSrvLDKISIGQLVSLLSNNLNKFDEGLA 196
Cdd:cd18592 35 VWYGILLVLGLflteLLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRS--LGDKSVGELINIFSNDGQRLFDAAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 197 LAHFVWIAPLQVTLLMGLLWDLLQAFTFCGLAFLVVLALLQAGLGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYC 276
Cdd:cd18592 113 FGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 277 WEEAMEKIIENLRQTELKLTRKAAYVRYLNSSAFFFSGFFVVFLSVLPYALLKGIIL-RKIFTTISFCIVLRMAVtRQFP 355
Cdd:cd18592 193 WEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLTaAQAFTVIAVFNSMRFSL-RMLP 271
|
250
....*....|....*.
gi 57526399 356 WAVQTWYDSLGAINKI 371
Cdd:cd18592 272 YAVKALAEAKVALQRI 287
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1213-1463 |
1.87e-20 |
|
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: 92.56 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKY--IDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGvswDSITLQQWRKAFGV 1289
Cdd:COG1124 4 VRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAgLERPWSGEVTFDG---RPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IpQKVFifsgtfrknLDPY---------------------EQWSDQEIWKVADEVGL-RSVIEQFPGKldfvlvdggcvL 1347
Cdd:COG1124 81 V-QMVF---------QDPYaslhprhtvdrilaeplrihgLPDREERIAELLEQVGLpPSFLDRYPHQ-----------L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1348 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY-QIIR--RTLKQAFaDCTVILSEH---RIEAMleCQRFLVIEENK 1421
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQaEILNllKDLREER-GLTYLFVSHdlaVVAHL--CDRVAVMQNGR 216
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 57526399 1422 vrqydsIQRMLSEKSLFRQAISPADRlKLLphrNSSRQRSRA 1463
Cdd:COG1124 217 ------IVEELTVADLLAGPKHPYTR-ELL---AASLAFERA 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
438-628 |
2.45e-20 |
|
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: 90.93 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKDN 504
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIfgvSYDEYRYRSVIKACQLEediskfsekdnivlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKE 584
Cdd:cd03369 102 LD---PFDEYSDEEIYGALRVS---------------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 57526399 585 IFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGT 628
Cdd:cd03369 164 IQKT-IREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
439-627 |
2.86e-20 |
|
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: 90.80 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYSWI--MPG--------TIKDNIIF- 507
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgyLPEerglypkmKVIDQLVYl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 508 ----GVSYDEYRYRSvikacqlEEDISKF--SEKDNIVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV-- 579
Cdd:cd03269 95 aqlkGLKKEEARRRI-------DEWLERLelSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPvn 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 580 --LTEKEIFEscvcKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYG 627
Cdd:cd03269 164 veLLKDVIRE----LARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1114-1422 |
5.41e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.18 E-value: 5.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1114 VTFISILTTG-----EGEGRVGIILT---LAMNIMGTLQWAVNSsidVDSLMRSVSRVFKFIDMptEDGKPNNSFRPSkd 1185
Cdd:PRK13657 252 ITMLAILVLGaalvqKGQLRVGEVVAfvgFATLLIGRLDQVVAF---INQVFMAAPKLEEFFEV--EDAVPDVRDPPG-- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1186 sqpskvmIIENQHVKkddiwpsgGQMTVKDLTAKYiDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-T 1264
Cdd:PRK13657 325 -------AIDLGRVK--------GAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDpQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1265 KGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDG 1343
Cdd:PRK13657 389 SGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRvGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGER 468
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1344 GCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
436-634 |
5.93e-20 |
|
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: 90.81 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG----------------RISFCSQ----YSW 495
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGMLFQggalFDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 496 ImpgTIKDNIIF------GVSYDEYRYR--SVIKACQLEEDISKF-SEkdnivlgeggitLSGGQRARISLARAVYKDAD 566
Cdd:COG1127 97 L---TVFENVAFplrehtDLSEAEIRELvlEKLELVGLPGAADKMpSE------------LSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 567 LYLLDSPFGYLDVLTEKEIFE---SCVCKLmaNKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQN 634
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDElirELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1211-1421 |
7.92e-20 |
|
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: 88.40 E-value: 7.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLL-LAFLRLLNTKGEIQIDGVSWDS--ITLQQWRKAF 1287
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLrCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQKVFIFSgtfrkNLDpyeqwsdqeiwkVADEVGLRsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKI 1367
Cdd:cd03229 79 GMVFQDFALFP-----HLT------------VLENIALG--------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1368 LLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRI-EAMLECQRFLVIEENK 1421
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
436-587 |
1.14e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.34 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI----KHSGRIS--------------FcsQYSWIM 497
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngQDLSRLKrreipylrrrigvvF--QDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 498 PG-TIKDNIIF-----GVSYDEYRYR--SVIKACQLEEDISKFSekdnivlgeggITLSGGQRARISLARAVYKDADLYL 569
Cdd:COG2884 92 PDrTVYENVALplrvtGKSRKEIRRRvrEVLDLVGLSDKAKALP-----------HELSGGEQQRVAIARALVNRPELLL 160
|
170
....*....|....*...
gi 57526399 570 LDSPFGYLDVLTEKEIFE 587
Cdd:COG2884 161 ADEPTGNLDPETSWEIME 178
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
439-627 |
1.42e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.13 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISfcsqySWIMPG-------TIKDNIIF---- 507
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGggfnpelTGRENIYLngrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 508 -GVSYDEYRyrsvikacQLEEDISKFSEkdnivLGEGG----ITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 582
Cdd:cd03220 112 lGLSRKEID--------EKIDEIIEFSE-----LGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 57526399 583 KEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYG 627
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
436-623 |
1.73e-19 |
|
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: 88.47 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------ISFCSQYSWIMPG-TIKD 503
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMVFQNYALYPHmTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFG-----VSYDEY--RYRSVIKACQLEEDISKFSEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:cd03301 92 NIAFGlklrkVPKDEIdeRVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 577 LDVLTEKEIFESCVcKLMAN--KTRILVT-SKMEHLKKADKILILHEGSV 623
Cdd:cd03301 161 LDAKLRVQMRAELK-RLQQRlgTTTIYVThDQVEAMTMADRIAVMNDGQI 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
436-587 |
1.73e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR----------ISFcsQYSWIMP-GTIKDN 504
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgaergVVF--QNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGV-------SYDEYRYRSVIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 577
Cdd:PRK11248 91 VAFGLqlagvekMQRLEIAHQMLKKVGLEGAEKRYIWQ-----------LSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170
....*....|
gi 57526399 578 DVLTEKEIFE 587
Cdd:PRK11248 160 DAFTREQMQT 169
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1213-1432 |
2.51e-19 |
|
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: 88.88 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaf-lrllnTKGEIQIDGVSWDSIT---LQQWRKAFG 1288
Cdd:COG1127 8 VRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVllkliigllrpDSGEILVDGQDITGLSekeLYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VipqkVF----IFSG-TFRKN----LDPYEQWSDQEIWKVADE----VGLRSVIEQFPGKLdfvlvDGGcvlshghkqlM 1355
Cdd:COG1127 86 M----LFqggaLFDSlTVFENvafpLREHTDLSEAEIRELVLEklelVGLPGAADKMPSEL-----SGG----------M 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1356 C----LARSVLSKAKILLLDEPSAHLDPIT----YQIIRRtLKQAFaDCTVILSEHRIEAMLE-CQRFLVIEENKVRQYD 1426
Cdd:COG1127 147 RkrvaLARALALDPEILLYDEPTAGLDPITsaviDELIRE-LRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*.
gi 57526399 1427 SIQRML 1432
Cdd:COG1127 225 TPEELL 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
436-628 |
3.37e-19 |
|
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: 88.95 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSwIMPG--T 500
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEP-PAPFglT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFGvsydeyRY-------------RSVIKACqLEE-DISKFSEKDnivLGEggitLSGGQRARISLARAVYKDAD 566
Cdd:COG1120 92 VRELVALG------RYphlglfgrpsaedREAVEEA-LERtGLEHLADRP---VDE----LSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 567 LYLLDSPFGYLDVLTEKEIFEsCVCKL--MANKTRILVTskmeH-----LKKADKILILHEGSVYFYGT 628
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLE-LLRRLarERGRTVVMVL----HdlnlaARYADRLVLLKDGRIVAQGP 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
437-621 |
4.55e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.79 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------------ISFCSQYSWIMPG 499
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserelarlrrrhIGFVFQFFNLLPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 -TIKDNI-----IFGVSYDEY--RYRSVIKACQLEEDISKF-SEkdnivlgeggitLSGGQRARISLARAVYKDADLYLL 570
Cdd:COG1136 101 lTALENValpllLAGVSRKERreRARELLERVGLGDRLDHRpSQ------------LSGGQQQRVAIARALVNRPKLILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 571 DSPFGYLDVLTEKEIFEscvckLMA------NKTRILVTSKMEHLKKADKILILHEG 621
Cdd:COG1136 169 DEPTGNLDSKTGEEVLE-----LLRelnrelGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
425-581 |
5.06e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.38 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 425 DTSLFFSNLLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR----------ISFcsQYS 494
Cdd:COG4525 8 HVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadrgVVF--QKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 495 WIMPG-TIKDNIIFGVsydeyRYRSVIKACQLEE--------DISKFsEKDNIvlgeggITLSGGQRARISLARAVYKDA 565
Cdd:COG4525 86 ALLPWlNVLDNVAFGL-----RLRGVPKAERRARaeellalvGLADF-ARRRI------WQLSGGMRQRVGIARALAADP 153
|
170
....*....|....*.
gi 57526399 566 DLYLLDSPFGYLDVLT 581
Cdd:COG4525 154 RFLLMDEPFGALDALT 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
392-1416 |
5.07e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 93.94 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 392 VVMENVTAFWE--EGFSKLFEKAK-----ENNNNRKISNCDTSLFFSNLLL------GTPVLKDISFKIERGQLLAVAGS 458
Cdd:PTZ00265 340 IILPNITEYMKslEATNSLYEIINrkplvENNDDGKKLKDIKKIQFKNVRFhydtrkDVEIYKDLNFTLTEGKTYAFVGE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 459 TGAGKTSLLMMIMGELEPSEGKI----KHS----------GRISFCSQYSWIMPGTIKDNIIFGV--------------- 509
Cdd:PTZ00265 420 SGCGKSTILKLIERLYDPTEGDIiindSHNlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyyne 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 510 ----SYDEYRYR---------------------------------------SVIKACQLEEDISKFSEKDNIVLGEGGIT 546
Cdd:PTZ00265 500 dgndSQENKNKRnscrakcagdlndmsnttdsneliemrknyqtikdsevvDVSKKVLIHDFVSALPDKYETLVGSNASK 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 547 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKeIFESCVCKLMANKTRI--LVTSKMEHLKKADKILILhegsvy 624
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY-LVQKTINNLKGNENRItiIIAHRLSTIRYANTIFVL------ 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 625 fygtfSELQNQRPDFSSKLMGCDTFDQFTAERRNSiitetlRRFSLEGDTSVSWNETKKPSF---KQTGEFGEKRKNSIL 701
Cdd:PTZ00265 653 -----SNRERGSTVDVDIIGEDPTKDNKENNNKNN------KDDNNNNNNNNNNKINNAGSYiieQGTHDALMKNKNGIY 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 702 NSINSIRKFSvvQKTSlQMNGIDGASDepleRRLSLVPHSEPGegilprSNAVNsgptflggrrqsvlnlMTCSSVNQGQ 781
Cdd:PTZ00265 722 YTMINNQKVS--SKKS-SNNDNDKDSD----MKSSAYKDSERG------YDPDE----------------MNGNSKHENE 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 782 SIhrkTATSTRKMSLAPQASlaeidiysrrlsqdtgleiseeiNEEDLRDCFFDDVENIPAVTTWNTYLRYITVHKSLMF 861
Cdd:PTZ00265 773 SA---SNKKSCKMSDENASE-----------------------NNAGGKLPFLRNLFKRKPKAPNNLRIVYREIFSYKKD 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 862 VLIwclVVFLVEVAASL--VVLCLFPKIL--LQDKGNSTKNaSNSYaviitstsSYYIFyiyvgvadtLLALGLFRGLPL 937
Cdd:PTZ00265 827 VTI---IALSILVAGGLypVFALLYAKYVstLFDFANLEAN-SNKY--------SLYIL---------VIAIAMFISETL 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 938 ---VHTLI--TVSKTLHHKMLQSVLQAPMSTLNTLK-TGGILN-RFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSV 1010
Cdd:PTZ00265 886 knyYNNVIgeKVEKTMKRRLFENILYQEISFFDQDKhAPGLLSaHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFY 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1011 LQPYIflATVPVIAAFILLRGYF----LHTSQQLKQLESEGRSPIFTH-------------LVTSLKGLWTLRAFGRQPY 1073
Cdd:PTZ00265 966 FCPIV--AAVLTGTYFIFMRVFAirarLTANKDVEKKEINQPGTVFAYnsddeifkdpsflIQEAFYNMNTVIIYGLEDY 1043
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1074 FETLFHKALNLhtanwflylstlrwfqmriemifviffiavtfisiltTGEGEGRVGIILTLAMNIMGTLQWAVNS---- 1149
Cdd:PTZ00265 1044 FCNLIEKAIDY-------------------------------------SNKGQKRKTLVNSMLWGFSQSAQLFINSfayw 1086
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1150 ---------SIDVDSLMRSVsrvFKFIDMPTEDGKPNNSFRPSKDSQ------------PSKVMIIENQHVK---KDDIw 1205
Cdd:PTZ00265 1087 fgsflirrgTILVDDFMKSL---FTFLFTGSYAGKLMSLKGDSENAKlsfekyypliirKSNIDVRDNGGIRiknKNDI- 1162
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1206 psGGQMTVKDLTAKYIDGGNA-ILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTK------------------- 1265
Cdd:PTZ00265 1163 --KGKIEIMDVNFRYISRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneq 1240
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1266 ------------------------------------GEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLD-PY 1308
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGK 1320
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1309 EQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRT 1388
Cdd:PTZ00265 1321 EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
1210 1220 1230
....*....|....*....|....*....|
gi 57526399 1389 LK--QAFADCTVILSEHRIEAMLECQRFLV 1416
Cdd:PTZ00265 1401 IVdiKDKADKTIITIAHRIASIKRSDKIVV 1430
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1212-1417 |
5.31e-19 |
|
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: 87.56 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYIDGG--NAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQ---WRK 1285
Cdd:cd03257 3 EVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILgLLKPTSGSIIFDGKDLLKLSRRLrkiRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1286 AFGVIPQKVF-----------IFSGTFRKNLDPYEQWSDQE-IWKVADEVGL-RSVIEQFPGKldfvlvdggcvLSHGHK 1352
Cdd:cd03257 83 EIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEaVLLLLVGVGLpEEVLNRYPHE-----------LSGGQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1353 QLMCLARSVLSKAKILLLDEPSAHLDPIT-YQIIR--RTLKQAFaDCTVILSEHRIEAMLE-CQRFLVI 1417
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVM 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
436-659 |
5.38e-19 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 88.76 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMgELEPSEGKIKHSG-----------RISF--CSQYSWIMPGTIK 502
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFgvIPQKVFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNI-IFGVSYDEYRYRsVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 581
Cdd:cd03289 95 KNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 582 EKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRPDFSSKLMGCDTFDQFTAERRNS 659
Cdd:cd03289 174 YQ-VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLFPRRNSSK 250
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
436-636 |
5.88e-19 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 88.01 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG----------------RISFCSQ-YSWIMP 498
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMIFQqFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 GTIKDNIIFGvsydeyR--YRSVIKACqleedISKFSEKDNIV----LGEGGI---------TLSGGQRARISLARAVYK 563
Cdd:cd03256 93 LSVLENVLSG------RlgRRSTWRSL-----FGLFPKEEKQRalaaLERVGLldkayqradQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 564 DADLYLLDSPFGYLDVLTEKEIFEscvckLMA------NKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQNQR 636
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMD-----LLKrinreeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
436-618 |
6.93e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG--RISFCSQYS---WIMPGTIKDNIIFGvs 510
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSevpDSLPLTVRDLVAMG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 511 ydeyRY-------------RSVIKACQLEEDISKFSEKDnivLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 577
Cdd:NF040873 82 ----RWarrglwrrltrddRAAVDDALERVGLADLAGRQ---LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 57526399 578 DVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILIL 618
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1212-1410 |
8.79e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 87.45 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaf-lrllnTKGEIQIDGVSwdsitLQQWRKAFGVI 1290
Cdd:COG1121 8 ELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTllkailgllppTSGTVRLFGKP-----PRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQKV------------FIFSGTFRKNldPYEQWSDQEIWKVADEVgLRSV-IEQFPGKldfvlvdggCV--LSHGHKQLM 1355
Cdd:COG1121 81 PQRAevdwdfpitvrdVVLMGRYGRR--GLFRRPSRADREAVDEA-LERVgLEDLADR---------PIgeLSGGQQQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1356 CLARSVLSKAKILLLDEPSAHLDPIT----YQIIRRtLKQafADCTVILSEHRIEAMLE 1410
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATeealYELLRE-LRR--EGKTILVVTHDLGAVRE 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
436-632 |
9.57e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.75 E-value: 9.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------ISFCSQySWI----MpgT 500
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQ-SYAlyphM--T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFG-----VSYDEY--RYRSVIKACQLEEdiskfsekdniVL----GEggitLSGGQRARISLARAVYKDADLYL 569
Cdd:COG3839 92 VYENIAFPlklrkVPKAEIdrRVREAAELLGLED-----------LLdrkpKQ----LSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 570 LDSPFGYLD----VLTEKEIFescvcKLMA--NKTRILVTskmeH-------LkkADKILILHEGSVYFYGTFSEL 632
Cdd:COG3839 157 LDEPLSNLDaklrVEMRAEIK-----RLHRrlGTTTIYVT----HdqveamtL--ADRIAVMNDGRIQQVGTPEEL 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
439-628 |
1.06e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.06 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRIsfcsqySWIM-PGTI-------KDNIIF--- 507
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SALLeLGAGfhpeltgRENIYLngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 508 --GVSYDEYRYRsvikacqlEEDISKFSEkdnivLGEgGI-----TLSGGQRARISLARAVYKDADLYLLDspfgylDVL 580
Cdd:COG1134 115 llGLSRKEIDEK--------FDEIVEFAE-----LGD-FIdqpvkTYSSGMRARLAFAVATAVDPDILLVD------EVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 581 T----------EKEIFEscvckLMAN-KTRILVTSKMEHLKK-ADKILILHEGSVYFYGT 628
Cdd:COG1134 175 AvgdaafqkkcLARIRE-----LRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
436-623 |
1.26e-18 |
|
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: 84.40 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRisfcsqyswimpgtikdniifgvsydEYR 515
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 516 YRSVIKACQLeediskfsekdnivlgegGIT----LSGGQRARISLARAVYKDADLYLLDSPFGYLDVlTEKEIFESCVC 591
Cdd:cd03216 66 FASPRDARRA------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTP-AEVERLFKVIR 126
|
170 180 190
....*....|....*....|....*....|....
gi 57526399 592 KLMAN-KTRILVTSKMEHLKK-ADKILILHEGSV 623
Cdd:cd03216 127 RLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1210-1414 |
1.51e-18 |
|
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: 85.61 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1210 QMTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKST--------LLLaflrllnTKGEIQIDGVSWDSITlQ 1281
Cdd:COG4133 2 MLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTllrilaglLPP-------SAGEVLWNGEPIRDAR-E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1282 QWRKAFGVIPQKVFIFSG-TFRKNLDPY-----EQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLM 1355
Cdd:COG4133 72 DYRRRLAYLGHADGLKPElTVRENLRFWaalygLRADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1356 CLARSVLSKAKILLLDEPSAHLDPIT----YQIIRRTLKQafaDCTVILSEHRIEAMLECQRF 1414
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAGvallAELIAAHLAR---GGAVLLTTHQPLELAAARVL 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1227-1422 |
1.56e-18 |
|
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: 86.37 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1227 ILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL 1305
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQpQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1306 dPY--EQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 1383
Cdd:cd03248 109 -AYglQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 57526399 1384 IIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:cd03248 188 QVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1213-1403 |
1.64e-18 |
|
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: 86.08 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKST------LLLAFLRLLNTKGEIQIDG--VSWDSITLQQWR 1284
Cdd:cd03260 3 LRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTllrllnRLNDLIPGAPDEGEVLLDGkdIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1285 KAFGVIPQKVFIFSGTFRKNLDpYEQW----SDQEIWKVADEVGLRSVieQFPGKLDFVLVDGGcvLSHGHKQLMCLARS 1360
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVA-YGLRlhgiKLKEELDERVEEALRKA--ALWDEVKDRLHALG--LSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 57526399 1361 VLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEH 1403
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH 198
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1211-1417 |
6.20e-18 |
|
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: 84.45 E-value: 6.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNA--ILENISFSISPGQRVGLLGRTGSGKSTlllaflrLLN--------TKGEIQIDGVSwdsitL 1280
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKST-------LLRiiaglerpTSGEVLVDGEP-----V 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1281 QQWRKAFGVIPQKVFIFS-GTFRKN-LDPYEQ--WSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHK 1352
Cdd:cd03293 69 TGPGPDRGYVFQQDALLPwLTVLDNvALGLELqgVPKAEARERAEEllelVGLSGFENAYPHQ-----------LSGGMR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1353 QLMCLARSVLSKAKILLLDEPSAHLDPIT--------YQIIRRTLKqafadcTVILSEHRI-EAMLECQRFLVI 1417
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTreqlqeelLDIWRETGK------TVLLVTHDIdEAVFLADRVVVL 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
437-628 |
6.23e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.06 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-----------RISFCSQ-YSWIMPGTIKDN 504
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQhYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGVSYDEYRYR---SVIKA--------CQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:PRK10851 95 IAFGLTVLPRRERpnaAAIKAkvtqllemVQLAHLADRYPAQ-----------LSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 574 FGYLDVLTEKEIfESCVCKLMANK--TRILVTSKMEH-LKKADKILILHEGSVYFYGT 628
Cdd:PRK10851 164 FGALDAQVRKEL-RRWLRQLHEELkfTSVFVTHDQEEaMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1230-1426 |
6.32e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 84.27 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1230 NISFSIsPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWD----SITLQQWRKAFGVIPQKVFIFSG-TFRK 1303
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKpDGGTIVLNGTVLFdsrkKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1304 NLD-PYEQWSDQEIWKVADEV----GLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1378
Cdd:cd03297 95 NLAfGLKRKRNREDRISVDELldllGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 1379 PITYQIIRRTLKQAFAD--CTVILSEHRI-EAMLECQRFLVIEENKVRQYD 1426
Cdd:cd03297 164 RALRLQLLPELKQIKKNlnIPVIFVTHDLsEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1212-1422 |
6.85e-18 |
|
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: 84.55 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYIDGGNAI--LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSIT---LQQWRK 1285
Cdd:cd03258 3 ELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERpTSGSVLVDGTDLTLLSgkeLRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1286 AFGVIPQKVFIFSG-TFRKNLD-PYE--QWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCL 1357
Cdd:cd03258 83 RIGMIFQHFNLLSSrTVFENVAlPLEiaGVPKAEIEERVLEllelVGLEDKADAYPAQ-----------LSGGQKQRVGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDPITYQIIRRTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV 1422
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEV 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1212-1422 |
7.34e-18 |
|
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: 84.54 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYIDGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGV---SWDSITLQQWRKAF 1287
Cdd:cd03256 2 EVENLSKTYPNGKKA-LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEpTSGSVLIDGTdinKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQK--------VF------------IFSGTFRknldpyeQWSDQEIWKVA---DEVGLRSVIEQFPGKldfvlvdgg 1344
Cdd:cd03256 81 GMIFQQfnlierlsVLenvlsgrlgrrsTWRSLFG-------LFPKEEKQRALaalERVGLLDKAYQRADQ--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1345 cvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFA--DCTVILSEHRIE-AMLECQRFLVIEENK 1421
Cdd:cd03256 145 --LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDlAREYADRIVGLKDGR 222
|
.
gi 57526399 1422 V 1422
Cdd:cd03256 223 I 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
436-634 |
7.40e-18 |
|
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: 84.48 E-value: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG----------------RISFCSQYSWI--- 496
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGMLFQSGALfds 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 497 MpgTIKDNIIFGVS----YDEYRYRSVIKAC----QLEEDISKF-SEkdnivlgeggitLSGGQRARISLARAVYKDADL 567
Cdd:cd03261 92 L--TVFENVAFPLRehtrLSEEEIREIVLEKleavGLRGAEDLYpAE------------LSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 568 YLLDSPFGYLDVLTeKEIFESCVCKL--MANKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQN 634
Cdd:cd03261 158 LLYDEPTAGLDPIA-SGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
437-623 |
7.63e-18 |
|
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: 84.06 E-value: 7.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-------------ISFCSQYSWIMPGTIKD 503
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFGVSYDEYRyrSVIKACQ---LEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVL 580
Cdd:cd03248 107 NIAYGLQSCSFE--CVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 57526399 581 TEKEIFESCVCKLmANKTRILVTSKMEHLKKADKILILHEGSV 623
Cdd:cd03248 185 SEQQVQQALYDWP-ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
436-632 |
7.79e-18 |
|
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: 84.13 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR--------------ISFCSQYSWIMPG-T 500
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNI-----IFGVSYDEYRYRsvikacqLEEDISKFsekdNI--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:cd03218 92 VEENIlavleIRGLSKKEREEK-------LEELLEEF----HIthLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 574 FGYLDVLTEKEIfESCVCKLMANKTRILVTSK--MEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:cd03218 161 FAGVDPIAVQDI-QKIIKILKDRGIGVLITDHnvRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
437-632 |
8.83e-18 |
|
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: 88.42 E-value: 8.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPS---EGKIKHSG-------------RISFCSQ--YSWIMP 498
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelsealrgrRIGMVFQdpMTQLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 GTIKDNIIF-----GVSYDEYRYR--SVIKACQLEEDISKFSEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLD 571
Cdd:COG1123 99 VTVGDQIAEalenlGLSRAEARARvlELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 572 SPFGYLDVLTEKEIFEsCVCKLMA--NKTRILVTSKMEH-LKKADKILILHEGSVYFYGTFSEL 632
Cdd:COG1123 168 EPTTALDVTTQAEILD-LLRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1213-1410 |
9.55e-18 |
|
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: 83.35 E-value: 9.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSwdsitLQQWRKAFGVIP 1291
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgLLKPTSGSIRVFGKP-----LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 QKvFIFSGTFRknLDPYE-------------QWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQL 1354
Cdd:cd03235 75 QR-RSIDRDFP--ISVRDvvlmglyghkglfRRLSKADKAKVDEalerVGLSELADRQIGE-----------LSGGQQQR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1355 MCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRIEAMLE 1410
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLE 197
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1213-1422 |
1.05e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 85.04 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVI- 1290
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKpQSGEIKIDGITISKENLKEIRKKIGIIf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 --PQKVFIFS--------GTFRKNLDPYEQWsdQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLArS 1360
Cdd:PRK13632 90 qnPDNQFIGAtveddiafGLENKKVPPKKMK--DIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA-S 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1361 VLS-KAKILLLDEPSAHLDPI----TYQIIRRTLKQafADCTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:PRK13632 156 VLAlNPEIIIFDESTSMLDPKgkreIKKIMVDLRKT--RKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1212-1434 |
1.31e-17 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 83.25 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaflrLLNT--------KGEIQIDGVSWDSITLQQw 1283
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTT-------LLKTimgllpprSGSIRFDGRDITGLPPHE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1284 RKAFGV--IPQKVFIFSG-TFRKNLdpyeqwsdqeiwKVADEVGLRS--------VIEQFPGKLDFVLVDGGcVLSHGHK 1352
Cdd:cd03224 72 RARAGIgyVPEGRRIFPElTVEENL------------LLGAYARRRAkrkarlerVYELFPRLKERRKQLAG-TLSGGEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1353 QLMCLARSVLSKAKILLLDEPSAHLDP-ITYQIIR--RTLKQafADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSI 1428
Cdd:cd03224 139 QMLAIARALMSRPKLLLLDEPSEGLAPkIVEEIFEaiRELRD--EGVTILLVEQNARFALEiADRAYVLERGRVVLEGTA 216
|
....*.
