|
Name |
Accession |
Description |
Interval |
E-value |
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-1464 |
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: 2390.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1 MQKSPLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSADSADHLSEKLEREWDREQAS-KKNPQLIHALRRCFFW 79
Cdd:TIGR01271 1 MQRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASaKKNPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 80 RFLFYGILLYLGEVTKAVQPVLLGRIIASYDPENKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSL 159
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 160 IYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAI 239
Cdd:TIGR01271 161 IYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 240 LGKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVF 319
Cdd:TIGR01271 241 LGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 320 LSVLPYTVINGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSFGMIRKIQDFLQKQEYKVLEYNLMTTGIIMENVTA 399
Cdd:TIGR01271 321 LSVVPYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 400 FWEEGFGELLEKVQQSNGDRKHSSDENNVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASE 479
Cdd:TIGR01271 401 SWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 480 GIIKHSGRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLA 559
Cdd:TIGR01271 481 GKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 560 RAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQSLRPD 639
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 640 FSSKLMGYDTFDQFTEERRSSILTETLRRFSVDDSSAP--WSKP-KQSFRQTG-EVGEKRKNS-ILNSFSSVRKISIVQK 714
Cdd:TIGR01271 641 FSSLLLGLEAFDNFSAERRNSILTETLRRVSIDGDSTVfsGPETiKQSFKQPPpEFAEKRKQSiILNPIASARKFSFVQM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 715 TPL-----CIDGESDDLQEKRLSLVPDSEQGEAALPRSNMIATGPTFPGRRRQSVLDLMTFTpNSGSSNLQRTRTSIRKI 789
Cdd:TIGR01271 721 GPQkaqatTIEDAVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHS-NRGENRREQLQTSFRKK 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 790 SLVPQ--ISLNEVDVYSRRLSQDSTLNITEEINEEDLKECFLDDVIKIPPVTTWNTYLRYFTLHKGLLLVLIWCVLVFLV 867
Cdd:TIGR01271 800 SSITQqnELASELDIYSRRLSKDSVYEISEEINEEDLKECFADERENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLA 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 868 EVAASLFVLWLLKNNPVNSG---NNGTKISN--SSYVVIITSTSFYYIFYIYVGVADTLLALSLFRGLPLVHTLITASKI 942
Cdd:TIGR01271 880 EVAASLLGLWLITDNPSAPNyvdQQHANASSpdVQKPVIITPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKR 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 943 LHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFI 1022
Cdd:TIGR01271 960 LHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFI 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1023 LLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIF 1102
Cdd:TIGR01271 1040 MLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIF 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1103 VLFFIVVTFISILTTGEGEGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDIQTEESMYTqiiKELPREG 1182
Cdd:TIGR01271 1120 VFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPS---GGGGKYQ 1196
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1183 SSDVLVIKNEHVKKsdIWPSGGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGD 1262
Cdd:TIGR01271 1197 LSTVLVIENPHAQK--CWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE 1274
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1263 IEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVL 1342
Cdd:TIGR01271 1275 IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVL 1354
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1343 SHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDS 1422
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....
gi 14141185 1423 LQALLSEKSIFQQAISSSEKMRFFQG--RHSSKHKPRTQITALK 1464
Cdd:TIGR01271 1435 IQKLLNETSLFKQAMSAADRLKLFPLhrRNSSKRKPQPKITALR 1478
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
389-670 |
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: 569.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 389 TTGIIMENVTAFWEEGFGELLEKVQQSNGDRKHSSDENNVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLL 468
Cdd:cd03291 1 TTGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 469 MLILGELEASEGIIKHSGRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTL 548
Cdd:cd03291 81 MLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYG 628
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 14141185 629 TFSELQSLRPDFSSKLMGYDTFDQFTEERRSSILTETLRRFS 670
Cdd:cd03291 241 TFSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRRFS 282
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
839-1162 |
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: 541.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 839 TTWNTYLRYFTLHKGLLLVLIWCVLVFLVEVAASLFVLWLLKNNPVNSGNNGTKISNSSYVVIITSTSFYYIFYIYVGVA 918
Cdd:cd18600 1 TTWNTYLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 919 DTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIG 998
Cdd:cd18600 81 DSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 999 AIIVVSALQPYIFLATVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALN 1078
Cdd:cd18600 161 AITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1079 LHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRV 1158
Cdd:cd18600 241 LHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
....
gi 14141185 1159 FKFI 1162
Cdd:cd18600 321 FKFI 324
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1204-1464 |
2.10e-171 |
|
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: 513.63 E-value: 2.10e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1204 GEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDGVSWNSVTLQEWRKAFG 1283
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKII 1363
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1364 LLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQAISSSEKM 1443
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
|
250 260
....*....|....*....|...
gi 14141185 1444 RFFQGRHSSKH--KPRTQITALK 1464
Cdd:cd03289 241 KLFPRRNSSKSkrKPRPQIQALQ 263
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-1433 |
8.92e-163 |
|
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: 531.44 E-value: 8.92e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 5 PLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSADSADHLSEKLEREWDREQAS--------------------- 63
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKtrkqpvsavygkkdpskpkgs 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 64 -------------------KKNPQLIHALRRCFFWRFLFYGILLYLGEVTKAVQPVLLGRIIASYDpeNKVERSIAIYLG 124
Cdd:TIGR00957 283 sqldaneevealivksphkPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVN--DPMAPDWQGYFY 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 125 IGLclLFI---VRTLLLHPAIFGLHRIGMQMRTAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFI 201
Cdd:TIGR00957 361 TGL--LFVcacLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 202 WIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAILGKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAM 281
Cdd:TIGR00957 439 WSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 282 EKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVFLSVLPYTVI---NGIVLRKIFTTISFCIVLRMSVTrQFPTAV 358
Cdd:TIGR00957 519 LDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVdenNILDAEKAFVSLALFNILRFPLN-ILPMVI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 359 QIWYDSFGMIRKIQDFLQKQEYK--VLEYNLMTTG----IIMENVTAFWEEGFgellekvqqsngdrkhssdennvsfsh 432
Cdd:TIGR00957 598 SSIVQASVSLKRLRIFLSHEELEpdSIERRTIKPGegnsITVHNATFTWARDL--------------------------- 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 433 lclvgNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSQFSWIMPGTIKENIIFGVSY 512
Cdd:TIGR00957 651 -----PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKAL 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 513 DEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVC 592
Cdd:TIGR00957 726 NEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 593 K--LMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQSlrpdfssklmgydtfdqfteerRSSILTETLRRFS 670
Cdd:TIGR00957 806 PegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ----------------------RDGAFAEFLRTYA 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 671 VDDSsapwskpkqsfrqtgevgekrknsilnsfssvrkisivqktplciDGESDDlqekrlslvpDSEQGEAAlprsnmi 750
Cdd:TIGR00957 864 PDEQ---------------------------------------------QGHLED----------SWTALVSG------- 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 751 atgptfPGRRRQSVLDLMTFTPNSGSsNLQRTRTSIRKISlvpqislnevDVYSRRLSQDSTLNITEEiNEED--LKECF 828
Cdd:TIGR00957 882 ------EGKEAKLIENGMLVTDVVGK-QLQRQLSASSSDS----------GDQSRHHGSSAELQKAEA-KEETwkLMEAD 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 829 LDDVIKIPPVTTWNtYLRYFtlhkGLLLVLIWCVLVFLVEVAASLFVLWL--LKNNP-VNSGNNGTKISNSSYVVIitst 905
Cdd:TIGR00957 944 KAQTGQVELSVYWD-YMKAI----GLFITFLSIFLFVCNHVSALASNYWLslWTDDPmVNGTQNNTSLRLSVYGAL---- 1014
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 906 sfyyifYIYVGVADTLLALSLFRGLplvhtlITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLT 985
Cdd:TIGR00957 1015 ------GILQGFAVFGYSMAVSIGG------IQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPV 1082
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 986 IFDFIQLVFIVIGAIIVVSALQPyIFLATVPGL-VVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFR 1064
Cdd:TIGR00957 1083 IKMFMGSLFNVIGALIVILLATP-IAAVIIPPLgLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE 1161
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1065 RQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMI---FVLFfiVVTFISILTTGEGEGTAGIILTLAMNIMSTLQWA 1141
Cdd:TIGR00957 1162 EQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWL 1239
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1142 VNSSIDTDSLMRSVSRVFKFIDIQTEESMytQIIKELPREGssdvlviknehvkksdiWPSGGEMVVKDLTVKYMDDGNA 1221
Cdd:TIGR00957 1240 VRMSSEMETNIVAVERLKEYSETEKEAPW--QIQETAPPSG-----------------WPPRGRVEFRNYCLRYREDLDL 1300
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-NIKGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNL 1300
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINeSAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1301 DPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVI 1380
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1381 RRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIF 1433
Cdd:TIGR00957 1461 QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-1440 |
4.86e-160 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 523.38 E-value: 4.86e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 5 PLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSADSADHLSEKLEREWdREQASKKNPQLIHALRRCFFWRFLFY 84
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCW-TEESRRPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 85 GILLYLGEVTKAVQPVLLGRIIASY---DPE-NKVERSIAIYLGIGLCLLFIVRTLLlhpaifGLHRIGMQMRTAMFSLI 160
Cdd:PLN03232 307 GIFKIGHDLSQFVGPVILSHLLQSMqegDPAwVGYVYAFLIFFGVTFGVLCESQYFQ------NVGRVGFRLRSTLVAAI 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAIL 240
Cdd:PLN03232 381 FHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 241 GKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVFL 320
Cdd:PLN03232 461 VRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLV 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 321 SVLPYTVING-IVLRKIFTTISFCIVLRMSVTrQFPTAVQIWYDSFGMIRKIQDFLQKQEyKVLEYNLM----TTGIIME 395
Cdd:PLN03232 541 SFGVFVLLGGdLTPARAFTSLSLFAVLRSPLN-MLPNLLSQVVNANVSLQRIEELLLSEE-RILAQNPPlqpgAPAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 396 NVTAFWeegfgellekvqqsngDRKHSsdennvsfshlclvgNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGEL 475
Cdd:PLN03232 619 NGYFSW----------------DSKTS---------------KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 476 ---EASEGIIKhsGRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQ 552
Cdd:PLN03232 668 shaETSSVVIR--GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQ 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 553 RARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSE 632
Cdd:PLN03232 746 KQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 633 LQslrpdfssklmgydtfdqfteerRSSILTETLRrfsvddssapwsKPKQSFRQTGEVGEKRKNsilnsfssvrkisIV 712
Cdd:PLN03232 826 LS-----------------------KSGSLFKKLM------------ENAGKMDATQEVNTNDEN-------------IL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 713 QKTPLCidgeSDDLQEKRLslvpdseqgeaalprsnmiatGPTFPGRRRQSVLdlmtftpnsgssnlqrtrtsirkislv 792
Cdd:PLN03232 858 KLGPTV----TIDVSERNL---------------------GSTKQGKRGRSVL--------------------------- 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 793 pqislnevdvysrrlsqdstlnITEEINEEDlkecflddvikippVTTWNTYLRYFTLHKGLLLVLIWCVLVFLVEVaas 872
Cdd:PLN03232 886 ----------------------VKQEERETG--------------IISWNVLMRYNKAVGGLWVVMILLVCYLTTEV--- 926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 873 lfvlwllknnpvnsgnngTKISNSSYVVIITSTS--------FYYIFYIYVGVADtlLALSLFRGLPLVHTLITASKILH 944
Cdd:PLN03232 927 ------------------LRVSSSTWLSIWTDQStpksyspgFYIVVYALLGFGQ--VAVTFTNSFWLISSSLHAAKRLH 986
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 945 RKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILL 1024
Cdd:PLN03232 987 DAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAA 1066
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1025 RAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIF-V 1103
Cdd:PLN03232 1067 YLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGgV 1146
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1104 LFFIVVTFiSILTTGEGE------GTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDiqteesmytqiike 1177
Cdd:PLN03232 1147 MIWLTATF-AVLRNGNAEnqagfaSTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYID-------------- 1211
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1178 LPREGSSdvlVIKNEHVKKSdiWPSGGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML 1257
Cdd:PLN03232 1212 LPSEATA---IIENNRPVSG--WPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV 1286
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1258 NI-KGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLV 1336
Cdd:PLN03232 1287 ELeKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVS 1366
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1337 DGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESN 1416
Cdd:PLN03232 1367 EGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQ 1446
|
1450 1460
....*....|....*....|....*
gi 14141185 1417 VWQYDSLQALLS-EKSIFQQAISSS 1440
Cdd:PLN03232 1447 VLEYDSPQELLSrDTSAFFRMVHST 1471
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-1440 |
1.58e-148 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 493.87 E-value: 1.58e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 5 PLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSADSADHLSEKLEREWDrEQASKKNPQLIHALRRCFFWRFLFY 84
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWD-EELKKPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 85 GILLYLGEVTKAVQPVLLGRIIASYDPENKVER----SIAIYLGIGLCLLFIVRTLLlhpaifGLHRIGMQMRTAMFSLI 160
Cdd:PLN03130 307 GFFKIGNDLSQFVGPLLLNLLLESMQNGEPAWIgyiyAFSIFVGVVLGVLCEAQYFQ------NVMRVGFRLRSTLVAAV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAIL 240
Cdd:PLN03130 381 FRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 241 GKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVFL 320
Cdd:PLN03130 461 ISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVV 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 321 SVLPYTVINGIVL-RKIFTTISFCIVLRMSVTrQFPTAVQIWYDSFGMIRKIQDFLQKQEyKVLEYNLMTT----GIIME 395
Cdd:PLN03130 541 SFGVFTLLGGDLTpARAFTSLSLFAVLRFPLF-MLPNLITQAVNANVSLKRLEELLLAEE-RVLLPNPPLEpglpAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 396 NVTAFWEegfgellekvqqSNGDRkhssdennvsfshlclvgnPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGEL 475
Cdd:PLN03130 619 NGYFSWD------------SKAER-------------------PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 476 EA-SEGIIKHSGRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRA 554
Cdd:PLN03130 668 PPrSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQ 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 555 RISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQ 634
Cdd:PLN03130 748 RVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 635 SLRPDFSsKLMgydtfdqfteERRSSI--LTETLRRFSVDDSSapwSKPKQsfrqTGEVGEKRKNSILNSFSSVRKISIV 712
Cdd:PLN03130 828 NNGPLFQ-KLM----------ENAGKMeeYVEENGEEEDDQTS---SKPVA----NGNANNLKKDSSSKKKSKEGKSVLI 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 713 QktplcidgesddlQEKRlslvpdsEQGeaalprsnmiatgptfpgrrrqsvldlmtftpnsgssnlqrtrtsirkislv 792
Cdd:PLN03130 890 K-------------QEER-------ETG---------------------------------------------------- 897
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 793 pqislnevdvysrrlsqdstlniteeineedlkecflddvikippVTTWNTYLRYFTLHKGLLLVLIwcvlVFLVEVAAS 872
Cdd:PLN03130 898 ---------------------------------------------VVSWKVLERYKNALGGAWVVMI----LFLCYVLTE 928
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 873 LFvlwllknnpvnsgnngtKISNSSYVVIITSTS-------FYYIFyIYVGVADTLLALSLFRGLPLVHTLITASKILHR 945
Cdd:PLN03130 929 VF-----------------RVSSSTWLSEWTDQGtpkthgpLFYNL-IYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHD 990
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 946 KMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILLR 1025
Cdd:PLN03130 991 AMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAY 1070
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1026 AYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLF 1105
Cdd:PLN03130 1071 LYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLM 1150
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1106 FIVVTFISILTTGEGEG------TAGIILTLAMNIMSTLQWAVN-SSIDTDSLmRSVSRVFKFIDIQTEESmytqiikel 1178
Cdd:PLN03130 1151 IWLTASFAVMQNGRAENqaafasTMGLLLSYALNITSLLTAVLRlASLAENSL-NAVERVGTYIDLPSEAP--------- 1220
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1179 pregssdvLVIKNEhvKKSDIWPSGGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN 1258
Cdd:PLN03130 1221 --------LVIENN--RPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVE 1290
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1259 I-KGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVD 1337
Cdd:PLN03130 1291 LeRGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSE 1370
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1338 GGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNV 1417
Cdd:PLN03130 1371 AGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
1450 1460
....*....|....*....|....
gi 14141185 1418 WQYDSLQALLS-EKSIFQQAISSS 1440
Cdd:PLN03130 1451 VEFDTPENLLSnEGSAFSKMVQST 1474
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
69-1447 |
3.25e-120 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 413.02 E-value: 3.25e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 69 LIHALRRCFFWRFLFygilLYLGEVTKAVQPVLLGRIIASYDPENKV-ERSIAiyLGIGLCLLFIVRTLLLHPAIFGLHR 147
Cdd:PTZ00243 238 LFAALPYYVWWQIPF----KLLSDVCTLTLPVLLKYFVKFLDADNATwGRGLG--LVLTLFLTQLIQSVCLHRFYYISIR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 148 IGMQMRTAMFSLIYKKTLKLSSRVLDK--ISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFC 225
Cdd:PTZ00243 312 CGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALM 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 226 GLGLLIILVIFQAILGKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFF 305
Cdd:PTZ00243 392 AVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 306 TSSAFFFSGFFVVFLSVLPYTVInGIVLRK--IFTTISFCIVLRMS---VTRQFPTAVQiWYDSFGMIRK---------- 370
Cdd:PTZ00243 472 TSFVNNATPTLMIAVVFTVYYLL-GHELTPevVFPTIALLGVLRMPffmIPWVFTTVLQ-FLVSIKRISTflecdnatcs 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 371 -IQDFlqkQEYKVLEYNLMTT---GIIMEN--VTAFW------------------------------------------- 401
Cdd:PTZ00243 550 tVQDM---EEYWREQREHSTAcqlAAVLENvdVTAFVpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedt 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 402 -------------EEGFGELLEKVQQSNGDRKHSSDENNVSFShlcLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLL 468
Cdd:PTZ00243 627 dygspssasrhivEGGTGGGHEATPTSERSAKTPKMKTDDFFE---LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 469 MLILGELEASEGIIKHSGRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTL 548
Cdd:PTZ00243 704 QSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYG 628
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 629 TFSelqslrpDFSsklmgydtfdqfteerRSSIlTETLRrfsvddssapwskpkqsfrqtgevGEKRKNSILNSFSSVRK 708
Cdd:PTZ00243 864 SSA-------DFM----------------RTSL-YATLA------------------------AELKENKDSKEGDADAE 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 709 ISivqktplcidgESDDLQEKRLSLVPDSEQGEAALPRSNMIATGPTfpgrrrqsvldlmtftpnsgssnlqrtrtsirk 788
Cdd:PTZ00243 896 VA-----------EVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDAA--------------------------------- 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 789 islvpqislnevdvysrrlsqDSTLNITEEineedlkecflddviKIPPVTTWNTYLRYFT----LHKGLLLVLIWCVlV 864
Cdd:PTZ00243 932 ---------------------AGRLMTREE---------------KASGSVPWSTYVAYLRfcggLHAAGFVLATFAV-T 974
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 865 FLVEVAASLFV-LWllknnpvnsGNNGTKISNSSYVVIitstsfyYIFYIYVGVADTLLALSLfrglpLVHTLITASKIL 943
Cdd:PTZ00243 975 ELVTVSSGVWLsMW---------STRSFKLSAATYLYV-------YLGIVLLGTFSVPLRFFL-----SYEAMRRGSRNM 1033
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 944 HRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFIL 1023
Cdd:PTZ00243 1034 HRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYR 1113
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1024 LRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFV 1103
Cdd:PTZ00243 1114 LMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSN 1193
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1104 LFFIVVTFISILTTGEGE-----GTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDIQTEESM--YTQIIK 1176
Cdd:PTZ00243 1194 IVVTVIALIGVIGTMLRAtsqeiGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEDMpeLDEEVD 1273
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1177 ELPREG--SSDV---LVIKNEHVKKSDIWP-SGGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLL 1250
Cdd:PTZ00243 1274 ALERRTgmAADVtgtVVIEPASPTSAAPHPvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLL 1353
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1251 SAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPG 1329
Cdd:PTZ00243 1354 LTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESE 1433
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1330 QLNFTLVDGGYVLSHGHKQLMCLARSVLSK-AKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQR 1408
Cdd:PTZ00243 1434 GIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDK 1513
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|...