gi 57526399 1429 QRMLSE 1434
Cdd:cd03224 217 AELLAD 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
436-661 |
1.32e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.97 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFcsqySWIMPG---------------- 499
Cdd:COG1118 14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----TNLPPRerrvgfvfqhyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 -TIKDNIIFGVSyDEYRYRSVIKA---CQLEE-DISKF-----SEkdnivlgeggitLSGGQRARISLARAVYKDADLYL 569
Cdd:COG1118 90 mTVAENIAFGLR-VRPPSKAEIRArveELLELvQLEGLadrypSQ------------LSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 570 LDSPFGYLDVLTEKEIfEScvcKLMA-----NKTRILVT-SKMEHLKKADKILILHEGSVYFYGTFSELQNqRP--DFSS 641
Cdd:COG1118 157 LDEPFGALDAKVRKEL-RR---WLRRlhdelGGTTVFVThDQEEALELADRVVVMNQGRIEQVGTPDEVYD-RPatPFVA 231
|
250 260
....*....|....*....|
gi 57526399 642 KLMGCDTFdqFTAERRNSII 661
Cdd:COG1118 232 RFLGCVNV--LRGRVIGGQL 249
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
436-636 |
1.37e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.24 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-------------ISFCSQYSWIMPGTIK 502
Cdd:PRK10790 353 DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvlrqgVAMVQQDPVVLADTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 582
Cdd:PRK10790 433 ANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTE 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 583 KEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQR 636
Cdd:PRK10790 513 QAI-QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1212-1432 |
1.73e-17 |
|
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: 83.50 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYiDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGV---SWDSITLqqwRKAF 1287
Cdd:cd03295 2 EFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEdirEQDPVEL---RRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQKVFIFSG-TFRKN--LDP-YEQWSDQEIWKVADE----VGL--RSVIEQFPGKldfvlvdggcvLSHGHKQLMCL 1357
Cdd:cd03295 78 GYVIQQIGLFPHmTVEENiaLVPkLLKWPKEKIRERADEllalVGLdpAEFADRYPHE-----------LSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDPITyqiiRRTLKQAFADC------TVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQR 1430
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPIT----RDQLQEEFKRLqqelgkTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDE 222
|
..
gi 57526399 1431 ML 1432
Cdd:cd03295 223 IL 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
437-632 |
1.76e-17 |
|
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: 84.23 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-----------------RISFCSQYSWIMPG 499
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 -TIKDNIIF-----GVSYDEYRYRS--VIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLD 571
Cdd:cd03294 117 rTVLENVAFglevqGVPRAEREERAaeALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 572 SPFGYLDVLTEKEIFESCVcKLMAN--KTRILVTSKM-EHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:cd03294 186 EAFSALDPLIRREMQDELL-RLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
438-627 |
2.21e-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: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEG------------KIKHSGRISFC----SQYSWIMP--- 498
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGevrvaglvpwkrRKKFLRRIGVVfgqkTQLWWDLPvid 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 --GTIKDniIFGVSYDEYRYRsvikacqleedISKFSEKDNI--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:cd03267 115 sfYLLAA--IYDLPPARFKKR-----------LDELSELLDLeeLLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 575 GYLDVLTEKEI--FESCVCKLmaNKTRILVTSK-MEHLKK-ADKILILHEGSVYFYG 627
Cdd:cd03267 182 IGLDVVAQENIrnFLKEYNRE--RGTTVLLTSHyMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
434-623 |
3.04e-17 |
|
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: 81.32 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 434 LLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRIsfcsqyswIMPGTIKDNIIFGVSYde 513
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP--------VTRRSPRDAIRAGIAY-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 514 yryrsvikacqLEED------ISKFSEKDNIVLgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFE 587
Cdd:cd03215 80 -----------VPEDrkreglVLDLSVAENIAL---SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 57526399 588 SCVCKLMANKTRILVTSKM-EHLKKADKILILHEGSV 623
Cdd:cd03215 146 LIRELADAGKAVLLISSELdELLGLCDRILVMYEGRI 182
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1213-1430 |
5.07e-17 |
|
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: 81.78 E-value: 5.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSiTLQQWRKAFGVIP 1291
Cdd:cd03263 3 IRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRpTSGTAYINGYSIRT-DRKAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 QKVFIFSG-TFRKNLDPY-------EQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLS 1363
Cdd:cd03263 82 QFDALFDElTVREHLRFYarlkglpKSEIKEEVELLLRVLGLTDKANKRART-----------LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1364 KAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQR 1430
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMdEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
439-623 |
5.08e-17 |
|
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: 81.84 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLL-----MMIMGELEPSEGKIKHSG---------------RISFCSQYSWIMP 498
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 GTIKDNIIFGVsydeyRYRSVIKACQLEEDISKFSEK----DNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:cd03260 95 GSIYDNVAYGL-----RLHGIKLKEELDERVEEALRKaalwDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 575 GYLD-VLTEKeiFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSV 623
Cdd:cd03260 170 SALDpISTAK--IEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRL 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1212-1423 |
7.90e-17 |
|
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: 80.72 E-value: 7.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSiTLQQWRKAFGVI 1290
Cdd:cd03268 2 KTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILgLIKPDSGEITFDGKSYQK-NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQKVFIFSGTFRKNL---DPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKI 1367
Cdd:cd03268 79 EAPGFYPNLTARENLrllARLLGIRKKRIDEVLDVVGLKDSAKKKVKG-----------FSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1368 LLLDEPSAHLDPITYQIIRRTLkQAFAD--CTVILSEHRIEAM-LECQRFLVIEENKVR 1423
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELI-LSLRDqgITVLISSHLLSEIqKVADRIGIINKGKLI 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1213-1422 |
8.45e-17 |
|
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: 81.00 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNA--ILENISFSISPGQRVGLLGRTGSGKSTlllaflrLLN--------TKGEIQIDGVSWDSITLQQ 1282
Cdd:cd03255 3 LKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKST-------LLNilggldrpTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1283 W----RKAFGVIPQK---------------VFIFSGTFRKNldpYEQWSDQeiwkVADEVGLRSVIEQFPGKldfvlvdg 1343
Cdd:cd03255 76 LaafrRRHIGFVFQSfnllpdltalenvelPLLLAGVPKKE---RRERAEE----LLERVGLGDRLNHYPSE-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1344 gcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQ--AFADCTVILSEHRIEAMLECQRFLVIEENK 1421
Cdd:cd03255 141 ---LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
.
gi 57526399 1422 V 1422
Cdd:cd03255 218 I 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
442-627 |
8.71e-17 |
|
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: 80.80 E-value: 8.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 442 DISFKIErGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYSWIMPG------------------TIKD 503
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkiglvfqqyalfphlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFGV-----SYDEYRYRSVIKACQLEEdiskfsekdniVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:cd03297 95 NLAFGLkrkrnREDRISVDELLDLLGLDH-----------LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 579 VLTeKEIFESCVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEGSVYFYG 627
Cdd:cd03297 164 RAL-RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
438-623 |
8.86e-17 |
|
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: 81.01 E-value: 8.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG----------------RISFCSQ--YSWIMPG 499
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQdpMSSLNPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 -TIKDNII------FGVSYDEYRYRSVI-KACQLEEDISKFSEKDNivlgeggiTLSGGQRARISLARAVYKDADLYLLD 571
Cdd:cd03257 99 mTIGEQIAeplrihGKLSKKEARKEAVLlLLVGVGLPEEVLNRYPH--------ELSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 572 SPFGYLDVLTEKEIFEscvckLMA------NKTRILVTSKMEHLKK-ADKILILHEGSV 623
Cdd:cd03257 171 EPTSALDVSVQAQILD-----LLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
436-631 |
9.59e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK--HSGRISFCSQYSWIMPG--TIKDNIIfgvsy 511
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKlgETVKIGYFDQHQEELDPdkTVLDELR----- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 512 DEYRYRSVIKACQL-------EEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTeKE 584
Cdd:COG0488 402 DGAPGGTEQEVRGYlgrflfsGDDAFKPVGV-----------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET-LE 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 585 I-------FESCVcklmanktrILVTskmeH----LKK-ADKILILHEGSVYFY-GTFSE 631
Cdd:COG0488 470 AleealddFPGTV---------LLVS----HdryfLDRvATRILEFEDGGVREYpGGYDD 516
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
436-634 |
9.84e-17 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 80.94 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR--------------ISFCSQYSWIMPG-T 500
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFGVSydeYRYRSVIKAcQLEEDISKFSekdniVLGE-----GGiTLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:cd03224 92 VEENLLLGAY---ARRRAKRKA-RLERVYELFP-----RLKErrkqlAG-TLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 576 YLDVLTEKEIFEsCVCKLMANKTRILVTSKMEH--LKKADKILILHEGSVYFYGTFSELQN 634
Cdd:cd03224 162 GLAPKIVEEIFE-AIRELRDEGVTILLVEQNARfaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
85-305 |
1.00e-16 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 82.21 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 85 GIILYLGEVTKAVQPLLLGRIIaSYDPDNKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKT 164
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLV-EFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 165 LKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQ-------AFTFCGLAFLVVLALLQ 237
Cdd:cd18598 82 LRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGvaflaglVFALVLIPINKWIAKRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 238 AGLGKMMMKYRDQRAGkinerlvITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRkaaYVRYL 305
Cdd:cd18598 162 GALSEKMMKHKDARVK-------LMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALK---GRKYL 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1213-1422 |
1.31e-16 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 81.26 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYiDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSI---TLQQWRKAFG 1288
Cdd:COG3638 5 LRNLSKRY-PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEpTSGEILVDGQDVTALrgrALRRLRRRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VIPQK--------VF------------IFSGTFRKnldpyeqWSDQEIWKVA---DEVGLrsvieqfpgkLDFVL--VDG 1343
Cdd:COG3638 84 MIFQQfnlvprlsVLtnvlagrlgrtsTWRSLLGL-------FPPEDRERALealERVGL----------ADKAYqrADQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1344 gcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRIE-AMLECQRFLVIEEN 1420
Cdd:COG3638 147 ---LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdgITVVVNLHQVDlARRYADRIIGLRDG 223
|
..
gi 57526399 1421 KV 1422
Cdd:COG3638 224 RV 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
436-635 |
1.42e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTP----VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG---------------RISFCSQYS-- 494
Cdd:PRK13637 15 GTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 495 WIMPGTIKDNIIFGVS----YDEYRYRSVIKACQLEE-DISKFSEKDNivlgeggITLSGGQRARISLARAVYKDADLYL 569
Cdd:PRK13637 95 QLFEETIEKDIAFGPInlglSEEEIENRVKRAMNIVGlDYEDYKDKSP-------FELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 570 LDSPFGYLDVLTEKEIFEScVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQNQ 635
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNK-IKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
430-627 |
3.42e-16 |
|
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: 79.33 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 430 FSNLLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQ----Y 493
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRLGFVSDstglY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 494 SWImpgTIKDNIIF-----GVSYDEYRYRsvikacqLEEDISKFSEKDNIVLGEGGitLSGGQRARISLARAVYKDADLY 568
Cdd:cd03266 91 DRL---TARENLEYfaglyGLKGDELTAR-------LEELADRLGMEELLDRRVGG--FSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 569 LLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYG 627
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
447-608 |
3.65e-16 |
|
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: 79.76 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 447 IERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-RISFCSQY-SWIMPGTIKD---NIIFGVSYDEYRYRSVIK 521
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYiKADYEGTVRDllsSITKDFYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 522 ACQLEEDIskfsekDNIVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVltEKEIFESCVCK---LMANKT 598
Cdd:cd03237 102 PLQIEQIL------DREVP-----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQRLMASKVIRrfaENNEKT 168
|
170
....*....|
gi 57526399 599 RILVtskmEH 608
Cdd:cd03237 169 AFVV----EH 174
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1206-1430 |
4.25e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.32 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1206 PSGGQMTVKDLTAkYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAflrllntkgeiqIDGVsWD----SITL- 1280
Cdd:COG4178 358 SEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA------------IAGL-WPygsgRIARp 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1281 QQWRKAFgvIPQKVFIFSGTFRKNL---DPYEQWSDQEIWKVADEVGLrsviEQFPGKLDFVlVDGGCVLSHGHKQLMCL 1357
Cdd:COG4178 424 AGARVLF--LPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL----GHLAERLDEE-ADWDQVLSLGEQQRLAF 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQR 1430
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEA 569
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
436-623 |
4.41e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.68 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------ISFCSQ-YSwIMPG-TIK 502
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQdYA-LFPHlTVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG-----VSYDEYRYR--SVIKACQLEEdiskFSEK--DnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:COG3842 96 ENVAFGlrmrgVPKAEIRARvaELLELVGLEG----LADRypH---------QLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 574 FGYLDV-LTE------KEIFEScvcklmANKTRILVT-SKMEHLKKADKILILHEGSV 623
Cdd:COG3842 163 LSALDAkLREemreelRRLQRE------LGITFIYVThDQEEALALADRIAVMNDGRI 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
436-579 |
6.45e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG--RISFCSQYSWIMPG-TIKDNIIFGVS-- 510
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLDGDAel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 511 ---YDEYRyRSVIKACQLEEDISKFSEKDN---------------IVLGEGGI----------TLSGGQRARISLARAVY 562
Cdd:COG0488 90 ralEAELE-ELEAKLAEPDEDLERLAELQEefealggweaearaeEILSGLGFpeedldrpvsELSGGWRRRVALARALL 168
|
170
....*....|....*..
gi 57526399 563 KDADLYLLDSPFGYLDV 579
Cdd:COG0488 169 SEPDLLLLDEPTNHLDL 185
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
440-637 |
6.95e-16 |
|
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: 78.66 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG---------RISFCSQYSWIMPGTIKDNIIFGVS 510
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitepgpdRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 511 ydeyryrsvikacQLEEDISKfSEKDNIV--------LGEGG----ITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:TIGR01184 81 -------------RVLPDLSK-SERRAIVeehialvgLTEAAdkrpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 579 VLTEKEIFEscvcKLM-----ANKTRILVTSKM-EHLKKADKILILHEGSVYFYGTFSELQNQRP 637
Cdd:TIGR01184 147 ALTRGNLQE----ELMqiweeHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEVPFPRP 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
436-635 |
7.35e-16 |
|
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: 78.43 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------ISFCSQYSWIMPG-TIKD 503
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFG-----VSYDEYRYR--SVIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:cd03300 92 NIAFGlrlkkLPKAEIKERvaEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 577 LDV-LTEKEIFESCVCKLMANKTRILVT-SKMEHLKKADKILILHEGSVYFYGTFSELQNQ 635
Cdd:cd03300 161 LDLkLRKDMQLELKRLQKELGITFVFVThDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
436-621 |
9.73e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.49 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPV----LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-----------------RISFCSQY- 493
Cdd:PRK13641 15 GTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 494 -SWIMPGTIKDNII-----FGVSYDEYRYRSV--IKACQLEEDISKFSEKDnivlgeggitLSGGQRARISLARAVYKDA 565
Cdd:PRK13641 95 eAQLFENTVLKDVEfgpknFGFSEDEAKEKALkwLKKVGLSEDLISKSPFE----------LSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 566 DLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 621
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHG 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
421-621 |
1.00e-15 |
|
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: 75.56 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 421 ISNCDTSLFFSnlllGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFC--SQyswimp 498
Cdd:cd03221 1 IELENLSKTYG----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGyfEQ------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 gtikdniifgvsydeyryrsvikacqleediskfsekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 579 VLT----EKEI--FESCVcklmanktrILVTSKMEHLKK-ADKILILHEG 621
Cdd:cd03221 103 LESiealEEALkeYPGTV---------ILVSHDRYFLDQvATKIIELEDG 143
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1219-1422 |
1.03e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.79 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1219 KYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLL-LAFLRLLNTKGEIQIDGVSWDSIT---LQQWRKAFGVIPQkv 1294
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLkLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRIGVVFQ-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1295 fifsgTFR--KNLDPYE---------QWSDQEIWK----VADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1359
Cdd:COG2884 87 -----DFRllPDRTVYEnvalplrvtGKSRKEIRRrvreVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1360 SVLSKAKILLLDEPSAHLDPITYQIIRRTLKQaFAD--CTVILSEHRIEAMLECQ-RFLVIEENKV 1422
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEE-INRrgTTVLIATHDLELVDRMPkRVLELEDGRL 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
436-587 |
1.04e-15 |
|
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: 77.83 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG----------------RISFCSQYSWIMPG 499
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 -TIKDNIIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:cd03292 93 rNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
....*....
gi 57526399 579 VLTEKEIFE 587
Cdd:cd03292 169 PDTTWEIMN 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1212-1422 |
1.45e-15 |
|
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: 81.49 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKY---IDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSIT---LQQWR 1284
Cdd:COG1123 262 EVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRpTSGSILFDGKDLTKLSrrsLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1285 KAFGVIPQkvfifsgtfrknlDPYEQ--------------------WSDQEIWKVADE----VGL-RSVIEQFPGKldfv 1339
Cdd:COG1123 342 RRVQMVFQ-------------DPYSSlnprmtvgdiiaeplrlhglLSRAERRERVAEllerVGLpPDLADRYPHE---- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1340 lvdggcvLSHGHKQLMCLARSVLSKAKILLLDEP-SAhLDPITY-QIIR--RTLKQAFaDCTVILSEHRIEAMLE-CQRF 1414
Cdd:COG1123 405 -------LSGGQRQRVAIARALALEPKLLILDEPtSA-LDVSVQaQILNllRDLQREL-GLTYLFISHDLAVVRYiADRV 475
|
....*...
gi 57526399 1415 LVIEENKV 1422
Cdd:COG1123 476 AVMYDGRI 483
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1211-1418 |
2.20e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 77.01 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNA--ILENISFSISPGQRVGLLGRTGSGKSTlllaflrLLN--------TKGEIQIDGV---SWDS 1277
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKST-------LLNilggldrpTSGEVLIDGQdisSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1278 ITLQQWR-KAFGVIPQK---------------VFIFSGTFRKNldpyeqwSDQEIWKVADEVGLRSVIEQFPGKldfvlv 1341
Cdd:COG1136 78 RELARLRrRHIGFVFQFfnllpeltalenvalPLLLAGVSRKE-------RRERARELLERVGLGDRLDHRPSQ------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1342 dggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRIEAMLECQRFLVIE 1418
Cdd:COG1136 145 -----LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLR 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1206-1426 |
3.24e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.49 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1206 PSGGQM-TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLlaflrllntK---GEIQIDG--VSWdSIT 1279
Cdd:COG0488 310 RLGKKVlELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLL---------KllaGELEPDSgtVKL-GET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1280 LQqwrkaFGVIPQKvfifSGTFRKNLDPYEqwsdqEIWKVAD---EVGLRSVIEQ--FPGKLDFVLVDggcVLSHGHKQL 1354
Cdd:COG0488 378 VK-----IGYFDQH----QEELDPDKTVLD-----ELRDGAPggtEQEVRGYLGRflFSGDDAFKPVG---VLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1355 MCLARSVLSKAKILLLDEPSAHLDPITyqiiRRTLKQAFADC--TVILSEH-R--IEAMleCQRFLVIEENKVRQYD 1426
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEALDDFpgTVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
436-628 |
3.49e-15 |
|
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: 80.33 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI----------------KHSGRISFCSQ--YSWIM 497
Cdd:COG1123 277 GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklsrrslrELRRRVQMVFQdpYSSLN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 498 PG-TIKDNI-----IFGVSYDEYRYRSV---IKACQLEED-ISKF-SEkdnivlgeggitLSGGQRARISLARAVYKDAD 566
Cdd:COG1123 357 PRmTVGDIIaeplrLHGLLSRAERRERVaelLERVGLPPDlADRYpHE------------LSGGQRQRVAIARALALEPK 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 567 LYLLDSPFGYLDVLTEKEIFEscvckLMA------NKTRILVT---SKMEHLkkADKILILHEGSVYFYGT 628
Cdd:COG1123 425 LLILDEPTSALDVSVQAQILN-----LLRdlqrelGLTYLFIShdlAVVRYI--ADRVAVMYDGRIVEDGP 488
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
85-350 |
5.29e-15 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 77.66 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 85 GIILYLGEVTKAVQPLLLGRII-----ASYDPDNKVERSIAIYL--------GIGLCLLFIVRTLLLHPAIFGLHHI--- 148
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVdyveeNTYSSSNSTDKLSVSYVtveeffsnGYVLAVILFLALLLQATFSQASYHIvir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 149 -GMQMRIAMFSLIYKKTLKLSSRVLD--KISIGQLVSLLS---NNLNKFdegLALAHFVWIAPLQVTLLMGLLWDLLQAF 222
Cdd:cd18591 83 eGIRLKTALQAMIYEKALRLSSWNLSsgSMTIGQITNHMSedaNNIMFF---FWLIHYLWAIPLKIIVGLILLYLKLGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 223 TFCGLAFLVVLALLQAGLGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYV 302
Cdd:cd18591 160 ALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVY 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 303 RYLNSSAFFFSGFFVVFLSVLPYALLKGIILR--KIFTTIS-----------FCIVLRMAV 350
Cdd:cd18591 240 WSLMTFLTQASPILVTLVTFGLYPYLEGEPLTaaKAFSSLAlfnqltvplfiFPVVIPILI 300
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
436-634 |
5.61e-15 |
|
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: 75.94 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-I---------------SFcsQYSWIMPG 499
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdItglppheiarlgigrTF--QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 -TIKDNIIFGVsydEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYL 569
Cdd:cd03219 90 lTVLENVMVAA---QARTGSGLLLARARREEREARERAEELLERVGLadladrpagELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 570 LDSPFGYLDvLTEKEIFESCVCKLMANKTRILVTskmEH-----LKKADKILILHEGSVYFYGTFSELQN 634
Cdd:cd03219 167 LDEPAAGLN-PEETEELAELIRELRERGITVLLV---EHdmdvvMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1214-1422 |
6.07e-15 |
|
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: 75.52 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1214 KDLTAKYiDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSI---TLQQWRKAFGV 1289
Cdd:cd03292 4 INVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSDLrgrAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFSgtfrkNLDPYE---------QWSDQEIWK----VADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMC 1356
Cdd:cd03292 83 VFQDFRLLP-----DRNVYEnvafalevtGVPPREIRKrvpaALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1357 LARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQA-FADCTVILSEHRIEAMLECQ-RFLVIEENKV 1422
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
436-674 |
8.71e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 8.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQYSWIMPG-TIK 502
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQFDNLDLEfTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DN-IIFGvsydeyRYRSvIKACQLEEDISKFSE------KDNIVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:PRK13536 133 ENlLVFG------RYFG-MSTREIEAVIPSLLEfarlesKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 576 YLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGsvyfygtfSELQNQRP-DFSSKLMGCDTFDQFT 653
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAG--------RKIAEGRPhALIDEHIGCQVIEIYG 273
|
250 260
....*....|....*....|...
gi 57526399 654 AERR--NSIITETLRRFSLEGDT 674
Cdd:PRK13536 274 GDPHelSSLVKPYARRIEVSGET 296
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1213-1425 |
1.10e-14 |
|
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: 74.62 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLL-LAFLRLLNTKGEIQIDGVSWDSITlqqwRKAFGVIP 1291
Cdd:cd03269 3 VENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIrMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 -----------QKVFIFSGTFrKNLDPYE--QWSDQEIWKVADEVGLRSVIEQfpgkldfvlvdggcvLSHGHKQLMCLA 1358
Cdd:cd03269 77 eerglypkmkvIDQLVYLAQL-KGLKKEEarRRIDEWLERLELSEYANKRVEE---------------LSKGNQQKVQFI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1359 RSVLSKAKILLLDEPSAHLDPITYQIIRRTL-KQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQY 1425
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLY 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
439-635 |
1.11e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 76.30 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI---------KHSGRISFcsqyswiMP---G-----TI 501
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgepldpEDRRRIGY-------LPeerGlypkmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 502 KDNIIF-----GVSydeyryRSVIKAcQLEEDISKF----SEKDNIvlgEggiTLSGGQRARISLARAVYKDADLYLLDS 572
Cdd:COG4152 89 GEQLVYlarlkGLS------KAEAKR-RADEWLERLglgdRANKKV---E---ELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 573 PFGYLDV----LTEKEIFEscvckLMAN-KTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQNQ 635
Cdd:COG4152 156 PFSGLDPvnveLLKDVIRE-----LAAKgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
447-579 |
1.26e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.70 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 447 IERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYswIMP---GTIKDNI-----IFGVSYdeyrYRS 518
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQY--IKPdydGTVEDLLrsitdDLGSSY----YKS 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 519 -VIKACQLEedisKFSEKDnivLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:PRK13409 436 eIIKPLQLE----RLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1213-1422 |
1.40e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.85 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGG---NAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVS-WD-SITLQQWRKA 1286
Cdd:PRK13637 5 IENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVDiTDkKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 FGVIPQ--KVFIFSGTFRK-------NLDPYEQWSDQEIWKVADEVGLRsvIEQFPGKLDFvlvdggcVLSHGHKQLMCL 1357
Cdd:PRK13637 85 VGLVFQypEYQLFEETIEKdiafgpiNLGLSEEEIENRVKRAMNIVGLD--YEDYKDKSPF-------ELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDP-----ITYQIirRTLKQAFaDCTVILSEHRIEAMLE-CQRFLVIEENKV 1422
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPkgrdeILNKI--KELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1212-1423 |
1.77e-14 |
|
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: 74.63 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLlaflrllNT--------KGEIQIDGVSwdsIT-LQQ 1282
Cdd:COG0410 5 EVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLL-------KAisgllpprSGSIRFDGED---ITgLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1283 WRKA---FGVIPQKVFIFSG-TFRKNLdpyeqwsdqEI--WKVADEVGLRSVIEQ----FPgkldfVLVD-----GGcVL 1347
Cdd:COG0410 73 HRIArlgIGYVPEGRRIFPSlTVEENL---------LLgaYARRDRAEVRADLERvyelFP-----RLKErrrqrAG-TL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1348 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT----YQIIRRtLKQafADCTVILSEHRIEAMLE-CQRFLVIEENKV 1422
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIveeiFEIIRR-LNR--EGVTILLVEQNARFALEiADRAYVLERGRI 214
|
.
gi 57526399 1423 R 1423
Cdd:COG0410 215 V 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
427-623 |
1.85e-14 |
|
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: 74.84 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 427 SLFFSNLLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQ- 492
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrRVQMVFQd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 493 -YSWIMPG-TIKDNI-----IFGVSYDEYRYRSVIKACQLEEDI-SKFSEKdnivlgeggitLSGGQRARISLARAVYKD 564
Cdd:COG1124 88 pYASLHPRhTVDRILaeplrIHGLPDREERIAELLEQVGLPPSFlDRYPHQ-----------LSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 565 ADLYLLDSPFGYLDVLTEKEIFEsCVCKLMA--NKTRILVT---SKMEHLkkADKILILHEGSV 623
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILN-LLKDLREerGLTYLFVShdlAVVAHL--CDRVAVMQNGRI 217
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
440-633 |
2.02e-14 |
|
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: 73.94 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQYSWIMPG-TIKDNI- 505
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 506 ----IFGVSYDEYRYR--SVIKACQLEEdiskfsEKDNIVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:cd03265 96 iharLYGVPGAERRERidELLDFVGLLE------AADRLVK-----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 580 LTEKEIFEScVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQ 633
Cdd:cd03265 165 QTRAHVWEY-IEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEELK 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
436-632 |
2.43e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.44 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTP----VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI--------------------KHSGrISFCS 491
Cdd:PRK13634 15 KTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagkknkklkplrKKVG-IVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 492 QYSWIMPGTIKDNIIFG-----VSYDE--YRYRSVIKACQLEEDISKFSEKDnivlgeggitLSGGQRARISLARAVYKD 564
Cdd:PRK13634 94 PEHQLFEETVEKDICFGpmnfgVSEEDakQKAREMIELVGLPEELLARSPFE----------LSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 565 ADLYLLDSPFGYLDVLTEKEIFEscvcklM-------ANKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSEL 632
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMME------MfyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1213-1424 |
2.51e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 73.38 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQrVGLLGRTGSGKST-LLLAFLRLLNTKGEIQIDGVSwDSITLQQWRKAFGVIP 1291
Cdd:cd03264 3 LENLTKRY--GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTlMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 QKVFIFSG-TFRKNLDpYEQW--------SDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSVL 1362
Cdd:cd03264 79 QEFGVYPNfTVREFLD-YIAWlkgipskeVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1363 SKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQ 1424
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVF 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
435-587 |
2.58e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.08 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 435 LGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-----------------RISFCSQYSWIM 497
Cdd:PRK11629 20 VQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 498 PG-TIKDNI-----IFGVSYDEY--RYRSVIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYL 569
Cdd:PRK11629 100 PDfTALENVampllIGKKKPAEInsRALEMLAAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLVL 168
|
170
....*....|....*...
gi 57526399 570 LDSPFGYLDVLTEKEIFE 587
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQ 186
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1216-1404 |
2.96e-14 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 72.97 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1216 LTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLA---FLRLLNTKGEIQIDGVswdSITLQQWRKAFGVIPQ 1292
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAlagRRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1293 K-VFIFSGTFRKNLDpyeqwsdqeiwkVAdeVGLRSvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 1371
Cdd:cd03213 90 DdILHPTLTVRETLM------------FA--AKLRG-------------------LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190
....*....|....*....|....*....|....
gi 57526399 1372 EPSAHLDPITYQIIRRTLKQ-AFADCTVILSEHR 1404
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQ 170
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
942-1167 |
3.58e-14 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 74.94 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 942 ITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPyIFLATVP 1021
Cdd:cd18559 67 IFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAAVGIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1022 VIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHTANWFLYLST---LRW 1098
Cdd:cd18559 146 LGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFE----WEEAFIRQVDAKRDNELAYLPSivyLRA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1099 FQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVSRVFKFI 1167
Cdd:cd18559 222 LAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
439-627 |
3.71e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 73.46 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEpsEGKIKhSGRISFCSQYSwiMPGTIKDNIIFGVSYD------ 512
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTT-SGQILFNGQPR--KPDQFQKCVAYVRQDDillpgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 513 ---EYRYRSVIkaCQLEEDISKFSEK---DNIVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYL 577
Cdd:cd03234 97 tvrETLTYTAI--LRLPRKSSDAIRKkrvEDVLLRDLALTriggnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 578 DVLTEKEIFEscVCKLMANKTRILVTS----KMEHLKKADKILILHEGSVYFYG 627
Cdd:cd03234 175 DSFTALNLVS--TLSQLARRNRIVILTihqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1213-1422 |
3.75e-14 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 73.87 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYiDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGvswDSIT------LQQWRK 1285
Cdd:TIGR02315 4 VENLSKVY-PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEG---TDITklrgkkLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1286 AFGVIPQK------------VFI----FSGTFRKNLDPYEQWSDQEIWKVADEVGLrsvieqfpgkLDFVL--VDGgcvL 1347
Cdd:TIGR02315 80 RIGMIFQHynlierltvlenVLHgrlgYKPTWRSLLGRFSEEDKERALSALERVGL----------ADKAYqrADQ---L 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1348 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRIE-AMLECQRFLVIEENKV 1422
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdgITVIINLHQVDlAKKYADRIVGLKAGEI 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
439-641 |
3.83e-14 |
|
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: 78.06 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKDNI 505
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 506 IFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEI 585
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 586 -------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRPDFSS 641
Cdd:TIGR00957 1461 qstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
436-657 |
3.96e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------ISFCSQYSWIMPG-TIKD 503
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFGVSYDEYRyRSVIKAcQLEEDISKFSEKDniVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvlteK 583
Cdd:PRK11607 111 NIAFGLKQDKLP-KAEIAS-RVNEMLGLVHMQE--FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD----K 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 584 EIFESCVCKLMANKTRILVTSKM------EHLKKADKILILHEGSVYFYGTFSEL-QNQRPDFSSKLMG-CDTFDQFTAE 655
Cdd:PRK11607 183 KLRDRMQLEVVDILERVGVTCVMvthdqeEAMTMAGRIAIMNRGKFVQIGEPEEIyEHPTTRYSAEFIGsVNVFEGVLKE 262
|
..
gi 57526399 656 RR 657
Cdd:PRK11607 263 RQ 264
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1213-1422 |
4.03e-14 |
|
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: 73.63 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLlaflrllN--------TKGEIQIDGVswDSITLQQWR 1284
Cdd:cd03219 3 VRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLF-------NlisgflrpTSGSVLFDGE--DITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1285 KA-------FgvipQKVFIFSG-TFRKNL---------DPYEQW----SDQEIWKVADE----VGLRSVIEQFPGKLdfv 1339
Cdd:cd03219 72 IArlgigrtF----QIPRLFPElTVLENVmvaaqartgSGLLLArarrEEREARERAEEllerVGLADLADRPAGEL--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1340 lvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI-TYQIIRRTLKQAFADCTVILSEHRIEAMLE-CQRFLVI 1417
Cdd:cd03219 145 --------SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVL 216
|
....*
gi 57526399 1418 EENKV 1422
Cdd:cd03219 217 DQGRV 221
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1223-1406 |
5.95e-14 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 72.07 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG--VSWDSITLQQWRKAFGVIPQkvfifsg 1299
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRpQSGAVLIDGepLDYSRKGLLERRQRVGLVFQ------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 tfrknlDPYEQWSDQEIWK-VA--------DEVGLRSVIEQFPGKLDFV-LVDGGC-VLSHGHKQLMCLARSVLSKAKIL 1368
Cdd:TIGR01166 76 ------DPDDQLFAADVDQdVAfgplnlglSEAEVERRVREALTAVGASgLRERPThCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 57526399 1369 LLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRIE 1406
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVD 188
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
431-623 |
6.40e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.56 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 431 SNLLLGTP--------------VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEG----------KIKHSGR 486
Cdd:PRK11247 5 ARLNQGTPlllnavskrygertVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtaplaEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 487 ISFcsQYSWIMP-GTIKDNIIFGVSYD-EYRYRSVIKACQLEEDIskfsekdnivlGEGGITLSGGQRARISLARAVYKD 564
Cdd:PRK11247 85 LMF--QDARLLPwKKVIDNVGLGLKGQwRDAALQALAAVGLADRA-----------NEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 565 ADLYLLDSPFGYLDVLTEKEIfESCVCKLMANK--TRILVTSKM-EHLKKADKILILHEGSV 623
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEM-QDLIESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
439-621 |
6.61e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 6.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQYSWIMPG-TIKDNI 505
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQFDNLDPDfTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 506 -IFGvsydeyRYRSvIKACQLEE------DISKFSEKDNIVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:PRK13537 102 lVFG------RYFG-LSAAAARAlvppllEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 57526399 579 VLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 621
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
430-632 |
7.21e-14 |
|
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: 72.61 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 430 FSNLLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGeLE-PSEGKIKHSG----------------RISFCSQ 492
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LErPTSGSVLVDGtdltllsgkelrkarrRIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 493 -YSWIMPGTIKDNI-----IFGVSyDEYRYRSVikacqleEDISKF---SEKDNIVLGEggitLSGGQRARISLARAVYK 563
Cdd:cd03258 90 hFNLLSSRTVFENValpleIAGVP-KAEIEERV-------LELLELvglEDKADAYPAQ----LSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 564 DADLYLLDSPFGYLDVLTEKEIFE---SCVCKLmaNKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSEL 632
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILAllrDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
446-579 |
8.90e-14 |
|
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: 75.98 E-value: 8.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 446 KIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQY-SWIMPGTIKDNI------IFGVSYdeyrYRS 518
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYiSPDYDGTVEEFLrsantdDFGSSY----YKT 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 519 -VIKACQLEedisKFSEKDnivLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:COG1245 438 eIIKPLGLE----KLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
436-634 |
1.05e-13 |
|
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: 75.61 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMG--ELEPSEGKIKHsgRISFCSQYSWIMP------------GTI 501
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIY--HVALCEKCGYVERpskvgepcpvcgGTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 502 KDNIIFGVSYDEYRYRSVIK--ACQLEEDISKFSEK---DNIV--LGEGG----------------------IT-----L 547
Cdd:TIGR03269 90 EPEEVDFWNLSDKLRRRIRKriAIMLQRTFALYGDDtvlDNVLeaLEEIGyegkeavgravdliemvqlshrIThiardL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 548 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSK----MEHLkkADKILILHEGSV 623
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevIEDL--SDKAIWLENGEI 247
|
250
....*....|.
gi 57526399 624 YFYGTFSELQN 634
Cdd:TIGR03269 248 KEEGTPDEVVA 258
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1213-1441 |
1.07e-13 |
|
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: 72.85 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaFLRLLN-----TKGEIQIDGVSWDSI-TLQQWRKA 1286
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKST----LAKLLNglllpTSGKVTVDGLDTLDEeNLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 FGVI---PQKVFIfSGTFR---------KNLDPYEQWsdQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQL 1354
Cdd:TIGR04520 79 VGMVfqnPDNQFV-GATVEddvafglenLGVPREEMR--KRVDEALKLVGMEDFRDREPHL-----------LSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1355 MCLArSVLS-KAKILLLDEPSAHLDPIT----YQIIRRTLKQafADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQ 1429
Cdd:TIGR04520 145 VAIA-GVLAmRPDIIILDEATSMLDPKGrkevLETIRKLNKE--EGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
250
....*....|..
gi 57526399 1430 RMLSEKSLFRQA 1441
Cdd:TIGR04520 222 EIFSQVELLKEI 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
436-635 |
1.28e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.85 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYSWI---------------MPGT 500
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFG-----VSYDEY--RYRSVIKACQLEEdiskFSEKdnivlgeGGITLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:PRK13647 97 VWDDVAFGpvnmgLDKDEVerRVEEALKAVRMWD----FRDK-------PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 574 FGYLDVLTEKEIFESCVCKLMANKTRILVTSKME-HLKKADKILILHEGSVYFYGTFSELQNQ 635
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1224-1438 |
1.69e-13 |
|
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: 72.58 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1224 GNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGvswdsitlqqwRKAFGviPQKVFIFSGTFR 1302
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSG-----------RISFS--SQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1303 KNLD---PYEQWSDQEIWKVADevgLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 1379
Cdd:cd03291 116 ENIIfgvSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1380 IT-YQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLF 1438
Cdd:cd03291 193 FTeKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1213-1403 |
1.73e-13 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 71.28 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLqqwrKAFGVIp 1291
Cdd:TIGR03740 3 TKNLSKRF--GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRpTSGEIIFDGHPWTRKDL----HKIGSL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 qkvfIFSGTFRKNLDPYEQW---------SDQEIWKVADEVGLRsVIEQFPGKlDFvlvdggcvlSHGHKQLMCLARSVL 1362
Cdd:TIGR03740 76 ----IESPPLYENLTARENLkvhttllglPDSRIDEVLNIVDLT-NTGKKKAK-QF---------SLGMKQRLGIAIALL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 57526399 1363 SKAKILLLDEPSAHLDPITYQIIRRtLKQAFAD--CTVILSEH 1403
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRE-LIRSFPEqgITVILSSH 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1223-1418 |
2.64e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.94 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSiTLQQWRKAFGVIPQkvfiFSG-- 1299
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPA-RARLARARIGVVPQ----FDNld 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 ---TFRKNLDPYEQW---SDQEIwkvadEVGLRSVIE--QFPGKLDFVLVDggcvLSHGHKQLMCLARSVLSKAKILLLD 1371
Cdd:PRK13536 127 lefTVRENLLVFGRYfgmSTREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 57526399 1372 EPSAHLDPITYQIIRRTLKQAFADC-TVILSEHRI-EAMLECQRFLVIE 1418
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGkTILLTTHFMeEAERLCDRLCVLE 246
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
438-636 |
3.16e-13 |
|
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: 71.48 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKDN 504
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKe 584
Cdd:cd03288 115 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN- 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 585 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQR 636
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1211-1423 |
3.84e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.09 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYID--GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSwdsiTLQQWRKA- 1286
Cdd:cd03266 2 ITADALTKRFRDvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpDAGFATVDGFD----VVKEPAEAr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 --FGVIPQKVFIFSG-TFRKNLDPY-------EQWSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMC 1356
Cdd:cd03266 78 rrLGFVSDSTGLYDRlTARENLEYFaglyglkGDELTARLEELADRLGMEELLDRRVGGF-----------STGMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1357 LARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRI-EAMLECQRFLVIEENKVR 1423
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMqEVERLCDRVVVLHRGRVV 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1213-1427 |
3.94e-13 |
|
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: 70.09 E-value: 3.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG--VSWDSITLqqwRKAFGV 1289
Cdd:cd03265 3 VENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGhdVVREPREV---RRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFSG-TFRKNLD--------PYEQWsDQEIWKVADEVGLrsvieqfpgkLDFV--LVdggCVLSHGHKQLMCLA 1358
Cdd:cd03265 78 VFQDLSVDDElTGWENLYiharlygvPGAER-RERIDELLDFVGL----------LEAAdrLV---KTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1359 RSVLSKAKILLLDEPSAHLDPIT----YQIIrRTLKQAFaDCTVILSEHRI-EAMLECQRFLVIEENKVRQYDS 1427
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTrahvWEYI-EKLKEEF-GMTILLTTHYMeEAEQLCDRVAIIDHGRIIAEGT 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
427-578 |
4.76e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.82 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 427 SLFFSNLLL---GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEP---SEGKIKHSGR-------------I 487
Cdd:COG4136 1 MLSLENLTItlgGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRrltalpaeqrrigI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 488 SFcsQYSWIMPG-TIKDNIIFGVSYD---EYRYRSVIKAcqLEE-DISKFSEKDNIvlgeggiTLSGGQRARISLARAVY 562
Cdd:COG4136 81 LF--QDDLLFPHlSVGENLAFALPPTigrAQRRARVEQA--LEEaGLAGFADRDPA-------TLSGGQRARVALLRALL 149
|
170
....*....|....*.
gi 57526399 563 KDADLYLLDSPFGYLD 578
Cdd:COG4136 150 AEPRALLLDEPFSKLD 165
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
438-613 |
4.77e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQYSWIMPG-TIKDN 504
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdlctyqkQLCFVGHRSGINPYlTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGVSYDEyryrsviKACQLEEDISKFSEKDNIVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTeke 584
Cdd:PRK13540 95 CLYDIHFSP-------GAVGITELCRLFSLEHLIDYPCG--LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS--- 162
|
170 180 190
....*....|....*....|....*....|...
gi 57526399 585 iFESCVCKLMANKTR---ILVTSKME-HLKKAD 613
Cdd:PRK13540 163 -LLTIITKIQEHRAKggaVLLTSHQDlPLNKAD 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
434-623 |
4.78e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.51 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 434 LLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR--------------ISFCS----QYSW 495
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 496 IMPGTIKDNIIFgVSYDEYRYRSVIKACQLEEDISKFSEKDNIVLgeGGI-----TLSGGQRARISLARAVYKDADLYLL 570
Cdd:COG1129 342 VLDLSIRENITL-ASLDRLSRGGLLDRRRERALAEEYIKRLRIKT--PSPeqpvgNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 571 DSPF-GyLDVLTEKEIFescvcKLMANKTR-----ILVTSKM-EHLKKADKILILHEGSV 623
Cdd:COG1129 419 DEPTrG-IDVGAKAEIY-----RLIRELAAegkavIVISSELpELLGLSDRILVMREGRI 472
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
415-607 |
5.04e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 415 NNNNRKISNCDTSLFFSNLLlgtpVLKDISFKIERGQLLAVAGSTGAGKTSLLMMI--MGELEPS---EGKIKHSG---- 485
Cdd:PRK14243 5 NGTETVLRTENLNVYYGSFL----AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGknly 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 486 -----------RISFCSQYSWIMPGTIKDNIIFGV-------SYDEYRYRSVIKACQLEEdiskfsEKDNivLGEGGITL 547
Cdd:PRK14243 81 apdvdpvevrrRIGMVFQKPNPFPKSIYDNIAYGAringykgDMDELVERSLRQAALWDE------VKDK--LKQSGLSL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 548 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIfESCVCKLMANKTRILVTSKME 607
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQ 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
439-627 |
5.75e-13 |
|
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: 69.53 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGqLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQYswimpgtikdnii 506
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQE------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 507 FGVsYDEYRYRSVIKACQLEEDISKFSEKDNI--VLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:cd03264 81 FGV-YPNFTVREFLDYIAWLKGIPSKEVKARVdeVLELVNLgdrakkkigSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57526399 576 YLDVlTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYG 627
Cdd:cd03264 160 GLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1228-1422 |
6.40e-13 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 70.94 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFlrllN-----TKGEIQIDGV---SWDSITLQQWRKAFGVipqkVF---- 1295
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHL----NgllkpTSGTVTIDGRditAKKKKKLKDLRKKVGL----VFqfpe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1296 --IFSGTFRK-------NLDpyeqWSDQEIWKVADE----VGL-RSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLArSV 1361
Cdd:TIGR04521 93 hqLFEETVYKdiafgpkNLG----LSEEEAEERVKEalelVGLdEEYLERSPFEL-----------SGGQMRRVAIA-GV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1362 LS-KAKILLLDEPSAHLDPITyqiiRRTLKQAFADC------TVILSEHRIEAMLE-CQRFLVIEENKV 1422
Cdd:TIGR04521 157 LAmEPEVLILDEPTAGLDPKG----RKEILDLFKRLhkekglTVILVTHSMEDVAEyADRVIVMHKGKI 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
436-585 |
7.95e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.68 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR----------ISFCSQ---YSWIMPGTIK 502
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQseeVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG-------VSYDEYRYRSVIKACQLEEDISKFSEKDnivLGEggitLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170
....*....|
gi 57526399 576 YLDVLTEKEI 585
Cdd:PRK15056 172 GVDVKTEARI 181
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
436-632 |
8.23e-13 |
|
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: 70.11 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGK----------------IKHsgRISFCSQ--YSWIM 497
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRK--RIGLVSPalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 498 PG-TIKDNII---FGVS--YDEYRYRSVIKACQ-LEE-DISKFSEKDnivLGeggiTLSGGQRARISLARAVYKDADLYL 569
Cdd:COG1119 93 RDeTVLDVVLsgfFDSIglYREPTDEQRERARElLELlGLAHLADRP---FG----TLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 570 LDSPFGYLDvLTEKEIFESCVCKLMAN--KTRILVT-SKMEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:COG1119 166 LDEPTAGLD-LGARELLLALLDKLAAEgaPTLVLVThHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
436-634 |
8.60e-13 |
|
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: 69.63 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR--------------ISFCSQYSWIMPG-T 500
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFGvsydeyRYRSVIKAcQLEEDIskfsekDNI-----VLGE-----GGiTLSGGQRARISLARAVYKDADLYLL 570
Cdd:COG0410 95 VEENLLLG------AYARRDRA-EVRADL------ERVyelfpRLKErrrqrAG-TLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 571 DSPfgyldvlTE-------KEIFEsCVCKLMANKTRILVTskmEH-----LKKADKILILHEGSVYFYGTFSELQN 634
Cdd:COG0410 161 DEP-------SLglaplivEEIFE-IIRRLNREGVTILLV---EQnarfaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
436-685 |
8.74e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.40 E-value: 8.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGrISFCSQYSwiMPGTIK-DNIIFGVSYDEY 514
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-IDTGDFSK--LQGIRKlVGIVFQNPETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 515 RYRSVikacqlEEDIS-----------KFSEKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:PRK13644 91 VGRTV------EEDLAfgpenlclppiEIRKRVDRALAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 575 GYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGtfsELQNQRPDFSSKLMGCDTfdqfta 654
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEG---EPENVLSDVSLQTLGLTP------ 235
|
250 260 270
....*....|....*....|....*....|...
gi 57526399 655 errNSII--TETLRRFSLEgdtsVSWNETKKPS 685
Cdd:PRK13644 236 ---PSLIelAENLKMHGVV----IPWENTSSPS 261
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
436-631 |
9.26e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.97 E-value: 9.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVL-KDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG--RISFCSQYSwimpgtiKDNIIFGVSYD 512
Cdd:PLN03073 520 GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkvRMAVFSQHH-------VDGLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 513 EYRYRSV--IKACQLEEDISKFSEKDNIVLgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVltekEIFESCV 590
Cdd:PLN03073 593 LYMMRCFpgVPEQKLRAHLGSFGVTGNLAL-QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL----DAVEALI 667
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 57526399 591 CKLMANKTRILVTSKMEHL--KKADKILILHEGSVY-FYGTFSE 631
Cdd:PLN03073 668 QGLVLFQGGVLMVSHDEHLisGSVDELWVVSEGKVTpFHGTFHD 711
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
440-664 |
9.37e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.99 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-----------------RISFCSQYSWIMPG-TI 501
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 502 KDNIIFG-----VSYDEYRYRSV--IKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:PRK10070 124 LDNTAFGmelagINAEERREKALdaLRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 575 GYLDVLTEKEIFESCVcKLMANKTRILVTSKM---EHLKKADKILILHEGSVYFYGTFSE-LQNQRPDFSSKLM-GCDTF 649
Cdd:PRK10070 193 SALDPLIRTEMQDELV-KLQAKHQRTIVFISHdldEAMRIGDRIAIMQNGEVVQVGTPDEiLNNPANDYVRTFFrGVDIS 271
|
250 260
....*....|....*....|
gi 57526399 650 DQFTAE---RR--NSIITET 664
Cdd:PRK10070 272 QVFSAKdiaRRtpNGLIRKT 291
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
416-634 |
9.95e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.02 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 416 NNNRKISNCDTSLFFSNLLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR--------- 486
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItiskenlke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 487 ------ISFCSQYSWIMPGTIKDNIIFGVS---YDEYRYRSVIKACQLEEDISKFSEKDNivlgeggITLSGGQRARISL 557
Cdd:PRK13632 81 irkkigIIFQNPDNQFIGATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDYLDKEP-------QNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 558 ARAVYKDADLYLLDSPFGYLDVLTEKEIFescvcKLM------ANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSE 631
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIK-----KIMvdlrktRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
|
...
gi 57526399 632 LQN 634
Cdd:PRK13632 229 ILN 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
436-623 |
1.45e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTP----VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-ISFCSQY---SWI-------MPGT 500
Cdd:COG1101 14 GTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYkraKYIgrvfqdpMMGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 -----IKDNII------------FGVSYDEY-RYRSVIKACQ--LEEDIskfseKDNIVLgeggitLSGGQRARISLARA 560
Cdd:COG1101 94 apsmtIEENLAlayrrgkrrglrRGLTKKRReLFRELLATLGlgLENRL-----DTKVGL------LSGGQRQALSLLMA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 561 VYKDADLYLLDSPFGYLD------V--LTEKEIFESCVCKLManktrilVTSKMEH-LKKADKILILHEGSV 623
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDpktaalVleLTEKIVEENNLTTLM-------VTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
443-638 |
1.54e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 68.63 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 443 ISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPsegkikHSGRISFCSQ-YSWIMPG-----------------TIKDN 504
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP------DSGRILWNGQdLTALPPAerpvsmlfqennlfphlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGVSYDeYRYRSVIKAcQLEEDISKfsekdnivLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:COG3840 92 IGLGLRPG-LKLTAEQRA-QVEQALER--------VGLAGLldrlpgQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 579 VLTEKEIFEsCVCKLMANK--TRILVTskmeH-----LKKADKILILHEGSVYFYGTFSELQNQRPD 638
Cdd:COG3840 162 PALRQEMLD-LVDELCRERglTVLMVT----HdpedaARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
425-627 |
1.66e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.06 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 425 DTSLFFSNLLLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELepsEGKIKHSGRISFCsqyswimpgtikdn 504
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYN-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 iifGVSYDEY--RYRSVIKACQlEEDIS----------KFSEK---DNIVLGeggitLSGGQRARISLARAVYKDADLYL 569
Cdd:cd03233 71 ---GIPYKEFaeKYPGEIIYVS-EEDVHfptltvretlDFALRckgNEFVRG-----ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 570 LDSPFGYLDVLTEKEIFeSCVcKLMANKTR------ILVTSKmEHLKKADKILILHEGSVYFYG 627
Cdd:cd03233 142 WDNSTRGLDSSTALEIL-KCI-RTMADVLKtttfvsLYQASD-EIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1221-1433 |
1.87e-12 |
|
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: 68.52 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1221 IDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVswDSITLQQWRKAFGVIPQKVFIFSG 1299
Cdd:cd03299 8 KDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAgFIKPDSGKILLNGK--DITNLPPEKRDISYVPQNYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 T---------FRKNLDPYEQwSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:cd03299 86 MtvykniaygLKKRKVDKKE-IERKVLEIAEMLGIDHLLNRKPETL-----------SGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1371 DEPSAHLDPITYQIIRRTLKQAF--ADCTVILSEHR-IEAMLECQRFLVIEENKVRQYDSIQRMLS 1433
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1441 |
2.36e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.11 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG--VSWDSITLQQWRKAF 1287
Cdd:PRK13636 6 LKVEELNYNYSDGTHA-LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQKV--FIFSGTFRKNLD--PYE-QWSDQEIWKVADEVGLRSVIEQFPGKLDFvlvdggcVLSHGHKQLMCLARSVL 1362
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTH-------CLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1363 SKAKILLLDEPSAHLDPITYQIIRRTLKQAFA--DCTVILSEHRIEAM-LECQRFLVIEENKVRQYDSIQRMLSEKSLFR 1439
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
..
gi 57526399 1440 QA 1441
Cdd:PRK13636 238 KV 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1213-1463 |
2.40e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.25 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGV-SWDSITLQQWRKAFGVI 1290
Cdd:PRK13644 4 LENVSYSYPDGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRpQKGKVLVSGIdTGDFSKLQGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 ---PQKVFIfSGTFRKNLDPYEQ---WSDQEIWKVAD----EVGLRSVIEQFPGkldfvlvdggcVLSHGHKQLMCLARS 1360
Cdd:PRK13644 83 fqnPETQFV-GRTVEEDLAFGPEnlcLPPIEIRKRVDralaEIGLEKYRHRSPK-----------TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1361 VLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADC-TVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFR 1439
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
250 260 270
....*....|....*....|....*....|....
gi 57526399 1440 QAISP------ADRLKL----LPHRNSSRQRSRA 1463
Cdd:PRK13644 231 LGLTPpslielAENLKMhgvvIPWENTSSPSSFA 264
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1213-1417 |
2.76e-12 |
|
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: 66.30 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGvswdsitlqqwrkafgvip 1291
Cdd:cd03216 3 LRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSgLYKPDSGEILVDG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 qkvfifsgtfrknlDPYEQWSDQEiwkvADEVGLRsVIEQfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 1371
Cdd:cd03216 62 --------------KEVSFASPRD----ARRAGIA-MVYQ---------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 1372 EPSAHLDP----ITYQIIRRtLKQafADCTVILSEHRIEAMLE-CQRFLVI 1417
Cdd:cd03216 108 EPTAALTPaeveRLFKVIRR-LRA--QGVAVIFISHRLDEVFEiADRVTVL 155
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1213-1379 |
3.09e-12 |
|
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: 67.55 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG--VSWDSITLQQWRKAFGV 1289
Cdd:cd03262 3 IKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpDSGTIIIDGlkLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFSG-TFRKN--LDPYE--QWSDQEIWKVA----DEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARS 1360
Cdd:cd03262 81 VFQQFNLFPHlTVLENitLAPIKvkGMSKAEAEERAlellEKVGLADKADAYPAQ-----------LSGGQQQRVAIARA 149
|
170
....*....|....*....
gi 57526399 1361 VLSKAKILLLDEPSAHLDP 1379
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDP 168
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
427-627 |
3.87e-12 |
|
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: 66.81 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 427 SLFFSNLLL---------GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSegkikhsgrisfcsqyswIM 497
Cdd:cd03213 3 TLSFRNLTVtvksspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL------------------GV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 498 PGTIKDNiifGVSYDEYRYRSvikacqleedISKFSEKDNIVLGEggIT-------------LSGGQRARISLARAVYKD 564
Cdd:cd03213 65 SGEVLIN---GRPLDKRSFRK----------IIGYVPQDDILHPT--LTvretlmfaaklrgLSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 565 ADLYLLDSPFGYLDVLTEKEIFEScvckLMA----NKTRILVT----SKMEHLkkADKILILHEGSVYFYG 627
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSL----LRRladtGRTIICSIhqpsSEIFEL--FDKLLLLSQGRVIYFG 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1212-1391 |
4.63e-12 |
|
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: 67.57 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSwdsITL----QQWRKA 1286
Cdd:cd03218 2 RAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVgLVKPDSGKILLDGQD---ITKlpmhKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 FGVIPQKVFIFSG-TFRKNL--------DPYEQWSDqEIWKVADEVGLRSVIEQFpgkldfvlvdgGCVLSHGHKQLMCL 1357
Cdd:cd03218 77 IGYLPQEASIFRKlTVEENIlavleirgLSKKEREE-KLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEI 144
|
170 180 190
....*....|....*....|....*....|....