gi 14141185 1409 FLVIEESNVWQYDSLQAL-LSEKSIFQ---QAISSSEKMRFFQ 1447
Cdd:PTZ00243 1514 IIVMDHGAVAEMGSPRELvMNRQSIFHsmvEALGRSEAKRFLQ 1556
|
|
| CFTR_R |
pfam14396 |
Cystic fibrosis TM conductance regulator (CFTR), regulator domain; |
639-844 |
9.18e-116 |
|
Cystic fibrosis TM conductance regulator (CFTR), regulator domain;
Pssm-ID: 464164 Cd Length: 213 Bit Score: 362.13 E-value: 9.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 639 DFSSKLMGYDTFDQFTEERRSSILTETLRRFSVD-DSSAPWSKP-KQSFRQTGEVGEKRKNS-ILNSFSSVRKISIVQKT 715
Cdd:pfam14396 1 DFSSLLMGLEAFDNFSAERRNSILTETLRRFSVDeDAGGSRNEPkKQSFKQTDDFNEKRKNSvILNPLAASRKFSIIQKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 716 PLCIDGESD---DLQEKRLSLVPDSEQGEAALPRSNMIATGPTFPGRRRQSVLDLMTFTPNSGSSNLQRTRTSIRKISLV 792
Cdd:pfam14396 81 QLQMNGIEEglsELPERRLSLVPESEQGEAALPRSNVLNTGPTLQGQRRQSVLALMTNTVAQGQGRREKGQSSFRKMSVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14141185 793 PQISL-NEVDVYSRRLSQDSTLNITEEINEEDLKECFLDDVIKIPPVTTWNTY 844
Cdd:pfam14396 161 PQSNLaSELDIYARRLSKDSVLDITEEINEEDLKECFADDIENVFETTTWNTY 213
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
83-372 |
7.95e-112 |
|
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: 354.63 E-value: 7.95e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 83 FYGILLYLGEVTKAVQPVLLGRIIASYDPENKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLIYK 162
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 163 KTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAILGK 242
Cdd:cd18594 81 KTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 243 MMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVFLSV 322
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 323 LPYTVI-NGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSFGMIRKIQ 372
Cdd:cd18594 241 VPYVLTgNTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
392-623 |
1.32e-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: 303.24 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 392 IIMENVTAFWEEGFGEllekvqqsngdrkhssdennvsfshlclvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLI 471
Cdd:cd03250 1 ISVEDASFTWDSGEQE-----------------------------TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 472 LGELEASEGIIKHSGRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGG 551
Cdd:cd03250 52 LGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 552 QRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCK-LMANKTRILVTSKMEHLRKADKILILHQGS 623
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGlLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1204-1422 |
7.18e-88 |
|
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: 285.16 E-value: 7.18e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1204 GEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1363 ILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDS 1422
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
837-1414 |
2.34e-79 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 273.96 E-value: 2.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 837 PVTTWNTYLRYFTLHKGLLLVLIwcvLVFLVEVAASLFVLWLLK---NNPVNSGNngtkisnssyvviitSTSFYYIFYI 913
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILAL---LLLLLSALLELLLPLLLGriiDALLAGGD---------------LSALLLLLLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 914 YVGVADTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLV 993
Cdd:COG1132 67 LLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 994 FIVIGAIIVVSALQPYIFLATVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLF 1073
Cdd:COG1132 147 VTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1074 HKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTAGII---LTLAMNIMSTLQWAVNSSIDTDS 1150
Cdd:COG1132 227 REANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLvafILYLLRLFGPLRQLANVLNQLQR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1151 LMRSVSRVFKFIDIQTEesmytqiIKELPREGSSDvlviknehvkksdiwPSGGEMVVKDLTVKYmDDGNAVLENISFSI 1230
Cdd:COG1132 307 ALASAERIFELLDEPPE-------IPDPPGAVPLP---------------PVRGEIEFENVSFSY-PGDRPVLKDISLTI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1231 SPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNL---DPNGKw 1306
Cdd:COG1132 364 PPGETVALVGPSGSGKSTLVNLLLRFYDPtSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPDAT- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1307 kDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQ 1386
Cdd:COG1132 443 -DEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER 521
|
570 580
....*....|....*....|....*...
gi 14141185 1387 AFAGCTVILCEHRIEAMLDCQRFLVIEE 1414
Cdd:COG1132 522 LMKGRTTIVIAHRLSTIRNADRILVLDD 549
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
854-1162 |
2.47e-77 |
|
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: 258.20 E-value: 2.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 854 LLLVLIWCVLVFLVEVAASLFVLWLLKNNPVNSGNNgtkisnssyvviitstSFYYIFYIYVGVADTLLALSLFRGLPLV 933
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSS----------------SGYYLGVYAALLVLASVLLVLLRWLLFV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 934 HTLITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLA 1013
Cdd:cd18580 65 LAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1014 TVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRW 1093
Cdd:cd18580 145 LPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1094 FQMRIDMIFVLFFIVVTFISILTTGE-GEGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFI 1162
Cdd:cd18580 225 LGLRLDLLGALLALVVALLAVLLRSSiSAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
857-1158 |
6.10e-76 |
|
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: 254.94 E-value: 6.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 857 VLIWCVLVFLVEVAASLFVL--WLLKNNPVNSGNNGTKI----SNSSYVVIITSTSFYYIFYIYVGVADTLLALSLFRGL 930
Cdd:cd18601 2 VFVFILLVLLNIAAQVLYVLsdWWLSYWANLEEKLNDTTdrvqGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 931 PLVHTLITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYI 1010
Cdd:cd18601 82 LFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1011 FLATVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLAT 1090
Cdd:cd18601 162 LIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLAT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1091 LRWFQMRIDMIFVLFFIVVTFISI-LTTGEGEGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRV 1158
Cdd:cd18601 242 SRWLAVRLDALCALFVTVVAFGSLfLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
818-1435 |
2.02e-67 |
|
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: 242.82 E-value: 2.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 818 EINEEDLKECFLDDVIKIPP----------VTTWNTYLRYFTLHKGLLL-VLIWCVLVFLVEVAASLFVLWLlknnpVNS 886
Cdd:COG2274 111 KLSLEEFAESWTGVALLLEPtpefdkrgekPFGLRWFLRLLRRYRRLLLqVLLASLLINLLALATPLFTQVV-----IDR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 887 GnngtkISNSSYVVIITSTSFYYIFYIYVGVadtllaLSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTISKLKAGG 966
Cdd:COG2274 186 V-----LPNQDLSTLWVLAIGLLLALLFEGL------LRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 967 ILNRFSkDIAILDDFLPLTIFD-FIQLVFIVIGaIIVVSALQPYIFLATVPGLVVFILLRAYFLHTAQQLKQLESEGRSP 1045
Cdd:COG2274 255 LASRFR-DVESIREFLTGSLLTaLLDLLFVLIF-LIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1046 IFTHLVTSLKGLWTLRAF----RRQTYFETLFHKALNL-----HTANWFMYLATLrwfqmridmIFVLFFIVVTFISILT 1116
Cdd:COG2274 333 RQSLLVETLRGIETIKALgaesRFRRRWENLLAKYLNArfklrRLSNLLSTLSGL---------LQQLATVALLWLGAYL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1117 TGEGEGTAGIILtlAMNIMStlqWAVNSSIdtdslMRSVSRVFKFIDIQTEESMYTQIIkELPREGSSDVLVIKNEHVKk 1196
Cdd:COG2274 404 VIDGQLTLGQLI--AFNILS---GRFLAPV-----AQLIGLLQRFQDAKIALERLDDIL-DLPPEREEGRSKLSLPRLK- 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1197 sdiwpsgGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-NIKGDIEIDGVSWNSVTL 1275
Cdd:COG2274 472 -------GDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRILIDGIDLRQIDP 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1276 QEWRKAFGVITQKVFIFSGTFRQNL-----DPNgkwkDEEIWKVADEVGLKSVIEQFPGQLNfTLV-DGGYVLSHGHKQL 1349
Cdd:COG2274 545 ASLRRQIGVVLQDVFLFSGTIRENItlgdpDAT----DEEIIEAARLAGLHDFIEALPMGYD-TVVgEGGSNLSGGQRQR 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1350 MCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSE 1429
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
....*.
gi 14141185 1430 KSIFQQ 1435
Cdd:COG2274 700 KGLYAE 705
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
83-371 |
2.44e-64 |
|
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: 220.56 E-value: 2.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 83 FYGILLYLGEVTKAVQPVLLGRIIASYDPENK-VERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLIY 161
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSsISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 162 KKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAILG 241
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 242 KMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVFLS 321
Cdd:cd18593 161 KLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 322 VLPYTVI-NGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSFGMIRKI 371
Cdd:cd18593 241 FLAYILLgNILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
959-1436 |
1.78e-62 |
|
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: 224.26 E-value: 1.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 959 ISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILL---RAYFL--HTAQ 1033
Cdd:COG4987 106 LARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLlplLAARLgrRAGR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1034 QLKQLESEGRspifTHLVTSLKGLWTLRAFRRQTYFEtlfhKALNLHTANWFMYLATLRWFQMRID--MIFVLFFIVVTF 1111
Cdd:COG4987 186 RLAAARAALR----ARLTDLLQGAAELAAYGALDRAL----ARLDAAEARLAAAQRRLARLSALAQalLQLAAGLAVVAV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1112 ISILTTGEGEGTAGIILtLAMNIMSTL--------------QWAvnssidtdSLMRSVSRVFkfidiqteesmytQIIKE 1177
Cdd:COG4987 258 LWLAAPLVAAGALSGPL-LALLVLAALalfealaplpaaaqHLG--------RVRAAARRLN-------------ELLDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1178 LPREgssdvlviknEHVKKSDIWPSGGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML 1257
Cdd:COG4987 316 PPAV----------TEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1258 NI-KGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNL---DPNGKwkDEEIWKVADEVGLKSVIEQFPGQLNF 1333
Cdd:COG4987 386 DPqSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRPDAT--DEELWAALERVGLGDWLAALPDGLDT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1334 TLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIE 1413
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|...
gi 14141185 1414 ESNVWQYDSLQALLSEKSIFQQA 1436
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
85-365 |
1.30e-57 |
|
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: 201.18 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 85 GILLYLGEVTKAVQPVLLGRIIASYDPENKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLIYKKT 164
Cdd:cd18579 3 GLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 165 LKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAILGKMM 244
Cdd:cd18579 83 LRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 245 VKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVFLSVLP 324
Cdd:cd18579 163 SKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFAT 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 14141185 325 YTVING-IVLRKIFTTISFCIVLRMsVTRQFPTAVQIWYDSF 365
Cdd:cd18579 243 YVLLGNpLTAAKVFTALSLFNLLRF-PLLMLPQAISSLIEAL 283
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1200-1422 |
4.70e-57 |
|
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: 196.48 E-value: 4.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1200 WPSGGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEW 1278
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1279 RKAFGVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVadevglksvieqfpgqlnFTLVDGGYVLSHGHKQLMCLARSVLS 1358
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 1359 KAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDS 1422
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
69-622 |
3.01e-54 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 200.39 E-value: 3.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 69 LIHALRRcfFWRFLFYGILLYLGE-VTKAVQPVLLGRIIASYdpENKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHR 147
Cdd:COG1132 12 LLRYLRP--YRGLLILALLLLLLSaLLELLLPLLLGRIIDAL--LAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 148 IGMQMRTAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLA-LAHFIWIAPLQVTLLMGLLWDL-LQFSAFC 225
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIGALVVLFVIdWRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 226 GLGLLIILVIFQAILGKMMVKYRDQRAA--KINERLVitsEIIDNIYSVKAYCWESAM----EKMIENLREVELKMTRka 299
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEAlaELNGRLQ---ESLSGIRVVKAFGREERElerfREANEELRRANLRAAR-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 300 aymrfftssafffsgffvvfLSVLPYTVINgivlrkIFTTISFCIVL----------RMSVTrQFPTAVQIwydSFGMIR 369
Cdd:COG1132 243 --------------------LSALFFPLME------LLGNLGLALVLlvggllvlsgSLTVG-DLVAFILY---LLRLFG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 370 KIQDFLQkqeykvlEYNLMTTGIimenvtAFWEEGFGELLEKVQQSNGDRKHSSDE-------NNVSFSHLclVGNPVLK 442
Cdd:COG1132 293 PLRQLAN-------VLNQLQRAL------ASAERIFELLDEPPEIPDPPGAVPLPPvrgeiefENVSFSYP--GDRPVLK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 443 NINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPGTIKENIIFG 509
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 510 V-SYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFE 588
Cdd:COG1132 438 RpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE 517
|
570 580 590
....*....|....*....|....*....|....
gi 14141185 589 ScVCKLMANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:COG1132 518 A-LERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
854-1162 |
4.62e-53 |
|
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: 188.93 E-value: 4.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 854 LLLVLiwcvLVFLVEVAASLFV-----LWLLKNNPVNSGNNGTKISNSSYVVIITSTSFYYIFYIYVGVAdtLLALSLFR 928
Cdd:cd18599 5 FLFVL----LLFILSVGSTVFSdwwlsYWLKQGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILV--ILLLSLIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 929 GLPLVHTLITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQP 1008
Cdd:cd18599 79 GFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1009 YIFLATVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYL 1088
Cdd:cd18599 159 WFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1089 ATLRWFQMRIDMIFVLFFIVVTFISILTTGE-GEGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFI 1162
Cdd:cd18599 239 CAMRWLAVRLDILAVLITLITALLVVLLKGSiSPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
859-1158 |
1.69e-52 |
|
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: 186.90 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 859 IWCVLVFLVEVAASLFVLWLLKnnpVNSGNNGTKISNSSYVViitSTSFYYIFYIYVGVADTLLalSLFRGLPLVHTLIT 938
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLG---IWASAYETSSALPPSEV---SVLYYLGIYALISLLSVLL--GTLRYLLFFFGSLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 939 ASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGL 1018
Cdd:cd18604 74 ASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1019 VVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRI 1098
Cdd:cd18604 154 ALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1099 DMIFVLFFIVVTFISILTTGEGEGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRV 1158
Cdd:cd18604 234 DLLGALFSFATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERI 293
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
992-1430 |
1.89e-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: 194.59 E-value: 1.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 992 LVFIVIGAIIVVSALqpyIFLATVPGLVVFILLrayFLHTAQQL--KQLESEGR-SpifTHLVTSLKGLWTLRAF---RR 1065
Cdd:COG4988 148 LILVAVFPLDWLSGL---ILLVTAPLIPLFMIL---VGKGAAKAsrRQWRALARlS---GHFLDRLRGLTTLKLFgraKA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1066 QTyfETLFHKALNLHTAnwfmylaTLRwfQMRIDM--IFVL-FF-------IVVTF-ISILTTGEGEGTAGIILTLA--- 1131
Cdd:COG4988 219 EA--ERIAEASEDFRKR-------TMK--VLRVAFlsSAVLeFFaslsialVAVYIgFRLLGGSLTLFAALFVLLLApef 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1132 ---MNIMSTlQW-----AVNSSidtdslmrsvSRVFKFIDIQTEEsmytqiikelPREGSsdvlviknehvkKSDIWPSG 1203
Cdd:COG4988 288 flpLRDLGS-FYharanGIAAA----------EKIFALLDAPEPA----------APAGT------------APLPAAGP 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1204 GEMVVKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-NIKGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:COG4988 335 PSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILINGVDLSDLDPASWRRQI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKVFIFSGTFRQNL---DPNGKwkDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSK 1359
Cdd:COG4988 414 AWVPQNPYLFAGTIRENLrlgRPDAS--DEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRD 491
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1360 AKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEK 1430
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
857-1142 |
2.82e-51 |
|
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: 182.46 E-value: 2.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 857 VLIWCVLVFLVEVAASLFVLWLLKNNPVNSGNNGTKISNssyvviitsTSFYYIFYIYVGVADTLLALSLFRGLplVHTL 936
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQA---------LNVYSLALLLLGLAQFILSFLQSYLL--NHTG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 937 ITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVP 1016
Cdd:pfam00664 70 ERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1017 GLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQM 1096
Cdd:pfam00664 150 VLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 14141185 1097 RIDMIFVLFFIVVTFISILTTGEGEGTAGIILTLAMnIMSTLQWAV 1142
Cdd:pfam00664 230 ITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLS-LFAQLFGPL 274
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1206-1414 |
3.78e-51 |
|
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: 177.96 E-value: 3.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFGV 1284
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFIFSGTFRQNLdpngkwkdeeiwkvadevglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 1365 LDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEE 1414
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1203-1430 |
1.10e-50 |
|
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: 180.10 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1203 GGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKA 1281
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 FGVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAK 1361
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1362 IILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEK 1430
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
904-1158 |
1.98e-50 |
|
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: 180.36 E-value: 1.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 904 STSFYYIFYIYVGVADTLLALSLFrgLPLVHTLITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLP 983
Cdd:cd18606 33 SQGFYIGIYAGLGVLQAIFLFLFG--LLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 984 LTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAF 1063
Cdd:cd18606 111 DSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1064 RRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTT-GEGEGTAGIILTLAMNIMSTLQWAV 1142
Cdd:cd18606 191 GAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRfSISPSSTGLVLSYVLQITQVLSWLV 270
|
250
....*....|....*.