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQ 1391
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
436-635 |
4.95e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.27 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTP----VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-----------------RISFCSQY- 493
Cdd:PRK13646 15 GTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 494 -SWIMPGTIKDNIIFG-----VSYDEYRYRsvikACQLEEDISkFSEKdniVLGEGGITLSGGQRARISLARAVYKDADL 567
Cdd:PRK13646 95 eSQLFEDTVEREIIFGpknfkMNLDEVKNY----AHRLLMDLG-FSRD---VMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 568 YLLDSPFGYLDVLTEKEIFESC-VCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQNQ 635
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLkSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
436-632 |
5.15e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 67.36 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR--------------ISFCSQYSWIMPG-T 500
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNI-----IFGVSYDEYRYRsvikacqLEE-----DISKFseKDNIvlgegGITLSGGQRARISLARAVYKDADLYLL 570
Cdd:COG1137 95 VEDNIlavleLRKLSKKEREER-------LEElleefGITHL--RKSK-----AYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 571 DSPFGYLDVLTEKEIfESCVCKLmanKTR---ILVTskmEH-----LKKADKILILHEGSVYFYGTFSEL 632
Cdd:COG1137 161 DEPFAGVDPIAVADI-QKIIRHL---KERgigVLIT---DHnvretLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1225-1448 |
6.11e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1225 NAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLrllntkGEIQIDGVSWDSItlqqwRKAFGVIPQKVFIFSGTFRKN 1304
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML------GELSHAETSSVVI-----RGSVAYVPQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1305 LDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQ 1383
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQ 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 1384 IIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQAISPADRL 1448
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKM 843
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1211-1448 |
6.81e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGvswDSITL----QQWRK 1285
Cdd:PRK10895 4 LTAKNLAKAY--KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVgIVPRDAGNIIIDD---EDISLlplhARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1286 AFGVIPQKVFIFSG-----------TFRKNLDPyEQWSDQeiwkvADEVGLRSVIEQFPGKLdfvlvdgGCVLSHGHKQL 1354
Cdd:PRK10895 79 GIGYLPQEASIFRRlsvydnlmavlQIRDDLSA-EQREDR-----ANELMEEFHIEHLRDSM-------GQSLSGGERRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1355 MCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAF-ADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQRML 1432
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEIL 225
|
250
....*....|....*.
gi 57526399 1433 SEKSLFRQAISPADRL 1448
Cdd:PRK10895 226 QDEHVKRVYLGEDFRL 241
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
440-628 |
7.12e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.47 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI----------------KHSGrISFCSQYSWIMPGTIKD 503
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklrKHIG-IVFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFG-----VSYDEYrYRSVIKACqleEDISKFSEKDNivlgeGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:PRK13648 104 DVAFGlenhaVPYDEM-HRRVSEAL---KQVDMLERADY-----EPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 579 VLTEKEIFeSCVCKLMANK--TRILVTSKMEHLKKADKILILHEGSVYFYGT 628
Cdd:PRK13648 175 PDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1212-1421 |
7.28e-12 |
|
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: 64.39 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKST-LLLAFLRLLNTKGEIQIDgvswDSITlqqwrkaFGVI 1290
Cdd:cd03221 2 ELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTlLKLIAGELEPDEGIVTWG----STVK-------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQkvfifsgtfrknldpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:cd03221 69 EQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1371 DEPSAHLDPITYQIIRRTLKQaFaDCTVILSEH-RieAMLE--CQRFLVIEENK 1421
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKE-Y-PGTVILVSHdR--YFLDqvATKIIELEDGK 144
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
440-635 |
9.24e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.73 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEG--------------KIKHSGR----ISFCSQYS--WIMPG 499
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyaipanlkKIKEVKRlrkeIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 TIKDNIIFGVSY----DEYRYRSV---IKACQLEEDISKFSEkdnivlgeggITLSGGQRARISLARAVYKDADLYLLDS 572
Cdd:PRK13645 107 TIEKDIAFGPVNlgenKQEAYKKVpelLKLVQLPEDYVKRSP----------FELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 573 PFGYLDVLTEKEiFESCVCKLMANKTR--ILVTSKMEH-LKKADKILILHEGSVYFYGT-FSELQNQ 635
Cdd:PRK13645 177 PTGGLDPKGEED-FINLFERLNKEYKKriIMVTHNMDQvLRIADEVIVMHEGKVISIGSpFEIFSNQ 242
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
442-579 |
9.42e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 9.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 442 DISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK------HSGRISFCSQYSWI--MPGtIKD------NIIF 507
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQDLLYLghQPG-IKTeltaleNLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 508 gvsydeyryrsvikACQLEEDISKFSEKDniVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:PRK13538 98 --------------YQRLHGPGDDEALWE--ALAQVGLagfedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
.
gi 57526399 579 V 579
Cdd:PRK13538 162 K 162
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
397-607 |
1.07e-11 |
|
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: 69.06 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 397 VTAFWEEGFSKLFEKA--KENNNNRKISNCDT--SLF---------FSNLLLGTPVLK--------------------DI 443
Cdd:TIGR03269 224 LTSHWPEVIEDLSDKAiwLENGEIKEEGTPDEvvAVFmegvsevekECEVEVGEPIIKvrnvskryisvdrgvvkavdNV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 444 SFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI----------------KHSGR----ISFCSQ-YSWIMPGTIK 502
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpDGRGRakryIGILHQeYDLYPHRTVL 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFGVSY---DEY-RYRSVI--KACQLEEdiskfsEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:TIGR03269 384 DNLTEAIGLelpDELaRMKAVItlKMVGFDE------EKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
250 260 270
....*....|....*....|....*....|..
gi 57526399 577 LDVLTEKEIFESCV-CKLMANKTRILVTSKME 607
Cdd:TIGR03269 458 MDPITKVDVTHSILkAREEMEQTFIIVSHDMD 489
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1206-1400 |
1.37e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 66.65 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1206 PSGGQMTVKDLTAKYI--DGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaflrLLN--------TKGEIQIDGVSW 1275
Cdd:COG1116 3 AAAPALELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKST-------LLRliaglekpTSGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1276 DSIT------LQQ-----WRK-----AFGVIPQKVfifsgtfrknldpyeqwSDQEIWKVADE----VGLRSVIEQFPGk 1335
Cdd:COG1116 76 TGPGpdrgvvFQEpallpWLTvldnvALGLELRGV-----------------PKAERRERAREllelVGLAGFEDAYPH- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1336 ldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT----YQIIRRTLKQafADCTVIL 1400
Cdd:COG1116 138 ----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerlQDELLRLWQE--TGKTVLF 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1214-1422 |
1.38e-11 |
|
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: 66.26 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1214 KDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaflrLLN--------TKG-EIQIDGVSWDSITLQQWR 1284
Cdd:COG1119 7 RNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKST-------LLSlitgdlppTYGnDVRLFGERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1285 KAFGVI----------PQKVF--IFSGtFRKNLDPYEQWSDQEI---WKVADEVGLRSVIEQFPGKldfvlvdggcvLSH 1349
Cdd:COG1119 78 KRIGLVspalqlrfprDETVLdvVLSG-FFDSIGLYREPTDEQReraRELLELLGLAHLADRPFGT-----------LSQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1350 GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRIEAMLEC-QRFLVIEENKV 1422
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRV 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
439-621 |
1.40e-11 |
|
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: 65.63 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG---------------RISFCSQYSWIMPG-TIK 502
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIF------GVSYDEY--RYRSVIKACQLEEDISKFSekdnivlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:cd03262 95 ENITLapikvkGMSKAEAeeRALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 575 GYLDVLTEKEIFEscVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEG 621
Cdd:cd03262 164 SALDPELVGEVLD--VMKDLAeeGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1211-1437 |
1.56e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.06 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG---VSWDsiTLQQWRKA 1286
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRaTSGRIVFDGkdiTDWQ--TAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 FGVIPQKVFIFSG-TFRKNLDPYEQWSDQEIWKVAdevgLRSVIEQFPGKLDFVLVDGGcVLSHGHKQLMCLARSVLSKA 1365
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQER----IKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1366 KILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQRMLSEKSL 1437
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1228-1435 |
1.57e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.78 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLL-AFLRLLNTKGEIQIDGvswDSITLQQWRKAFGVIPQKV---FIFSGT--F 1301
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQhFNALLKPSSGTITIAG---YHITPETGNKNLKKLRKKVslvFQFPEAqlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1302 R-----------KNLDPYEQWSDQEIWKVADEVGLR-SVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1369
Cdd:PRK13641 100 EntvlkdvefgpKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFE-----------LSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1370 LDEPSAHLDPITyqiiRRTLKQAFADC-----TVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQRMLSEK 1435
Cdd:PRK13641 169 LDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
438-632 |
1.76e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIM------------------GEL------------------------- 474
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtNDMtneqdyqgdeeqnvgmknvnefslt 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 475 -EPSEGK----IKHSGRI-------------------SFCSQYSWIMPGTIKDNIIFGvsYDEYRYRSVIKACQ---LEE 527
Cdd:PTZ00265 1262 kEGGSGEdstvFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKfaaIDE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 528 DISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCV-CKLMANKTRILVTSKM 606
Cdd:PTZ00265 1340 FIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdIKDKADKTIITIAHRI 1419
|
250 260 270
....*....|....*....|....*....|.
gi 57526399 607 EHLKKADKILILHE----GS-VYFYGTFSEL 632
Cdd:PTZ00265 1420 ASIKRSDKIVVFNNpdrtGSfVQAHGTHEEL 1450
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
438-641 |
2.96e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.61 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIKDN 504
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 I-IFGVSYDEYRYRSVIKAcQLEEDISKFSEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE- 582
Cdd:PLN03130 1333 LdPFNEHNDADLWESLERA-HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDa 1411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 583 ------KEIFESCVCKLMANKTRILVTSkmehlkkaDKILILHEGSVYFYGTFSEL-QNQRPDFSS 641
Cdd:PLN03130 1412 liqktiREEFKSCTMLIIAHRLNTIIDC--------DRILVLDAGRVVEFDTPENLlSNEGSAFSK 1469
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
436-621 |
4.73e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.51 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-IS------------FCSqYSWIMPGTIK 502
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdIThvpaenrhvntvFQS-YALFPHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG-----VSYDEYRYR--SVIKACQLEEdiskfsekdnivLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:PRK09452 105 ENVAFGlrmqkTPAAEITPRvmEALRMVQLEE------------FAQRKPHqLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 575 GYLDVLTEKEifescvcklMANK----------TRILVTSKMEH-LKKADKILILHEG 621
Cdd:PRK09452 173 SALDYKLRKQ---------MQNElkalqrklgiTFVFVTHDQEEaLTMSDRIVVMRDG 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
436-579 |
4.78e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.79 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-ISFCS--QYSWIMPGTIKDNiifGVSYD 512
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdVEALSarAASRRVASVPQDT---SLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 513 eYRYRSVIKACQLEEdISKFSEKDNI-------VLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:PRK09536 92 -FDVRQVVEMGRTPH-RSRFDTWTETdraaverAMERTGVaqfadrpvtSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
...
gi 57526399 577 LDV 579
Cdd:PRK09536 170 LDI 172
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1228-1427 |
4.88e-11 |
|
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: 64.28 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDG-VSWDSitLQQWRKAFGVI-PQKvfifsGTFRKN 1304
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSgLLQPTSGEVRVAGlVPWKR--RKKFLRRIGVVfGQK-----TQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1305 LDPYEQWS-DQEIWKVaDEVGLRSVIEQFPGKLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 1381
Cdd:cd03267 110 LPVIDSFYlLAAIYDL-PPARFKKRLDELSELLDLEELLDTPVrqLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 1382 YQIIRRTLKQAFAD--CTVILSEHR---IEAMleCQRFLVIEENKVrQYDS 1427
Cdd:cd03267 189 QENIRNFLKEYNRErgTTVLLTSHYmkdIEAL--ARRVLVIDKGRL-LYDG 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1211-1459 |
6.05e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.71 E-value: 6.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGG-------NAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQ 1282
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1283 WRkAFGVIPQKVF---------------IFSGTFRK--NLDPYEQwsDQEIWKVADEVGLR-SVIEQFPGKldfvlvdgg 1344
Cdd:PRK10419 84 RK-AFRRDIQMVFqdsisavnprktvreIIREPLRHllSLDKAER--LARASEMLRAVDLDdSVLDKRPPQ--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1345 cvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQIIR--RTLKQAFADCTVILSeHRIEaMLE--CQRFLVIEE 1419
Cdd:PRK10419 152 --LSGGQLQRVCLARALAVEPKLLILDEAVSNLDlVLQAGVIRllKKLQQQFGTACLFIT-HDLR-LVErfCQRVMVMDN 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 57526399 1420 NKVRQYDSIQRMLSEKS----LFRQAISPAdrlklLPHRNSSRQ 1459
Cdd:PRK10419 228 GQIVETQPVGDKLTFSSpagrVLQNAVLPA-----FPVRRRTTE 266
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
435-646 |
6.89e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 435 LGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-ISFCSQYSWIMPGTI-------KDNII 506
Cdd:PRK10762 263 LSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHeVVTRSPQDGLANGIVyisedrkRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 507 FGVSYDE------YRYRS----VIKACQLEEDISKFSEKDNI-------VLGEggitLSGGQRARISLARAVYKDADLYL 569
Cdd:PRK10762 343 LGMSVKEnmsltaLRYFSraggSLKHADEQQAVSDFIRLFNIktpsmeqAIGL----LSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 570 LDSPFGYLDVLTEKEIFEscvcklMANKTR------ILVTSKM-EHLKKADKILILHEGSVyfYGTFSELQ-NQRpdfss 641
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQ------LINQFKaeglsiILVSSEMpEVLGMSDRILVMHEGRI--SGEFTREQaTQE----- 485
|
....*
gi 57526399 642 KLMGC 646
Cdd:PRK10762 486 KLMAA 490
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
436-579 |
7.69e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.35 E-value: 7.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYSWIM-----------PGTIKDN 504
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylghrnamkpALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGVSY---DEYRYRSVIKACQLeediskfsekdnivlgeGGIT------LSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:PRK13539 94 LEFWAAFlggEELDIAAALEAVGL-----------------APLAhlpfgyLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
....
gi 57526399 576 YLDV 579
Cdd:PRK13539 157 ALDA 160
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
436-559 |
7.92e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.58 E-value: 7.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISFCSQYSWIMPGTIK 502
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 503 DNIIFgvSYDEYRYRSVIKAcqLEEDISKFSEKDNIVlgEGGIT-LSGGQRARISLAR 559
Cdd:PRK10247 99 DNLIF--PWQIRNQQPDPAI--FLDDLERFALPDTIL--TKNIAeLSGGEKQRISLIR 150
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1212-1427 |
8.16e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.55 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaflrllnT-----------KGEIQIDGVSWDSITL 1280
Cdd:COG1118 4 EVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTT----------LlriiagletpdSGRIVLNGRDLFTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1281 QQWRK--------------------AFG--VIPqkvfifsgtfrknldpyeqWSDQEIWKVADE----VGLRSVIEQFPG 1334
Cdd:COG1118 72 PRERRvgfvfqhyalfphmtvaeniAFGlrVRP-------------------PSKAEIRARVEEllelVQLEGLADRYPS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1335 KldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEH-RIEAMLEC 1411
Cdd:COG1118 133 Q-----------LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHdQEEALELA 201
|
250
....*....|....*.
gi 57526399 1412 QRFLVIEENKVRQYDS 1427
Cdd:COG1118 202 DRVVVMNQGRIEQVGT 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
442-627 |
8.19e-11 |
|
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: 63.28 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 442 DISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------ISFCSQYSWIMPG-TIKDNIIFGV 509
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 510 SyDEYRYRsvikacqlEEDiskfSEKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVL 580
Cdd:cd03298 96 S-PGLKLT--------AED----RQAIEVALARVGLaglekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 581 TEKEIFEsCVCKLMANK--TRILVTSKMEHLKK-ADKILILHEGSVYFYG 627
Cdd:cd03298 163 LRAEMLD-LVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
97-361 |
1.01e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) 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: 350040 [Multi-domain] Cd Length: 309 Bit Score: 64.82 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 97 VQPLLLGRIIASYDPDNKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKL--------- 167
Cdd:cd18596 15 APPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssks 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 168 ----------SSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLlmgllwdllqAFTF----------CGL 227
Cdd:cd18596 95 seskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVI----------AIVFlyrllgwsalVGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 228 AFLVVLALLQAGLGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLNS 307
Cdd:cd18596 165 AVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLLS 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 308 SAFFFSGFFVVFLSVLPYALLKGIILR--KIFTTISFCIVLRMAVTR---QFPWAVQTW 361
Cdd:cd18596 245 LLWFLIPILVTVVTFATYTLVMGQELTasVAFTSLALFNMLRGPLNVlpeLITQLLQAK 303
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
440-635 |
1.06e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.72 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI------------KHSGRISFC----SQYSWIMPgtIKD 503
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvpfkrrkEFARRIGVVfgqrSQLWWDLP--AID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NI-----IFGVSYDEYRYRsvikacqLEEdiskFSEkdniVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDS 572
Cdd:COG4586 116 SFrllkaIYRIPDAEYKKR-------LDE----LVE----LLDLGELldtpvrQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 573 P-FGyLDVLTEKEI--FESCVCKlmANKTRILVTSK-MEHLKK-ADKILILHEGSVYFYGTFSELQNQ 635
Cdd:COG4586 181 PtIG-LDVVSKEAIreFLKEYNR--ERGTTILLTSHdMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1188-1421 |
1.20e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.44 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1188 PSKVMIIENQHVKKddiwpSGGQMTVKDltakyidggnaileNISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKG 1266
Cdd:PRK13537 2 PMSVAPIDFRNVEK-----RYGDKLVVD--------------GLSFHVQRGECFGLLGPNGAGKTTTLRMLLgLTHPDAG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1267 EIQIDGVSWDSiTLQQWRKAFGVIPQkvfiFSgtfrkNLDPyeQWSDQEIWKV-ADEVGLRS--VIEQFPGKLDFVLVDG 1343
Cdd:PRK13537 63 SISLCGEPVPS-RARHARQRVGVVPQ----FD-----NLDP--DFTVRENLLVfGRYFGLSAaaARALVPPLLEFAKLEN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1344 GC-----VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADC-TVILSEHRI-EAMLECQRFLV 1416
Cdd:PRK13537 131 KAdakvgELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHFMeEAERLCDRLCV 210
|
....*
gi 57526399 1417 IEENK 1421
Cdd:PRK13537 211 IEEGR 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
437-632 |
1.32e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.88 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR---------------ISFCSQYSWIMPGTI 501
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwdvrrqvgMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 502 KDNIIF-----GVSYDEY--RYRSVIKACQLEEdiskFSEKDNivlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 574
Cdd:PRK13635 100 QDDVAFgleniGVPREEMveRVDQALRQVGMED----FLNREP-------HRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 575 GYLDVLTEKEIFEscVCKLMANKTRILV---TSKMEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:PRK13635 169 SMLDPRGRREVLE--TVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1213-1378 |
1.42e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLllaflrllnTK---GEIQIDGvswDSITLQQ-WRkaFG 1288
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTL---------LKilaGELEPDS---GEVSIPKgLR--IG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VIPQKVFIFSGT------------FRKNLDPYEQ------WSDQEIWKVA------DEVG---LRSVIEQFPGKLDFVLV 1341
Cdd:COG0488 65 YLPQEPPLDDDLtvldtvldgdaeLRALEAELEEleaklaEPDEDLERLAelqeefEALGgweAEARAEEILSGLGFPEE 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 57526399 1342 DGGC---VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1378
Cdd:COG0488 145 DLDRpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1211-1406 |
1.58e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.26 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKGEIQIDG-VSWDSITLQ-------Q 1282
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGsIVYNGHNIYsprtdtvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1283 WRKAFGVIPQKVFIFSGTFRKNLdPY----EQWSDQEIWKVADEVGLR--SVIEQFPGKLDfvlvDGGCVLSHGHKQLMC 1356
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENV-VYglrlKGIKDKQVLDEAVEKSLKgaSIWDEVKDRLH----DSALGLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 1357 LARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIE 1406
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
426-650 |
1.70e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.11 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 426 TSLFFSNLLLG---TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------------RISF 489
Cdd:PRK11231 1 MTLRTENLTVGygtKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 490 CSQYSWIMPG-TIKDNIIFGVS-----------YDEYRYRSVIKACQLEEdiskfsekdnivLGEGGIT-LSGGQRARIS 556
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGRSpwlslwgrlsaEDNARVNQAMEQTRINH------------LADRRLTdLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 557 LARAVYKDADLYLLDSPFGYLDVLTEKEIFescvcKLM-----ANKTRILVtskMEHLKKA----DKILILHEGSVYFYG 627
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELM-----RLMrelntQGKTVVTV---LHDLNQAsrycDHLVVLANGHVMAQG 220
|
250 260
....*....|....*....|...
gi 57526399 628 TFSELqnqrpdFSSKLMgCDTFD 650
Cdd:PRK11231 221 TPEEV------MTPGLL-RTVFD 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
437-633 |
1.72e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.57 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGK----------------IKHSGRISFCSQYSWIMPGT 500
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKvyvdgldtsdeenlwdIRNKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFG-----VSYDEYRYR--SVIKACQLEEdISKFSEKdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:PRK13633 103 VEEDVAFGpenlgIPPEEIRERvdESLKKVGMYE-YRRHAPH----------LLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 574 FGYLDVLTEKEIFeSCVCKLmaNK----TRILVTSKMEHLKKADKILILHEGSVYFYGT----FSELQ 633
Cdd:PRK13633 172 TAMLDPSGRREVV-NTIKEL--NKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTpkeiFKEVE 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1213-1441 |
1.75e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.60 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLL-AFLRLLNTKGEIQIDGVSWDSITLQQWRKAFGVIP 1291
Cdd:PRK13647 7 VEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLhLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 QKV--FIFSGTFRKNL--DPYEQWSDQEIWKVADEVGLRSV-IEQFPGKLDFvlvdggcVLSHGHKQLMCLARSVLSKAK 1366
Cdd:PRK13647 86 QDPddQVFSSTVWDDVafGPVNMGLDKDEVERRVEEALKAVrMWDFRDKPPY-------HLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1367 ILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSiQRMLSEKSLFRQA 1441
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDEDIVEQA 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1213-1422 |
1.91e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.50 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKAFGVI- 1290
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNgLLLPEAGTITVGGMVLSEETVWDVRRQVGMVf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 --PQKVFIfsGT---------FRKNLDPYEQWSDQEIWKVaDEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1359
Cdd:PRK13635 88 qnPDNQFV--GAtvqddvafgLENIGVPREEMVERVDQAL-RQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1360 SVLSKAKILLLDEPSAHLDPITYQ----IIRRTLKQafADCTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRRevleTVRQLKEQ--KGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
99-356 |
1.91e-10 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 63.77 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 99 PLLLGRIIASYDPDNKVERSIAIYLgIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIG 178
Cdd:cd18559 17 PSNLWLLLWFDDPVNGPQEHGQVYL-SVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 179 QLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQAFTFCGLAFLVVLALLQA-------GLGKMMMKYRDQR 251
Cdd:cd18559 96 ELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRvyaassrQLKRLESVSKDPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 252 AGKINERLVitsemieNIQSVKAYCWEEAMEKIIENLRQTELKLTRKAAYVRYLNSSAFFFSGFFVVFLSVLPYAL---L 328
Cdd:cd18559 176 YKLFNETLL-------GISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSrhsL 248
|
250 260
....*....|....*....|....*...
gi 57526399 329 KGIILRKIFTTISFCIVLRMAVtRQFPW 356
Cdd:cd18559 249 AGLVALKVFYSLALTTYLNWPL-NMSPE 275
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-611 |
2.03e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMI--MGELEpseGKIKHSGRISFCSQYSW--------------------- 495
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELE---SEVRVEGRVEFFNQNIYerrvnlnrlrrqvsmvhpkpn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 496 IMPGTIKDNIIFGVSYDEYRYR--------SVIKACQLEEDISKfsekdniVLGEGGITLSGGQRARISLARAVYKDADL 567
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVGWRPKleiddiveSALKDADLWDEIKH-------KIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 57526399 568 YLLDSPFGYLDVLTEKEIfESCV--CKLMANKTRILVTSKMEHLKK 611
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKV-ESLIqsLRLRSELTMVIVSHNLHQVSR 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
436-632 |
2.22e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.17 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------------ISFCSQYSWIMP 498
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevrktvgIVFQNPDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 GTIKDNIIFG-----VSYDEY--RYRSVIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLD 571
Cdd:PRK13639 94 PTVEEDVAFGplnlgLSKEEVekRVKEALKAVGMEGFENKPPHH-----------LSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 572 SPFGYLDVLTEKEIFescvcKLMA--NK---TRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSEL 632
Cdd:PRK13639 163 EPTSGLDPMGASQIM-----KLLYdlNKegiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
411-587 |
2.22e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 411 KAKENNNNRKISNCDTSLFFSNLLL----GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGeLEPS-EGKIKH-- 483
Cdd:COG4178 346 DALPEAASRIETSEDGALALEDLTLrtpdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARpa 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 484 SGRISFCSQYSWIMPGTIKDNIIF---GVSYDEYRYRSVIKACQLEEDISKFSEKDNIvlgegGITLSGGQRARISLARA 560
Cdd:COG4178 425 GARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGEQQRLAFARL 499
|
170 180
....*....|....*....|....*..
gi 57526399 561 VYKDADLYLLDSPFGYLDVLTEKEIFE 587
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQ 526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
436-634 |
2.26e-10 |
|
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: 65.81 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR------------ISFCSQYSWIMPG-TIK 502
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFgvsYDEYRYRSVIKAcQLE-----EDiSKFSEKDNivlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 577
Cdd:TIGR01257 1022 EHILF---YAQLKGRSWEEA-QLEmeamlED-TGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 578 DVLTEKEIFEsCVCKLMANKTRILVTSKMEHLK-KADKILILHEGSVYFYGTFSELQN 634
Cdd:TIGR01257 1093 DPYSRRSIWD-LLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1227-1403 |
2.26e-10 |
|
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: 62.29 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1227 ILENISFSISPGQRVGLLGRTGSGKSTL----LLAFLRLLNTKGEIQIDGVswdSITLQQWRKAFGVIPQkvfifSGTFR 1302
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLldaiSGRVEGGGTTSGQILFNGQ---PRKPDQFQKCVAYVRQ-----DDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1303 KNLDPYEQW------------SDQEIWKVADEVGLRSV-IEQFPGKldfvLVDGgcvLSHGHKQLMCLARSVLSKAKILL 1369
Cdd:cd03234 94 PGLTVRETLtytailrlprksSDAIRKKRVEDVLLRDLaLTRIGGN----LVKG---ISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 57526399 1370 LDEPSAHLDPIT-YQIIrRTLKQ-AFADCTVILSEH 1403
Cdd:cd03234 167 LDEPTSGLDSFTaLNLV-STLSQlARRNRIVILTIH 201
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1232-1433 |
2.45e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.29 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1232 SFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVswDSITLQQWRKAFGVIPQKVFIFSG-TFRKN----- 1304
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAgFLTPASGSLTLNGQ--DHTTTPPSRRPVSMLFQENNLFSHlTVAQNiglgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1305 -----LDPYEQWSDQEIwkvADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 1379
Cdd:PRK10771 97 npglkLNAAQREKLHAI---ARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1380 ITYQIIRRTLKQAFAD--CTVILSEHRIE-AMLECQRFLVIEENKVrQYD-SIQRMLS 1433
Cdd:PRK10771 163 ALRQEMLTLVSQVCQErqLTLLMVSHSLEdAARIAPRSLVVADGRI-AWDgPTDELLS 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
444-645 |
2.90e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.91 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 444 SFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-----------ISFCSQYSWIMPG-TIKDNIIFGV-- 509
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHlTVAQNIGLGLnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 510 -----SYDEYRYRSVIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKE 584
Cdd:PRK10771 99 glklnAAQREKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 585 IFE--SCVCKlMANKTRILVTSKMEH-LKKADKILILHEGSVYFYGTFSELQNQRPDfSSKLMG 645
Cdd:PRK10771 168 MLTlvSQVCQ-ERQLTLLMVSHSLEDaARIAPRSLVVADGRIAWDGPTDELLSGKAS-ASALLG 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1211-1423 |
2.98e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGV 1289
Cdd:PRK09536 4 IDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKV---FIFSG--TFRKNLDPYEQWSDQeiWKVADEVGLRSVIEQfPGKLDFV--LVDGgcvLSHGHKQLMCLARSVL 1362
Cdd:PRK09536 82 VPQDTslsFEFDVrqVVEMGRTPHRSRFDT--WTETDRAAVERAMER-TGVAQFAdrPVTS---LSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1363 SKAKILLLDEPSAHLDpITYQIirRTLK--QAFADC--TVILSEHRIE-AMLECQRFLVIEENKVR 1423
Cdd:PRK09536 156 QATPVLLLDEPTASLD-INHQV--RTLElvRRLVDDgkTAVAAIHDLDlAARYCDELVLLADGRVR 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1213-1427 |
2.99e-10 |
|
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: 62.36 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQwrKAFGVIP 1291
Cdd:cd03296 5 VRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERpDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 QKVFIFSG-TFRKNL-------DPYEQWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1359
Cdd:cd03296 81 QHYALFRHmTVFDNVafglrvkPRSERPPEAEIRAKVHEllklVQLDWLADRYPAQ-----------LSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 1360 SVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD---CTVILSEHRIEAMLECQRFLVIEENKVRQYDS 1427
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1206-1422 |
3.21e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1206 PSGGQMTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKG-----------EIQIDG-V 1273
Cdd:PRK11247 8 NQGTPLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAgellagtaplaEAREDTrL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1274 SWDSITLQQWRKafgVIPQKVFIFSGtfrknldpyeQWSDQEIwKVADEVGLRSVIEQFPGkldfvlvdggcVLSHGHKQ 1353
Cdd:PRK11247 86 MFQDARLLPWKK---VIDNVGLGLKG----------QWRDAAL-QALAAVGLADRANEWPA-----------ALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 1354 LMCLARSVLSKAKILLLDEPSAHLDPIT----YQIIRRT-LKQAFadcTVILSEHRI-EAMLECQRFLVIEENKV 1422
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTriemQDLIESLwQQHGF---TVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1212-1422 |
3.36e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.56 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYIDGGNAI--LENISFSISPGQRVGLLGRTGSGKSTlllaf-lrllnTKGEIQIDGVswdSIT------LQQ 1282
Cdd:COG1135 3 ELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTlircinllerpTSGSVLVDGV---DLTalsereLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1283 WRKAFGVIPQKvfiF----SGTFRKNLD-PYEQ--WSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGH 1351
Cdd:COG1135 80 ARRKIGMIFQH---FnllsSRTVAENVAlPLEIagVPKAEIRKRVAEllelVGLSDKADAYPSQ-----------LSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1352 KQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQI------IRRTLKqafadCTVILSEH------RIeamleCQRFLVIE 1418
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPeTTRSIldllkdINRELG-----LTIVLITHemdvvrRI-----CDRVAVLE 215
|
....
gi 57526399 1419 ENKV 1422
Cdd:COG1135 216 NGRI 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1223-1378 |
3.78e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKGEIQIDGVSwdsitLQQW-RKAfgVIP-----QKVF- 1295
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQP-----LHNLnRRQ--LLPvrhriQVVFq 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1296 ---------------IFSG--TFRKNLDPYEQwsDQEIWKVADEVGLRSVIEQ-FPGKldfvlvdggcvLSHGHKQLMCL 1357
Cdd:PRK15134 370 dpnsslnprlnvlqiIEEGlrVHQPTLSAAQR--EQQVIAVMEEVGLDPETRHrYPAE-----------FSGGQRQRIAI 436
|
170 180
....*....|....*....|.