gi 14141185 1143 NSSIDTDSLMRSVSRV 1158
Cdd:cd18606 271 RQFAEVENNMNSVERL 286
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
885-1158 |
1.24e-47 |
|
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: 173.17 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 885 NSGNNGTKISNSSYVVIITSTSFYYIFyIYVGVADTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTISKLKA 964
Cdd:cd18602 28 ANHDVASVVFNITSSSLEDDEVSYYIS-VYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 965 GGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILLRAYFLHTAQQLKQLESEGRS 1044
Cdd:cd18602 107 GRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1045 PIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGE--- 1121
Cdd:cd18602 187 PVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYisp 266
|
250 260 270
....*....|....*....|....*....|....*..
gi 14141185 1122 GTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRV 1158
Cdd:cd18602 267 SLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERV 303
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
858-1158 |
2.27e-46 |
|
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: 169.20 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 858 LIWCVLVFLVEVAASLFV-LWLLK--NNPVNSGNNGTkisnssyvviiTSTSFYYIFYIYVGVADTLLalSLFRGLPLVH 934
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSnIWLSEwsDDPALNGTQDT-----------EQRDYRLGVYGALGLGQAIF--VFLGSLALAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 935 TLITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLAT 1014
Cdd:cd18603 68 GCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1015 VPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWF 1094
Cdd:cd18603 148 IPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1095 QMRIDMI--FVLFF---IVVTFISILTTgegeGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRV 1158
Cdd:cd18603 228 AVRLEFLgnLIVLFaalFAVLSRDSLSP----GLVGLSISYALQITQTLNWLVRMTSELETNIVSVERI 292
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
857-1162 |
5.39e-44 |
|
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: 162.31 E-value: 5.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 857 VLIWCVLVFLVEVAASLFVLWLlkNNPVNSGNNgtkisnSSYVVIITSTSFYYIFYIYVGVADTLLALslFRGLPLVHTL 936
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWL--SYWVSHSNN------SFFNFINDSFNFFLTVYGFLAGLNSLFTL--LRAFLFAYGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 937 ITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVP 1016
Cdd:cd18605 71 LRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1017 GLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQM 1096
Cdd:cd18605 151 LAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1097 RIDMIFVLFFIVVTFISILTTGEGE----GTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFI 1162
Cdd:cd18605 231 RLQLLGVLIVTFVALTAVVQHFFGLsidaGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
437-623 |
6.74e-44 |
|
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: 159.03 E-value: 6.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII-----------------KHSGRVSFCSQFSWIMP 499
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 GTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14141185 580 VFTEEQVFESCVCKLMAN--KTRILVTSKMEHLRKADKILILHQGS 623
Cdd:cd03290 173 IHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
426-640 |
2.15e-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: 170.40 E-value: 2.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLCLvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCS 492
Cdd:COG2274 477 ENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSWIMPGTIKENIIFG---VSYDEyryksVVKACQ---LQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDA 566
Cdd:COG2274 556 QDVFLFSGTIRENITLGdpdATDEE-----IIEAARlagLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNP 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 567 DLYLLDSPFGYLDVFTEEQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQSLRPDF 640
Cdd:COG2274 631 RILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
426-622 |
3.73e-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: 155.23 E-value: 3.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHlclvGN---PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVS 489
Cdd:cd03228 4 KNVSFSY----PGrpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 490 FCSQFSWIMPGTIKENIifgvsydeyryksvvkacqlqqditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLY 569
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14141185 570 LLDSPFGYLDVFTEEQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:cd03228 119 ILDEATSALDPETEALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
426-635 |
4.18e-42 |
|
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: 163.78 E-value: 4.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLclVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCS 492
Cdd:COG4988 340 EDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSWIMPGTIKENIIFG-VSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG4988 418 QNPYLFAGTIRENLRLGrPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 572 DSPFGYLDVFTEEQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQS 635
Cdd:COG4988 498 DEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1204-1430 |
4.52e-42 |
|
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: 154.31 E-value: 4.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1204 GEMVVKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPqKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKVFIFSGTFRQNL---DPNGKwkDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSK 1359
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIrlgRPNAT--DEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1360 AKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEK 1430
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
957-1399 |
1.34e-39 |
|
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: 155.60 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 957 STISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILLR-AYFLHTAQQL 1035
Cdd:TIGR02868 102 AGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVApLVSLRAARAA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1036 KQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKA-LNLHTAN----WFMYLAtlrwfqmriDMIFVLFFIVVT 1110
Cdd:TIGR02868 182 EQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEAdRELTRAErraaAATALG---------AALTLLAAGLAV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1111 FISILTTGEG---EGTAGIILTL-------AMNIMSTLQWAVNSsidTDSLMRSVSRVFkfidiQTEESMYTQIIKELPR 1180
Cdd:TIGR02868 253 LGALWAGGPAvadGRLAPVTLAVlvllplaAFEAFAALPAAAQQ---LTRVRAAAERIV-----EVLDAAGPVAEGSAPA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1181 EGSSDvlviknehvkksdiwPSGGEMVVKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-I 1259
Cdd:TIGR02868 325 AGAVG---------------LGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDpL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1260 KGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNL---DPNGKwkDEEIWKVADEVGLKSVIEQFPGQLNFTLV 1336
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRPDAT--DEELWAALERVGLADWLRALPDGLDTVLG 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1337 DGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHR 1399
Cdd:TIGR02868 467 EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1207-1435 |
7.08e-39 |
|
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: 145.07 E-value: 7.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFGVI 1285
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1286 TQKVFIFSGTFRQNL---DPNGkwKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:cd03251 82 SQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1363 ILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQ 1435
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
426-640 |
1.94e-38 |
|
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: 153.00 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLClVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCS 492
Cdd:COG4987 337 EDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSWIMPGTIKENIIFG---VSYDEYRykSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLY 569
Cdd:COG4987 416 QRPHLFDTTLRENLRLArpdATDEELW--AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 570 LLDSPFGYLDVFTEEQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQSLRPDF 640
Cdd:COG4987 494 LLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
426-633 |
1.99e-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: 143.91 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLclVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCS 492
Cdd:cd03254 6 ENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSWIMPGTIKENIIFGVSY-DEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLL 571
Cdd:cd03254 84 QDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 572 DSPFGYLDVFTEEQVfESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:cd03254 164 DEATSNIDTETEKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1201-1435 |
3.61e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 149.20 E-value: 3.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1201 PSGGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWNSVTLQEWR 1279
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQqGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1280 KAFGVITQKVFIFSGTFRQNL---DPNGkwKDEEIWKVADEVGLKSVIEQFPGqLNFTLVDGGYVLSHGHKQLMCLARSV 1356
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEKLLEDDKG-LNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1357 LSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQ 1435
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
85-303 |
4.39e-37 |
|
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: 142.21 E-value: 4.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 85 GILLYLGEVTKAVQPVLLGRII------ASYDPENKVERSIAiyLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFS 158
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLInfvedaYLGGPPPSIGYGIG--YAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 159 LIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQA 238
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 239 ILGKMMVKYRdQRAAKI-NERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMR 303
Cdd:cd18597 161 FLMKKLFKLR-KKANKItDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILR 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1204-1413 |
6.31e-37 |
|
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: 139.26 E-value: 6.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1204 GEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKVFIFSGTFRQNL---DPNGkwKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSK 1359
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1360 AKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIeAMLD-CQRFLVIE 1413
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDlVDRIIVMD 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
437-633 |
2.28e-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: 138.13 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-------------VSFCSQFSWIMPGTIK 503
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFGVS-YDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 582
Cdd:cd03251 94 ENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 583 EEQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:cd03251 174 ERLVQAA-LERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
992-1412 |
6.81e-36 |
|
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: 144.35 E-value: 6.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 992 LVFIVIGAIIVVSALqpyIFLATVPGLVVFILLRAYFLHTAQQlKQLESEGRspIFTHLVTSLKGLWTLRAFRRQT-YFE 1070
Cdd:TIGR02857 134 AILAAVFPQDWISGL---ILLLTAPLIPIFMILIGWAAQAAAR-KQWAALSR--LSGHFLDRLRGLPTLKLFGRAKaQAA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1071 TLFHKALNLHTANwfmyLATLRwfqmridMIFVLFFIVVTFISIlttgegeGTAGIILTLAMNIMS---TLQWAVNSSI- 1146
Cdd:TIGR02857 208 AIRRSSEEYRERT----MRVLR-------IAFLSSAVLELFATL-------SVALVAVYIGFRLLAgdlDLATGLFVLLl 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1147 ----------------DTDSLMRSVSRVFKFIDIQteesmytqiikELPREGSSDVLviknehvkksdiWPSGGEMVVKD 1210
Cdd:TIGR02857 270 apefylplrqlgaqyhARADGVAAAEALFAVLDAA-----------PRPLAGKAPVT------------AAPASSLEFSG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1211 LTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFGVITQKV 1289
Cdd:TIGR02857 327 VSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPtEGSIAVNGVPLADADADSWRDQIAWVPQHP 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1290 FIFSGTFRQNL---DPNGKwkDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:TIGR02857 406 FLFAGTIAENIrlaRPDAS--DAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 14141185 1367 EPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVI 1412
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1223-1370 |
2.45e-35 |
|
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: 132.00 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSG-TFRQNL 1300
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 1301 -------DPNGKWKDEEIWKVADEVGLksvieqfPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSA 1370
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGL-------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1207-1433 |
1.02e-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: 133.51 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFGVI 1285
Cdd:cd03253 2 EFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVsSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1286 TQKVFIFSGTFRQNL---DPNGKwkDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:cd03253 81 PQDTVLFNDTIGYNIrygRPDAT--DEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1363 ILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIF 1433
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLY 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
426-619 |
1.25e-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: 140.50 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLclVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCS 492
Cdd:TIGR02857 325 SGVSVAYP--GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVP 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSWIMPGTIKENIIFGVSY-DEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLL 571
Cdd:TIGR02857 403 QHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14141185 572 DSPFGYLDVFTEEQVFEScVCKLMANKTRILVTSKMEHLRKADKILIL 619
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1207-1414 |
4.14e-34 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 130.66 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVI 1285
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGpTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1286 TQ--KVFIFSGTFRQNLD---PNGKWKDEEIWKVADE----VGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCLArSV 1356
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAfglENLGLPEEEIEERVEEalelVGLEGLRDRSP-----------FTLSGGQKQRVAIA-GV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1357 LS-KAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRIEAMLD-CQRFLVIEE 1414
Cdd:cd03225 149 LAmDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLED 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1208-1435 |
7.81e-34 |
|
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: 130.53 E-value: 7.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:COG1122 3 LENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTL----LRLLNgllkpTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVitqkVF------IFSGTFRQ-------NLdpngKWKDEEIWKVADE----VGLKSVIEQFPgqlnftlvdggYVLSHG 1345
Cdd:COG1122 78 GL----VFqnpddqLFAPTVEEdvafgpeNL----GLPREEIRERVEEalelVGLEHLADRPP-----------HELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1346 HKQLMCLArSVLS-KAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRIEAMLD-CQRFLVIEESNVWQYDS 1422
Cdd:COG1122 139 QKQRVAIA-GVLAmEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
250
....*....|...
gi 14141185 1423 LQALLSEKSIFQQ 1435
Cdd:COG1122 218 PREVFSDYELLEE 230
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
82-303 |
1.12e-33 |
|
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: 132.21 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 82 LFYGILLYlgevtkaVQPVLLGRIIaSYDPENKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLIY 161
Cdd:cd18595 7 LLSDILLF-------ASPQLLKLLI-NFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 162 KKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAILG 241
Cdd:cd18595 79 RKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 242 KMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMR 303
Cdd:cd18595 159 RKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLN 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1205-1435 |
1.23e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 138.44 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1205 EMVVKDLTVkYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDGVSWNSVTLQEWRKAFGV 1284
Cdd:PRK11174 349 TIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFIFSGTFRQNL---DPNGKwkDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAK 1361
Cdd:PRK11174 428 VGQNPQLPHGTLRDNVllgNPDAS--DEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 1362 IILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQ 1435
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT 579
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
441-575 |
3.93e-32 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 122.76 E-value: 3.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIK-------------HSGRVSFCSQFSWIMPG-TIKENI 506
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 507 IFGVsyDEYRYKSVVKACQLQQDITKFA--EQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGlgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1211-1435 |
2.01e-31 |
|
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: 123.75 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1211 LTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM-LNIKGDIEIDGVSWNSVTLQEWRKAFGVITQKV 1289
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1290 FIFSGTFRQNL---DPNGKWkdEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:cd03252 86 VLFNRSIRDNIalaDPGMSM--ERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1367 EPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQ 1435
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
426-633 |
3.37e-31 |
|
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: 123.11 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLclVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-VSFCSQFSW-----IMP 499
Cdd:cd03253 4 ENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdIREVTLDSLrraigVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 -------GTIKENIIFG---VSYDEYRykSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLY 569
Cdd:cd03253 82 qdtvlfnDTIGYNIRYGrpdATDEEVI--EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 570 LLDSPFGYLDVFTEEQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:cd03253 160 LLDEATSALDTHTEREIQAA-LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1207-1417 |
4.55e-31 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 120.78 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVI 1285
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1286 TQKVFIFSGTFRQNldpngkwkdeeiwkvadevglksvieqfpgqlnftlvdggyVLSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:cd03246 82 PQDDELFSGSIAEN-----------------------------------------ILSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1366 DEPSAHLDPITYQVIRRVLKQA-FAGCTVILCEHRIEAMLDCQRFLVIEESNV 1417
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1222-1435 |
5.50e-31 |
|
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: 122.65 E-value: 5.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNL 1300
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1301 ---DPNGKwkDEEIWKVADEVGLKSVIEQFPGQLNfTLV-DGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPIT 1376
Cdd:cd03249 98 rygKPDAT--DEEVEEAAKKANIHDFIMSLPDGYD-TLVgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1377 YQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQ 1435
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAK 233
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
81-303 |
8.86e-31 |
|
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: 123.14 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 81 FLFYGILLYLGEVTKAVQPVLLGRIIASYDPENKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLI 160
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFS-AFCGLGLLIILVIFQAI 239
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 240 LGKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMR 303
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVAN 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
426-622 |
2.96e-30 |
|
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: 120.00 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLCLvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCS 492
Cdd:cd03245 6 RNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSWIMPGTIKENIIFGVSY-DEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLL 571
Cdd:cd03245 85 QDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 572 DSPFGYLDVFTEEQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:cd03245 165 DEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1208-1414 |
4.60e-30 |
|
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: 116.96 E-value: 4.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFGVIT 1286
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPtSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QkvfifsgtfrqnldpngkwkdeeiwkvadevglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 1367 EPSAHLDPITYQVIRRVLKQAFA-GCTVILCEHRIE-AMLDCQRFLVIEE 1414
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPElAELAADRVIVLKD 155
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1208-1429 |
8.05e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.01 E-value: 8.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSvTLQEWRKAFGVIT 1286
Cdd:COG1131 3 VRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFIFSG-TFRQNLD-------PNGKWKDEEIWKVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLS 1358
Cdd:COG1131 80 QEPALYPDlTVRENLRffarlygLPRKEARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1359 KAKIILLDEPSAHLDPITYQVIRRVLKQAFA-GCTVILCEHRI-EAMLDCQRFLVIEESNVWQYDSLQALLSE 1429
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLeEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1206-1414 |
2.69e-29 |
|
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: 115.87 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVswNSVTLQE-WRKAFG 1283
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKpQQGEITLDGV--PVSDLEKaLSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQKVFIFSGTFRQNLdpngkwkdeeiwkvadevglksvieqfpgqlnftlvdgGYVLSHGHKQLMCLARSVLSKAKII 1363
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1364 LLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEE 1414
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLEN 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
426-633 |
4.08e-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: 117.26 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII-------------KHSGRVSFCS 492
Cdd:cd03249 4 KNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSWIMPGTIKENIIFGVSYDEYryKSVVKACQL---QQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLY 569
Cdd:cd03249 84 QEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 570 LLDSPFGYLDVFTEEQVFESCVcKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALD-RAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
438-622 |
1.09e-28 |
|
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: 113.85 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRvsfcsqfswimpgtikenIIFGVSYDEYR- 516
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA------------------DISQWDPNELGd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 517 ---YksvvkacqLQQDITKFAeqdntvlgeGGVT---LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESC 590
Cdd:cd03246 77 hvgY--------LPQDDELFS---------GSIAeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|..
gi 14141185 591 VCKLMANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:cd03246 140 AALKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
407-641 |
3.24e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 121.88 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 407 ELLE--KVQQSNGDRKHSSDE-NNVSFSHLCLV---GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELeASEG 480
Cdd:PRK11174 326 TFLEtpLAHPQQGEKELASNDpVTIEAEDLEILspdGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 481 IIKHSG-------RVSFCSQFSWI------MPGTIKENIIFG-VSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGV 546
Cdd:PRK11174 405 SLKINGielreldPESWRKHLSWVgqnpqlPHGTLRDNVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAA 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 547 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYF 626
Cdd:PRK11174 485 GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA-LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
|
250
....*....|....*
gi 14141185 627 YGTFSELQSLRPDFS 641
Cdd:PRK11174 564 QGDYAELSQAGGLFA 578
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
437-622 |
6.94e-28 |
|
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: 112.97 E-value: 6.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPGTIK 503
Cdd:cd03244 16 LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENI-IFGVSYDEYRYkSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 582
Cdd:cd03244 96 SNLdPFGEYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14141185 583 EEQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:cd03244 175 DALIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1208-1417 |
1.16e-27 |
|
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: 110.95 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSvTLQEWRKAFGVIT 1286
Cdd:cd03230 3 VRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFIFSG-TFRQNLDpngkwkdeeiwkvadevglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:cd03230 80 EEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14141185 1366 DEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRIEAMLD-CQRFLVIEESNV 1417
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
426-622 |
2.14e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 109.64 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLclvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRvsfcsQFSWIMPGTIKEN 505
Cdd:cd00267 3 ENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIFgvsydeyryksvvkacqLQQditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQ 585
Cdd:cd00267 75 IGY-----------------VPQ-------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 14141185 586 VFESCVCKLMANKTRILVTSKMEHLRKA-DKILILHQG 622
Cdd:cd00267 119 LLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
426-638 |
3.98e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.39 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLcLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-------------VSFCS 492
Cdd:PRK11160 342 NNVSFTYP-DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSWIMPGTIKENIIFGV--SYDEyRYKSVvkacqLQQ-DITKFAEQD---NTVLGEGGVTLSGGQRARISLARAVYKDA 566
Cdd:PRK11160 421 QRVHLFSATLRDNLLLAApnASDE-ALIEV-----LQQvGLEKLLEDDkglNAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 567 DLYLLDSPFGYLDVFTEEQVFESCVcKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQSLRP 638
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLA-EHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1208-1420 |
4.69e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.45 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVIT 1286
Cdd:cd03214 2 VENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QkvfifsgtfrqnldpngkwkdeeiwkVADEVGLKSVIEQfpgqlNFTlvdggyVLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:cd03214 80 Q--------------------------ALELLGLAHLADR-----PFN------ELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1367 EPSAHLDpITYQVirRVLK--QAFA---GCTVILCEHRIE-AMLDCQRFLVIEESNVWQY 1420
Cdd:cd03214 123 EPTSHLD-IAHQI--ELLEllRRLArerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQ 179
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
437-604 |
4.96e-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: 117.46 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPGTIK 503
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFG---VSYDEYRykSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:TIGR02868 427 ENLRLArpdATDEELW--AALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....