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLD 1378
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLD 457
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1211-1422 |
4.46e-10 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 61.52 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGvswDSITLQ----QWRK 1285
Cdd:TIGR04406 2 LVAENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVgLVRPDAGKILIDG---QDITHLpmheRARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1286 AFGVIPQKVFIFSG-----------TFRKNLDPYEQwsDQEIWKVADEVGLRSVIEQfpgkldfvlvdGGCVLSHGHKQL 1354
Cdd:TIGR04406 77 GIGYLPQEASIFRKltveenimavlEIRKDLDRAER--EERLEALLEEFQISHLRDN-----------KAMSLSGGERRR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1355 MCLARSVLSKAKILLLDEPSAHLDPITYQIIR---RTLKQafADCTVILSEHRIEAMLE-CQRFLVIEENKV 1422
Cdd:TIGR04406 144 VEIARALATNPKFILLDEPFAGVDPIAVGDIKkiiKHLKE--RGIGVLITDHNVRETLDiCDRAYIISDGKV 213
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
440-639 |
4.50e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-RISFCSQYSWIMPGTIKDNIIFGVSYDEYRYRS 518
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 519 VIKACQL--------EEDISKFSEKDNIVLG-------EGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEK 583
Cdd:PRK13643 102 VLKDVAFgpqnfgipKEKAEKIAAEKLEMVGladefweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 584 EIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELqNQRPDF 639
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV-FQEVDF 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
439-579 |
5.28e-10 |
|
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: 60.58 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK------HSGRISFCSQYSWI--MPG-----TIKDNI 505
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggplDFQRDSIARGLLYLghAPGikttlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 506 IFgvsydeyrYRSVIKACQLEEDISKfsekdnivLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:cd03231 95 RF--------WHADHSDEQVEEALAR--------VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1211-1404 |
5.50e-10 |
|
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: 59.86 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAkYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRL-LNTKGEIQIdgvswdsitLQQWRKAFgv 1289
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSGRIGM---------PEGEDLLF-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFSGTFRknldpyEQ----WSDqeiwkvadevglrsvieqfpgkldfvlvdggcVLSHGHKQLMCLARSVLSKA 1365
Cdd:cd03223 69 LPQRPYLPLGTLR------EQliypWDD--------------------------------VLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 57526399 1366 KILLLDEPSAHLDPITYQIIRRTLKQAFAdcTVILSEHR 1404
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
434-624 |
5.53e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.04 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 434 LLGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG----------------RISFCSQ-YSWI 496
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflrrQIGMIFQdHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 497 MPGTIKDN-----IIFGVSYDEYRYR--SVIKACQLEEDISKFSekdnivlgeggITLSGGQRARISLARAVYKDADLYL 569
Cdd:PRK10908 92 MDRTVYDNvaiplIIAGASGDDIRRRvsAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 570 LDSPFGYLD-VLTEK--EIFESC----VCKLMANKTRILVTskmehlKKADKILILHEGSVY 624
Cdd:PRK10908 161 ADEPTGNLDdALSEGilRLFEEFnrvgVTVLMATHDIGLIS------RRSYRMLTLSDGHLH 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
430-618 |
7.98e-10 |
|
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: 59.09 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 430 FSNLLLGTP----VLKDISFKIERGQLLAVAGSTGAGKTSLLmMIMGELEPS-EGKIKH--SGRISFCSQYSWIMPGTIK 502
Cdd:cd03223 3 LENLSLATPdgrvLLKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLWPWgSGRIGMpeGEDLLFLPQRPYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIfgvsydeYRYRSVikacqleediskfsekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 582
Cdd:cd03223 82 EQLI-------YPWDDV---------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*..
gi 57526399 583 KEIFESCVCKLMAnktrILVTSKMEHLKK-ADKILIL 618
Cdd:cd03223 128 DRLYQLLKELGIT----VISVGHRPSLWKfHDRVLDL 160
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
439-579 |
8.30e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG--RISFCSQ--------------YSWIMPGTIK 502
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQklyldttlpltvnrFLRLRPGTKK 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 503 DNIIfgvsydeyryrSVIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:PRK09544 99 EDIL-----------PALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
439-628 |
8.47e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.18 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEG-------------------------KIKHSGR----ISF 489
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnhelitnpyskKIKNFKElrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 490 CSQYS--WIMPGTIKDNIIFG-VSYDEYRYRSVIKAcqleediSKFSEK---DNIVLGEGGITLSGGQRARISLARAVYK 563
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGpVALGVKKSEAKKLA-------KFYLNKmglDDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 564 DADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSVYFYGT 628
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGT 259
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
914-1114 |
9.47e-10 |
|
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: 61.41 E-value: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 914 YIFYIYVGVADTLLALGLFRGLPLVHTLITVSKTLHH---KMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLT 990
Cdd:cd07346 37 LLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDlrrDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 991 IFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGR 1070
Cdd:cd07346 117 LLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 57526399 1071 QPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAV 1114
Cdd:cd07346 197 EEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
447-636 |
9.68e-10 |
|
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: 59.51 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 447 IERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-RISFCSQYswimpgtikdniifgvsydeyryrsvikacql 525
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 526 eediskfsekdnivlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVltEKEIFESCVCKLM---ANKTRILV 602
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI--EQRLNAARAIRRLseeGKKTALVV 128
|
170 180 190
....*....|....*....|....*....|....
gi 57526399 603 TSKMEHLKKADKILILHEGSVYFYGTFSELQNQR 636
Cdd:cd03222 129 EHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTR 162
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
436-632 |
1.04e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.68 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI--------------KHSGRISFCSQYSWIMPG-T 500
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhaRARRGIGYLPQEASIFRRlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNI--IFGVSYDEYRYRSVIKACQLEEDISKFSEKDNIvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:PRK10895 95 VYDNLmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 579 ---VLTEKEIFEscvcKLMANKTRILVTSK--MEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:PRK10895 170 pisVIDIKRIIE----HLRDSGLGVLITDHnvRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1211-1441 |
1.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRL----LNTKGEIQIDGVSWDSITLQQWRKA 1286
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 FGVIPQkvfifsgtfrknlDPYEQWSDQeiwKVADEV--GL--------------RSVIEQFpGKLDFVLVDGGcVLSHG 1350
Cdd:PRK13640 86 VGIVFQ-------------NPDNQFVGA---TVGDDVafGLenravprpemikivRDVLADV-GMLDYIDSEPA-NLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1351 HKQLMCLARSVLSKAKILLLDEPSAHLDPI----TYQIIRRTLKQafADCTVILSEHRIEAMLECQRFLVIEENKVRQYD 1426
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAgkeqILKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
250
....*....|....*
gi 57526399 1427 SIQRMLSEKSLFRQA 1441
Cdd:PRK13640 226 SPVEIFSKVEMLKEI 240
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1211-1400 |
1.36e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.44 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTL------LLAFLRLLNTKGEIQIDGV-----SWDSIT 1279
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNDLIPGARVEGEILLDGEdiydpDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1280 LqqwRKAFGVIPQKVFIFSGTFRKN----------LDPYE-----QWS--DQEIWkvaDEVGlrsvieqfpGKLDfvlvD 1342
Cdd:COG1117 90 L---RRRVGMVFQKPNPFPKSIYDNvayglrlhgiKSKSEldeivEESlrKAALW---DEVK---------DRLK----K 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1343 GGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI-TYQI---IRRtLKQafaDCTVIL 1400
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKIeelILE-LKK---DYTIVI 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
439-623 |
1.42e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG--------------------------RISFCSQ 492
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 493 YS--WIMPgTIKDNI------IFGVSYDEYRYRSVikacqleedisKFSEK---DNIVLGEGGITLSGGQRARISLARAV 561
Cdd:PRK10619 100 HFnlWSHM-TVLENVmeapiqVLGLSKQEARERAV-----------KYLAKvgiDERAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 562 YKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSV 623
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKI 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
439-645 |
1.60e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.27 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-------------ISFCSqYSWIMPGTIKDNI 505
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdicMVFQS-YALFPHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 506 -----IFGVSYDEYRYRsVIKACQLeEDISKFSEK--DNIvlgeggitlSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:PRK11432 100 gyglkMLGVPKEERKQR-VKEALEL-VDLAGFEDRyvDQI---------SGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 579 VLTEKEIFEscvcKLMANKTRILVTS------KMEHLKKADKILILHEGSVYFYGTFSELQnQRPD--FSSKLMG 645
Cdd:PRK11432 169 ANLRRSMRE----KIRELQQQFNITSlyvthdQSEAFAVSDTVIVMNKGKIMQIGSPQELY-RQPAsrFMASFMG 238
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1213-1441 |
1.78e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.48 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG--VSWDSITLQQWRKAFGV 1289
Cdd:PRK13639 4 TRDLKYSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGepIKYDKKSLLEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKV--FIFSGTFRK-------NLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARS 1360
Cdd:PRK13639 83 VFQNPddQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGMEGFENKPPHH-----------LSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1361 VLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQRMLSEKSLF 1438
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDlVPVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
...
gi 57526399 1439 RQA 1441
Cdd:PRK13639 232 RKA 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1203-1405 |
1.94e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.49 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1203 DIWPSGGQMTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNT------KGEIQIDGVS-W 1275
Cdd:PRK14271 14 DVDAAAPAMAAVNLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrySGDVLLGGRSiF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1276 DSITLQQWRKAFGVIPQKVFIFSGTFRKNL----DPYEQWSDQEIWKVAD----EVGLRSVIEQfpgkldfVLVDGGCVL 1347
Cdd:PRK14271 92 NYRDVLEFRRRVGMLFQRPNPFPMSIMDNVlagvRAHKLVPRKEFRGVAQarltEVGLWDAVKD-------RLSDSPFRL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1348 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRI 1405
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1228-1448 |
2.01e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLrllntkGEIQidGVSWDSITLqqwRKAFGVIPQKVFIFSGTFRKNL-- 1305
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAML------GELP--PRSDASVVI---RGTVAYVPQVSWIFNATVRDNIlf 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1306 -DPYEQwsdQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQ 1383
Cdd:PLN03130 702 gSPFDP---ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQ 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 1384 IIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRMLSEKSLFRQAISPADRL 1448
Cdd:PLN03130 779 VFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKM 843
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
425-607 |
2.01e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.79 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 425 DTSLFFSNlllgTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMI--MGELEPS---EGKIKHSGR------------- 486
Cdd:PRK14239 10 DLSVYYNK----KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtvdlr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 487 --ISFCSQYSWIMPGTIKDNIIFGVSYDEYRYRSVIKACqLEEDISKFSEKDNI--VLGEGGITLSGGQRARISLARAVY 562
Cdd:PRK14239 86 keIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEA-VEKSLKGASIWDEVkdRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 57526399 563 KDADLYLLDSPFGYLDVLTEKEIfESCVCKLMANKTRILVTSKME 607
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-632 |
2.26e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYSWIMPG------------------- 499
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 -TIKDNIIFGVSYDEYRYRSVIKACqLEEDISKFSEKDNIV--LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEKREIKKI-VEECLRKVGLWKEVYdrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 577 LDVLTEKEIfESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSEL 632
Cdd:PRK14246 184 IDIVNSQAI-EKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
438-632 |
2.33e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.13 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI---------------KHSGRISFCSQYSWIMPGTIK 502
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenvwdiRHKIGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFG-----VSYDEYRYRsVIKACQLEeDISKFSEKDNIvlgeggiTLSGGQRARISLARAVYKDADLYLLDS----- 572
Cdd:PRK13650 101 DDVAFGlenkgIPHEEMKER-VNEALELV-GMQDFKEREPA-------RLSGGQKQRVAIAGAVAMRPKIIILDEatsml 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 573 -PFGYLDVL-TEKEIFEScvcklmANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:PRK13650 172 dPEGRLELIkTIKGIRDD------YQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
436-632 |
2.95e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.86 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYSWI-------MPGTIKDNIIFG 508
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMklresvgMVFQDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 509 VS-YDEYRYRSVikACQLEEDisKFSEKDNIVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:PRK13636 98 ASvYQDVSFGAV--NLKLPED--EVRKRVDNALKRTGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 579 VLTEKEIFEscVCKLMANK---TRILVTSKMEHLK-KADKILILHEGSVYFYGTFSEL 632
Cdd:PRK13636 174 PMGVSEIMK--LLVEMQKElglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
436-641 |
3.97e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTP-VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-------------ISFCSQYSWIMPGTI 501
Cdd:PTZ00243 1321 GLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReigayglrelrrqFSMIPQDPVLFDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 502 KDNIIfgvSYDEYRYRSVIKACQL---EEDISKFSEK-DNIVLgEGGITLSGGQRARISLARAVYK-DADLYLLDSPFGY 576
Cdd:PTZ00243 1401 RQNVD---PFLEASSAEVWAALELvglRERVASESEGiDSRVL-EGGSNYSVGQRQLMCMARALLKkGSGFILMDEATAN 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 577 LDVLTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSVYFYGTFSEL-QNQRPDFSS 641
Cdd:PTZ00243 1477 IDPALDRQI-QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHS 1541
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
438-623 |
4.59e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.43 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEP---SEGKIKHSGrISFCSQYSW----------------IMP 498
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDG-ITLTAKTVWdirekvgivfqnpdnqFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 GTIKDNIIFGVSYDEYRYRSVIKACQ--LEE-DISKF--SEKDNivlgeggitLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRdvLADvGMLDYidSEPAN---------LSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 574 FGYLDVLTEKEIFeSCVCKLMANK--TRILVTSKMEHLKKADKILILHEGSV 623
Cdd:PRK13640 171 TSMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1211-1408 |
4.76e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLA---FLRLLNTKGEI------------------- 1268
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVlrgMDQYEPTSGRIiyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1269 --------------QIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFR------KNLDPYEQWSDQEIWKVADevglrsV 1328
Cdd:TIGR03269 79 gepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvlEALEEIGYEGKEAVGRAVD------L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1329 IEQFpgKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAF--ADCTVILSEHRIE 1406
Cdd:TIGR03269 153 IEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPE 230
|
..
gi 57526399 1407 AM 1408
Cdd:TIGR03269 231 VI 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1212-1433 |
5.03e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.23 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidgGNAILeNISFSISPGQRVGLLGRTGSGKSTlllaflrLLN--------TKGEIQIDGVSWDSI----- 1278
Cdd:COG3840 3 RLDDLTYRY---GDFPL-RFDLTIAAGERVAILGPSGAGKST-------LLNliagflppDSGRILWNGQDLTALppaer 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1279 ---------------TLQQwRKAFGVIPqkvfifsgtfRKNLDPYEQwsdQEIWKVADEVGLRSVIEQFPGKldfvlvdg 1343
Cdd:COG3840 72 pvsmlfqennlfphlTVAQ-NIGLGLRP----------GLKLTAEQR---AQVEQALERVGLAGLLDRLPGQ-------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1344 gcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP--------ITYQIIRRTlkQAfadcTVILSEHRIE-AMLECQRF 1414
Cdd:COG3840 130 ---LSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrqemldLVDELCRER--GL----TVLMVTHDPEdAARIADRV 200
|
250
....*....|....*....
gi 57526399 1415 LVIEENKVRQYDSIQRMLS 1433
Cdd:COG3840 201 LLVADGRIAADGPTAALLD 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
436-486 |
5.51e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.63 E-value: 5.51e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR 486
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR 64
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1223-1450 |
7.72e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.33 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG--VS------------------------W 1275
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHqTSGHIRFHGtdVSrlhardrkvgfvfqhyalfrhmtvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1276 DSItlqqwrkAFG--VIPQkvfifsgtfRKNLDPYEqwSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQ 1353
Cdd:PRK10851 93 DNI-------AFGltVLPR---------RERPNAAA--IKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1354 LMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQ---AFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQR 1430
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlheELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
250 260
....*....|....*....|
gi 57526399 1431 MLSEkslfrqaisPADRLKL 1450
Cdd:PRK10851 224 VWRE---------PATRFVL 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1211-1379 |
7.89e-09 |
|
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: 56.98 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTakYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIqidgvSWDSITLQQWRKafgv 1289
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAgLLRPDSGEV-----RWNGTPLAEQRD---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFSG---------TFRKNLD---PYEQWSDQEIWKVADEVGLRSvIEQFPGKldfvlvdggcVLSHGHKQLMCL 1357
Cdd:TIGR01189 70 EPHENILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG-FEDLPAA----------QLSAGQQRRLAL 138
|
170 180
....*....|....*....|..
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDP 1379
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-623 |
1.03e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.93 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLL-----MMIMGELEPSEGKIKHSGR---------------ISFCSQYSWIMP 498
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVRLFGRniyspdvdpievrreVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 G-TIKDNIIFGVSYD---------EYRYRSVIKACQLEEDIskfseKDNivLGEGGITLSGGQRARISLARAVYKDADLY 568
Cdd:PRK14267 99 HlTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEV-----KDR--LNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 569 LLDSPFGYLDVLTEKEIfESCVCKLMANKTRILVT-SKMEHLKKADKILILHEGSV 623
Cdd:PRK14267 172 LMDEPTANIDPVGTAKI-EELLFELKKEYTIVLVThSPAQAARVSDYVAFLYLGKL 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
437-623 |
1.15e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.28 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELE--PSEGKIKhsgrisfcsqyswimpgtIKDNIIfgvsydeY 514
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD------------------VPDNQF-------G 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 515 RYRSVIKACQLEEDISKFSEkdniVLGEGGI-----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEK 583
Cdd:COG2401 98 REASLIDAIGRKGDFKDAVE----LLNAVGLsdavlwlrrfkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 57526399 584 EIfESCVCKLM--ANKTRILVTSKMEhLKKA---DKILILHEGSV 623
Cdd:COG2401 174 RV-ARNLQKLArrAGITLVVATHHYD-VIDDlqpDLLIFVGYGGV 216
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
420-589 |
1.22e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 59.76 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 420 KISNCDTSLFFSNLLLGTP----VLKDISFKIERGQLLAVAGSTGAGKTSLLMmIMGELEPSEG---KIKHSGRISFCSQ 492
Cdd:TIGR00954 444 IVEYQDNGIKFENIPLVTPngdvLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQ 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 493 YSWIMPGTIKDNIIFGVSYDEYRYRSVIKAcQLEEdISKFSEKDNIVLGEGGIT--------LSGGQRARISLARAVYKD 564
Cdd:TIGR00954 523 RPYMTLGTLRDQIIYPDSSEDMKRRGLSDK-DLEQ-ILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMARLFYHK 600
|
170 180
....*....|....*....|....*
gi 57526399 565 ADLYLLDSPFGYLDVLTEKEIFESC 589
Cdd:TIGR00954 601 PQFAILDECTSAVSVDVEGYMYRLC 625
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1212-1465 |
1.24e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.20 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaflrllnT-----------KGEIQIDGvswDSITL 1280
Cdd:COG4152 3 ELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTT----------TiriilgilapdSGEVLWDG---EPLDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1281 QQwRKAFGVIP--------QKVF---IFSGTfRKNLDPYEqwSDQEIWKVADEVGLRSV----IEQfpgkldfvlvdggc 1345
Cdd:COG4152 68 ED-RRRIGYLPeerglypkMKVGeqlVYLAR-LKGLSKAE--AKRRADEWLERLGLGDRankkVEE-------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1346 vLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLK-QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVR 1423
Cdd:COG4152 130 -LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIReLAAKGTTVIFSSHQMELVEElCDRIVIINKGRKV 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 57526399 1424 QY---DSIQRMLSEKSLFRQAISPADRLKLLPH-RNSSRQRSRANI 1465
Cdd:COG4152 209 LSgsvDEIRRQFGRNTLRLEADGDAGWLRALPGvTVVEEDGDGAEL 254
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
440-623 |
1.24e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-ISFCSqyswimPG------------------- 499
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpVRIRS------PRdaialgigmvhqhfmlvpn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 500 -TIKDNIIFGVsydEYRYRSVIKACQLEEDISKFSEK-------DNIVlgEggiTLSGGQRARISLARAVYKDADLYLLD 571
Cdd:COG3845 95 lTVAENIVLGL---EPTKGGRLDRKAARARIRELSERygldvdpDAKV--E---DLSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 572 SPFGyldVLTEKEI---FEscVCKLMAN--KTRILVTSKMEHLKK-ADKILILHEGSV 623
Cdd:COG3845 167 EPTA---VLTPQEAdelFE--ILRRLAAegKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
439-634 |
1.27e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.17 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI----------KHSG----------------------- 485
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKekekvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 486 ----RISFCSQYS--WIMPGTIKDNIIFG-VSYD------EYRYRSVIKACQLEEDISKFSEKDnivlgeggitLSGGQR 552
Cdd:PRK13651 102 eirrRVGVVFQFAeyQLFEQTIEKDIIFGpVSMGvskeeaKKRAAKYIELVGLDESYLQRSPFE----------LSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 553 ARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSVYFYG-TFS 630
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGdTYD 251
|
....
gi 57526399 631 ELQN 634
Cdd:PRK13651 252 ILSD 255
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1232-1422 |
1.34e-08 |
|
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: 56.73 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1232 SFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVswDSITLQQWRKAFGVIPQKVFIFSG-TFRKN----- 1304
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAgFETPQSGRVLINGV--DVTAAPPADRPVSMLFQENNLFAHlTVEQNvglgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1305 -----LDPYEQwsdQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 1379
Cdd:cd03298 96 spglkLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 1380 ityqIIRRTLKQAFADC------TVILSEHRIEAMLEC-QRFLVIEENKV 1422
Cdd:cd03298 162 ----ALRAEMLDLVLDLhaetkmTVLMVTHQPEDAKRLaQRVVFLDNGRI 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1223-1453 |
1.64e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.02 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSW--DSITLQQWRKAFGVIPQKVFIFSG 1299
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEiTSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 -TFRKNL--DPYE--QWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:PRK09493 92 lTALENVmfGPLRvrGASKEEAEKQAREllakVGLAERAHHYPSE-----------LSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1371 DEPSAHLDPITYQIIRRTLKQ-AFADCTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQRMLSEkslfrqaiSPADRL 1448
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIKN--------PPSQRL 232
|
....*.
gi 57526399 1449 K-LLPH 1453
Cdd:PRK09493 233 QeFLQH 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1212-1407 |
1.66e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 57.09 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTakYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDG---VSWDSITLQQWRkaf 1287
Cdd:PRK13548 4 EARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGrplADWSPAELARRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQKVfifSGTFrknldPyeqwsdqeiWKVADEVGL-RSVIEQFPGKLDfVLVDG-----GCV---------LSHGHK 1352
Cdd:PRK13548 79 AVLPQHS---SLSF-----P---------FTVEEVVAMgRAPHGLSRAEDD-ALVAAalaqvDLAhlagrdypqLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1353 QLMCLARsVL-------SKAKILLLDEPSAHLDPITYQIIRRTLKQ--------------------AFADCTVILSEHRI 1405
Cdd:PRK13548 141 QRVQLAR-VLaqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQlaherglavivvlhdlnlaaRYADRIVLLHQGRL 219
|
..
gi 57526399 1406 EA 1407
Cdd:PRK13548 220 VA 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1211-1410 |
1.69e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDggNAILENISFSISPGQRVGLLGRTGSGKSTlllaflRLLNTKGEI--QIDGVSWDSITLQQWRKAFG 1288
Cdd:PRK13638 2 LATSDLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKST------LFMNLSGLLrpQKGAVLWQGKPLDYSKRGLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VIPQKV-FIFSG----TFRKNLDPYEQWSDQEIWKVADEVGlRSVIEQfpgkldFVLVDG--------GCvLSHGHKQLM 1355
Cdd:PRK13638 74 ALRQQVaTVFQDpeqqIFYTDIDSDIAFSLRNLGVPEAEIT-RRVDEA------LTLVDAqhfrhqpiQC-LSHGQKKRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1356 CLARSVLSKAKILLLDEPSAHLDPI----TYQIIRRTLKQAfadCTVILSEHRIEAMLE 1410
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAgrtqMIAIIRRIVAQG---NHVIISSHDIDLIYE 201
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
439-623 |
2.33e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.58 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKtSLLMMIMGELE-PSEGKIKHSGR-ISfcsqyswimpgTIKDNII-------FGV 509
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGK-STLMNILGCLDkPTSGTYRVAGQdVA-----------TLDADALaqlrrehFGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 510 SYDEYRYRSVIKACQLEE--------DISKFSEKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDS 572
Cdd:PRK10535 91 IFQRYHLLSHLTAAQNVEvpavyaglERKQRLLRAQELLQRLGLedrveyqpsQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57526399 573 PFGYLDVLTEKEIFesCVCKLMANK--TRILVTSKMEHLKKADKILILHEGSV 623
Cdd:PRK10535 171 PTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
440-581 |
2.42e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIkHSG---RISFCSQYSWIM-P-GTIKDNI--------I 506
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGtklEVAYFDQHRAELdPeKTVMDNLaegkqevmV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 507 FGVS-----------YDEYRYRSVIKAcqleediskfsekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:PRK11147 414 NGRPrhvlgylqdflFHPKRAMTPVKA------------------------LSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
....*.
gi 57526399 576 YLDVLT 581
Cdd:PRK11147 470 DLDVET 475
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
440-638 |
3.17e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 56.56 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLM----MIMGELEPS------------EGKIK--------HSGRISfcSQYSW 495
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGshiellgrtvqrEGRLArdirksraNTGYIF--QQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 496 IMPGTIKDNIIFGVSYDEYRYRSVIK---ACQLEEDISKFSEKDNIVLGEGGI-TLSGGQRARISLARAVYKDADLYLLD 571
Cdd:PRK09984 98 VNRLSVLENVLIGALGSTPFWRTCFSwftREQKQRALQALTRVGMVHFAHQRVsTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 572 SPFGYLDVLTEKEIFESCVCKLMANKTRILVT-SKMEH-LKKADKILILHEGSVYFYGTFSELQNQRPD 638
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFD 246
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
442-623 |
3.30e-08 |
|
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: 57.91 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 442 DISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPS-EGKIKHSGR---ISFCSQYswIMPGTI-------KDNII--FG 508
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvdIRNPAQA--IRAGIAmvpedrkRHGIVpiLG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 509 V-------SYDEYRYRSVIKACQ----LEEDISKFSEKD-NIVLGEGGitLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:TIGR02633 356 VgknitlsVLKSFCFKMRIDAAAelqiIGSAIQRLKVKTaSPFLPIGR--LSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57526399 577 LDVLTEKEIFescvcKLMANKTR-----ILVTSKM-EHLKKADKILILHEGSV 623
Cdd:TIGR02633 434 VDVGAKYEIY-----KLINQLAQegvaiIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1210-1422 |
3.73e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.18 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1210 QMTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTK-GEIQIDGVSWDSITLQQWRKAFG 1288
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VIPQKVFIFSGTFRKNL-----DPY-EQW-----SDQEIWKVADEvglRSVIEQFPGKLdfvLVDggcvLSHGHKQLMCL 1357
Cdd:PRK11231 80 LLPQHHLTPEGITVRELvaygrSPWlSLWgrlsaEDNARVNQAME---QTRINHLADRR---LTD----LSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDpITYQI----IRRTLKQAFAdcTVILSEHRI-EAMLECQRFLVIEENKV 1422
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLD-INHQVelmrLMRELNTQGK--TVVTVLHDLnQASRYCDHLVVLANGHV 216
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
438-585 |
3.80e-08 |
|
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: 56.99 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGeLEPSEGKIkhSGRISFCSQyswimpgtikDniIFGVSYDE---Y 514
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGIT--SGEILFDGE----------D--LLKLSEKElrkI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 515 RYRSV----------------IKAcQLEE------DISKfSEKDNIV---LGEGGIT------------LSGGQRARISL 557
Cdd:COG0444 84 RGREIqmifqdpmtslnpvmtVGD-QIAEplrihgGLSK-AEARERAielLERVGLPdperrldrypheLSGGMRQRVMI 161
|
170 180
....*....|....*....|....*...
gi 57526399 558 ARAVYKDADLYLLDSPFGYLDVLTEKEI 585
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQI 189
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1212-1427 |
4.12e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 57.03 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaf-lrllnTKGEIQIDGVSWDsitlqqwrkafGVI 1290
Cdd:COG3842 7 ELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTllrmiagfetpDSGRILLDGRDVT-----------GLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQK-----VF--------------I-FSGTFRKnldpyeqWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcv 1346
Cdd:COG3842 74 PEKrnvgmVFqdyalfphltvaenVaFGLRMRG-------VPKAEIRARVAEllelVGLEGLADRYPHQ----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1347 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQafadctvILSEHRI----------EAMLECQRFLV 1416
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRR-------LQRELGItfiyvthdqeEALALADRIAV 208
|
250
....*....|.