gi 14141185 581 FTEEQVFEScVCKLMANKTRILVT 604
Cdd:TIGR02868 505 ETADELLED-LLAALSGRTVVLIT 527
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1204-1429 |
1.31e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 116.74 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1204 GEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:PRK10789 312 GELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVsEGDIRFHDIPLTKLQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKVFIFSGTFRQNL---DPNGkwKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSK 1359
Cdd:PRK10789 392 AVVSQTPFLFSDTVANNIalgRPDA--TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1360 AKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSE 1429
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1206-1421 |
1.99e-26 |
|
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: 108.76 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVSWNSVTlqEWRK 1280
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAglerpDSGEILIDGRDVTGVP--PERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFGVITQKVFIFSG-TFRQN----LDPNGKWKDEEIWKV---ADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCL 1352
Cdd:cd03259 73 NIGMVFQDYALFPHlTVAENiafgLKLRGVPKAEIRARVrelLELVGLEGLLNRYPHE-----------LSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEH-RIEAMLDCQRFLVIEESNVWQYD 1421
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKelQRELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1197-1435 |
2.08e-26 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 116.36 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1197 SDIWP-SGGEMVVKDLTVKYMDDgNAVLENISFSISPGQRVGLLGRTGSGKSTLlsAFLRMLNI---KGDIEIDGVSWNS 1272
Cdd:PRK10790 331 NDDRPlQSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTL--ASLLMGYYpltEGEIRLDGRPLSS 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1273 VTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCL 1352
Cdd:PRK10790 408 LSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSI 1432
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGR 567
|
...
gi 14141185 1433 FQQ 1435
Cdd:PRK10790 568 YWQ 570
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1208-1414 |
2.41e-26 |
|
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: 115.39 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML----NIKGDIEIDGVSWNSVTLQEWRKAFG 1283
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggRISGEVLLDGRDLLELSEALRGRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQ---KVFIFSGTFRQ------NLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:COG1123 87 MVFQdpmTQLNPVTVGDQiaealeNLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1355 SVLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEHRIEAMLD-CQRFLVIEE 1414
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDD 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1102-1435 |
1.46e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 113.58 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1102 FVLFfiVVTFISILTTGEGeGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDIQTEESmytqiikelprE 1181
Cdd:PRK11176 265 FVLY--AASFPSVMDTLTA-GTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKD-----------E 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1182 GSSDVlviknEHVKksdiwpsgGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-K 1260
Cdd:PRK11176 331 GKRVI-----ERAK--------GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIdE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1261 GDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNL--DPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDG 1338
Cdd:PRK11176 398 GEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGEN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1339 GYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVW 1418
Cdd:PRK11176 478 GVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
330
....*....|....*..
gi 14141185 1419 QYDSLQALLSEKSIFQQ 1435
Cdd:PRK11176 558 ERGTHAELLAQNGVYAQ 574
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
437-622 |
1.63e-25 |
|
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: 113.30 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII----------------KHSG----RVSFcsqfsw 496
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreelgRHIGylpqDVEL------ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 497 iMPGTIKENII-FGVSYDEyrykSVVKACQL---QQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG4618 418 -FDGTIAENIArFGDADPE----KVVAAAKLagvHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14141185 573 SPFGYLDVFTEEQVFEScvckLMANKTR----ILVTSKMEHLRKADKILILHQG 622
Cdd:COG4618 493 EPNSNLDDEGEAALAAA----IRALKARgatvVVITHRPSLLAAVDKLLVLRDG 542
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1208-1442 |
1.69e-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: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSwNSVTLQEWRKAFGVIT 1286
Cdd:COG4555 4 VENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSILIDGED-VRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFIFSG-TFRQNLDPNGkwkdeEIWKVADEVgLKSVIEQFPGQLNFTLVDGGYV--LSHGHKQLMCLARSVLSKAKII 1363
Cdd:COG4555 81 DERGLYDRlTVRENIRYFA-----ELYGLFDEE-LKKRIEELIELLGLEEFLDRRVgeLSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1364 LLDEPSAHLDPITYQVIRRVLKQAFA-GCTVILCEH---RIEAMLDcqRFLVIEESNVWQYDSLQALLSE------KSIF 1433
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHimqEVEALCD--RVVILHKGKVVAQGSLDELREEigeenlEDAF 232
|
....*....
gi 14141185 1434 QQAISSSEK 1442
Cdd:COG4555 233 VALIGSEEG 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1208-1417 |
2.05e-25 |
|
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: 106.43 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVT---LQEWRKAFG 1283
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpDSGEVLIDGEDISGLSeaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQKVFIFSG-TFRQN----LDPNGKWKDEEIWKVA----DEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:cd03261 81 MLFQSGALFDSlTVFENvafpLREHTRLSEEEIREIVleklEAVGLRGAEDLYPAE-----------LSGGMKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1355 SVLSKAKIILLDEPSAHLDPITY----QVIRRvLKQAFaGCTVILCEHRI-EAMLDCQRFLVIEESNV 1417
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASgvidDLIRS-LKKEL-GLTSIMVTHDLdTAFAIADRIAVLYDGKI 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
426-619 |
2.15e-25 |
|
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: 105.69 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFShlcLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG--------RVSFCSQ---F 494
Cdd:cd03235 3 EDLTVS---YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQrrsI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 495 SWIMPGTIKE--------NIIFGVSYDEYRYKSVVKAcqLQQ-DITKFAEQDntvLGEggvtLSGGQRARISLARAVYKD 565
Cdd:cd03235 80 DRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEA--LERvGLSELADRQ---IGE----LSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 566 ADLYLLDSPFGYLDVFTEEQVFEsCVCKL-MANKTRILVTSKMEHLRK-ADKILIL 619
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYE-LLRELrREGMTILVVTHDLGLVLEyFDRVLLL 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1208-1414 |
2.79e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.28 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFGVIT 1286
Cdd:COG4619 3 LEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFIFSGTFRQNLDP-----NGKWKDEEIWKVADEVGL------KSVIEqfpgqlnftlvdggyvLSHGHKQLMCLARS 1355
Cdd:COG4619 81 QEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLppdildKPVER----------------LSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 1356 VLSKAKIILLDEPSAHLDP----ITYQVIRRVLKQafAGCTVILCEH-RIEAMLDCQRFLVIEE 1414
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPentrRVEELLREYLAE--EGRAVLWVSHdPEQIERVADRVLTLEA 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1206-1432 |
3.46e-25 |
|
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: 106.28 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGV 1284
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFI-FSGTFRQ--------NLDPNGKW--KDEEI-WKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCL 1352
Cdd:COG1120 80 VPQEPPApFGLTVRElvalgrypHLGLFGRPsaEDREAvEEALERTGLEHLADRPVDE-----------LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDpITYQV-IRRVLKQ--AFAGCTVILCEHRIE-AMLDCQRFLVIEESNVWQYDSLQALLS 1428
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLD-LAHQLeVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
....
gi 14141185 1429 EKSI 1432
Cdd:COG1120 228 PELL 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
946-1437 |
4.62e-25 |
|
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: 112.91 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 946 KMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVsALQPYIFLATVPGLVVFILLR 1025
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLV-RQNMLLFLLSLLSIPVYAVII 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1026 AYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRA-----FRRQ---TYFETLFHKALNLHTAnwfmylatlRWFQMR 1097
Cdd:TIGR01193 313 ILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSltseaERYSkidSEFGDYLNKSFKYQKA---------DQGQQA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1098 IDMIFVLFFIVVtfisILTTGegegtAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKfidIQTEESMYTQIike 1177
Cdd:TIGR01193 384 IKAVTKLILNVV----ILWTG-----AYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPK---LQAARVANNRL--- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1178 lpregsSDVLVIKNEHVKKSDIWPS---GGEMVVKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL 1254
Cdd:TIGR01193 449 ------NEVYLVDSEFINKKKRTELnnlNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLV 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1255 RMLNIK-GDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNL--DPNGKWKDEEIWKVADEVGLKSVIEQFPGQL 1331
Cdd:TIGR01193 522 GFFQARsGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGY 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1332 NFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQ-VIRRVLKqaFAGCTVILCEHRIEAMLDCQRFL 1410
Cdd:TIGR01193 602 QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKkIVNNLLN--LQDKTIIFVAHRLSVAKQSDKII 679
|
490 500
....*....|....*....|....*..
gi 14141185 1411 VIEESNVWQYDSLQALLSEKSIFQQAI 1437
Cdd:TIGR01193 680 VLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1206-1414 |
5.33e-25 |
|
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: 104.09 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYMDD---GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrmlnikGDIE-IDGvswnSVTlqeWRKA 1281
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL------GELEkLSG----SVS---VPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 FGVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNfTLV-DGGYVLSHGHKQLMCLARSVLSKA 1360
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDL-TEIgEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1361 KIILLDEPSAHLDP-----ITYQVIRRVLKQafaGCTVILCEHRIEAMLDCQRFLVIEE 1414
Cdd:cd03250 147 DIYLLDDPLSAVDAhvgrhIFENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
428-648 |
5.81e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.56 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 428 VSFSHLCLV--GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG--------RVSFCSQ---F 494
Cdd:COG1121 7 IELENLTVSygGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQraeV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 495 SWIMPGTIKENIIFGvsydeyRY-------------KSVVKACqLQQ-DITKFAEQDntvLGEggvtLSGGQRARISLAR 560
Cdd:COG1121 87 DWDFPITVRDVVLMG------RYgrrglfrrpsradREAVDEA-LERvGLEDLADRP---IGE----LSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 561 AVYKDADLYLLDSPFGYLDVFTEEQVFEscvckLMA-----NKTRILVTSKMEHLRK-ADKILILHQGsSYFYGTFSELq 634
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYE-----LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPPEEV- 225
|
250
....*....|....
gi 14141185 635 sLRPDFSSKLMGYD 648
Cdd:COG1121 226 -LTPENLSRAYGGP 238
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1208-1427 |
6.10e-25 |
|
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: 105.06 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVT---LQEWRKAFG 1283
Cdd:COG1127 8 VRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPdSGEILVDGQDITGLSekeLYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VitqkVF----IFSG-TFRQN----LDPNGKWKDEEIWKVADE----VGLKSVIEQFPGQLNftlvdGGyvlshghkqlM 1350
Cdd:COG1127 86 M----LFqggaLFDSlTVFENvafpLREHTDLSEAEIRELVLEklelVGLPGAADKMPSELS-----GG----------M 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1351 C----LARSVLSKAKIILLDEPSAHLDPIT----YQVIRRvLKQAFaGCTVILCEHRIEAMLD-CQRFLVIEESNVWQYD 1421
Cdd:COG1127 147 RkrvaLARALALDPEILLYDEPTAGLDPITsaviDELIRE-LRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*.
gi 14141185 1422 SLQALL 1427
Cdd:COG1127 225 TPEELL 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
426-628 |
6.19e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 103.28 E-value: 6.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHlclVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKhsgrvsfcsqfswimpgtiken 505
Cdd:cd03214 3 ENLSVGY---GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 iIFGVSYDEYRYKSVVKAC----Q-LQQ-DITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03214 58 -LDGKDLASLSPKELARKIayvpQaLELlGLAHLADRPFN-------ELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14141185 580 VFTEEQVFEScVCKLMA--NKTRILVTSKMEH-LRKADKILILHQGSSYFYG 628
Cdd:cd03214 130 IAHQIELLEL-LRRLARerGKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1208-1412 |
1.01e-24 |
|
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: 104.12 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTlQEWRKAFGV 1284
Cdd:cd03257 4 VKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPtSGSIIFDGKDLLKLS-RRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFifsgtfrQN----LDP---------------NGKWKDEEIWKVADE----VGL-KSVIEQFPGQlnftlvdggy 1340
Cdd:cd03257 83 EIQMVF-------QDpmssLNPrmtigeqiaeplrihGKLSKKEARKEAVLLllvgVGLpEEVLNRYPHE---------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 1341 vLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPIT-YQVIR--RVLKQAFaGCTVILCEHRIEAMLD-CQRFLVI 1412
Cdd:cd03257 146 -LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVM 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
427-633 |
1.06e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.74 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 427 NVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQ 493
Cdd:TIGR00958 483 DVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 494 FSWIMPGTIKENIIFGVSY-DEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLD 572
Cdd:TIGR00958 563 EPVLFSGSVRENIAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 573 SPFGYLDVFTEEQVFEScvcKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:TIGR00958 643 EATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
440-633 |
1.30e-24 |
|
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: 104.11 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPGTIKENI 506
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 507 IFG-VSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvFTEEQ 585
Cdd:cd03252 97 ALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-YESEH 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14141185 586 VFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:cd03252 176 AIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
426-628 |
2.77e-24 |
|
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: 101.24 E-value: 2.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLclvGN--PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASegiikhSGRVSFCSQFSWIMPGTIK 503
Cdd:cd03247 4 NNVSFSYP---EQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ------QGEITLDGVPVSDLEKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIifgvsydeyryksvvkaCQLQQDITKFaeqDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 583
Cdd:cd03247 75 SLI-----------------SVLNQRPYLF---DTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14141185 584 EQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYG 628
Cdd:cd03247 135 RQLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
439-622 |
3.49e-24 |
|
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: 102.18 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------------VSFCSQFSWIMPG- 500
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLPDl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENI-----IFGVSYDEY--RYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:cd03255 98 TALENVelpllLAGVPKKERreRAEELLERVGLGDRLNHYPSE-----------LSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 574 PFGYLDVFTEEQVFEscvckLM------ANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:cd03255 167 PTGNLDSETGKEVME-----LLrelnkeAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1208-1414 |
4.36e-24 |
|
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: 102.96 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKY--MDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVswnSVTLQEWRKAFGV 1284
Cdd:COG1124 4 VRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGR---PVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ItQKVFifsgtfrQN----LDP---------------NGKWKDEEIWKVADEVGL-KSVIEQFPGQlnftlvdggyvLSH 1344
Cdd:COG1124 81 V-QMVF-------QDpyasLHPrhtvdrilaeplrihGLPDREERIAELLEQVGLpPSFLDRYPHQ-----------LSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1345 GHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEH---RIEAMldCQRFLVIEE 1414
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHdlaVVAHL--CDRVAVMQN 214
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
85-294 |
6.15e-24 |
|
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: 103.79 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 85 GILLYLGEVTKAVQPVLLGRIIaSYDPENKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLIYKKT 164
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLV-EFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 165 LKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAILGKMM 244
Cdd:cd18598 82 LRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 245 VKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELK 294
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1208-1414 |
8.41e-24 |
|
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: 99.95 E-value: 8.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN-----IKGDIEIDGVSWNSVT--LQEWRK 1280
Cdd:cd03229 3 LKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLL----RCIAgleepDSGSILIDGEDLTDLEdeLPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFGVITQKVFIFSG-TFRQNLdpngkwkdeeiwkvadevglksvieqfpgqlnftlvdgGYVLSHGHKQLMCLARSVLSK 1359
Cdd:cd03229 77 RIGMVFQDFALFPHlTVLENI--------------------------------------ALGLSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1360 AKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEHRI-EAMLDCQRFLVIEE 1414
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLdEAARLADRVVVLRD 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
438-633 |
1.36e-23 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 107.11 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIK-HS------------GRVSFCSQFSWIMPGTIKE 504
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDipltklqldswrSRLAVVSQTPFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFGV-SYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 583
Cdd:PRK10789 408 NIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 584 EQVFEScVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:PRK10789 488 HQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1208-1398 |
1.74e-23 |
|
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: 100.72 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK------GDIEIDG--VSWNSVTLQEWR 1279
Cdd:cd03260 3 LRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdeGEVLLDGkdIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1280 KAFGVITQKVFIFSGTFRQNLD----PNGKWKDEEIwKVADEVGLKSVieQFPGQLNFTLVDGGyvLSHGHKQLMCLARS 1355
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEEL-DERVEEALRKA--ALWDEVKDRLHALG--LSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14141185 1356 VLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEH 1398
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH 198
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1204-1427 |
3.68e-23 |
|
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: 105.99 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1204 GEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRML-----NIKGDIEIDGV---SWNSVTL 1275
Cdd:COG4618 329 GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLLvgvwpPTAGSVRLDGAdlsQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1276 QEWrkaFGVITQKVFIFSGTFRQNL----DPNgkwkDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMC 1351
Cdd:COG4618 405 GRH---IGYLPQDVELFDGTIAENIarfgDAD----PEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1352 LARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA-GCTVILCEHRIEAMLDCQRFLVIEESNVWQY----DSLQAL 1426
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFgprdEVLARL 557
|
.