gi 57526399 1417 IEENKVRQYDS 1427
Cdd:COG3842 209 MNDGRIEQVGT 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1228-1378 |
5.02e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 57.39 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKGEIQIDGVSWDSIT---LQQWRKAFGVIPQkvfifsgtfrkn 1304
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQ------------ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1305 lDPY---------------------EQWSDQE----IWKVADEVGL-RSVIEQFPGKldfvlvdggcvLSHGHKQLMCLA 1358
Cdd:COG4172 370 -DPFgslsprmtvgqiiaeglrvhgPGLSAAErrarVAEALEEVGLdPAARHRYPHE-----------FSGGQRQRIAIA 437
|
170 180
....*....|....*....|.
gi 57526399 1359 RSVLSKAKILLLDEP-SAhLD 1378
Cdd:COG4172 438 RALILEPKLLVLDEPtSA-LD 457
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1214-1441 |
5.04e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.96 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1214 KDLTAKYiDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQ 1292
Cdd:PRK13652 7 RDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKpTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1293 KV--FIFSGTFRK-------NLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLS 1363
Cdd:PRK13652 86 NPddQIFSPTVEQdiafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1364 KAKILLLDEPSAHLDPI-TYQIIR--RTLKQAFAdCTVILSEHRIEAMLECQRFL-VIEENKVRQYDSIQRMLSEKSLFR 1439
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQgVKELIDflNDLPETYG-MTVIFSTHQLDLVPEMADYIyVMDKGRIVAYGTVEEIFLQPDLLA 233
|
..
gi 57526399 1440 QA 1441
Cdd:PRK13652 234 RV 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1220-1391 |
5.50e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.11 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1220 YIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFS 1298
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISpTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1299 GTFRKNLD-PYEQWSDQeiwkvADEVGLRSVIEQFpGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 1377
Cdd:PRK10247 95 DTVYDNLIfPWQIRNQQ-----PDPAIFLDDLERF-ALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170
....*....|....*...
gi 57526399 1378 DP----ITYQIIRRTLKQ 1391
Cdd:PRK10247 169 DEsnkhNVNEIIHRYVRE 186
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1228-1429 |
5.57e-08 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 56.24 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGvsWDsITLQ--QWRKAFGVIPQKVFIFSG-TFRK 1303
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRpTSGTARVAG--YD-VVREprKVRRSIGIVPQYASVDEDlTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1304 NL----DPYEqWSDQEIWKVADEVglrsvIEQFPgkldfvLVDGGCVL----SHGHKQLMCLARSVLSKAKILLLDEPSA 1375
Cdd:TIGR01188 86 NLemmgRLYG-LPKDEAEERAEEL-----LELFE------LGEAADRPvgtySGGMRRRLDIAASLIHQPDVLFLDEPTT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1376 HLDPITYQIIR---RTLKQafADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQ 1429
Cdd:TIGR01188 154 GLDPRTRRAIWdyiRALKE--EGVTILLTTHYMeEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
437-578 |
5.63e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-------RISFCSqYSWIMPGTIKD-----N 504
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktatrgdRSRFMA-YLGHLPGLKADlstleN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 505 IIFGVSYDEYRYRSVIKACQLEEDISKFSekDNIVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 578
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAGYE--DTLVR-----QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
436-492 |
5.64e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 5.64e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHS--GRISFCSQ 492
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIGYYAQ 389
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
440-643 |
6.62e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.36 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPS---EGKIKHSG---------RIS-FCSQYSWIMPG-TIKDNI 505
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemrAISaYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 506 IF--------GVSYDEYRYRsvikacqLEEDISKFSEKD--NIVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:TIGR00955 121 MFqahlrmprRVTKKEKRER-------VDEVLQALGLRKcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 574 FGYLDVLTEKEIFEscVCKLMANKTRILV------TSKMEHLkkADKILILHEGSVYFYGTFSELqnqrPDFSSKL 643
Cdd:TIGR00955 194 TSGLDSFMAYSVVQ--VLKGLAQKGKTIIctihqpSSELFEL--FDKIILMAEGRVAYLGSPDQA----VPFFSDL 261
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1225-1422 |
7.83e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.40 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1225 NAILENISFSISPGQRVGLLGRTGSGKSTLLLaflrllNTKGEIQIDGVSWDSITL---------------QQWRKAFGV 1289
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLR------HLSGLITGDKSAGSHIELlgrtvqregrlardiRKSRANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQK------------VFIFS-GT---FRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGkldfvlvdggcVLSHGHKQ 1353
Cdd:PRK09984 91 IFQQfnlvnrlsvlenVLIGAlGStpfWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVS-----------TLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1354 LMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRIE-AMLECQRFLVIEENKV 1422
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
436-623 |
8.15e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMI-----------------MGELEPSEGKIkhsGRIsFCSqYSWIMP 498
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsgdlfigekrMNDVPPAERGV---GMV-FQS-YALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 GTIKDNIIFGV-------SYDEYRYRSVIKACQLEEDISKfSEKDnivlgeggitLSGGQRARISLARAVYKDADLYLLD 571
Cdd:PRK11000 90 LSVAENMSFGLklagakkEEINQRVNQVAEVLQLAHLLDR-KPKA----------LSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 572 SPFGYLD----VLTEKEIfescvCKLMA--NKTRILVT-SKMEHLKKADKILILHEGSV 623
Cdd:PRK11000 159 EPLSNLDaalrVQMRIEI-----SRLHKrlGRTMIYVThDQVEAMTLADKIVVLDAGRV 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1213-1400 |
9.53e-08 |
|
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: 55.44 E-value: 9.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKY-IDGGNA-ILENISFSISPGQRVGLLGRTGSGKSTLLLA----FLRLLNTKGEIQIDGVSWDSITLQQWRKA 1286
Cdd:COG0444 4 VRNLKVYFpTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAilglLPPPGITSGEILFDGEDLLKLSEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 ----FGVIPQkvfifsgtfrknlDPY----------EQ----------WSDQEIWKVADE----VGL---RSVIEQFPGK 1335
Cdd:COG0444 84 rgreIQMIFQ-------------DPMtslnpvmtvgDQiaeplrihggLSKAEARERAIEllerVGLpdpERRLDRYPHE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1336 ldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQIIR--RTLKQAFaDCTVIL 1400
Cdd:COG0444 151 -----------LSGGMRQRVMIARALALEPKLLIADEPTTALDVtIQAQILNllKDLQREL-GLAILF 206
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
449-612 |
1.05e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.76 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 449 RGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKhsgrisfcsqyswimpgTIKDNIIFGVSYDEYRyrsvikacqleed 528
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-----------------YIDGEDILEEVLDQLL------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 529 iskfsekdNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTR------ILV 602
Cdd:smart00382 51 --------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSeknltvILT 122
|
170
....*....|
gi 57526399 603 TSKMEHLKKA 612
Cdd:smart00382 123 TNDEKDLGPA 132
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
442-645 |
1.09e-07 |
|
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: 55.88 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 442 DISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK-----------------HSGRISFCSQYSWIMPG-TIKD 503
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsargiflppHRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFGvsydeyryrsvIKACQLEEDISKFsekDNIV--LGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:COG4148 97 NLLYG-----------RKRAPRAERRISF---DEVVelLGIGHLldrrpaTLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 576 YLDVLTEKEI---FEScvcklMANKTRI---LVT---SKMEHLkkADKILILHEGSVYFYGTFSELQNqRPDFSSKLMG 645
Cdd:COG4148 163 ALDLARKAEIlpyLER-----LRDELDIpilYVShslDEVARL--ADHVVLLEQGRVVASGPLAEVLS-RPDLLPLAGG 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1214-1422 |
1.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.09 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1214 KDLTAKYIDGGNA----ILENISFSISPGQRVGLLGRTGSGKSTLLL-AFLRLLNTKGEIQIDGVSW-DSITLQQWRKAF 1287
Cdd:PRK13633 8 KNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKhMNALLIPSEGKVYVDGLDTsDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQK--------------VFifsGTFRKNLDPyeqwsdQEIWKVADEvGLRSV----IEQFPGKLdfvlvdggcvLSH 1349
Cdd:PRK13633 88 GMVFQNpdnqivativeedvAF---GPENLGIPP------EEIRERVDE-SLKKVgmyeYRRHAPHL----------LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 1350 GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
439-623 |
1.12e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 53.68 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMG--ELEPSEGKIkhsgrisfcsqyswimpgTIKDNIIFGVSYDEYRY 516
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI------------------LFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 517 RSVIKACQLEEDISKFSEKDNI-VLGEGgitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFEScVCKLMA 595
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLrYVNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV-INKLRE 152
|
170 180 190
....*....|....*....|....*....|.
gi 57526399 596 NKTRILVTSKMEHL---KKADKILILHEGSV 623
Cdd:cd03217 153 EGKSVLIITHYQRLldyIKPDRVHVLYDGRI 183
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1210-1403 |
1.31e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.53 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1210 QMTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL------RLLNTKGEIQIDGVSWDSITLQQW 1283
Cdd:PRK14247 3 KIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrlielyPEARVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1284 RKAFGVIPQ------KVFIFSGTF-----------RKNLDPYEQWS--DQEIWkvaDEVGLRsvIEQFPGKLdfvlvdgg 1344
Cdd:PRK14247 81 RRRVQMVFQipnpipNLSIFENVAlglklnrlvksKKELQERVRWAleKAQLW---DEVKDR--LDAPAGKL-------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1345 cvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEH 1403
Cdd:PRK14247 148 ---SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
440-644 |
1.38e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.71 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR---------------ISFCSQYSWIMPGTIKDN 504
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkigMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGVSYDEYRYRSVIKACQ---LEEDISKFSEKDNivlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 581
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDealLAVNMLDFKTREP-------ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 582 EKEIFEscVCKLMANK---TRILVTSKMEHLKKADKILILHEGSVYFYGTFSELQNQRPD---------FSSKLM 644
Cdd:PRK13642 176 RQEIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDmveigldvpFSSNLM 248
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1212-1422 |
1.41e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.19 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYIDGGNAI--LENISFSISPGQRVGLLGRTGSGKSTlllaFLRLLN-----TKGEIQIDGV---SWDSITLQ 1281
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKST----LIRCINllerpTSGRVLVDGQdltALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1282 QWRKAFGVIPQKVFIFSG-TFRKNLD-PYE--QWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQ 1353
Cdd:PRK11153 79 KARRQIGMIFQHFNLLSSrTVFDNVAlPLElaGTPKAEIKARVTEllelVGLSDKADRYPAQ-----------LSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1354 LMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRIEAMLE-CQRFLVIEENKV 1422
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElgLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1213-1424 |
1.50e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKGEIQIDG--------VSWDSITLQQWR 1284
Cdd:PRK14258 10 VNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqnIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1285 KAFGVIPQKVFIFSGTFRKNL----------------DPYEQ-WSDQEIWkvaDEVglrsvieqfPGKLDFVLVDggcvL 1347
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVaygvkivgwrpkleidDIVESaLKDADLW---DEI---------KHKIHKSALD----L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1348 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAF--ADCTVILSEHRIEAMLECQRFLVI---EENKV 1422
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFfkgNENRI 231
|
..
gi 57526399 1423 RQ 1424
Cdd:PRK14258 232 GQ 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1223-1385 |
1.58e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTK-GEIQIDGVSWD------SITLQQWRKAFGVIPQKVF 1295
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRsGTLNIAGNHFDfsktpsDKAIRELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1296 IFSG-TFRKNL--DPYE--QWSDQEIWKVADEVGLRSVIEQFPGKldFVLVdggcvLSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:PRK11124 93 LWPHlTVQQNLieAPCRvlGLSKDQALARAEKLLERLRLKPYADR--FPLH-----LSGGQQQRVAIARALMMEPQVLLF 165
|
170
....*....|....*.
gi 57526399 1371 DEPSAHLDP-ITYQII 1385
Cdd:PRK11124 166 DEPTAALDPeITAQIV 181
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
436-645 |
1.69e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.99 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK------HSGR---------------ISFCSQYS 494
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditiDTARslsqqkglirqlrqhVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 495 WIMPG-TIKDNIIFGvsydeyryRSVIKACQLEEDISKFSEkdniVLGEGGIT---------LSGGQRARISLARAVYKD 564
Cdd:PRK11264 95 NLFPHrTVLENIIEG--------PVIVKGEPKEEATARARE----LLAKVGLAgketsyprrLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 565 ADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYGT----FSELQNQRP-D 638
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPakalFADPQQPRTrQ 242
|
....*..
gi 57526399 639 FSSKLMG 645
Cdd:PRK11264 243 FLEKFLL 249
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1211-1424 |
1.82e-07 |
|
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: 53.41 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGV---SWD------SITL 1280
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAgLEEPTSGRIYIGGRdvtDLPpkdrdiAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1281 QQwrkaFGVIPQK-VF--IFSGTFRKNLDPYEqwSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCL 1357
Cdd:cd03301 79 QN----YALYPHMtVYdnIAFGLKLRKVPKDE--IDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDPITYQIIRRTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQ 1424
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQ 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
439-642 |
1.85e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.42 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR---------------ISFCSQYSWIMPGTIKD 503
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFG---VSYDE----YRYRSVIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:PRK13652 99 DIAFGpinLGLDEetvaHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 577 LDVLTEKEIFescvckLMANK-------TRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQNQrPDFSSK 642
Cdd:PRK13652 168 LDPQGVKELI------DFLNDlpetygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ-PDLLAR 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1213-1404 |
1.92e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.71 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNT-KGEIQIDgvswDSITLqqwrkafGVIP 1291
Cdd:TIGR03719 325 AENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPdSGTIEIG----ETVKL-------AYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1292 QkvfifsgtFRKNLDP----YEQWSD-QEIWKVAD-EVGLRSVIEQFPGKldfvlvdGG------CVLSHGHKQLMCLAR 1359
Cdd:TIGR03719 392 Q--------SRDALDPnktvWEEISGgLDIIKLGKrEIPSRAYVGRFNFK-------GSdqqkkvGQLSGGERNRVHLAK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 57526399 1360 SVLSKAKILLLDEPSAHLDPITYqiirRTLKQA---FADCTVILSEHR 1404
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETL----RALEEAllnFAGCAVVISHDR 500
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1223-1391 |
2.14e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 53.86 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAF-LRLLNTKGEIQIDGVSWD------SITLQQWRKAFGVIPQKVF 1295
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDSGQLNIAGHQFDfsqkpsEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1296 IFSG-TFRKNLDPYEQW----SDQEIWKVADEVGLRSVIEQFPGKldFVLVdggcvLSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:COG4161 93 LWPHlTVMENLIEAPCKvlglSKEQAREKAMKLLARLRLTDKADR--FPLH-----LSGGQQQRVAIARALMMEPQVLLF 165
|
170 180
....*....|....*....|....
gi 57526399 1371 DEPSAHLDP-ITYQI--IRRTLKQ 1391
Cdd:COG4161 166 DEPTAALDPeITAQVveIIRELSQ 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
436-634 |
2.20e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-ISFCSQYSWIMPG--------------T 500
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQeMRFASTTAALAAGvaiiyqelhlvpemT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFG--------VSYDEYRYRSVIKACQLEEDISKfsekdNIVLGEggitLSGGQRARISLARAVYKDADLYLLDS 572
Cdd:PRK11288 96 VAENLYLGqlphkggiVNRRLLNYEAREQLEHLGVDIDP-----DTPLKY----LSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 573 PFGYLDVlTEKEIFESCVCKLMANKTRIL-VTSKMEHL-KKADKILILHEGSvyFYGTFSELQN 634
Cdd:PRK11288 167 PTSSLSA-REIEQLFRVIRELRAEGRVILyVSHRMEEIfALCDAITVFKDGR--YVATFDDMAQ 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1223-1427 |
3.12e-07 |
|
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: 53.01 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVswDSITLQQWRKAFGVIPQKVFIFS--- 1298
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAgFETPTSGEILLDGK--DITNLPPHKRPVNTVFQNYALFPhlt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1299 -------GTFRKNLDPYEQwsDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 1371
Cdd:cd03300 89 vfeniafGLRLKKLPKAEI--KERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1372 EPSAHLDPITYQIIRRTLK--QAFADCTVILSEH-RIEAMLECQRFLVIEENKVRQYDS 1427
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKrlQKELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1224-1378 |
3.30e-07 |
|
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: 52.72 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1224 GNAILENISFSISPGQRVGLLGRTGSGKSTLLLAflrllnTKGEIQ-IDG-VSWDSI---------TLQQWRKAFGVIPQ 1292
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLA------ILGEMQtLEGkVHWSNKnesepsfeaTRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1293 KVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDE 1372
Cdd:cd03290 87 KPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
....*.
gi 57526399 1373 PSAHLD 1378
Cdd:cd03290 167 PFSALD 172
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
439-631 |
3.31e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPS--EGKIKHSG---------RISFCSQYSWIMPG-TIKDNII 506
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNrkptkqilkRTGFVTQDDILYPHlTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 507 F--------GVSYDEyryrsviKACQLEEDISK--FSEKDNIVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:PLN03211 163 FcsllrlpkSLTKQE-------KILVAESVISElgLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 576 YLDVLTEKEIFESCVCklMANKTRILVTSKMEHLKKA----DKILILHEGSVYFYGTFSE 631
Cdd:PLN03211 236 GLDATAAYRLVLTLGS--LAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1223-1403 |
3.77e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLA------FLRLLNTKGEIQIDGVSWDSITLQ--QWRKAFGVipqkV 1294
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrlleLNEEARVEGEVRLFGRNIYSPDVDpiEVRREVGM----V 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1295 FIFSGTF---------------------RKNLDPYEQWSDQE--IWkvaDEVGLRsvIEQFPGKLdfvlvdggcvlSHGH 1351
Cdd:PRK14267 91 FQYPNPFphltiydnvaigvklnglvksKKELDERVEWALKKaaLW---DEVKDR--LNDYPSNL-----------SGGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1352 KQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEH 1403
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
439-581 |
4.31e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.56 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK--HSGRISFCSQyswiMPGTIKDNiifgvsydeyry 516
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEigETVKLAYVDQ----SRDALDPN------------ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 517 RSVIkacqleEDISKFSekDNIVLGEGGI---------------------TLSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:TIGR03719 401 KTVW------EEISGGL--DIIKLGKREIpsrayvgrfnfkgsdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTN 472
|
....*.
gi 57526399 576 YLDVLT 581
Cdd:TIGR03719 473 DLDVET 478
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1211-1404 |
4.65e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDggNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSwdsitLQQWRKAFgv 1289
Cdd:PRK13540 2 LDVIELDFDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNpEKGEILFERQS-----IKKDLCTY-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 ipQKVFIFSGtFRKNLDPYEQWSDQ---EIWKVADEVGLRSVIEQFpgKLDFvLVDGGC-VLSHGHKQLMCLARSVLSKA 1365
Cdd:PRK13540 73 --QKQLCFVG-HRSGINPYLTLRENclyDIHFSPGAVGITELCRLF--SLEH-LIDYPCgLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 57526399 1366 KILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHR 1404
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKgGAVLLTSHQ 186
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
454-631 |
5.04e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.72 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 454 AVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISF-CSQYSWIMP-----G------------TIKDNIIFGVSydeyr 515
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKGICLPPekrriGyvfqdarlfphyKVRGNLRYGMA----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 516 yrsvikacqlEEDISKFsekDNIV--LGEGG------ITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEife 587
Cdd:PRK11144 103 ----------KSMVAQF---DKIValLGIEPlldrypGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE--- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 588 scvckLMAN--------KTRIL-VTSKM-EHLKKADKILILHEGSVYFYGTFSE 631
Cdd:PRK11144 167 -----LLPYlerlareiNIPILyVSHSLdEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
440-579 |
6.48e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.04 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSL---LMMImgElEPSEGKIKHSGRISfcSQYSwimPGTIKD-----NIIFGVSY 511
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMI--E-TPTGGELYYQGQDL--LKAD---PEAQKLlrqkiQIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 512 DEYRYRSVIKAcQLEE------DISKFSEKDNI--VLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:PRK11308 103 GSLNPRKKVGQ-ILEEpllintSLSAAERREKAlaMMAKVGLrpehydryphMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
....*.
gi 57526399 574 FGYLDV 579
Cdd:PRK11308 182 VSALDV 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
441-623 |
6.59e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 441 KDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG-RISFCSQYSWIMPG-----------------TIK 502
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkDISPRSPLDAVKKGmayitesrrdngffpnfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFGVSYDEYRYRSVIKACQlEEDISKFSEKDNIVLG------EGGIT-LSGGQRARISLARAVYKDADLYLLDSPFG 575
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMGLFH-EVDEQRTAENQRELLAlkchsvNQNITeLSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 57526399 576 YLDVLTEKEIFescvcKLM-----ANKTRILVTSKM-EHLKKADKILILHEGSV 623
Cdd:PRK09700 439 GIDVGAKAEIY-----KVMrqladDGKVILMVSSELpEIITVCDRIAVFCEGRL 487
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1211-1378 |
7.00e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.30 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTaKYIDGGNAIlENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVswDSITLQQWRKAFGV 1289
Cdd:PRK11607 20 LEIRNLT-KSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAgFEQPTAGQIMLDGV--DLSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFSG-TFRKNLD---PYEQWSDQEI-WKVADEVGLRSvIEQFPGKLDFvlvdggcVLSHGHKQLMCLARSVLSK 1364
Cdd:PRK11607 96 MFQSYALFPHmTVEQNIAfglKQDKLPKAEIaSRVNEMLGLVH-MQEFAKRKPH-------QLSGGQRQRVALARSLAKR 167
|
170
....*....|....
gi 57526399 1365 AKILLLDEPSAHLD 1378
Cdd:PRK11607 168 PKLLLLDEPMGALD 181
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
439-632 |
7.09e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYSWIMPG---------------TIKD 503
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 504 NIIFGVSY-DEYRYRSVIKacQLEEDISKFSEKDNIVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 582
Cdd:PRK11614 100 NLAMGGFFaERDQFQERIK--WVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 583 KEIFEScVCKLMANKTRILVTSK--MEHLKKADKILILHEGSVYFYGTFSEL 632
Cdd:PRK11614 174 QQIFDT-IEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1212-1427 |
7.33e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 53.15 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTlllaflrLLN--------TKGEIQIDGvswdsitlqqw 1283
Cdd:COG3839 5 ELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKST-------LLRmiagledpTSGEILIGG----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1284 RKAFGVIPQK-----VF----IF-SGTFRKNL---------DPYEQwsDQEIWKVADEVGLRSVIEQFPGKldfvlvdgg 1344
Cdd:COG3839 65 RDVTDLPPKDrniamVFqsyaLYpHMTVYENIafplklrkvPKAEI--DRRVREAAELLGLEDLLDRKPKQ--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1345 cvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEH-RIEAMLECQRFLVIEENK 1421
Cdd:COG3839 134 --LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlgTTTIYVTHdQVEAMTLADRIAVMNDGR 211
|
....*.
gi 57526399 1422 VRQYDS 1427
Cdd:COG3839 212 IQQVGT 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
442-621 |
9.35e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 442 DISFKIERGQLLAVAGSTGAGKTSLLMMIMGELE-PSEGKIKHSGR---ISFCSQ--------------YSWIMPG-TIK 502
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvkIRNPQQaiaqgiamvpedrkRDGIVPVmGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNIIFgVSYDEYRYRSVIKAC----QLEEDISKFSEK-DNIVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 577
Cdd:PRK13549 360 KNITL-AALDRFTGGSRIDDAaelkTILESIQRLKVKtASPELAIA--RLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 578 DVLTEKEIFescvcKLMANKTR-----ILVTSKM-EHLKKADKILILHEG 621
Cdd:PRK13549 437 DVGAKYEIY-----KLINQLVQqgvaiIVISSELpEVLGLSDRVLVMHEG 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1219-1378 |
9.80e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1219 KYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLlntkgEIQIDGVSW--DSITLqqwrkafGVIPQK--- 1293
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----DKDFNGEARpqPGIKV-------GYLPQEpql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1294 ---------VFIFSGTFRKNLDPYEQWS------DQEIWKVADEVG-LRSVIEQFPG-----KLDFVLVDGGC------- 1345
Cdd:TIGR03719 80 dptktvrenVEEGVAEIKDALDRFNEISakyaepDADFDKLAAEQAeLQEIIDAADAwdldsQLEIAMDALRCppwdadv 159
|
170 180 190
....*....|....*....|....*....|....
gi 57526399 1346 -VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1378
Cdd:TIGR03719 160 tKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1228-1426 |
1.10e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.40 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTlllaflrllnT-----------KGEIQIDG-VSWD-------SITL------QQ 1282
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKST----------TikmltgilvptSGEVRVLGyVPFKrrkefarRIGVvfgqrsQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1283 W------------RKAFGvIPQKVfifsgtFRKNLDpyeqwsdqeiwKVADEVGLRSVIEQfPgkldfvlvdggcV--LS 1348
Cdd:COG4586 108 WwdlpaidsfrllKAIYR-IPDAE------YKKRLD-----------ELVELLDLGELLDT-P------------VrqLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1349 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQ--AFADCTVILSEHR---IEAMleCQRFLVIEENKVr 1423
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDmddIEAL--CDRVIVIDHGRI- 233
|
...
gi 57526399 1424 QYD 1426
Cdd:COG4586 234 IYD 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
438-637 |
1.11e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.69 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 438 PVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG----------------RISFCSQYSWIMPG-T 500
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrsrlytvrkRMSMLFQSGALFTDmN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFGVSydeyryrsviKACQLEEDI--SKFSEKDNIVLGEGGIT-----LSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:PRK11831 101 VFDNVAYPLR----------EHTQLPAPLlhSTVMMKLEAVGLRGAAKlmpseLSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 574 FGYLDVLTekeifESCVCKLMA--NK----TRILVTSKM-EHLKKADKILILHEGSVYFYGTFSELQ-NQRP 637
Cdd:PRK11831 171 FVGQDPIT-----MGVLVKLISelNSalgvTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQaNPDP 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1214-1438 |
1.21e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.41 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1214 KDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG--VSWDSItlQQwrKAFGVI 1290
Cdd:PRK11432 10 KNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDGedVTHRSI--QQ--RDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQKVFIFSgtfrkNLDPYEQ---------WSDQEIWKVADE----VGLRSVIEQFpgkldfvlVDGgcvLSHGHKQLMCL 1357
Cdd:PRK11432 84 FQSYALFP-----HMSLGENvgyglkmlgVPKEERKQRVKEalelVDLAGFEDRY--------VDQ---ISGGQQQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDPITYQIIR---RTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQRM-LS 1433
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMRekiRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELyRQ 227
|
....*
gi 57526399 1434 EKSLF 1438
Cdd:PRK11432 228 PASRF 232
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1228-1403 |
1.23e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 51.38 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKGEIQIDGV---SWDSITLQQWRkafGVIPQ--------KVFI 1296
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRplsDWSAAELARHR---AYLSQqqsppfamPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1297 FSGTFR-KNLDPYEQwsDQEIWKVADEVGL-----RSViEQfpgkldfvlvdggcvLSHGHKQLMCLARSVL-------S 1363
Cdd:COG4138 89 YLALHQpAGASSEAV--EQLLAQLAEALGLedklsRPL-TQ---------------LSGGEWQRVRLAAVLLqvwptinP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 57526399 1364 KAKILLLDEPSAHLDpITYQIIRRTLKQAFADC--TVILSEH 1403
Cdd:COG4138 151 EGQLLLLDEPMNSLD-VAQQAALDRLLRELCQQgiTVVMSSH 191
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
440-691 |
1.25e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.86 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRisfcsQYSWIMPGTIKDNIIfGVSYDEYryrSV 519
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI-----NYNKLDHKLAAQLGI-GIIYQEL---SV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 520 IKACQLEE------------------DISKFSEKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDS 572
Cdd:PRK09700 92 IDELTVLEnlyigrhltkkvcgvniiDWREMRVRAAMMLLRVGLkvdldekvaNLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 573 PfgyLDVLTEKEI---FescvckLMANKTR------ILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQNQrpDFSSK 642
Cdd:PRK09700 172 P---TSSLTNKEVdylF------LIMNQLRkegtaiVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSND--DIVRL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 57526399 643 LMGCDTFDQFTAERRN--SIITETLrrFSLEGDTSVSWNETKKPSFK-QTGE 691
Cdd:PRK09700 241 MVGRELQNRFNAMKENvsNLAHETV--FEVRNVTSRDRKKVRDISFSvCRGE 290
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1212-1412 |
1.51e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.64 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAkyIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWD------SIT----- 1279
Cdd:PRK13539 4 EGEDLAC--VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAgLLPPAAGTIKLDGGDIDdpdvaeACHylghr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1280 ------------LQQWRKAFGvipqkvfifsgtfRKNLDPYEqwsdqeiwkVADEVGLrSVIEQFPGKldfvlvdggcVL 1347
Cdd:PRK13539 82 namkpaltvaenLEFWAAFLG-------------GEELDIAA---------ALEAVGL-APLAHLPFG----------YL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1348 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ----IIRRTLKQafaDCTVILSEHRIEAMLECQ 1412
Cdd:PRK13539 129 SAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAlfaeLIRAHLAQ---GGIVIAATHIPLGLPGAR 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1213-1378 |
1.60e-06 |
|
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: 50.90 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1213 VKDLTAKYIDGGNA--ILENISFSISPGQRVGLLGRTGSGKSTlllaf-lrllnTKGEIQIDGVSWDSIT---LQQWRka 1286
Cdd:COG4181 11 LRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTllgllagldrpTSGTVRLAGQDLFALDedaRARLR-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 fgviPQKV-FIF-------SGTFRKN-LDPYEQWSDQEIWKVA----DEVGLRSVIEQFPGkldfvlvdggcVLSHGHKQ 1353
Cdd:COG4181 89 ----ARHVgFVFqsfqllpTLTALENvMLPLELAGRRDARARArallERVGLGHRLDHYPA-----------QLSGGEQQ 153
|
170 180
....*....|....*....|....*
gi 57526399 1354 LMCLARSVLSKAKILLLDEPSAHLD 1378
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLD 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
436-585 |
1.64e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.33 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR--------------ISFCSQYSWIMPG-T 500
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFGvsyDEYRYRSVIKACQLEEDISKfsekdniVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLD 571
Cdd:COG1129 96 VAENIFLG---REPRRGGLIDWRAMRRRARE-------LLARLGLdidpdtpvgDLSVAQQQLVEIARALSRDARVLILD 165
|
170
....*....|....