gi 14141185 1427 L 1427
Cdd:COG4618 558 A 558
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1208-1409 |
5.55e-23 |
|
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: 98.32 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRML-----NIKGDIEIDGVSWNSVTlQEWRKAF 1282
Cdd:COG4133 5 AENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllpPSAGEVLWNGEPIRDAR-EDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKVFIFSG-TFRQNLD-----PNGKWKDEEIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSV 1356
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14141185 1357 LSKAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRIEAMLDCQRF 1409
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1208-1405 |
1.07e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSwnsvtLQEWRKAFGVIT 1286
Cdd:COG1121 9 LENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPtSGTVRLFGKP-----PRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKvFIFSGTF--------RQNLDPNGKW------KD-EEIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMC 1351
Cdd:COG1121 82 QR-AEVDWDFpitvrdvvLMGRYGRRGLfrrpsrADrEAVDEALERVGLEDLADRPIGE-----------LSGGQQQRVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1352 LARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRIEAMLD 1405
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVRE 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
426-633 |
1.43e-22 |
|
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: 98.17 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLClvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFC- 491
Cdd:COG1122 4 ENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 492 ----SQFswIMPgTIKENIIFG-----VSYDEYRyKSVVKAcqLQQ-DITKFAEQDntVLgeggvTLSGGQRARISLARA 561
Cdd:COG1122 82 qnpdDQL--FAP-TVEEDVAFGpenlgLPREEIR-ERVEEA--LELvGLEHLADRP--PH-----ELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 562 VYKDADLYLLDSPFGYLDVFTEEQVFEsCVCKL-MANKTRILVTSKMEHLRK-ADKILILHQGSSYFYGTFSEL 633
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLE-LLKRLnKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
426-622 |
1.74e-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: 97.15 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHlclvGN---PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG-------------IIKHSGRVS 489
Cdd:cd03225 3 KNLSFSY----PDgarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGevlvdgkdltklsLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 490 FC-----SQFswIMPgTIKENIIFG-----VSYDEyRYKSVVKACQLqQDITKFAEQDNTvlgeggvTLSGGQRARISLA 559
Cdd:cd03225 79 LVfqnpdDQF--FGP-TVEEEVAFGlenlgLPEEE-IEERVEEALEL-VGLEGLRDRSPF-------TLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 560 RAVYKDADLYLLDSPFGYLDVFTEEQVFEScVCKLMA-NKTRILVTSKMEHLRK-ADKILILHQG 622
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLEL-LKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
437-622 |
2.34e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.81 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPGTIK 503
Cdd:COG4619 12 GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFGVSYDEYRYKsvvkacqlQQDITKFAEQ---DNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:COG4619 92 DNLPFPFQLRERKFD--------RERALELLERlglPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14141185 581 FTEEQVfESCVCKLMANKTR--ILVTSKMEHL-RKADKILILHQG 622
Cdd:COG4619 164 ENTRRV-EELLREYLAEEGRavLWVSHDPEQIeRVADRVLTLEAG 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
437-633 |
3.79e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.06 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG------------RVSFCSQFSWIMPG-TIK 503
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENI-----IFGVSYDEY--RYKSVVKACQLQQDITKFAEqdntvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:COG1131 92 ENLrffarLYGLPRKEAreRIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 577 YLDVFTEEQVFEsCVCKLMANKTRILVTSkmeHL-----RKADKILILHQGSSYFYGTFSEL 633
Cdd:COG1131 161 GLDPEARRELWE-LLRELAAEGKTVLLST---HYleeaeRLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
437-648 |
4.00e-22 |
|
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: 96.99 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPG-TI 502
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 503 KENIIFGVS---YDEYRYKSVVKacQLQQ----DITKFAEQdntVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:cd03295 93 EENIALVPKllkWPKEKIRERAD--ELLAlvglDPAEFADR---YPHE----LSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 576 GYLDVFTEEQVFESCV-CKLMANKTRILVTSKM-EHLRKADKILILHQGSSYFYGTFSE-LQSLRPDFSSKLMGYD 648
Cdd:cd03295 164 GALDPITRDQLQEEFKrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEiLRSPANDFVAEFVGAD 239
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
85-342 |
4.46e-22 |
|
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: 98.85 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 85 GILLYLGEVTKAVQPVLLGRII-----ASYDPENKVERSIAIY------------LGIGLCLLFIVRTLLLHPAIFGLHR 147
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVdyveeNTYSSSNSTDKLSVSYvtveeffsngyvLAVILFLALLLQATFSQASYHIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 148 IGMQMRTAMFSLIYKKTLKLSSRVLD--KISIGQLVSLLS---NNLNKFdegLALAHFIWIAPLQVTLLMGLLWDLLQFS 222
Cdd:cd18591 83 EGIRLKTALQAMIYEKALRLSSWNLSsgSMTIGQITNHMSedaNNIMFF---FWLIHYLWAIPLKIIVGLILLYLKLGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 223 AFCGLGLLIILVIFQAILGKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYM 302
Cdd:cd18591 160 ALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 14141185 303 RFFTSSAFFFSGFFVVFLSVLPYTVINGIVLR--KIFTTISF 342
Cdd:cd18591 240 WSLMTFLTQASPILVTLVTFGLYPYLEGEPLTaaKAFSSLAL 281
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
121-365 |
6.14e-22 |
|
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: 97.63 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 121 IYLGIGLCLLF----IVRTLLLHPAIFGLHRIGMQMRTAMFSLIYKKTLKLSSrvLDKISIGQLVSLLSNNLNKFDEGLA 196
Cdd:cd18592 35 VWYGILLVLGLflteLLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRS--LGDKSVGELINIFSNDGQRLFDAAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 197 LAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAILGKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYC 276
Cdd:cd18592 113 FGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 277 WESAMEKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVFLSVLPYTVI-NGIVLRKIFTTISFCIVLRMSVtRQFP 355
Cdd:cd18592 193 WEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALgNDLTAAQAFTVIAVFNSMRFSL-RMLP 271
|
250
....*....|
gi 14141185 356 TAVQIWYDSF 365
Cdd:cd18592 272 YAVKALAEAK 281
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
438-633 |
9.49e-22 |
|
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: 95.26 E-value: 9.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG---IIKHSGR---------VSFCSQFSWIMPG-TIKE 504
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtayINGYSIRtdrkaarqsLGYCPQFDALFDElTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIF-----GVSYDEYRYKS--VVKACQLQQDITKFAeqdntvlgeggVTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03263 95 HLRFyarlkGLPKSEIKEEVelLLRVLGLTDKANKRA-----------RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 578 LDVFTEEQVFEsCVCKLMANKTRILVTSKM---EHLrkADKILILHQGSSYFYGTFSEL 633
Cdd:cd03263 164 LDPASRRAIWD-LILEVRKGRSIILTTHSMdeaEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1202-1414 |
9.89e-22 |
|
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: 101.44 E-value: 9.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1202 SGGEMVVKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRK 1280
Cdd:COG5265 354 GGGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVtSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFGVITQKVFIFSGTFRQNL---DPNGkwKDEEIWKVADEVGLKSVIEQFPGQLNfTLV-DGGYVLSHGHKQLMCLARSV 1356
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIaygRPDA--SEEEVEAAARAAQIHDFIESLPDGYD-TRVgERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1357 LSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEE 1414
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEA 567
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1208-1428 |
1.44e-21 |
|
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: 95.34 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNI-----KGDIEIDGVSWNSVT---LQE 1277
Cdd:cd03258 4 LKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGlerptSGSVLVDGTDLTLLSgkeLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1278 WRKAFGVITQKVFIFSG-TFRQNLD-P--NGKWKDEEIWKVADE----VGLKSVIEQFPGQlnftlvdggyvLSHGHKQL 1349
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSrTVFENVAlPleIAGVPKAEIEERVLEllelVGLEDKADAYPAQ-----------LSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1350 MCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEHRIEAMLD-CQRFLVIEESNVWQYDSLQAL 1426
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
..
gi 14141185 1427 LS 1428
Cdd:cd03258 229 FA 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
427-633 |
1.55e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 100.86 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 427 NVSFSHlclVG--NPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFC 491
Cdd:PRK11176 346 NVTFTY---PGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 492 SQFSWIMPGTIKENIIFGVSyDEYRYKSVVKACQLQQD---ITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADL 568
Cdd:PRK11176 423 SQNVHLFNDTIANNIAYART-EQYSREQIEEAARMAYAmdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 569 YLLDSPFGYLDvfTE-EQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:PRK11176 502 LILDEATSALD--TEsERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
437-622 |
2.50e-21 |
|
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: 92.46 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKhsgrvsfcsqfswimpgtikeniIFGVSYDEYR 516
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-----------------------VLGKDIKKEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 517 YKSVVKACQLQQDITKFAE---QDNtvlgeggVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVcK 593
Cdd:cd03230 69 EEVKRRIGYLPEEPSLYENltvREN-------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR-E 140
|
170 180 190
....*....|....*....|....*....|.
gi 14141185 594 LMANKTRILVTS-KMEHL-RKADKILILHQG 622
Cdd:cd03230 141 LKKEGKTILLSShILEEAeRLCDRVAILNNG 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1208-1412 |
2.65e-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: 94.08 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSwnsvtLQEWRKAFGV 1284
Cdd:cd03293 3 VRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVLVDGEP-----VTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFIFS-GTFRQN----LDPNGkWKDEEIWKVADE----VGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARS 1355
Cdd:cd03293 78 VFQQDALLPwLTVLDNvalgLELQG-VPKAEARERAEEllelVGLSGFENAYPHQ-----------LSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1356 VLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEHRI-EAMLDCQRFLVI 1412
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIdEAVFLADRVVVL 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
437-622 |
3.64e-21 |
|
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: 93.35 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII-----------KHSGRVSFCSQFSWIMPG-TIKE 504
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgvpPERRNIGMVFQDYALFPHlTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFGVsydeyrYKSVVKACQLQQDITKFAEQdntvLGEGGV------TLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:cd03259 92 NIAFGL------KLRGVPKAEIRARVRELLEL----VGLEGLlnryphELSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14141185 579 DVFTEEQVFEScVCKLMAN--KTRILVTSKM-EHLRKADKILILHQG 622
Cdd:cd03259 162 DAKLREELREE-LKELQRElgITTIYVTHDQeEALALADRIAVMNEG 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1208-1410 |
4.77e-21 |
|
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: 93.79 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVT---LQEWRKAFG 1283
Cdd:cd03256 3 VENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPtSGSVLIDGTDINKLKgkaLRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQK--------VF--IFSG------TFRQNLdpnGKWKDEEIWKVA---DEVGLKSVIEQFPGQlnftlvdggyvLSH 1344
Cdd:cd03256 82 MIFQQfnlierlsVLenVLSGrlgrrsTWRSLF---GLFPKEEKQRALaalERVGLLDKAYQRADQ-----------LSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1345 GHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEHRIE-AMLDCQRFL 1410
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDlAREYADRIV 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
439-619 |
4.98e-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: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG--------IIKHSGRVSFCSQ----FSWImpgTIKENI 506
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGevlvdgepVTGPGPDRGYVFQqdalLPWL---TVLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 507 IFGVsydeyRYKSVVKAcQLQQDITKFAEQdntvLGEGGV------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03293 95 ALGL-----ELQGVPKA-EARERAEELLEL----VGLSGFenayphQLSGGMRQRVALARALAVDPDVLLLDEPFSALDA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14141185 581 FTEEQVFEScvckLMA-----NKTRILVT-SKMEHLRKADKILIL 619
Cdd:cd03293 165 LTREQLQEE----LLDiwretGKTVLLVThDIDEAVFLADRVVVL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1208-1398 |
5.71e-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: 98.44 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGN---AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFG 1283
Cdd:COG1123 263 VRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPtSGSILFDGKDLTKLSRRSLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VItQKVFifsgtfrQN----LDP--------------NGKWKDEEIWKVADE----VGL-KSVIEQFPGQlnftlvdggy 1340
Cdd:COG1123 343 RV-QMVF-------QDpyssLNPrmtvgdiiaeplrlHGLLSRAERRERVAEllerVGLpPDLADRYPHE---------- 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1341 vLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEH 1398
Cdd:COG1123 405 -LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISH 463
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1209-1427 |
6.27e-21 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 93.52 E-value: 6.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1209 KDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVSWNSVTLQEWRKAFG 1283
Cdd:cd03295 4 ENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTT----MKMINrliepTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQKVFIFSG-TFRQN--LDPN-GKWKDEEIWKVADE----VGL--KSVIEQFPGQlnftlvdggyvLSHGHKQLMCLA 1353
Cdd:cd03295 79 YVIQQIGLFPHmTVEENiaLVPKlLKWPKEKIRERADEllalVGLdpAEFADRYPHE-----------LSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1354 RSVLSKAKIILLDEPSAHLDPITyqviRRVLKQAFA------GCTVILCEHRI-EAMLDCQRFLVIEESNVWQYDSLQAL 1426
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPIT----RDQLQEEFKrlqqelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
.
gi 14141185 1427 L 1427
Cdd:cd03295 224 L 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1209-1414 |
6.86e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.81 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1209 KDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVswNSVTLQEW-----RKAF 1282
Cdd:COG2884 5 ENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVNGQ--DLSRLKRReipylRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQkvfifsgTFR--------QN----LDPNGKwKDEEIWK----VADEVGLKSVIEQFPGQlnftlvdggyvLSHGH 1346
Cdd:COG2884 82 GVVFQ-------DFRllpdrtvyENvalpLRVTGK-SRKEIRRrvreVLDLVGLSDKAKALPHE-----------LSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1347 KQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQaF--AGCTVILCEHRIEAMLDCQ-RFLVIEE 1414
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEE-InrRGTTVLIATHDLELVDRMPkRVLELED 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1208-1405 |
1.01e-20 |
|
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: 92.21 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-NIKGDIEIDGVSwnsvtLQEWRKAFGVIT 1286
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGKP-----LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QK----------VFIFSGTFRQNLDPNGKWKDEEIWKVADE----VGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCL 1352
Cdd:cd03235 75 QRrsidrdfpisVRDVVLMGLYGHKGLFRRLSKADKAKVDEalerVGLSELADRQIGE-----------LSGGQQQRVLL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRIEAMLD 1405
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLE 197
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
439-588 |
1.38e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.00 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR----------VSFcsQFSWIMPG-TIKENII 507
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadrgVVF--QKDALLPWlNVLDNVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 508 FGVsydeyRYKSVVKACQLQQditkfAEQDNTVLGEGGV------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 581
Cdd:COG4525 99 FGL-----RLRGVPKAERRAR-----AEELLALVGLADFarrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
....*..
gi 14141185 582 TEEQVFE 588
Cdd:COG4525 169 TREQMQE 175
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1208-1412 |
1.51e-20 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 92.81 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGV---SWNSVTLQEWRKAFG 1283
Cdd:COG3638 5 LRNLSKRY-PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPtSGEILVDGQdvtALRGRALRRLRRRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQKvfifsgtFrqNLDPN----------------------GKWKDEEIWKVA---DEVGLKSVIEQFPGQLnftlvdg 1338
Cdd:COG3638 84 MIFQQ-------F--NLVPRlsvltnvlagrlgrtstwrsllGLFPPEDRERALealERVGLADKAYQRADQL------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 1339 gyvlSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEHRIE-AMLDCQRFLVI 1412
Cdd:COG3638 148 ----SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDlARRYADRIIGL 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
437-637 |
1.52e-20 |
|
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: 92.61 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSQFSW-----IMPG--------TIK 503
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqigVLPDerglydrlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENI-----IFGVSYDEYRYK--SVVKACQLQQDITKFAEqdntvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:COG4555 93 ENIryfaeLYGLFDEELKKRieELIELLGLEEFLDRRVG-----------ELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 577 YLDVFTEEQVFEScVCKLMANKTRILVTS----KMEHLrkADKILILHQGSSYFYGTFSELQSLR 637
Cdd:COG4555 162 GLDVMARRLLREI-LRALKKEGKTVLFSShimqEVEAL--CDRVVILHKGKVVAQGSLDELREEI 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1208-1398 |
1.63e-20 |
|
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: 91.78 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsaflrmLNI--------KGDIEIDGVSWNSVTLQE 1277
Cdd:cd03255 3 LKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTL-------LNIlggldrptSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1278 W----RKAFGvitqkvFIFSG-------TFRQN------LDPNGKWKDEE-IWKVADEVGLKSVIEQFPGQlnftlvdgg 1339
Cdd:cd03255 76 LaafrRRHIG------FVFQSfnllpdlTALENvelpllLAGVPKKERRErAEELLERVGLGDRLNHYPSE--------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1340 yvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQ--AFAGCTVILCEH 1398
Cdd:cd03255 141 --LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTH 199
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
437-588 |
1.68e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.84 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR----------VSFcsQFSWIMP-GTIKEN 505
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgaergVVF--QNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIFG-----VSYDEYRYKS--VVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK11248 91 VAFGlqlagVEKMQRLEIAhqMLKKVGLEGAEKRYIWQ-----------LSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170
....*....|
gi 14141185 579 DVFTEEQVFE 588
Cdd:PRK11248 160 DAFTREQMQT 169
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
437-622 |
1.79e-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: 90.32 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII---------------KHSGRVSFCSQFSWIMPG- 500
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgedltdledelpPLRRRIGMVFQDFALFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENIIFGvsydeyryksvvkacqlqqditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03229 92 TVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14141185 581 FTEEQVfESCVCKLMAN--KTRILVTSKMEHLRK-ADKILILHQG 622
Cdd:cd03229 134 ITRREV-RALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1204-1427 |
2.19e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.34 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1204 GEMVVKDLTVKYMDDGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:PRK13657 333 GAVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQsGRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKVFIFSGTFRQNL---DPNGkwKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSK 1359
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIrvgRPDA--TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1360 AKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALL 1427
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV 557
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1201-1419 |
2.39e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.19 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1201 PSGGEMVVKDLTVkYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAflrmlnikgdieIDGVsWN----SVTL- 1275
Cdd:COG4178 358 SEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA------------IAGL-WPygsgRIARp 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1276 QEWRKAFgvITQKVFIFSGTFRQNL---DPNGKWKDEEIWKVADEVGLksviEQFPGQLNfTLVDGGYVLSHGHKQLMCL 1352
Cdd:COG4178 424 AGARVLF--LPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL----GHLAERLD-EEADWDQVLSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQ 1419
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQ 563
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
439-622 |
2.77e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 91.26 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------------VSFCSQFSWIMPG- 500
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserelarlrrrhIGFVFQFFNLLPEl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENI-----IFGVSYDEY--RYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:COG1136 102 TALENValpllLAGVSRKERreRARELLERVGLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 574 PFGYLDVFTEEQVFEscvckLMA------NKTRILVTSKMEHLRKADKILILHQG 622
Cdd:COG1136 171 PTGNLDSKTGEEVLE-----LLRelnrelGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
407-633 |
6.43e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 95.94 E-value: 6.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 407 ELLEKVQQSNG--DRKHSS---DENNVSFSHLclVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGI 481
Cdd:PRK10790 320 ELMDGPRQQYGndDRPLQSgriDIDNVSFAYR--DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 482 IKHSGR-------------VSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTL 548
Cdd:PRK10790 398 IRLDGRplsslshsvlrqgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTeEQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYG 628
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGT-EQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
|
....*
gi 14141185 629 TFSEL 633
Cdd:PRK10790 557 THQQL 561
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1206-1413 |
9.32e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 89.72 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsaflrmLNI--------KGDIEIDGV---SWNS 1272
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTL-------LNIlggldrptSGEVLIDGQdisSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1273 VTLQEWR-KAFGvitqkvFIFSG-------TFRQN----LDPNGKWKDE---EIWKVADEVGLKSVIEQFPGQlnftlvd 1337
Cdd:COG1136 78 RELARLRrRHIG------FVFQFfnllpelTALENvalpLLLAGVSRKErreRARELLERVGLGDRLDHRPSQ------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1338 ggyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPIT----YQVIRRVLKQafAGCTVILCEHRIEAMLDCQRFLVIE 1413
Cdd:COG1136 145 ----LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRE--LGTTIVMVTHDPELAARADRVIRLR 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
405-642 |
9.65e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.03 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 405 FGELLEKVQQSNgDRKHSSDE---------NNVSFSHlclvGN--PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILG 473
Cdd:PRK13657 309 FFEVEDAVPDVR-DPPGAIDLgrvkgavefDDVSFSY----DNsrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 474 ELEASEGIIK---------------HSGRVSFcsQFSWIMPGTIKENIIFG---VSYDEYRykSVVKACQLQQDITKFAE 535
Cdd:PRK13657 384 VFDPQSGRILidgtdirtvtraslrRNIAVVF--QDAGLFNRSIEDNIRVGrpdATDEEMR--AAAERAQAHDFIERKPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 536 QDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCkLMANKTRILVTSKMEHLRKADK 615
Cdd:PRK13657 460 GYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE-LMKGRTTFIIAHRLSTVRNADR 538
|
250 260
....*....|....*....|....*..