gi 57526399 572 SPfgyLDVLTEKEI 585
Cdd:COG1129 166 EP---TASLTEREV 176
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1211-1406 |
1.84e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.85 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWD------SITLQQ- 1282
Cdd:PRK11248 2 LQISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAgFVPYQHGSITLDGKPVEgpgaerGVVFQNe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1283 ----WRK-----AFGVIPQKVfifsgtfrknldPYEQwSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQ 1353
Cdd:PRK11248 80 gllpWRNvqdnvAFGLQLAGV------------EKMQ-RLEIAHQMLKKVGLEGAEKRYIWQ-----------LSGGQRQ 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 1354 LMCLARSVLSKAKILLLDEPSAHLDPIT--------YQIIRRTLKQafadctVILSEHRIE 1406
Cdd:PRK11248 136 RVGIARALAANPQLLLLDEPFGALDAFTreqmqtllLKLWQETGKQ------VLLITHDIE 190
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1220-1403 |
1.96e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.20 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1220 YIDGgNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNT-KGEIQIDG---------VSWDSITLqqwRKAFGV 1289
Cdd:PRK14246 19 YIND-KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGkvlyfgkdiFQIDAIKL---RKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVFIFS-----GTFRKNLDPYEQWSDQEIWKVADE----VGL-RSVIEQfpgkldfvLVDGGCVLSHGHKQLMCLAR 1359
Cdd:PRK14246 95 VFQQPNPFPhlsiyDNIAYPLKSHGIKEKREIKKIVEEclrkVGLwKEVYDR--------LNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 57526399 1360 SVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEH 1403
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1227-1253 |
2.15e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.85 E-value: 2.15e-06
10 20
....*....|....*....|....*..
gi 57526399 1227 ILENISFSISPGQRVGLLGRTGSGKST 1253
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKST 67
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
436-573 |
2.36e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR--------------ISFCSQYSWIMPG-T 500
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 501 IKDNIIFGVSYDEYRYRSVIK-----ACQLEEDISkfsekdnivlgegGITLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQllaalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1228-1433 |
2.66e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.57 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWR-----------KAFGVIPQKVF 1295
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1296 IFSGTFRKNLDPYEQWSDQEiwKVAD---EVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDE 1372
Cdd:PRK10070 124 LDNTAFGMELAGINAEERRE--KALDalrQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1373 PSAHLDPITYQIIRRTLK--QAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQRMLS 1433
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1340-1406 |
2.68e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.55 E-value: 2.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1340 LVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIE 1406
Cdd:PRK14243 145 LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
436-578 |
2.78e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGeLEP-SEGKIKHSGR-----------ISFCSQYSWIMPG-TIK 502
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LERiTSGEIWIGGRvvnelepadrdIAMVFQNYALYPHmSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 503 DNI-----IFGVSYDEYRYRsVIKACQLEEdISKFSE-KDNivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:PRK11650 95 ENMayglkIRGMPKAEIEER-VAEAARILE-LEPLLDrKPR--------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
..
gi 57526399 577 LD 578
Cdd:PRK11650 165 LD 166
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-642 |
3.20e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 420 KISNCDTSLFFSNlllgTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMI--MGELEPS---EGKIKHSG--------- 485
Cdd:PRK14247 3 KIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifkmdvi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 486 ----RISFCSQYSWIMPG-TIKDNIIFGVSYD---------EYRYRSVIKACQLEEDIskfseKDNivLGEGGITLSGGQ 551
Cdd:PRK14247 79 elrrRVQMVFQIPNPIPNlSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-----KDR--LDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 552 RARISLARAVYKDADLYLLDSPFGYLDVLTEKEIfESCVCKLMANKTRILVTS-KMEHLKKADKILILHEGSVYFYGTFS 630
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTR 230
|
250
....*....|...
gi 57526399 631 EL-QNQRPDFSSK 642
Cdd:PRK14247 231 EVfTNPRHELTEK 243
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
441-581 |
3.53e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 441 KDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK--HSGRISFCSQyswiMPGTIKDNiifgvsydeyryRS 518
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKigETVKLAYVDQ----SRDALDPN------------KT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 519 VIkacqleEDISkfSEKDNIVLGEGGI---------------------TLSGGQRARISLARAVYKDADLYLLDSPFGYL 577
Cdd:PRK11819 405 VW------EEIS--GGLDIIKVGNREIpsrayvgrfnfkggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
....
gi 57526399 578 DVLT 581
Cdd:PRK11819 477 DVET 480
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
440-585 |
3.75e-06 |
|
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: 51.22 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGeLEPSEGKIKHSGR------------------ISFCSQYSWIMPG-T 500
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdldglsrralrplrrrmqVVFQDPFGSLSPRmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDnII--------FGVSYDEyRYRSVIKAcqLEE------DISKF-SEkdnivlgeggitLSGGQRARISLARAVYKDA 565
Cdd:COG4172 381 VGQ-IIaeglrvhgPGLSAAE-RRARVAEA--LEEvgldpaARHRYpHE------------FSGGQRQRIAIARALILEP 444
|
170 180
....*....|....*....|
gi 57526399 566 DLYLLDSPFGYLDVLTEKEI 585
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQI 464
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1211-1379 |
4.42e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 49.75 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTK------GEIQIDGvswdSITLQQWR 1284
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirvGDITIDT----ARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1285 KAFGVIPQKV-FIFSGTfrkNLDPY--------------EQWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggc 1345
Cdd:PRK11264 78 GLIRQLRQHVgFVFQNF---NLFPHrtvleniiegpvivKGEPKEEATARAREllakVGLAGKETSYPRR---------- 144
|
170 180 190
....*....|....*....|....*....|....
gi 57526399 1346 vLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 1379
Cdd:PRK11264 145 -LSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1223-1419 |
4.55e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.94 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQ-QWRKAFGVIPQK------- 1293
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNINYNKLDHKlAAQLGIGIIYQElsvidel 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1294 -----VFIFSGTFRKNLD-PYEQWSDQEIWK--VADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKA 1365
Cdd:PRK09700 96 tvlenLYIGRHLTKKVCGvNIIDWREMRVRAamMLLRVGLKVDLDEKVAN-----------LSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 1366 KILLLDEPSAHL--DPITY--QIIRRTLKQAFAdctVILSEHRIEAMLE-CQRFLVIEE 1419
Cdd:PRK09700 165 KVIIMDEPTSSLtnKEVDYlfLIMNQLRKEGTA---IVYISHKLAEIRRiCDRYTVMKD 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1211-1421 |
5.45e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.60 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLlaflrllN--------TKGEIQIDGVSWDSI---- 1278
Cdd:PRK11300 6 LSVSGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVF-------NcltgfykpTGGTILLRGQHIEGLpghq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1279 --------TLQQWR--KAFGVIPQ---------KVFIFSGTF---------RKNLDPYEQWSDQeiwkvadeVGLRSVIE 1330
Cdd:PRK11300 77 iarmgvvrTFQHVRlfREMTVIENllvaqhqqlKTGLFSGLLktpafrraeSEALDRAATWLER--------VGLLEHAN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1331 QFPGKLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP---ITYQIIRRTLKQAFaDCTVILSEHRIE- 1406
Cdd:PRK11300 149 RQAGNL-----------AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPketKELDELIAELRNEH-NVTVLLIEHDMKl 216
|
250
....*....|....*
gi 57526399 1407 AMLECQRFLVIEENK 1421
Cdd:PRK11300 217 VMGISDRIYVVNQGT 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1230-1424 |
5.53e-06 |
|
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: 49.56 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1230 NISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSIT---LQQWRK--------AFGVIPQKVFIF 1297
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSrkeLRELRRkkismvfqSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1298 SGTFR---KNLDPYEQWSDQEiwKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPS 1374
Cdd:cd03294 122 NVAFGlevQGVPRAEREERAA--EALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1375 AHLDPityqIIRRTLKQAFADC------TVILSEHR-IEAMLECQRFLVIEENKVRQ 1424
Cdd:cd03294 189 SALDP----LIRREMQDELLRLqaelqkTIVFITHDlDEALRLGDRIAIMKDGRLVQ 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1211-1404 |
7.11e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNT-KGEI--------------QIDGVSW 1275
Cdd:PRK10636 313 LKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPvSGEIglakgiklgyfaqhQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1276 DSITLQQW-RKAFGVIPQKVFIFSGTFRKNLDpyeqwsdqeiwKVADEVglrsviEQFPGkldfvlvdggcvlshGHKQL 1354
Cdd:PRK10636 391 DESPLQHLaRLAPQELEQKLRDYLGGFGFQGD-----------KVTEET------RRFSG---------------GEKAR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1355 MCLARSVLSKAKILLLDEPSAHLDpityQIIRRTLKQAFAD---CTVILSEHR 1404
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEALIDfegALVVVSHDR 487
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1211-1422 |
9.55e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.94 E-value: 9.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNA-ILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNT-KGEIQIDGVSWDSITLQQWRKAFG 1288
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VI---PQKVFIfSGTFRKNLD---PYEQWSDQEIWKVADEVGLRSVIeqfpgkLDFVLVDGGcVLSHGHKQLMCLARSVL 1362
Cdd:PRK13642 85 MVfqnPDNQFV-GATVEDDVAfgmENQGIPREEMIKRVDEALLAVNM------LDFKTREPA-RLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1363 SKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
392-639 |
9.72e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 392 VVMENVTAFWeegfsKLFEKAKENNNNRKISNCDTSLFFSnlllgtpvLKDISFKIERGQLLAVAGSTGAGKTSLLMMIM 471
Cdd:PRK13546 5 VNIKNVTKEY-----RIYRTNKERMKDALIPKHKNKTFFA--------LDDISLKAYEGDVIGLVGINGSGKSTLSNIIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 472 GELEPSEGKIKHSGRISFCSqyswIMPG-----TIKDNIIFGVSYDEYRyRSVIKacQLEEDISKFSEkdnivLGE---- 542
Cdd:PRK13546 72 GSLSPTVGKVDRNGEVSVIA----ISAGlsgqlTGIENIEFKMLCMGFK-RKEIK--AMTPKIIEFSE-----LGEfiyq 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 543 GGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD-VLTEKeifesCVCKLM----ANKTRILVTSKMEHLKK-ADKIL 616
Cdd:PRK13546 140 PVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDqTFAQK-----CLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIA 214
|
250 260
....*....|....*....|...
gi 57526399 617 ILHEGSVYFYGTFSELQNQRPDF 639
Cdd:PRK13546 215 WIEGGKLKDYGELDDVLPKYEAF 237
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
436-655 |
1.05e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.97 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTP----VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-ISFCSQYSWIMPGTIKDNIIFGVS 510
Cdd:PRK13649 15 GTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlITSTSKNKDIKQIRKKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 511 YDEYRYRSVIK---------ACQLEEDISKFSEKDNIVlgegGIT----------LSGGQRARISLARAVYKDADLYLLD 571
Cdd:PRK13649 95 ESQLFEETVLKdvafgpqnfGVSQEEAEALAREKLALV----GISeslfeknpfeLSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 572 SPFGYLDVLTEKE---IFESCVCKLMankTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELqNQRPDF-SSKLMGC 646
Cdd:PRK13649 171 EPTAGLDPKGRKElmtLFKKLHQSGM---TIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI-FQDVDFlEEKQLGV 246
|
....*....
gi 57526399 647 DTFDQFTAE 655
Cdd:PRK13649 247 PKITKFAQR 255
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
1223-1422 |
1.10e-05 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 48.66 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVswDSITLQQWRKAfgvipqkvfifsgtf 1301
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAgALRPDAGTVDLAGV--DLHGLSRRARA--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1302 rKNLDPYEQWSDQEI-WKVADEVGL-----RSVIEQFP----GKLDFVLVDGGC---------VLSHGHKQLMCLARSVL 1362
Cdd:TIGR03873 75 -RRVALVEQDSDTAVpLTVRDVVALgriphRSLWAGDSphdaAVVDRALARTELshladrdmsTLSGGERQRVHVARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 57526399 1363 SKAKILLLDEPSAHLDpITYQI--IRRTLKQAFADCTVILSEHRIE-AMLECQRFLVIEENKV 1422
Cdd:TIGR03873 154 QEPKLLLLDEPTNHLD-VRAQLetLALVRELAATGVTVVAALHDLNlAASYCDHVVVLDGGRV 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1223-1378 |
1.11e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFlrllntKGEIQIDGVS------WDSITLQQWRKAFGViPQKVFI 1296
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL------KNEISADGGSytfpgnWQLAWVNQETPALPQ-PALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1297 FSG--TFRKnldpyeqwSDQEIwKVADEVGLRSVIEQFPGKLDFV-----------LVDGgcvLSHGHKQL--------- 1354
Cdd:PRK10636 85 IDGdrEYRQ--------LEAQL-HDANERNDGHAIATIHGKLDAIdawtirsraasLLHG---LGFSNEQLerpvsdfsg 152
|
170 180
....*....|....*....|....*....
gi 57526399 1355 -----MCLARSVLSKAKILLLDEPSAHLD 1378
Cdd:PRK10636 153 gwrmrLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1210-1403 |
1.19e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.88 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1210 QMTVKDLTAkyIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEiqidgVSWDSITLQQWRKAF- 1287
Cdd:PRK13538 1 MLEARNLAC--ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAgLARPDAGE-----VLWQGEPIRRQRDEYh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 ----------GVIPQkvfifsgtfrknLDPYE--QW--------SDQEIWKVADEVGLRSViEQFPGKldfvlvdggcVL 1347
Cdd:PRK13538 74 qdllylghqpGIKTE------------LTALEnlRFyqrlhgpgDDEALWEALAQVGLAGF-EDVPVR----------QL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1348 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDpityqiirrtlKQAFADCTVILSEH 1403
Cdd:PRK13538 131 SAGQQRRVALARLWLTRAPLWILDEPFTAID-----------KQGVARLEALLAQH 175
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
442-486 |
1.25e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 1.25e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 57526399 442 DISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR 486
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR 68
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1234-1418 |
1.26e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 48.56 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1234 SISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGvswDSITLQqwrkafgviPQKV----------FIFSGTFR 1302
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKpDEGDIEIEL---DTVSYK---------PQYIkadyegtvrdLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1303 KNLDPYeqwsdqeiWK--VADEVGLRSVIEQfpgkldfVLVDggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP- 1379
Cdd:cd03237 89 FYTHPY--------FKteIAKPLQIEQILDR-------EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVe 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 57526399 1380 ---ITYQIIRRTLKQafADCTVILSEHRI-EAMLECQRFLVIE 1418
Cdd:cd03237 150 qrlMASKVIRRFAEN--NEKTAFVVEHDIiMIDYLADRLIVFE 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1223-1417 |
1.57e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.25 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLllaflrllnTK----------GEIQIDG--VSWDSItLQQWRKAFGVI 1290
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTL---------MKilsgvyqpdsGEILLDGepVRFRSP-RDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1291 PQKV--F--------IFSGTFRKN---LDpyeqWSDQEIW--KVADEVGLRsvieqfpgkLDF-VLVDGgcvLSHGHKQL 1354
Cdd:COG1129 85 HQELnlVpnlsvaenIFLGREPRRgglID----WRAMRRRarELLARLGLD---------IDPdTPVGD---LSVAQQQL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 57526399 1355 MCLARSVLSKAKILLLDEPSAHLDP----ITYQIIRRtLKQafADCTVILSEHRIEAMLE-CQRFLVI 1417
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEreveRLFRIIRR-LKA--QGVAIIYISHRLDEVFEiADRVTVL 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1223-1378 |
1.90e-05 |
|
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: 47.10 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEiqidgVSWDSITLQQWRKAFgvipQKVFIFSG-- 1299
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAgLSPPLAGR-----VLLNGGPLDFQRDSI----ARGLLYLGha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 -------TFRKNLDPYEQW-SDQEIWKVADEVGLRSViEQFPGKldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLD 1371
Cdd:cd03231 82 pgikttlSVLENLRFWHADhSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILD 150
|
....*..
gi 57526399 1372 EPSAHLD 1378
Cdd:cd03231 151 EPTTALD 157
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1211-1422 |
2.26e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.80 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKY-IDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTK-GEIQIDGvswDSITLQQ-W--RK 1285
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDG---DLLTEENvWdiRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1286 AFGVI---PQKVFIFS--------GTFRKNLDpyeqwsDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHG 1350
Cdd:PRK13650 82 KIGMVfqnPDNQFVGAtveddvafGLENKGIP------HEEMKERVNEalelVGMQDFKEREPAR-----------LSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1351 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
440-632 |
2.73e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.48 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQYSWimpGTIKDNIIFGVSYDEYRYRSV 519
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY---RSQRIRMIFQDPSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 520 IKAC-----QLEEDISKFSEKDNIV--LGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 582
Cdd:PRK15112 106 ISQIldfplRLNTDLEPEQREKQIIetLRQVGLlpdhasyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 583 KEIFeSCVCKLMANK--TRILVTSK---MEHLkkADKILILHEGSVYFYGTFSEL 632
Cdd:PRK15112 186 SQLI-NLMLELQEKQgiSYIYVTQHlgmMKHI--SDQVLVMHQGEVVERGSTADV 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
439-623 |
3.13e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFcsqyswimpGTIKDNIIFGVSYDEYRYRS 518
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL---------GYFAQHQLEFLRADESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 519 VIKAC------QLEEDISKFSEKDNIVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV-----LTEKEI-F 586
Cdd:PRK10636 398 LARLApqeleqKLRDYLGGFGFQGDKVTEETR-RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLdmrqaLTEALIdF 476
|
170 180 190
....*....|....*....|....*....|....*....
gi 57526399 587 ESCvcklmanktrILVTSKMEHLKKA--DKILILHEGSV 623
Cdd:PRK10636 477 EGA----------LVVVSHDRHLLRSttDDLYLVHDGKV 505
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
437-481 |
3.34e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 47.77 E-value: 3.34e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGeLE-PSEGKI 481
Cdd:COG1135 18 VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LErPTSGSV 62
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1223-1380 |
3.43e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKaFGV--IPQKVFIFSG 1299
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAgIVPPDSGTLEIGGNPCARLTPAKAHQ-LGIylVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 -TFRKNLD---PYEQwsdqeiwkvADEVGLRSVIEQFPGKLDFVLVDGgcVLSHGHKQLMCLARSVLSKAKILLLDEPSA 1375
Cdd:PRK15439 101 lSVKENILfglPKRQ---------ASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
....*
gi 57526399 1376 HLDPI 1380
Cdd:PRK15439 170 SLTPA 174
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1212-1378 |
3.47e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1212 TVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLrllntkGEIQIDG--VSWDSitlqqwRKAFGV 1289
Cdd:PRK15064 321 EVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV------GELEPDSgtVKWSE------NANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 IPQKVfifSGTFRKNLDPYEqWSDQeiWKVA--DEVGLRSVIeqfpGKLDFVLVDGG---CVLSHGHKQLMCLARSVLSK 1364
Cdd:PRK15064 387 YAQDH---AYDFENDLTLFD-WMSQ--WRQEgdDEQAVRGTL----GRLLFSQDDIKksvKVLSGGEKGRMLFGKLMMQK 456
|
170
....*....|....
gi 57526399 1365 AKILLLDEPSAHLD 1378
Cdd:PRK15064 457 PNVLVMDEPTNHMD 470
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1226-1424 |
4.14e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.70 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1226 AILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQwRKAF-----GVIPQKvFIFSG 1299
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgSSGEVSLVGQPLHQMDEEA-RAKLrakhvGFVFQS-FMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 TF--RKNLD-------PYEQWSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:PRK10584 102 TLnaLENVElpallrgESSRQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1371 DEPSAHLDPITYQIIRR---TLKQAFAdCTVILSEHRIEAMLECQRFLVIEENKVRQ 1424
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADllfSLNREHG-TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
439-621 |
4.86e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGElepSEGKiKHSGR-------ISFCS-----------------QYS 494
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SYGR-NISGTvfkdgkeVDVSTvsdaidaglayvtedrkGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 495 WIMPGTIKDNI----IFGVSY-------------DEYRYRSVIKACQLEEDISKfsekdnivlgeggitLSGGQRARISL 557
Cdd:NF040905 351 LNLIDDIKRNItlanLGKVSRrgvideneeikvaEEYRKKMNIKTPSVFQKVGN---------------LSGGNQQKVVL 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 558 ARAVYKDADLYLLDSPFGYLDVLTEKEIFesCVCKLMAN--KTRILVTSKM-EHLKKADKILILHEG 621
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGIDVGAKYEIY--TIINELAAegKGVIVISSELpELLGMCDRIYVMNEG 480
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
436-579 |
5.27e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-ISFCSQYSW-----------------IM 497
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdITGLSPRERrrlgvayipedrlgrglVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 498 PGTIKDNIIFGvSYDEYRY-------RSVIKAcQLEEDISKFsekdNIVLgeGGI-----TLSGG--QRArIsLARAVYK 563
Cdd:COG3845 350 DMSVAENLILG-RYRRPPFsrggfldRKAIRA-FAEELIEEF----DVRT--PGPdtparSLSGGnqQKV-I-LARELSR 419
|
170
....*....|....*..
gi 57526399 564 DADLYLLDSP-FGyLDV 579
Cdd:COG3845 420 DPKLLIAAQPtRG-LDV 435
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1216-1378 |
6.44e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1216 LTAKYID---GGNAILENISFSISPGQRVGLLGRTGSGKSTLLL---------AFLRLLNTKGEIQIDGVSWDSITLQQW 1283
Cdd:PRK13547 2 LTADHLHvarRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKalagdltggGAPRGARVTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1284 RKAFGVIPQ---KVFIFSGTFRKNLDPYEQWSDQEIWKVADevglRSVIEQFPGKLDFVLVDGGCV--LSHGHKQLMCLA 1358
Cdd:PRK13547 82 ARLRAVLPQaaqPAFAFSAREIVLLGRYPHARRAGALTHRD----GEIAWQALALAGATALVGRDVttLSGGELARVQFA 157
|
170 180 190
....*....|....*....|....*....|
gi 57526399 1359 RsVLSK----------AKILLLDEPSAHLD 1378
Cdd:PRK13547 158 R-VLAQlwpphdaaqpPRYLLLDEPTAALD 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1207-1464 |
8.74e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1207 SGGQMT----VKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSiTLQ 1281
Cdd:TIGR01257 1930 SGGNKTdilrLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTvTSGDATVAGKSILT-NIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1282 QWRKAFGVIPQkvfiFSG-----TFRKNLDPYEQWS---DQEIWKVAD----EVGLRSVIEQFPGkldfvlvdggcVLSH 1349
Cdd:TIGR01257 2009 DVHQNMGYCPQ----FDAiddllTGREHLYLYARLRgvpAEEIEKVANwsiqSLGLSLYADRLAG-----------TYSG 2073
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1350 GHKQLMCLARSVLSKAKILLLDEPSAHLDP----ITYQIIRRTLKQAFAdctVILSEHRIEAMLE-CQRFLVIEENKVRQ 1424
Cdd:TIGR01257 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPqarrMLWNTIVSIIREGRA---VVLTSHSMEECEAlCTRLAIMVKGAFQC 2150
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 57526399 1425 YDSIQRMlseKSLFRQAI-------SPADrlKLLPHRNSSRQRSRAN 1464
Cdd:TIGR01257 2151 LGTIQHL---KSKFGDGYivtmkikSPKD--DLLPDLNPVEQFFQGN 2192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1211-1406 |
8.79e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.74 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLL---NTKGEIQIDGVSWDSITLQQW-RKA 1286
Cdd:TIGR02633 2 LEMKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWDGEIYWSGSPLKASNIRDTeRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1287 FGVIPQKVfifsgTFRKNLDPYEQ-WSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCV------LSHGHKQLMCLAR 1359
Cdd:TIGR02633 80 IVIIHQEL-----TLVPELSVAENiFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtrpvgdYGGGQQQLVEIAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 1360 SVLSKAKILLLDEPSAHLDPITYQI---IRRTLKQAFADCTVIlsEHRIE 1406
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEIlldIIRDLKAHGVACVYI--SHKLN 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
434-579 |
8.82e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 434 LLGTPVLKDisfkierGQLLAVAGSTGAGKTSLLMMIMGELEP------------------------------SEGKIKH 483
Cdd:PRK13409 90 LYGLPIPKE-------GKVTGILGPNGIGKTTAVKILSGELIPnlgdyeeepswdevlkrfrgtelqnyfkklYNGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 484 SGRIsfcsQYSWIMP----GTIKDNIIfgvSYDEY-RYRSVIKACQLEE----DISkfsekdnivlgeggiTLSGGQRAR 554
Cdd:PRK13409 163 VHKP----QYVDLIPkvfkGKVRELLK---KVDERgKLDEVVERLGLENildrDIS---------------ELSGGELQR 220
|
170 180
....*....|....*....|....*
gi 57526399 555 ISLARAVYKDADLYLLDSPFGYLDV 579
Cdd:PRK13409 221 VAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1228-1440 |
8.86e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.31 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSIT----LQQWRKAFGVIPQ---------- 1292
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITITHKTkdkyIRPVRKRIGMVFQfpesqlfedt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1293 --KVFIFS-GTFRKNLDPYEQWSdqeiWKVADEVGL-RSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKIL 1368
Cdd:PRK13646 103 veREIIFGpKNFKMNLDEVKNYA----HRLLMDLGFsRDVMSQSPFQ-----------MSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1369 LLDEPSAHLDPITYQIIRRTLK--QAFADCTVILSEHRieaMLECQRFlvIEENKVRQYDSIQRMLSEKSLFRQ 1440
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHD---MNEVARY--ADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1211-1410 |
9.18e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGvswdsitlQQWRKAfgv 1289
Cdd:PRK15056 7 IVVNDVTVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISILG--------QPTRQA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 ipqkvfifsgtFRKNLDPYEQWSDQEIWK----VADEVGL----------------RSVIEQFPGKLDFVLVDGGCV--L 1347
Cdd:PRK15056 75 -----------LQKNLVAYVPQSEEVDWSfpvlVEDVVMMgryghmgwlrrakkrdRQIVTAALARVDMVEFRHRQIgeL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1348 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRIEAMLE 1410
Cdd:PRK15056 144 SGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTE 207
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
434-579 |
1.10e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.44 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 434 LLGTPVLKDisfkierGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKikhsgrisFCSQYSWimpgtikDNIIfgvsyDE 513
Cdd:cd03236 17 LHRLPVPRE-------GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDW-------DEIL-----DE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 514 YR------YRSVIKACQL--------------------EEDISKFSEKDNI-----VLGEGGI------TLSGGQRARIS 556
Cdd:cd03236 70 FRgselqnYFTKLLEGDVkvivkpqyvdlipkavkgkvGELLKKKDERGKLdelvdQLELRHVldrnidQLSGGELQRVA 149
|
170 180
....*....|....*....|...
gi 57526399 557 LARAVYKDADLYLLDSPFGYLDV 579
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDI 172
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1226-1422 |
1.13e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.64 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1226 AILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG---VSWDSITLQQWRKA-FGVIPQKVFIFSG- 1299
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKpTSGTYRVAGqdvATLDADALAQLRREhFGFIFQRYHLLSHl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 TFRKNLD-P--YEQWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDE 1372
Cdd:PRK10535 102 TAAQNVEvPavYAGLERKQRLLRAQEllqrLGLEDRVEYQPSQ-----------LSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 1373 PSAHLDPITYQIIRRTLKQAFADC-TVILSEHRIEAMLECQRFLVIEENKV 1422
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
436-621 |
1.28e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR-ISFCSQYSWIMPG--------------T 500
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeIDFKSSKEALENGismvhqelnlvlqrS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 501 IKDNIIFGvsydeyRYRS----VIKACQLEEDISKFSEKD-NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPfg 575
Cdd:PRK10982 90 VMDNMWLG------RYPTkgmfVDQDKMYRDTKAIFDELDiDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP-- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 57526399 576 yLDVLTEKEI--FESCVCKLMANKTRILVTS-KMEHLKK-ADKILILHEG 621
Cdd:PRK10982 162 -TSSLTEKEVnhLFTIIRKLKERGCGIVYIShKMEEIFQlCDEITILRDG 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
435-623 |
1.30e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 435 LGTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIK-HSGRISFCSQYSWIMPGtikdniiFGVSYDE 513
Cdd:PRK10982 259 LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITlHGKKINNHNANEAINHG-------FALVTEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 514 YR-----------YRSVIKacQLEEDISKFSEKDNI--------------VLGEGGIT----LSGGQRARISLARAVYKD 564
Cdd:PRK10982 332 RRstgiyayldigFNSLIS--NIRNYKNKVGLLDNSrmksdtqwvidsmrVKTPGHRTqigsLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 565 ADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKM-EHLKKADKILILHEGSV 623
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLV 469
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1206-1253 |
1.34e-04 |
|
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: 44.83 E-value: 1.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 57526399 1206 PSGGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKST 1253
Cdd:cd03220 16 GSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKST 63
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
436-632 |
1.44e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.47 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMiMGELEPSEGKIKHSG--------------------RISFCSQYSW 495
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRT-LNRMNDKVSGYRYSGdvllggrsifnyrdvlefrrRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 496 IMPGTIKDNIIFGVSYDEY----RYRSVIKAcQLEEDISKFSEKDNivLGEGGITLSGGQRARISLARAVYKDADLYLLD 571
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLvprkEFRGVAQA-RLTEVGLWDAVKDR--LSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 572 SPFGYLDVLTEKEIfESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSEL 632
Cdd:PRK14271 189 EPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1212-1274 |
1.45e-04 |
|
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: 44.44 E-value: 1.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1212 TVKDLTAKyiDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN---TKGEIQIDGVS 1274
Cdd:cd03217 2 EIKDLHVS--VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevTEGEILFKGED 65
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
906-1124 |
1.70e-04 |
|
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: 45.13 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 906 IITSTSSYYIFYIYVGVADTLLA---LGLFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSkDIAV 982
Cdd:cd18570 32 IIPSGDINLLNIISIGLILLYLFqslLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 983 LDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPYIFLATVPVIAAFILLRGYFLHTSQQLKQLESEGRSPIFTHLVTSLKGL 1062
Cdd:cd18570 111 IREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 57526399 1063 WTLRAFGRQPYF----ETLFHKALN--LHTANWFLYLSTLRWFqmrIEMIFVIFFIAVTFISI----LTTGE 1124
Cdd:cd18570 191 ETIKSLNAEEQFlkkiEKKFSKLLKksFKLGKLSNLQSSIKGL---ISLIGSLLILWIGSYLVikgqLSLGQ 259
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
439-627 |
1.79e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPS----EGKIKHSG------------RISFCSQYSWIMPG-TI 501
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGitpeeikkhyrgDVVYNAETDVHFPHlTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 502 KDNIIF------------GVSYDEYR--YRSVIKAcqleedISKFSEKDNIVLGEGGIT-LSGGQRARISLARAVYKDAD 566
Cdd:TIGR00956 156 GETLDFaarcktpqnrpdGVSREEYAkhIADVYMA------TYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 567 LYLLDSPFGYLDVLTEKEiFESCVcKLMAN--KTRILVT---SKMEHLKKADKILILHEGSVYFYG 627
Cdd:TIGR00956 230 IQCWDNATRGLDSATALE-FIRAL-KTSANilDTTPLVAiyqCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
546-641 |
2.06e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 546 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDvLTEKEIFESCVCKLmaNKTRILVTSKMEHLKK-ADKILILHEGSVY 624
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD-LHAVLWLETYLLKW--PKTFIVVSHAREFLNTvVTDILHLHGQKLV 420
|
90 100
....*....|....*....|....*.
gi 57526399 625 F----YGTF-----SELQNQRPDFSS 641
Cdd:PLN03073 421 TykgdYDTFertreEQLKNQQKAFES 446
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1211-1419 |
2.10e-04 |
|
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: 43.57 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKyidggnAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKA-FG 1288
Cdd:cd03215 5 LEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFgLRPPASGEITLDGKPVTRRSPRDAIRAgIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1289 VIPQKvfifsgtfRKnldpyeqwsdqeiwkvadEVGL---RSVIEqfpgklDFVLvdgGCVLSHGHKQLMCLARSVLSKA 1365
Cdd:cd03215 79 YVPED--------RK------------------REGLvldLSVAE------NIAL---SSLLSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1366 KILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVIL-SEHRIEAMLECQRFLVIEE 1419
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLiSSELDELLGLCDRILVMYE 179
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
951-1083 |
2.17e-04 |
|
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: 44.86 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 951 KMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQP---YIFLATVPVIAAFI 1027
Cdd:cd18557 74 DLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWkltLVLLLVIPLLLIAS 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 1028 LLRGYFLhtsQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALN 1083
Cdd:cd18557 154 KIYGRYI---RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALD 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1424 |
2.29e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 44.74 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKAFGV 1289
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIgIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1290 I---PQKVFIFSGT-------FRKNLDPYEQWSdQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1359
Cdd:PRK13648 88 VfqnPDNQFVGSIVkydvafgLENHAVPYDEMH-RRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 57526399 1360 SVLSKAKILLLDEPSAHLDPITYQIIRRTLK--QAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 1424
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1210-1422 |
2.81e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 44.69 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1210 QMTVKDLTAKYiDGGNAI----LENISFSISPGQRVGLLGRTGSGKSTLLL-AFLRLLNTKGEIQIDGVSW--------- 1275
Cdd:PRK13651 2 QIKVKNIVKIF-NKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEhLNALLLPDTGTIEWIFKDEknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1276 ----DSITLQ-----------QWRKAFGVIPQkvF----IFSGTFRKNL--DPYEQW-SDQEIWKVADE----VGLRsvi 1329
Cdd:PRK13651 81 ekvlEKLVIQktrfkkikkikEIRRRVGVVFQ--FaeyqLFEQTIEKDIifGPVSMGvSKEEAKKRAAKyielVGLD--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1330 EQFPGKLDFvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADC-TVILSEHRIEAM 1408
Cdd:PRK13651 156 ESYLQRSPF-------ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDNV 228
|
250
....*....|....*
gi 57526399 1409 LE-CQRFLVIEENKV 1422
Cdd:PRK13651 229 LEwTKRTIFFKDGKI 243
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
402-625 |
2.90e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 402 EEGFSKLFeKAKENNNNRKISNCDTS---LFFSNLLLGTPV-------LKDISFKIERGQLLAVAGSTGAGKTSLLMMIM 471
Cdd:TIGR00956 732 VLGSTDLT-DESDDVNDEKDMEKESGediFHWRNLTYEVKIkkekrviLNNVDGWVKPGTLTALMGASGAGKTTLLNVLA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 472 GELEP---SEGKIKHSGR---------ISFCSQYSWIMP-GTIKDNIIFG--------VS-YDEYRY-RSVIKACQLEed 528
Cdd:TIGR00956 811 ERVTTgviTGGDRLVNGRpldssfqrsIGYVQQQDLHLPtSTVRESLRFSaylrqpksVSkSEKMEYvEEVIKLLEME-- 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 529 iskfSEKDNIVlGEGGITLSGGQRARISLA-RAVYKDADLYLLDSPFGYLDVLTEKEIfescvCKLM---ANKTR-ILVT 603
Cdd:TIGR00956 889 ----SYADAVV-GVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQTAWSI-----CKLMrklADHGQaILCT 958
|
250 260 270
....*....|....*....|....*....|
gi 57526399 604 SkmeHLKKA------DKILILHEG--SVYF 625
Cdd:TIGR00956 959 I---HQPSAilfeefDRLLLLQKGgqTVYF 985
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1223-1378 |
2.93e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 44.94 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQwRK---------------- 1285
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETpDSGRIMLDGQDITHVPAEN-RHvntvfqsyalfphmtv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1286 ----AFGVIPQKVfifsgtfrknldpyeqwSDQEIWK-VADevGLRSV-IEQF----PGKldfvlvdggcvLSHGHKQLM 1355
Cdd:PRK09452 104 fenvAFGLRMQKT-----------------PAAEITPrVME--ALRMVqLEEFaqrkPHQ-----------LSGGQQQRV 153
|
170 180
....*....|....*....|...
gi 57526399 1356 CLARSVLSKAKILLLDEPSAHLD 1378
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALD 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
434-579 |
3.02e-04 |
|
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: 45.16 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 434 LLGTPVLKdisfkieRGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKI-----------KHSG---------------RI 487
Cdd:COG1245 90 LYGLPVPK-------KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGtelqdyfkklangeiKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 488 SFCSQYSWIMP----GTIKDNIifgVSYDEY-RYRSVIKACQLEE----DISkfsekdnivlgeggiTLSGGQRARISLA 558
Cdd:COG1245 163 AHKPQYVDLIPkvfkGTVRELL---EKVDERgKLDELAEKLGLENildrDIS---------------ELSGGELQRVAIA 224
|
170 180
....*....|....*....|.
gi 57526399 559 RAVYKDADLYLLDSPFGYLDV 579
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLDI 245
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1223-1403 |
3.13e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 44.33 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLlaflrllntkgEIQIDGVSWDSITLQQWRK-AFGVIPQKVFIFSG-- 1299
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLV-----------RVVLGLVAPDEGVIKRNGKlRIGYVPQKLYLDTTlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 -TFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1378
Cdd:PRK09544 84 lTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190
....*....|....*....|....*....|...
gi 57526399 1379 pITYQI--------IRRTLkqafaDCTVILSEH 1403
Cdd:PRK09544 153 -VNGQValydlidqLRREL-----DCAVLMVSH 179
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1228-1379 |
3.72e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 44.34 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQ----WRKAFGVIPQ--KVFIFSGT 1300
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1301 FRKNLDPYEQ---WSDQEIWKVADE----VGLRsviEQFPGKLDFvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEP 1373
Cdd:PRK13643 102 VLKDVAFGPQnfgIPKEKAEKIAAEklemVGLA---DEFWEKSPF-------ELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
....*.
gi 57526399 1374 SAHLDP 1379
Cdd:PRK13643 172 TAGLDP 177
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1223-1407 |
5.50e-04 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 42.61 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1223 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEI------------QIDGVSW-------DSITLQQ 1282
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAgVLRPTSGTVrraggarvayvpQRSEVPDslpltvrDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1283 WRKafgvipqkvfifsgtfRKNLDPYEQWSDQEIWKVADEVGL-----RSVIEqfpgkldfvlvdggcvLSHGHKQLMCL 1357
Cdd:NF040873 83 WAR----------------RGLWRRLTRDDRAAVDDALERVGLadlagRQLGE----------------LSGGQRQRALL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 57526399 1358 ARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFAD-CTVILSEHRIEA 1407
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLEL 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1227-1408 |
5.85e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1227 ILENISFSISPGQRVGLLGRTGSGKSTLLLAFLR-LLNTKGEIQIDG---VSwdsiTLQQ--WRKAFGvipqKVFIFS-- 1298
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGeVLLDDGRIIYEQdliVA----RLQQdpPRNVEG----TVYDFVae 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1299 --GTFRKNLDPYEQWSDQeiwkVADE---------VGLRSVIE-----QFPGKLDFVLVDGG-------CVLSHGHKQLM 1355
Cdd:PRK11147 90 giEEQAEYLKRYHDISHL----VETDpseknlnelAKLQEQLDhhnlwQLENRINEVLAQLGldpdaalSSLSGGWLRKA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 1356 CLARSVLSKAKILLLDEPSAHLDPITYQIIRRTLKqAFADCTVILSEHR--IEAM 1408
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK-TFQGSIIFISHDRsfIRNM 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
439-578 |
6.02e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPS--EGKIKHSG---------RIS-FCSQYSWIMPG-TIKDNI 505
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkkqetfaRISgYCEQNDIHSPQvTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 506 IFG--------VSYDEyryrSVIKACQLEEDISKFSEKDNIVlGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGY 576
Cdd:PLN03140 975 IYSaflrlpkeVSKEE----KMMFVDEVMELVELDNLKDAIV-GLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
..
gi 57526399 577 LD 578
Cdd:PLN03140 1050 LD 1051
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1228-1385 |
6.62e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTK-GEIQIDGVSWDSIT---LQQWRKAFGvipqkvFIFSGTFrK 1303
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSpgkLQALRRDIQ------FIFQDPY-A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1304 NLDPYEQ--WSDQEIWKV----------------ADEVGLRSVIE-QFPGKldfvlvdggcvLSHGHKQLMCLARSVLSK 1364
Cdd:PRK10261 413 SLDPRQTvgDSIMEPLRVhgllpgkaaaarvawlLERVGLLPEHAwRYPHE-----------FSGGQRQRICIARALALN 481
|
170 180
....*....|....*....|..
gi 57526399 1365 AKILLLDEPSAHLD-PITYQII 1385
Cdd:PRK10261 482 PKVIIADEAVSALDvSIRGQII 503
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
439-628 |
9.45e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 439 VLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELepSEGKIKHSGRISfcsqyswimpGTIKDNIIFGVSYDEYRY-- 516
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL--TGGGAPRGARVT----------GDVTLNGEPLAAIDAPRLar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 517 -RSVIKacQLEEDISKFSEKDNIVLG--------------EGGI-------------------TLSGGQRARISLARAVY 562
Cdd:PRK13547 84 lRAVLP--QAAQPAFAFSAREIVLLGrypharragalthrDGEIawqalalagatalvgrdvtTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 57526399 563 K---------DADLYLLDSPFGYLDVLTEKEIFEScvCKLMANKTRILVTSKMEHL----KKADKILILHEGSVYFYGT 628
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDT--VRRLARDWNLGVLAIVHDPnlaaRHADRIAMLADGAIVAHGA 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
437-489 |
1.06e-03 |
|
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: 43.52 E-value: 1.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIkhSGRISF 489
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHP--SGSILF 73
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1214-1392 |
1.14e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1214 KDLTAKYIDGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSITLQQWRKAFGVIPQ 1292
Cdd:PRK10522 326 RNVTFAYQDNGFS-VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTgLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1293 KVFIFSgtfrKNLDPYEQWSDQEI---WkvADEVGLRSvieqfpgKLDFvlvDGGCV----LSHGHKQLMCLARSVLSKA 1365
Cdd:PRK10522 405 DFHLFD----QLLGPEGKPANPALvekW--LERLKMAH-------KLEL---EDGRIsnlkLSKGQKKRLALLLALAEER 468
|
170 180 190
....*....|....*....|....*....|.
gi 57526399 1366 KILLLDEPSAHLDP----ITYQIIRRTLKQA 1392
Cdd:PRK10522 469 DILLLDEWAADQDPhfrrEFYQVLLPLLQEM 499
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
442-573 |
1.15e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 442 DISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSG------------RISFCSQ----YSWImpgTIKDNI 505
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdagdiatrrRVGYMSQafslYGEL---TVRQNL 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 57526399 506 -----IFGVSYDEYRYR--SVIKACQLEEDISKFSEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSP 573
Cdd:NF033858 361 elharLFHLPAAEIAARvaEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1228-1379 |
1.23e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.42 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSWDSIT----LQQWRKAFGVIPQ--KVFIFSGT 1300
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNgLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1301 FRKNLDPYEQ---WSDQEIWKVADE-VGLRSVIEQFPGKLDFvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 1376
Cdd:PRK13649 103 VLKDVAFGPQnfgVSQEEAEALAREkLALVGISESLFEKNPF-------ELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
...
gi 57526399 1377 LDP 1379
Cdd:PRK13649 176 LDP 178
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1228-1408 |
1.33e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.09 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLlaflrllN--------TKGEIQIDGV------SWDSITL------QQwrkaF 1287
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLM-------KilyglyqpDSGEILIDGKpvrirsPRDAIALgigmvhQH----F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1288 GVIPQkvfiFS----------GTFRKNLDpyeqwsdqeiWKVADEVgLRSVIEQFPGKLDF-VLVDGgcvLSHGHKQ--- 1353
Cdd:COG3845 90 MLVPN----LTvaenivlglePTKGGRLD----------RKAARAR-IRELSERYGLDVDPdAKVED---LSVGEQQrve 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 57526399 1354 -LMCLARsvlsKAKILLLDEPSAHLDP----ITYQIIRRtLKQafADCTVILSEHRI-EAM 1408
Cdd:COG3845 152 iLKALYR----GARILILDEPTAVLTPqeadELFEILRR-LAA--EGKSIIFITHKLrEVM 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1211-1252 |
1.58e-03 |
|
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: 42.75 E-value: 1.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 57526399 1211 MTVKDLTAKYIDGGNA--ILENISFSISPGQRVGLLGRTGSGKS 1252
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKS 50
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1227-1406 |
1.74e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.48 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1227 ILENISFSISPGQRVGLLGRTGSGKSTLLlaflrllntkgeiqidgvswdsitlqqwRKAFGVIPQKVfiFSGTFRKnld 1306
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLL----------------------------RLLAGALKGTP--VAGCVDV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1307 PYEQWSDQeiwkvadevglRSVIEQFPGKLDF-----VLVDGGCV-----------LSHGHKQLMCLARSVLSKAKILLL 1370
Cdd:COG2401 92 PDNQFGRE-----------ASLIDAIGRKGDFkdaveLLNAVGLSdavlwlrrfkeLSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 57526399 1371 DEPSAHLDPITYQIIRRTLKQAF--ADCTVILSEHRIE 1406
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHHYD 198
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
960-1120 |
1.92e-03 |
|
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: 42.09 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 960 PMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQP---YIFLATVPVIAAFILLRGYF--- 1033
Cdd:cd18576 83 PLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLLMLATVPVVVLVAVLFGRRirk 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1034 LHTSQQLKQLESegrspiFTHLVTSLKGLWTLRAFGRQPYFETLFHKALN--LHTAnwfLYLSTLR-WFqmrieMIFVIF 1110
Cdd:cd18576 163 LSKKVQDELAEA------NTIVEETLQGIRVVKAFTREDYEIERYRKALErvVKLA---LKRARIRaLF-----SSFIIF 228
|
170
....*....|
gi 57526399 1111 FIAVTFISIL 1120
Cdd:cd18576 229 LLFGAIVAVL 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1228-1451 |
2.00e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 41.92 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTK------GEIQIDGVSWDSITLQQWRKAFGVIPQ--KVFIFSG 1299
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgqtivGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1300 TFRKNL--DPYEQWSD-QEIWK-VADEVGLRSVIEQFPGKLDFVLvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSA 1375
Cdd:PRK13645 107 TIEKDIafGPVNLGENkQEAYKkVPELLKLVQLPEDYVKRSPFEL-------SGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1376 HLDPITYQ----IIRRTLKQAFAdcTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQRMLSEKSLFRQ-AISPADRLK 1449
Cdd:PRK13645 180 GLDPKGEEdfinLFERLNKEYKK--RIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSNQELLTKiEIDPPKLYQ 257
|
..
gi 57526399 1450 LL 1451
Cdd:PRK13645 258 LM 259
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1219-1253 |
2.04e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 2.04e-03
10 20 30
....*....|....*....|....*....|....*
gi 57526399 1219 KYIDGGNAILENISFSISPGQRVGLLGRTGSGKST 1253
Cdd:PRK11819 14 KVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKST 48
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1216-1384 |
2.08e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 41.90 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1216 LTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGVSWDSITLQQWRKAFGVIPQKV 1294
Cdd:PRK10253 13 LTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1295 FIFSGTFRKNLDPYEQWSDQEI---WKVADEVGLRSVIeQFPGKLDFVL--VDggcVLSHGHKQLMCLARSVLSKAKILL 1369
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQPLftrWRKEDEEAVTKAM-QATGITHLADqsVD---TLSGGQRQRAWIAMVLAQETAIML 166
|
170
....*....|....*
gi 57526399 1370 LDEPSAHLDpITYQI 1384
Cdd:PRK10253 167 LDEPTTWLD-ISHQI 180
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1227-1403 |
2.36e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 42.34 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1227 ILENISFSISPGQRVGLLGRTGSGKST--LLLAFLRLLNTK--GEIQIDGVswdSITLQQWRKAFGVIPQ-KVFI----- 1296
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTlmNALAFRSPKGVKgsGSVLLNGM---PIDAKEMRAISAYVQQdDLFIptltv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1297 -----FSGTFRKNLDPYEQWSDQEIWKVADEVGLRS---VIEQFPGKLDfvlvdggcVLSHGHKQLMCLARSVLSKAKIL 1368
Cdd:TIGR00955 117 rehlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcanTRIGVPGRVK--------GLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 57526399 1369 LLDEPSAHLDPIT-YQIIRRTLKQAFADCTVILSEH 1403
Cdd:TIGR00955 189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1347-1387 |
2.37e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 41.61 E-value: 2.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 57526399 1347 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP--------ITYQIIRR 1387
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPktaalvleLTEKIVEE 197
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1237-1403 |
2.46e-03 |
|
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: 41.58 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1237 PGQRVGLLGRTGSGKSTLLLAFLrllntkGEIQ------IDGVSWDSItLQQWRkafGVIPQKVF--IFSGTFRKNLDPy 1308
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILA------GKLKpnlgkfDDPPDWDEI-LDEFR---GSELQNYFtkLLEGDVKVIVKP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1309 eQWSDQ----------EIWKVADEVG-LRSVIEQFpgKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 1377
Cdd:cd03236 94 -QYVDLipkavkgkvgELLKKKDERGkLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|..
gi 57526399 1378 DpiTYQ------IIRRTLKQAFAdctVILSEH 1403
Cdd:cd03236 171 D--IKQrlnaarLIRELAEDDNY---VLVVEH 197
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
437-638 |
2.55e-03 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 437 TPVLKDISFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGR------------ISFCSQYSWImpgtikDN 504
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisdvhqnMGYCPQFDAI------DD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 505 IIFGVS--YDEYRYRSVIKacqleEDISKFSekdNIVLGEGGITL---------SGGQRARISLARAVYKDADLYLLDSP 573
Cdd:TIGR01257 2026 LLTGREhlYLYARLRGVPA-----EEIEKVA---NWSIQSLGLSLyadrlagtySGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 57526399 574 FGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSVYFYGTFSELQNQRPD 638
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFGD 2163
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1228-1429 |
2.78e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFL-RLLNTKGEIQIDGVSwdsitlQQWRKAFGVIPQKVFIFSgtfrknld 1306
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSgNYQPDAGSILIDGQE------MRFASTTAALAAGVAIIY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1307 pyeqwsdQEIWKVADevglRSVIE-----QFPGKLDFvlVDGGCV-----------------------LSHGHKQLMCLA 1358
Cdd:PRK11288 86 -------QELHLVPE----MTVAEnlylgQLPHKGGI--VNRRLLnyeareqlehlgvdidpdtplkyLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1359 RSVLSKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILS-EHRIEAMLE-CQRFLVIEE-NKVRQYDSIQ 1429
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYvSHRMEEIFAlCDAITVFKDgRYVATFDDMA 226
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
894-1140 |
2.81e-03 |
|
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: 41.69 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 894 NSTKNASNSYAVIITSTSSYYIFYIYVGVAdtLLALGLFRGLPLVHTLITVSKTLHHKMLQSVLQAPMSTLNTLKTGGIL 973
Cdd:cd18577 30 TDFGSGESSPDEFLDDVNKYALYFVYLGIG--SFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 974 NRFSKDIAVLDDL----LPLTIFDFIQLL-LIVIGavvvvsvlqpYIF--------LATVPVIAAFILLRGYFLHTSQQl 1040
Cdd:cd18577 108 SRLTSDTNLIQDGigekLGLLIQSLSTFIaGFIIA----------FIYswkltlvlLATLPLIAIVGGIMGKLLSKYTK- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1041 KQLESEGR-SPIFTHLVTSLKglwTLRAFGRQPYFETLFHKALNlHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFI-- 1117
Cdd:cd18577 177 KEQEAYAKaGSIAEEALSSIR---TVKAFGGEEKEIKRYSKALE-KARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWyg 252
|
250 260
....*....|....*....|...
gi 57526399 1118 SILTTgEGEGRVGIILTLAMNIM 1140
Cdd:cd18577 253 SRLVR-DGEISPGDVLTVFFAVL 274
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1228-1406 |
3.35e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 41.16 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDGvswDSITLQQWRKAFGVIPQKVFI---------F 1297
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTIGE---RVITAGKKNKKLKPLRKKVGIvfqfpehqlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1298 SGTFRK-------NLDPYEQWSDQEIWKVADEVGL-RSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1369
Cdd:PRK13634 100 EETVEKdicfgpmNFGVSEEDAKQKAREMIELVGLpEELLARSPFE-----------LSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 57526399 1370 LDEPSAHLDPITyqiiRRTLKQAFA------DCTVILSEHRIE 1406
Cdd:PRK13634 169 LDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSME 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
436-585 |
3.97e-03 |
|
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: 41.73 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 436 GTPVLKDISFKIERGQLLAVAGSTGAGKtSLLMMIMGELEPS---EGKIKHSGR--------------ISFCSQYSWIMP 498
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGK-STLMKILSGVYPHgtwDGEIYWSGSplkasnirdteragIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 499 G-TIKDNIIFG---------VSYDEYRYRSVIKACQLEEDISKfsekDNIVLGEGGitlsGGQRARISLARAVYKDADLY 568
Cdd:TIGR02633 92 ElSVAENIFLGneitlpggrMAYNAMYLRAKNLLRELQLDADN----VTRPVGDYG----GGQQQLVEIAKALNKQARLL 163
|
170
....*....|....*..
gi 57526399 569 LLDSPFGyldVLTEKEI 585
Cdd:TIGR02633 164 ILDEPSS---SLTEKET 177
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
944-1120 |
4.17e-03 |
|
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: 40.87 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 944 VSKTLHHKMLQSVLQAPMSTLNTLKTGGILNRFSKDIAVLDDLLPLTIFDFIQLLLIVIGAVVVVSVLQPY---IFLATV 1020
Cdd:cd18552 70 VVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKltlIALVVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1021 PVIAAFI-LLRGYFLHTSQqlKQLESEGRspIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNlhtanwflylsTLRWF 1099
Cdd:cd18552 150 PLAALPIrRIGKRLRKISR--RSQESMGD--LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANE-----------RLRRL 214
|
170 180
....*....|....*....|....*..
gi 57526399 1100 QMRIEMI------FVIFFIAVTFISIL 1120
Cdd:cd18552 215 SMKIARAralsspLMELLGAIAIALVL 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1211-1377 |
4.45e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLL---NTKGEIQIDG--VSWDSITLQQwRK 1285
Cdd:PRK13549 6 LEMKNITKTF--GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYEGEIIFEGeeLQASNIRDTE-RA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1286 AFGVIPQKVfifsgTFRKNLdpyeqwsdqeiwKVADEVGLRSVIEQFpGKLDFVLVDGGCV------------------L 1347
Cdd:PRK13549 83 GIAIIHQEL-----ALVKEL------------SVLENIFLGNEITPG-GIMDYDAMYLRAQkllaqlkldinpatpvgnL 144
|
170 180 190
....*....|....*....|....*....|
gi 57526399 1348 SHGHKQLMCLARSVLSKAKILLLDEPSAHL 1377
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1228-1403 |
5.15e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.30 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1228 LENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLNTKGEIQIDGVS---WDSITL--------QQWRKAFGVipqKVFI 1296
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPleaWSAAELarhraylsQQQTPPFAM---PVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 1297 FsgtfrknLDPYEQWSDQEiwkVADEVGLRSVIEQFpgKLDFVLVDGGCVLSHGHKQLMCLARSVL-------SKAKILL 1369
Cdd:PRK03695 89 Y-------LTLHQPDKTRT---EAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 57526399 1370 LDEPSAHLDpIT-----YQIIRRTLKQAFAdctVILSEH 1403
Cdd:PRK03695 157 LDEPMNSLD-VAqqaalDRLLSELCQQGIA---VVMSSH 191
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1211-1253 |
5.32e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.29 E-value: 5.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKST 1253
Cdd:PRK11701 7 LSVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTT 47
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
440-571 |
5.92e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57526399 440 LKDISFKIERGQLLA------------VAGSTGAGKTSLLMMIMGELEPSEGKIK-HSGRIS-----FCS----QYSWIM 497
Cdd:PRK13541 4 LHQLQFNIEQKNLFDlsitflpsaityIKGANGCGKSSLLRMIAGIMQPSSGNIYyKNCNINniakpYCTyighNLGLKL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 498 PGTIKDNIIFGVSYdeyrYRSVIkacQLEEDISKFSEKDniVLGEGGITLSGGQRARISLARAVYKDADLYLLD 571
Cdd:PRK13541 84 EMTVFENLKFWSEI----YNSAE---TLYAAIHYFKLHD--LLDEKCYSLSSGMQKIVAIARLIACQSDLWLLD 148
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1211-1280 |
6.48e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 40.07 E-value: 6.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 57526399 1211 MTVKDLTAKYidGGNAILENISFSISPGQRVGLLGRTGSGKSTLLLAFLRLLN-TKGEIQIDG---VSWDSITL 1280
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPpDSGEVLVDGldvATTPSREL 73
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1347-1389 |
8.62e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.45 E-value: 8.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 57526399 1347 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTL 1389
Cdd:PRK13543 138 LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| |