gi 14141185 616 ILILHQGSSYFYGTFSELQSLRPDFSS 642
Cdd:PRK13657 539 ILVFDNGRVVESGSFDELVARGGRFAA 565
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1208-1413 |
1.33e-19 |
|
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: 89.03 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWNSVTLQEwRKAFGV-- 1284
Cdd:cd03224 3 VENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRsGSIRFDGRDITGLPPHE-RARAGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFIFSG-TFRQNL--------DPNGKWKDEEIWkvadevGLKSVIEQFPGQLnftlvdgGYVLSHGHKQLMCLARS 1355
Cdd:cd03224 80 VPEGRRIFPElTVEENLllgayarrRAKRKARLERVY------ELFPRLKERRKQL-------AGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1356 VLSKAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRIEAMLD-CQRFLVIE 1413
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLE 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
428-619 |
1.75e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 89.76 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 428 VSFSHLCLV------GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG--------RVSFCSQ 493
Cdd:COG1116 8 LELRGVSKRfptgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 494 ----FSWImpgTIKENIIFGVsydeyRYKSVVKAcQLQQDITKFAEQdntvLGEGGV------TLSGGQRARISLARAVY 563
Cdd:COG1116 88 epalLPWL---TVLDNVALGL-----ELRGVPKA-ERRERARELLEL----VGLAGFedayphQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 564 KDADLYLLDSPFGYLDVFTEEQVfESCVCKLMA--NKTRILVTskmeH-----LRKADKILIL 619
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERL-QDELLRLWQetGKTVLFVT----HdvdeaVFLADRVVVL 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
426-622 |
1.91e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 86.35 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLclvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSgrvsfcsqfswimpgtiken 505
Cdd:cd03221 4 ENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 iifgvsydeyrykSVVKACQLQQditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQ 585
Cdd:cd03221 61 -------------STVKIGYFEQ-------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14141185 586 V------FESCVcklmanktrILVTSKMEHLRK-ADKILILHQG 622
Cdd:cd03221 109 LeealkeYPGTV---------ILVSHDRYFLDQvATKIIELEDG 143
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
936-1435 |
2.04e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.79 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 936 LITASKI---LHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFL 1012
Cdd:TIGR00958 226 NYTMARInlrIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTM 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1013 AT---VPglVVFILLRAYFLHTAQQLKQL-ESEGRSpifTHLV-TSLKGLWTLRAFRRQTYFETLFHKALN-LHTANW-- 1084
Cdd:TIGR00958 306 VTlinLP--LVFLAEKVFGKRYQLLSEELqEAVAKA---NQVAeEALSGMRTVRSFAAEEGEASRFKEALEeTLQLNKrk 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1085 ----FMYLATLRWFQMRIdmifvlffivvtFISILTTG-----EGEGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSV 1155
Cdd:TIGR00958 381 alayAGYLWTTSVLGMLI------------QVLVLYYGgqlvlTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAV 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1156 ---SRVFKFIDiQTEESMYTQIIKELPREGssdvlVIKNEHVKKSdiWPSGGEmvvkdltvkymddgNAVLENISFSISP 1232
Cdd:TIGR00958 449 gasEKVFEYLD-RKPNIPLTGTLAPLNLEG-----LIEFQDVSFS--YPNRPD--------------VPVLKGLTFTLHP 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1233 GQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWK-DEE 1310
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQpTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTpDEE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1311 IWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKqaFAG 1390
Cdd:TIGR00958 587 IMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RAS 664
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 14141185 1391 CTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQ 1435
Cdd:TIGR00958 665 RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
437-605 |
2.18e-19 |
|
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: 87.92 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG------RVSFCSQFSWIMPG-------TIK 503
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHAdglkpelTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIF-----GVSYDEYRYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:COG4133 94 ENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*..
gi 14141185 579 DVfTEEQVFESCVCKLMANKTRILVTS 605
Cdd:COG4133 163 DA-AGVALLAELIAAHLARGGAVLLTT 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
256-1411 |
2.52e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.10 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 256 NERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFftssafffsgffvvflsvLPYTVINGIVLrk 335
Cdd:PTZ00265 233 NNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMES------------------LHIGMINGFIL-- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 336 ifttISFcivlrmsvtrqfptAVQIWYDSFGMIRKIQDFLQKQEYK----------VLEYNLMTTgIIMENVTAFWE--E 403
Cdd:PTZ00265 293 ----ASY--------------AFGFWYGTRIIISDLSNQQPNNDFHggsvisillgVLISMFMLT-IILPNITEYMKslE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 404 GFGELLEKVQ-----QSNGDRKHSSDEN-----NVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILG 473
Cdd:PTZ00265 354 ATNSLYEIINrkplvENNDDGKKLKDIKkiqfkNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 474 ELEASEG--IIKHS------------GRVSFCSQFSWIMPGTIKENIIFGV----------------SYDEYRYKSVVKA 523
Cdd:PTZ00265 434 LYDPTEGdiIINDShnlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedGNDSQENKNKRNS 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 524 CQLQ-----QDITKFAEQD-------------------------------------NTVLGEGGVTLSGGQRARISLARA 561
Cdd:PTZ00265 514 CRAKcagdlNDMSNTTDSNeliemrknyqtikdsevvdvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 562 VYKDADLYLLDSPFGYLDVFTEEQVfESCVCKLMANKTRI--LVTSKMEHLRKADKILILhqgssyfygtfselqslrpd 639
Cdd:PTZ00265 594 IIRNPKILILDEATSSLDNKSEYLV-QKTINNLKGNENRItiIIAHRLSTIRYANTIFVL-------------------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 640 fSSKLMGYDTFDQFTEERRSSILTETLRRFSVDDSSAPWSKPKQSFRQTG----EVGE-----KRKNSILNSFSSVRKIS 710
Cdd:PTZ00265 653 -SNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGsyiiEQGThdalmKNKNGIYYTMINNQKVS 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 711 IVQKTplciDGESDDLQEKRLSLVPDSEQGeaalprsnmiatgptfpgrrrqsvldlmtFTPNSGSSNLQRTRTSIRkis 790
Cdd:PTZ00265 732 SKKSS----NNDNDKDSDMKSSAYKDSERG-----------------------------YDPDEMNGNSKHENESAS--- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 791 lvpqislnevDVYSRRLSQDSTLNiteeiNEEDLKECFLDDVIKIPPVTTWN---TYLRYFTLHKGLLLVliwcvlVFLV 867
Cdd:PTZ00265 776 ----------NKKSCKMSDENASE-----NNAGGKLPFLRNLFKRKPKAPNNlriVYREIFSYKKDVTII------ALSI 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 868 EVAASLFVLWLLknnpVNSGNNGTKISNSSyvviITSTSFYYIFYIYVgvadtlLALSLFRGLPL---VHTLI--TASKI 942
Cdd:PTZ00265 835 LVAGGLYPVFAL----LYAKYVSTLFDFAN----LEANSNKYSLYILV------IAIAMFISETLknyYNNVIgeKVEKT 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 943 LHRKMLHSILHAPMSTISKLK-AGGILN-RFSKDIAILDDFLPLTIFDFIQlvFIVIgaiIVVSALQPYIF---LATVPG 1017
Cdd:PTZ00265 901 MKRRLFENILYQEISFFDQDKhAPGLLSaHINRDVHLLKTGLVNNIVIFTH--FIVL---FLVSMVMSFYFcpiVAAVLT 975
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1018 LVVFILLRAYFLHTA-QQLKQLESEGRS-PIFTHLVTSLKGLWTLRAFRRQTYFetlfhkaLNLHTAnwfmylatlrwfq 1095
Cdd:PTZ00265 976 GTYFIFMRVFAIRARlTANKDVEKKEINqPGTVFAYNSDDEIFKDPSFLIQEAF-------YNMNTV------------- 1035
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1096 mridMIFVL--FFIVVTFISILTTGEGEGTAGIILTLAMNIMSTLQWAVNS-------------SIDTDSLMRSVsrvFK 1160
Cdd:PTZ00265 1036 ----IIYGLedYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSfaywfgsflirrgTILVDDFMKSL---FT 1108
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1161 FI--------------DIQTEESMYTQIIKELPREGSSDV-----LVIKNehvkKSDIwpsGGEMVVKDLTVKYMDDGNA 1221
Cdd:PTZ00265 1109 FLftgsyagklmslkgDSENAKLSFEKYYPLIIRKSNIDVrdnggIRIKN----KNDI---KGKIEIMDVNFRYISRPNV 1181
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 -VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK---------------------------------------- 1260
Cdd:PTZ00265 1182 pIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefslt 1261
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1261 ---------------GDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNLDpNGKWKD--EEIWKVADEVGLKSV 1323
Cdd:PTZ00265 1262 keggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKEDAtrEDVKRACKFAAIDEF 1340
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1324 IEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEHRIE 1401
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIA 1420
|
1370
....*....|
gi 14141185 1402 AMLDCQRFLV 1411
Cdd:PTZ00265 1421 SIKRSDKIVV 1430
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1201-1421 |
3.61e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1201 PSGGEMV-VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNikGDIEIDG--VSWnSVTLQe 1277
Cdd:COG0488 310 RLGKKVLeLEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLLA--GELEPDSgtVKL-GETVK- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1278 wrkaFGVITQKvfifsgtfRQNLDPNGK-WkdEEIWKVADEVGLKSVIeQFPGQLNF------TLVDggyVLSHGHKQLM 1350
Cdd:COG0488 380 ----IGYFDQH--------QEELDPDKTvL--DELRDGAPGGTEQEVR-GYLGRFLFsgddafKPVG---VLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 1351 CLARSVLSKAKIILLDEPSAHLDPITyqviRRVLKQA---FAGcTVILCEH-RieAMLD--CQRFLVIEESNVWQYD 1421
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEAlddFPG-TVLLVSHdR--YFLDrvATRILEFEDGGVREYP 511
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1436 |
3.69e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 89.28 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKST---LLSAFLRMLniKGDIEIDGVSWNSVTLQEWRKAFGV 1284
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQ--SGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQ---KVFIFS--------GTFRQNLDPNGKWKdeEIWKVADEVGLKSVIEQFPgqLNftlvdggyvLSHGHKQLMCLA 1353
Cdd:PRK13632 88 IFQnpdNQFIGAtveddiafGLENKKVPPKKMKD--IIDDLAKKVGMEDYLDKEP--QN---------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1354 rSVLS-KAKIILLDEPSAHLDPI----TYQVIRRVLKQAFAgcTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLS 1428
Cdd:PRK13632 155 -SVLAlNPEIIIFDESTSMLDPKgkreIKKIMVDLRKTRKK--TLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
....*...
gi 14141185 1429 EKSIFQQA 1436
Cdd:PRK13632 232 NKEILEKA 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1208-1398 |
5.38e-19 |
|
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: 87.20 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRMLNI-----KGDIEIDGVSWNSvTLQEWRKaf 1282
Cdd:cd03262 3 IKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKST----LLRCINLleepdSGTIIIDGLKLTD-DKKNINE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 gvITQKV-FIFsgtfrQ--NLDPN--------------GKWKDEEIWKVA----DEVGLKSVIEQFPGQlnftlvdggyv 1341
Cdd:cd03262 74 --LRQKVgMVF-----QqfNLFPHltvlenitlapikvKGMSKAEAEERAlellEKVGLADKADAYPAQ----------- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1342 LSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEH 1398
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTH 193
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1206-1401 |
5.92e-19 |
|
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: 87.74 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGvswNSVT------LQEW 1278
Cdd:TIGR02315 2 LEVENLSKVY-PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPsSGSILLEG---TDITklrgkkLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1279 RKAFGVITQK------------VFI----FSGTFRQNLdpnGKWKDEEIWK---VADEVGLKSVIEQFPGQLnftlvdgg 1339
Cdd:TIGR02315 78 RRRIGMIFQHynlierltvlenVLHgrlgYKPTWRSLL---GRFSEEDKERalsALERVGLADKAYQRADQL-------- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1340 yvlSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLK---QAFaGCTVILCEHRIE 1401
Cdd:TIGR02315 147 ---SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKrinKED-GITVIINLHQVD 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
437-619 |
5.98e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.52 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG--RVSFCSQFS---WIMPGTIKENIIFGV- 510
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSevpDSLPLTVRDLVAMGRw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 511 -------SYDEYRYKSVVKACQlQQDITKFAEQDntvLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 583
Cdd:NF040873 84 arrglwrRLTRDDRAAVDDALE-RVGLADLAGRQ---LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 14141185 584 EQVFESCVCKLMANKTRILVTSKMEHLRKADKILIL 619
Cdd:NF040873 156 ERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
426-629 |
1.53e-18 |
|
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: 87.02 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLclvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCS 492
Cdd:COG1120 5 ENLSVGYG---GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSwIMPG--TIKENIIFGvsydeyRY-------------KSVVKACqLQQ-DITKFAEQDNTvlgeggvTLSGGQRARI 556
Cdd:COG1120 82 QEP-PAPFglTVRELVALG------RYphlglfgrpsaedREAVEEA-LERtGLEHLADRPVD-------ELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 557 SLARAVYKDADLYLLDSPFGYLDVFTEEQVFEsCVCKL--MANKTRILVTskmeH-----LRKADKILILHQGSSYFYGT 629
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLE-LLRRLarERGRTVVMVL----HdlnlaARYADRLVLLKDGRIVAQGP 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
427-622 |
2.06e-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: 85.99 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 427 NVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-------------VSFCSQ 493
Cdd:cd03248 16 NVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 494 FSWIMPGTIKENIIFGVSYDEYryKSVVKACQ---LQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYL 570
Cdd:cd03248 96 EPVLFARSLQDNIAYGLQSCSF--ECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14141185 571 LDSPFGYLDVFTEEQVFESCVCKLmANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWP-ERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
428-579 |
2.13e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.49 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 428 VSFSHLCLV---GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR----------------- 487
Cdd:COG2884 2 IRFENVSKRypgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 488 -VSFcsQFSWIMPG-TIKENIIF-----GVSYDEYRYK--SVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISL 558
Cdd:COG2884 82 gVVF--QDFRLLPDrTVYENVALplrvtGKSRKEIRRRvrEVLDLVGLSDKAKALPHE-----------LSGGEQQRVAI 148
|
170 180
....*....|....*....|.
gi 14141185 559 ARAVYKDADLYLLDSPFGYLD 579
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLD 169
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
97-361 |
2.18e-18 |
|
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: 87.55 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 97 VQPVLLGRIIASYDPENKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLIYKKTLKL--------- 167
Cdd:cd18596 15 APPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssks 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 168 ----------SSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGllwdllqF-------SAFCGLGLL 230
Cdd:cd18596 95 seskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIV-------FlyrllgwSALVGLAVM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 231 IILVIFQAILGKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFFTSSAF 310
Cdd:cd18596 168 VLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLW 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 311 FFSGFFVVFLSVLPYTVINGIVLR--KIFTTISFCIVLRMSVTR---QFPTAVQIW 361
Cdd:cd18596 248 FLIPILVTVVTFATYTLVMGQELTasVAFTSLALFNMLRGPLNVlpeLITQLLQAK 303
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
436-647 |
2.83e-18 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 85.85 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 436 VGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-----------RVSFCSQFSWIMPG-TIK 503
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFGVSYDEYRYKSVVKACqlqQDITKFAEQDNtVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 583
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKV---LEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 584 EQVFESC-VCKLMANKTRILVTSKMEHLRK-ADKILILHQGSSYFYGTFSE-LQSLRPDFSSKLMGY 647
Cdd:cd03299 166 EKLREELkKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEvFKKPKNEFVAEFLGF 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1208-1417 |
3.24e-18 |
|
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: 86.33 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVSW-NSVTLQEWRKA 1281
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTL----AKLLNglllpTSGKVTVDGLDTlDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 FGVitqkVFifsgtfrQNLD----------------PNGKWKDEEIWK----VADEVGLKSVIEQFPGQlnftlvdggyv 1341
Cdd:TIGR04520 79 VGM----VF-------QNPDnqfvgatveddvafglENLGVPREEMRKrvdeALKLVGMEDFRDREPHL----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1342 LSHGHKQLMCLArSVLS-KAKIILLDEPSAHLDPIT----YQVIRRVLKQafAGCTVILCEHRIEAMLDCQRFLVIEESN 1416
Cdd:TIGR04520 137 LSGGQKQRVAIA-GVLAmRPDIIILDEATSMLDPKGrkevLETIRKLNKE--EGITVISITHDMEEAVLADRVIVMNKGK 213
|
.
gi 14141185 1417 V 1417
Cdd:TIGR04520 214 I 214
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1218-1401 |
3.56e-18 |
|
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: 84.01 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1218 DGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDG--VSWNSVTLQEWRKAFGVITQKV--FIF 1292
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRpQSGAVLIDGepLDYSRKGLLERRQRVGLVFQDPddQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1293 SGTFRQNLD--P-NGKWKDEEIWKVADE----VGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:TIGR01166 83 AADVDQDVAfgPlNLGLSEAEVERRVREaltaVGASGLRERPTHCL-----------SGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 14141185 1366 DEPSAHLDPITYQVIRRVLKQAFA-GCTVILCEHRIE 1401
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAeGMTVVISTHDVD 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1222-1417 |
3.98e-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: 85.22 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNL 1300
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPqGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1301 DPN-GKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQV 1379
Cdd:cd03248 109 AYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 14141185 1380 IRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNV 1417
Cdd:cd03248 189 VQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1219-1398 |
4.59e-18 |
|
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: 84.38 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1219 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM-LNIKGDIEIDGVSWNSV---TLQEWRKAFGVITQKvfifsg 1294
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLrgrAIPYLRRKIGVVFQD------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 tFRQNLDPN---------------GKWKDEEIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSK 1359
Cdd:cd03292 87 -FRLLPDRNvyenvafalevtgvpPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14141185 1360 AKIILLDEPSAHLDPITYQVIRRVLKQA-FAGCTVILCEH 1398
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH 194
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1207-1428 |
4.64e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.81 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKYmddGNAVLeNISFSISPGQRVGLLGRTGSGKSTLLSA---FLRMlnIKGDIEIDGVSWNSVTLQEwRKaFG 1283
Cdd:COG3840 3 RLDDLTYRY---GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLiagFLPP--DSGRILWNGQDLTALPPAE-RP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQKVFIFSG-TFRQN----LDPNGKWKDEEIWKV---ADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARS 1355
Cdd:COG3840 75 MLFQENNLFPHlTVAQNiglgLRPGLKLTAEQRAQVeqaLERVGLAGLLDRLPGQL-----------SGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1356 VLSKAKIILLDEPSAHLDPI----TYQVIRRVLKQafAGCTVILCEHRIEAMLD-CQRFLVIEESNVWQYDSLQALLS 1428
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPAlrqeMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1436 |
5.36e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM-LNIKGDIEIDGVSWNSVTLQEWRKAFGVIT 1286
Cdd:PRK13647 7 VEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKV--FIFSGTF-------RQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCLARSVL 1357
Cdd:PRK13647 86 QDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1358 SKAKIILLDEPSAHLDPITYQVIRRVLKQAF-AGCTVILCEHRIEAMLD-CQRFLVIEESNVWQYDSlQALLSEKSIFQQ 1435
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDEDIVEQ 233
|
.
gi 14141185 1436 A 1436
Cdd:PRK13647 234 A 234
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1208-1432 |
6.14e-18 |
|
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: 84.65 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWNSVTLQE-WRKAFGVI 1285
Cdd:COG0410 6 VENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRsGSIRFDGEDITGLPPHRiARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1286 TQKVFIFSG-TFRQNLD---PNGKWKDEEIWKVADevglksVIEQFP------GQLnftlvdGGYvLSHGHKQLMCLARS 1355
Cdd:COG0410 84 PEGRRIFPSlTVEENLLlgaYARRDRAEVRADLER------VYELFPrlkerrRQR------AGT-LSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1356 VLSKAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRIEAMLD-CQRFLVIEE-SNVWQyDSLQALLSEKSI 1432
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRlNREGVTILLVEQNARFALEiADRAYVLERgRIVLE-GTAAELLADPEV 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1208-1395 |
8.20e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 84.76 E-value: 8.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNA--VLENISFSISPGQRVGLLGRTGSGKSTLlsafLRML-----NIKGDIEIDGVSWN------SVT 1274
Cdd:COG1116 10 LRGVSKRFPTGGGGvtALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIaglekPTSGEVLVDGKPVTgpgpdrGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1275 LQE-----WRkafgvitqkvfifsgTFRQN----LDPNGKWKDE---EIWKVADEVGLKSVIEQFPGQlnftlvdggyvL 1342
Cdd:COG1116 86 FQEpallpWL---------------TVLDNvalgLELRGVPKAErreRARELLELVGLAGFEDAYPHQ-----------L 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 1343 SHGHKQLMCLARSVLSKAKIILLDEPSAHLDPIT----YQVIRRVLKQafAGCTVIL 1395
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerlQDELLRLWQE--TGKTVLF 194
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
439-622 |
8.38e-18 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 84.31 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------VSFCSQFSWIMPG-TIKENI 506
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 507 IFGV---------SYDEYRYK--SVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:cd03296 96 AFGLrvkprserpPEAEIRAKvhELLKLVQLDWLADRYPAQ-----------LSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 576 GYLDVFTEEQVfESCVCKLM--ANKTRILVT-SKMEHLRKADKILILHQG 622
Cdd:cd03296 165 GALDAKVRKEL-RRWLRRLHdeLHVTTVFVThDQEEALEVADRVVVMNKG 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
437-622 |
9.18e-18 |
|
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: 83.46 E-value: 9.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------VSFCSQFSWIMPG-TIKE 504
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMVFQNYALYPHmTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFG-----VSYDEY--RYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03301 92 NIAFGlklrkVPKDEIdeRVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14141185 578 LDVFTEEQVFESCVcKLMAN--KTRILVT-SKMEHLRKADKILILHQG 622
Cdd:cd03301 161 LDAKLRVQMRAELK-RLQQRlgTTTIYVThDQVEAMTMADRIAVMNDG 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
440-623 |
1.29e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.29 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-----------RVSFCSQ-FSWIMPGTIKENII 507
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQhYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 508 FGV---------SYDEYRYK--SVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK10851 97 FGLtvlprrerpNAAAIKAKvtQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 577 YLD--VFTE-----EQVFEScvCKLmankTRILVTSKMEH-LRKADKILILHQGS 623
Cdd:PRK10851 166 ALDaqVRKElrrwlRQLHEE--LKF----TSVFVTHDQEEaMEVADRVVVMSQGN 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
440-628 |
2.05e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 82.97 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSfcsqfSWIMPG-------TIKENIIF---- 508
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGggfnpelTGRENIYLngrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 509 -GVSYDEYRYKSvvkacqlqQDITKFAEqdntvLGEGG----VTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 583
Cdd:cd03220 112 lGLSRKEIDEKI--------DEIIEFSE-----LGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14141185 584 EQVFESCVCKLMANKTRILVTSKMEHLRK-ADKILILHQGSSYFYG 628
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
426-634 |
2.44e-17 |
|
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: 82.93 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFShlcLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG----------------RVS 489
Cdd:cd03261 4 RGLTKS---FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 490 FCSQFSWI---MpgTIKENIIFGVS----YDEYRYKSVVKAC----QLQQDITKFAEQdntvlgeggvtLSGGQRARISL 558
Cdd:cd03261 81 MLFQSGALfdsL--TVFENVAFPLRehtrLSEEEIREIVLEKleavGLRGAEDLYPAE-----------LSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 559 ARAVYKDADLYLLDSPFGYLDVFTEEqVFESCVCKL--MANKTRILVTSKMEHLRK-ADKILILHQGSSYFYGTFSELQ 634
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASG-VIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELR 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
439-622 |
3.14e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 84.81 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFcsqfSWIMPG-----------------T 501
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----TNLPPRerrvgfvfqhyalfphmT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENIIFGVSyDEYRYKSVVKACQLQQ----DITKFAE----QdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:COG1118 92 VAENIAFGLR-VRPPSKAEIRARVEELlelvQLEGLADrypsQ-----------LSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 574 PFGYLD-------------VFTEEQVfescvcklmankTRILVT-SKMEHLRKADKILILHQG 622
Cdd:COG1118 160 PFGALDakvrkelrrwlrrLHDELGG------------TTVFVThDQEEALELADRVVVMNQG 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1208-1384 |
3.17e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.90 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDdgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDG-VSWNSVTLQ-------EWR 1279
Cdd:PRK14239 8 VSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGsIVYNGHNIYsprtdtvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1280 KAFGVITQKVFIFSGTFRQN----LDPNGKwKDEEIWKVADEVGLK--SVIEQFPGQLNftlvDGGYVLSHGHKQLMCLA 1353
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENvvygLRLKGI-KDKQVLDEAVEKSLKgaSIWDEVKDRLH----DSALGLSGGQQQRVCIA 160
|
170 180 190
....*....|....*....|....*....|.
gi 14141185 1354 RSVLSKAKIILLDEPSAHLDPITYQVIRRVL 1384
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1208-1411 |
3.95e-17 |
|
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: 82.48 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMlnIKGDIEIDGVSwnsVT-LQEWRKA-F 1282
Cdd:cd03219 3 VRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLfnlISGFLRP--TSGSVLFDGED---ITgLPPHEIArL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVI-T-QKVFIFSG-TFRQNL--------------DPNGKWKD---EEIWKVADEVGLKSVIEQFPGQLnftlvdggyvl 1342
Cdd:cd03219 76 GIGrTfQIPRLFPElTVLENVmvaaqartgsglllARARREERearERAEELLERVGLADLADRPAGEL----------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1343 SHGHKQLMCLARSVLSKAKIILLDEPSAHLDPI-TYQVIRRVLKQAFAGCTVILCEHRIEAMLD-CQRFLV 1411
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTV 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
428-622 |
3.98e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 84.74 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 428 VSFSHLCLV--GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVsfcsqFSWIMPG----- 500
Cdd:COG3839 4 LELENVSKSygGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-----VTDLPPKdrnia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 ------------TIKENIIFG-----VSYDEY--RYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARA 561
Cdd:COG3839 79 mvfqsyalyphmTVYENIAFPlklrkVPKAEIdrRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVALGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 562 VYKDADLYLLDSPFGYLDVFTEEQVfESCVCKLMA--NKTRILVTskmeH-----LRKADKILILHQG 622
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEM-RAEIKRLHRrlGTTTIYVT----HdqveaMTLADRIAVMNDG 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1220-1443 |
4.73e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 87.72 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1220 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDgvswnsvtlqeWRKAFGVITQKVFIFSGTFRQN 1299
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1300 LDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDP-ITYQ 1378
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQ 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1379 VIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQAISSSEKM 1443
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKM 843
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
437-660 |
5.31e-17 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 82.98 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILgELEASEGIIKHSG-----------RVSF--CSQFSWIMPGTIK 503
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFgvIPQKVFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENI-IFGVSYDEYRYKsVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 582
Cdd:cd03289 95 KNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 583 eEQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFTEERRSS 660
Cdd:cd03289 174 -YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLFPRRNSSK 250
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1206-1426 |
5.56e-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: 81.40 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSvTLQEWRKAFGV 1284
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFIFSG-TFRQNLD-------PNGKWKDEEIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSV 1356
Cdd:cd03263 80 CPQFDALFDElTVREHLRfyarlkgLPKSEIKEEVELLLRVLGLTDKANKRART-----------LSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1357 LSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRI-EAMLDCQRFLVIEESNVWQYDSLQAL 1426
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMdEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1208-1414 |
8.03e-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: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSvTLQEWRKAFGVIT 1286
Cdd:cd03268 3 TNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFIFSGTFRQNLDPNGK---WKDEEIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKII 1363
Cdd:cd03268 80 APGFYPNLTARENLRLLARllgIRKKRIDEVLDVVGLKDSAKKKVKG-----------FSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1364 LLDEPSAHLDPITYQVIRR-VLKQAFAGCTVILCEHRIEAM-LDCQRFLVIEE 1414
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRElILSLRDQGITVLISSHLLSEIqKVADRIGIINK 201
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1225-1421 |
1.06e-16 |
|
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: 80.42 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1225 NISFSIsPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSW----NSVTLQEWRKAFGVITQKVFIFSG-TFRQ 1298
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPdGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1299 NL------DPNGKWKDEEIwKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHL 1372
Cdd:cd03297 95 NLafglkrKRNREDRISVD-ELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1373 DPITYQVIRRVLKQAFA--GCTVILCEHRI-EAMLDCQRFLVIEESNVWQYD 1421
Cdd:cd03297 163 DRALRLQLLPELKQIKKnlNIPVIFVTHDLsEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1203-1399 |
1.56e-16 |
|
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: 79.52 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1203 GGEMVVKDLTV----KYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAF---LRMLNIKGDIEIDGVswnSVTL 1275
Cdd:cd03213 1 GVTLSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGVSGEVLINGR---PLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1276 QEWRKAFGVITQK-VFIFSGTFRQNLDPNGKwkdeeiwkvadevgLKSvieqfpgqlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:cd03213 78 RSFRKIIGYVPQDdILHPTLTVRETLMFAAK--------------LRG-------------------LSGGERKRVSIAL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14141185 1355 SVLSKAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHR 1399
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQ 170
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1227-1428 |
1.58e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.40 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1227 SFSISPGQRVGLLGRTGSGKSTLLS---AFLRMlnIKGDIEIDGVSWNSVTLQewRKAFGVITQKVFIFSG-TFRQN--- 1299
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNliaGFLTP--ASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1300 -LDPNGKWKDEE---IWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPI 1375
Cdd:PRK10771 95 gLNPGLKLNAAQrekLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1376 TYQVIRRVLKQAfagC-----TVILCEHRIE-AMLDCQRFLVIEESNVWqYD-SLQALLS 1428
Cdd:PRK10771 164 LRQEMLTLVSQV---CqerqlTLLMVSHSLEdAARIAPRSLVVADGRIA-WDgPTDELLS 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
388-629 |
1.89e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 388 MTTGIIMENVT-AFW-----EEGFGELLEKVQQSNGDRKHssdennvsfshlclvgnpVLKNINLNIEKGEMLAITGSTG 461
Cdd:COG1134 1 MSSMIEVENVSkSYRlyhepSRSLKELLLRRRRTRREEFW------------------ALKDVSFEVERGESVGIIGRNG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 462 SGKTSLLMLILGELEASEGIIKHSGRVS--------FCSQFSwimpGtiKENIIF-----GVSYDEYRYKsvvkacqlQQ 528
Cdd:COG1134 63 AGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPELT----G--RENIYLngrllGLSRKEIDEK--------FD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 529 DITKFAEqdntvLGE------GgvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV-FTE--EQVFEscvcKLMAN-K 598
Cdd:COG1134 129 EIVEFAE-----LGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAaFQKkcLARIR----ELRESgR 197
|
250 260 270
....*....|....*....|....*....|..
gi 14141185 599 TRILVTSKMEHLRK-ADKILILHQGSSYFYGT 629
Cdd:COG1134 198 TVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1208-1412 |
2.18e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.21 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTL----AKLLNglllpEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKV-FIFSGTFRQN-----LDPNGKWKDEEIWKV---ADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLA 1353
Cdd:PRK13635 84 GMVFQNPdNQFVGATVQDdvafgLENIGVPREEMVERVdqaLRQVGMEDFLNREPHR-----------LSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1354 RSVLSKAKIILLDEPSAHLDPITYQ----VIRRVLKQafAGCTVILCEHRIEAMLDCQRFLVI 1412
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRRevleTVRQLKEQ--KGITVLSITHDLDEAAQADRVIVM 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
437-622 |
2.73e-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: 82.07 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------VSFCSQ----FswimPG- 500
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQdyalF----PHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENIIFG-----VSYDEyRYKSVVKACQLQQdITKFAE----QdntvlgeggvtLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG3842 93 TVAENVAFGlrmrgVPKAE-IRARVAELLELVG-LEGLADryphQ-----------LSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 572 DSPFGYLDVFTEEQV-FEscVCKLMA--NKTRILVT-SKMEHLRKADKILILHQG 622
Cdd:COG3842 160 DEPLSALDAKLREEMrEE--LRRLQRelGITFIYVThDQEEALALADRIAVMNDG 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
438-633 |
3.18e-16 |
|
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: 83.80 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEAS---EGIIKHSG-------------RVSFCSQ--FSWIMP 499
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelsealrgrRIGMVFQdpMTQLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 GTIKENIIF-----GVSYDEYRYKsvVKACQLQQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:COG1123 99 VTVGDQIAEalenlGLSRAEARAR--VLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMALALDPDLLIADEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 575 FGYLDVFTEEQVFEsCVCKLMA--NKTRILVTSKMEH-LRKADKILILHQGSSYFYGTFSEL 633
Cdd:COG1123 170 TTALDVTTQAEILD-LLRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1208-1374 |
4.23e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 79.27 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNI-----KGDIEIDG--VSWNSVTLQEWRK 1280
Cdd:COG1126 4 IENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLL----RCINLleepdSGTITVDGedLTDSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFGVitqkVFifsgtfrQ--NLDPN--------------GKWKDEEIWKVADE----VGLKSVIEQFPGQLnftlvdggy 1340
Cdd:COG1126 78 KVGM----VF-------QqfNLFPHltvlenvtlapikvKKMSKAEAEERAMEllerVGLADKADAYPAQL--------- 137
|
170 180 190
....*....|....*....|....*....|....
gi 14141185 1341 vlSHGHKQLMCLARSVLSKAKIILLDEPSAHLDP 1374
Cdd:COG1126 138 --SGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
437-634 |
7.57e-16 |
|
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: 78.76 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG----------------RVSFCSQ-FSWIMP 499
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMIFQqFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 GTIKENI-------------IFGVSYDEYRYKSvvKACQLQQDITKFAEQ--DntvlgeggvTLSGGQRARISLARAVYK 564
Cdd:cd03256 93 LSVLENVlsgrlgrrstwrsLFGLFPKEEKQRA--LAALERVGLLDKAYQraD---------QLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 565 DADLYLLDSPFGYLDVFTEEQVFEscvckLMA------NKTRILVTSKMEHLRK-ADKILILHQGSSYFYGTFSELQ 634
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMD-----LLKrinreeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELT 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
441-628 |
8.61e-16 |
|
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: 77.72 E-value: 8.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIE---KGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSQFSWIMPG----------------- 500
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkiglvfqqyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 -TIKENIIFGV-----SYDEYRYKSVVKACQLQQditkfaeqdntVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:cd03297 90 lNVRENLAFGLkrkrnREDRISVDELLDLLGLDH-----------LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 575 FGYLDVFTEEQVfESCVCKLMA--NKTRILVTSKMEHL-RKADKILILHQGSSYFYG 628
Cdd:cd03297 159 FSALDRALRLQL-LPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
423-634 |
9.11e-16 |
|
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: 78.48 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 423 SDENNVSFSHLCLV--GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR------------- 487
Cdd:COG1127 1 MSEPMIEVRNLTKSfgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 488 -----VSFcsQ----FSWImpgTIKENIIF------GVSYDEYRykSVVKAC----QLQQDITKF-AEqdntvlgeggvt 547
Cdd:COG1127 81 rrrigMLF--QggalFDSL---TVFENVAFplrehtDLSEAEIR--ELVLEKlelvGLPGAADKMpSE------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 548 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTeEQVFESCVCKL--MANKTRILVTSKMEHLRK-ADKILILHQGSS 624
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPIT-SAVIDELIRELrdELGLTSVVVTHDLDSAFAiADRVAVLADGKI 220
|
250
....*....|
gi 14141185 625 YFYGTFSELQ 634
Cdd:COG1127 221 IAEGTPEELL 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
437-622 |
1.11e-15 |
|
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: 75.93 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRvsfcsqfswimpgtikeniifgvsydEYR 516
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 517 YKSVVKACQLqqditkfaeqdntvlgegGVT----LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFEsCVC 592
Cdd:cd03216 66 FASPRDARRA------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK-VIR 126
|
170 180 190
....*....|....*....|....*....|..
gi 14141185 593 KLMAN-KTRILVTSKMEHLRK-ADKILILHQG 622
Cdd:cd03216 127 RLRAQgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1219-1445 |
1.27e-15 |
|
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: 79.13 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1219 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDG-VSWNSvtlqewrkafgvitQKVFIFSGTF 1296
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEpSEGKIKHSGrISFSS--------------QFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1297 RQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPIT 1376
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1377 -YQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFqqaisSSEKMRF 1445
Cdd:cd03291 195 eKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF-----SSKLMGY 259
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1208-1412 |
1.56e-15 |
|
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: 77.41 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNI-----KGDIEIDGVSWNSvTLQEWRK 1280
Cdd:cd03266 4 ADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGllepdAGFATVDGFDVVK-EPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFGVITQKVFIFSG-TFRQNL----DPNGKWKDE---EIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCL 1352
Cdd:cd03266 79 RLGFVSDSTGLYDRlTARENLeyfaGLYGLKGDEltaRLEELADRLGMEELLDRRVGG-----------FSTGMRQKVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRI-EAMLDCQRFLVI 1412
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMqEVERLCDRVVVL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
438-622 |
1.64e-15 |
|
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: 77.55 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRV----------SFCSQFSWIM--PG----- 500
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkIRRKEIQMVFqdPMsslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 --TIKENI-----IFGVSYDEYRYKSVV--KACQLQQD---ITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADL 568
Cdd:cd03257 98 rmTIGEQIaeplrIHGKLSKKEARKEAVllLLVGVGLPeevLNRYPHE-----------LSGGQRQRVAIARALALNPKL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 569 YLLDSPFGYLDVFTEEQVFEscvckLMA------NKTRILVTSKMEHLRK-ADKILILHQG 622
Cdd:cd03257 167 LIADEPTSALDVSVQAQILD-----LLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAG 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1208-1413 |
4.20e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.58 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNI-----KGDIEIDGVSWNSVT---LQE 1277
Cdd:COG1135 4 LENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTL----IRCINLlerptSGSVLVDGVDLTALSereLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1278 WRKAFGVITQKvfiF----SGTFRQN------LDpngKWKDEEIWKVADE----VGLKSVIEQFPGQlnftlvdggyvLS 1343
Cdd:COG1135 80 ARRKIGMIFQH---FnllsSRTVAENvalpleIA---GVPKAEIRKRVAEllelVGLSDKADAYPSQ-----------LS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1344 HGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEH------RIeamldCQRFLVIE 1413
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHemdvvrRI-----CDRVAVLE 215
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1208-1414 |
4.22e-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: 73.64 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAflrmlnIKGDIEIDGvswnsvtlqewrkafGVITQ 1287
Cdd:cd03221 3 LENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKL------IAGELEPDE---------------GIVTW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1288 KVFIFSGTFRQnldpngkwkdeeiwkvadevglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:cd03221 60 GSTVKIGYFEQ-------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 1368 PSAHLDPITYQVIRRVLKQaFAGcTVILCEH-RieAMLD--CQRFLVIEE 1414
Cdd:cd03221 97 PTNHLDLESIEALEEALKE-YPG-TVILVSHdR--YFLDqvATKIIELED 142
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
437-632 |
6.04e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIK--HSGRVSFCSQ-----------FSWI---MPG 500
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKlgETVKIGYFDQhqeeldpdktvLDELrdgAPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENII-----FGVSYDeyryksvvkacqlqqDITKFAEqdntvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:COG0488 407 GTEQEVRgylgrFLFSGD---------------DAFKPVG-----------VLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 576 GYLDVFT----EE--QVFESCVcklmanktrILVTskmeH----LRK-ADKILILHQGS-SYFYGTFSE 632
Cdd:COG0488 461 NHLDIETlealEEalDDFPGTV---------LLVS----HdryfLDRvATRILEFEDGGvREYPGGYDD 516
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1208-1395 |
7.01e-15 |
|
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: 77.40 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML----NIKGDIEIDGVSWNSVTLQEWRKA 1281
Cdd:COG0444 4 VRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppgITSGEILFDGEDLLKLSEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 FGVITQKVFifsgtfrQN----LDP--------------NGKWKDEEIWKVADE----VGL---KSVIEQFPGQlnftlv 1336
Cdd:COG0444 84 RGREIQMIF-------QDpmtsLNPvmtvgdqiaeplriHGGLSKAEARERAIEllerVGLpdpERRLDRYPHE------ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1337 dggyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDP-ITYQVIR--RVLKQAFaGCTVIL 1395
Cdd:COG0444 151 -----LSGGMRQRVMIARALALEPKLLIADEPTTALDVtIQAQILNllKDLQREL-GLAILF 206
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1222-1401 |
7.58e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.90 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNI-----KGDIEIDGVSWN--SVTLQEWRKAFGVITQKVFIFSG 1294
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLL----RCINKleeitSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 -TFRQN-----LDPNGKWKdEEIWKVADE----VGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:PRK09493 92 lTALENvmfgpLRVRGASK-EEAEKQAREllakVGLAERAHHYPSEL-----------SGGQQQRVAIARALAVKPKLML 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 14141185 1365 LDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRIE 1401
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIG 197
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1206-1375 |
8.20e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.23 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM------LNIKGDIEIDGV-----SWNSVT 1274
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgARVEGEILLDGEdiydpDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1275 LqewRKAFGVITQKVFIFSGTFRQN----LDPNGKWKDEEI-------------WkvaDEVglKsvieqfpGQLNftlvD 1337
Cdd:COG1117 90 L---RRRVGMVFQKPNPFPKSIYDNvaygLRLHGIKSKSELdeiveeslrkaalW---DEV--K-------DRLK----K 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 14141185 1338 GGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPI 1375
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI 188
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
439-622 |
8.79e-15 |
|
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: 74.76 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPGTIKEN 505
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIfgvSYDEYRYKSVVKACQLQqditkfaeqdntvlgEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQ 585
Cdd:cd03369 102 LD---PFDEYSDEEIYGALRVS---------------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 14141185 586 VFEScVCKLMANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:cd03369 164 IQKT-IREEFTNSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1209-1414 |
9.78e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 75.51 E-value: 9.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1209 KDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaflrMLNikGD--------IEIDGVSWNSVTLQEWRK 1280
Cdd:COG1119 7 RNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS----LIT--GDlpptygndVRLFGERRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFGVIT----------QKVF--IFSGTFrqnlDPNGKWK--DEEIWKVADE----VGLKSVIEQFPGQlnftlvdggyvL 1342
Cdd:COG1119 79 RIGLVSpalqlrfprdETVLdvVLSGFF----DSIGLYRepTDEQRERAREllelLGLAHLADRPFGT-----------L 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1343 SHGHKQLMCLARSVLSKAKIILLDEPSAHLDPI-TYQVIRRVLKQAFAG-CTVILCEHRIEAMLDC-QRFLVIEE 1414
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGaRELLLALLDKLAAEGaPTLVLVTHHVEEIPPGiTHVLLLKD 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1197-1400 |
9.86e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.29 E-value: 9.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1197 SDIWPSGGEMVVKDLTVKYMddGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM------LNIKGDIEIDGVS- 1269
Cdd:PRK14271 13 ADVDAAAPAMAAVNLTLGFA--GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGGRSi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1270 WNSVTLQEWRKAFGVITQKVFIF---------SGTFRQNLDPNGKWKDEEIWKVAdEVGLKSVIEQfpgqlnfTLVDGGY 1340
Cdd:PRK14271 91 FNYRDVLEFRRRVGMLFQRPNPFpmsimdnvlAGVRAHKLVPRKEFRGVAQARLT-EVGLWDAVKD-------RLSDSPF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1341 VLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRI 1400
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1208-1399 |
1.42e-14 |
|
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: 72.96 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVkYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN-----IKGDIEIDGVSwnsvtlqewRKAF 1282
Cdd:cd03223 3 LENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF----RALAglwpwGSGRIGMPEGE---------DLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 gvITQKVFIFSGTFRQnldpngkwkdeeiwkvadevglksvieqfpgQLNFTLVDggyVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:cd03223 69 --LPQRPYLPLGTLRE-------------------------------QLIYPWDD---VLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 14141185 1363 ILLDEPSAHLDPITYQVIRRVLKQafAGCTVILCEHR 1399
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1223-1430 |
1.52e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.02 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVT----LQEWRKAFGVITQ--KVFIFSGT 1295
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAGYHITPETgnknLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1296 FRQ-------NLDPNGKWKDEEIWKVADEVGLK-SVIEQFPgqlnftlvdggYVLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:PRK13641 103 VLKdvefgpkNFGFSEDEAKEKALKWLKKVGLSeDLISKSP-----------FELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1368 PSAHLDPITyqviRRVLKQAF-----AGCTVILCEHRIEAMLD-CQRFLVIEESNVWQYDSLQALLSEK 1430
Cdd:PRK13641 172 PAAGLDPEG----RKEMMQLFkdyqkAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
440-622 |
1.81e-14 |
|
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: 74.52 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGeLEASEGIIKHSGRVSFCSQ--FSWIM------------------- 498
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNR-LNDLIPGAPDEGEVLLDGKdiYDLDVdvlelrrrvgmvfqkpnpf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 499 PGTIKENIIFGVSYDEYRYKSVVKAcQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:cd03260 94 PGSIYDNVAYGLRLHGIKLKEELDE-RVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14141185 579 D-VFTEEqvFESCVCKLMANKTRILVTSKMEH-LRKADKILILHQG 622
Cdd:cd03260 173 DpISTAK--IEELIAELKKEYTIVIVTHNMQQaARVADRTAFLLNG 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
441-638 |
2.11e-14 |
|
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: 74.42 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR----------VSF--CSQFSWImpgTIKENIIF 508
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrmVVFqnYSLLPWL---TVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 509 GV-------SYDEYR--YKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:TIGR01184 78 AVdrvlpdlSKSERRaiVEEHIALVGLTEAADKRPGQ-----------LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 580 VFTEEQVFEscvcKLM-----ANKTRILVTSKM-EHLRKADKILILHQGSSYFYGTFSELQSLRP 638
Cdd:TIGR01184 147 ALTRGNLQE----ELMqiweeHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEVPFPRP 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1401 |
2.66e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsaFLRMLNI----KGDIEIDG--VSWNSVTLQEWRKA 1281
Cdd:PRK13639 4 TRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTL---FLHFNGIlkptSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 FGVITQKV--FIFSGTFRQNL--DP-NGKWKDEEIWKVADE----VGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCL 1352
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVafGPlNLGLSKEEVEKRVKEalkaVGMEGFENKPP-----------HHLSGGQKKRVAI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAF-AGCTVILCEHRIE 1401
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkEGITIIISTHDVD 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
447-637 |
2.91e-14 |
|
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: 74.37 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 447 NIEKGEMLAITGSTGSGKTSLLMLILGELEASEG-IIKHSGRVSFCSQF-SWIMPGTIKE---NIIFGVSYDEYRYKSVV 521
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdIEIELDTVSYKPQYiKADYEGTVRDllsSITKDFYTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 522 KACQLQQDItkfaeqDNTVLgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVftEEQVFESCVCK---LMANK 598
Cdd:cd03237 101 KPLQIEQIL------DREVP-----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQRLMASKVIRrfaENNEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14141185 599 TRILVtskmEH-LRKADKI---LILHQGSSYFYGTFSELQSLR 637
Cdd:cd03237 168 TAFVV----EHdIIMIDYLadrLIVFEGEPSVNGVANPPQSLR 206
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
431-632 |
3.36e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 431 SHLCLVGNP----VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG---------------RVSFC 491
Cdd:PRK13637 9 THIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 492 SQFS--WIMPGTIKENIIFGVS----YDEYRYKSVVKACQLQQ-DITKFAEQDNtvlgeggVTLSGGQRARISLARAVYK 564
Cdd:PRK13637 89 FQYPeyQLFEETIEKDIAFGPInlglSEEEIENRVKRAMNIVGlDYEDYKDKSP-------FELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 565 DADLYLLDSPFGYLDVFTEEQVFEScVCKLMA--NKTRILVTSKMEHLRK-ADKILILHQGSSYFYGTFSE 632
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNK-IKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1207-1427 |
3.76e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 75.57 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMlnI-------KGDIEIDGVSWNS-VTLQEW 1278
Cdd:COG1118 4 EVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTL----LRI--IagletpdSGRIVLNGRDLFTnLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1279 RKAFgvitqkVFifsgtfrQN--LDPN-------------GKWKDEEIWKVADE----VGLKSVIEQFPGQlnftlvdgg 1339
Cdd:COG1118 76 RVGF------VF-------QHyaLFPHmtvaeniafglrvRPPSKAEIRARVEEllelVQLEGLADRYPSQ--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1340 yvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEH-RIEAMLDCQRFLVIEESN 1416
Cdd:COG1118 134 --LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGR 211
|
250
....*....|.
gi 14141185 1417 VWQYDSLQALL 1427
Cdd:COG1118 212 IEQVGTPDEVY 222
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
858-1125 |
4.43e-14 |
|
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: 74.51 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 858 LIWCVLVFLVEVAASLFVLWLLKnnpvnsgnngtkisnssYVV--IITSTSFYYIFYIYVGVADTLLALSLFRGLPLVHT 935
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTK-----------------LLIddVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 936 LITASKILH--RKMLHS-ILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFL 1012
Cdd:cd07346 64 ARLGQRVVFdlRRDLFRhLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1013 ATVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLR 1092
Cdd:cd07346 144 VALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA 223
|
250 260 270
....*....|....*....|....*....|...
gi 14141185 1093 WFQMRIDMIFVLFFIVVTFISILTTGEGEGTAG 1125
Cdd:cd07346 224 LFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG 256
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
440-628 |
4.51e-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: 73.07 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELE---ASEGIIKHSG----------RVSFCSQFSWIMPG-TIKEN 505
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGqprkpdqfqkCVAYVRQDDILLPGlTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIFGV-------SYDEYRYKSVvkacqlqqDITKFAEQDNTVLGEGGVT-LSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03234 102 LTYTAilrlprkSSDAIRKKRV--------EDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 578 LDVFTEEQVFEscVCKLMANKTRILVTS----KMEHLRKADKILILHQGSSYFYG 628
Cdd:cd03234 174 LDSFTALNLVS--TLSQLARRNRIVILTihqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
937-1162 |
5.50e-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: 74.17 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 937 ITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPyIFLATVP 1016
Cdd:cd18559 67 IFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAAVGIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1017 GLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRrqtyFETLFHKALNLHTANWFMYL---ATLRW 1093
Cdd:cd18559 146 LGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFE----WEEAFIRQVDAKRDNELAYLpsiVYLRA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1094 FQMRIDMIFVLFFIVVTFISILTTGEGEGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFI 1162
Cdd:cd18559 222 LAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1208-1403 |
6.08e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 75.13 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMlnI-------KGDIEIDGVSWNSVTLQEwRK 1280
Cdd:COG3842 8 LENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTL----LRM--IagfetpdSGRILLDGRDVTGLPPEK-RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 aFGVitqkVFifsgtfrQN--LDPN-------------GKWKDEEIWKVADE----VGLKSVIEQFPGQlnftlvdggyv 1341
Cdd:COG3842 79 -VGM----VF-------QDyaLFPHltvaenvafglrmRGVPKAEIRARVAEllelVGLEGLADRYPHQ----------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 1342 LSHGHKQLMCLARSVLSKAKIILLDEPSAHLDP----ITYQVIRRVLKQafAGCTVILCEH-RIEAM 1403
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQRE--LGITFIYVTHdQEEAL 200
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1208-1414 |
6.49e-14 |
|
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: 73.64 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDG---NAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN--IK---GDIEIDGVSWNS---VTLQ 1276
Cdd:TIGR04521 3 LKNVSYIYQPGTpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLI----QHLNglLKptsGTVTIDGRDITAkkkKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1277 EWRKAFGVitqkVF------IFSGTFR-------QNLdpngKWKDEEIWKVADE----VGL-KSVIEQFPgqlnFTLvdg 1338
Cdd:TIGR04521 79 DLRKKVGL----VFqfpehqLFEETVYkdiafgpKNL----GLSEEEAEERVKEalelVGLdEEYLERSP----FEL--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1339 gyvlSHGHKQLMCLArSVLS-KAKIILLDEPSAHLDPITYQVIRRVLKQAF--AGCTVILCEHRIEAMLD-CQRFLVIEE 1414
Cdd:TIGR04521 144 ----SGGQMRRVAIA-GVLAmEPEVLILDEPTAGLDPKGRKEILDLFKRLHkeKGLTVILVTHSMEDVAEyADRVIVMHK 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1208-1412 |
8.62e-14 |
|
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: 70.54 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflrmlNI--------KGDIEIDG--VSWNSVTlQE 1277
Cdd:cd03216 3 LRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLM-------KIlsglykpdSGEILVDGkeVSFASPR-DA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1278 WRKAFGVITQkvfifsgtfrqnldpngkwkdeeiwkvadevglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVL 1357
Cdd:cd03216 73 RRAGIAMVYQ------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1358 SKAKIILLDEPSAHLDP----ITYQVIRRVLKQafaGCTVILCEHRI-EAMLDCQRFLVI 1412
Cdd:cd03216 99 RNARLLILDEPTAALTPaeveRLFKVIRRLRAQ---GVAVIFISHRLdEVFEIADRVTVL 155
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1208-1401 |
9.18e-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: 71.84 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQrVGLLGRTGSGKSTL---LSAFLRMlnIKGDIEIDGVSwNSVTLQEWRKAFGV 1284
Cdd:cd03264 3 LENLTKRY--GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLmriLATLTPP--SSGTIRIDGQD-VLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFIFSG-TFRQNLD-------PNGKWKDEEIWKVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSV 1356
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDyiawlkgIPSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14141185 1357 LSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIE 1401
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVE 190
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
435-622 |
9.28e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 70.92 E-value: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 435 LVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVsfcsqfswIMPGTIKENIIFGVSY-- 512
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP--------VTRRSPRDAIRAGIAYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 513 DEYRYKSVVkacqLQQDITkfaeqDNTVLGeggVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVC 592
Cdd:cd03215 82 EDRKREGLV----LDLSVA-----ENIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
170 180 190
....*....|....*....|....*....|.
gi 14141185 593 KLMANKTRILVTSKM-EHLRKADKILILHQG 622
Cdd:cd03215 150 LADAGKAVLLISSELdELLGLCDRILVMYEG 180
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1223-1443 |
9.73e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.70 E-value: 9.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRmlnikgdiEIDGVSWNSVTLqewRKAFGVITQKVFIFSGTFRQNLDP 1302
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG--------ELPPRSDASVVI---RGTVAYVPQVSWIFNATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1303 NGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDP-ITYQVIR 1381
Cdd:PLN03130 702 GSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFD 781
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1382 RVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQAISSSEKM 1443
Cdd:PLN03130 782 KCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKM 843
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
433-586 |
1.02e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 71.74 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 433 LCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASegiIKHSGRVSF----CS-------------QFS 495
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA---FSASGEVLLngrrLTalpaeqrrigilfQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 496 WIMPG-TIKENIIFGVSYD---EYRYKSVVKAcqLQQ-DITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYL 570
Cdd:COG4136 86 LLFPHlSVGENLAFALPPTigrAQRRARVEQA--LEEaGLAGFADRDPA-------TLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|....*.
gi 14141185 571 LDSPFGYLDVFTEEQV 586
Cdd:COG4136 157 LDEPFSKLDAALRAQF 172
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
437-580 |
1.13e-13 |
|
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: 72.27 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------VSFCSQFSWIMPG-TIKE 504
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFGVsydeyRYKSVVKACQLQQ-----DITKFAEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03300 92 NIAFGL-----RLKKLPKAEIKERvaealDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
.
gi 14141185 580 V 580
Cdd:cd03300 163 L 163
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
443-580 |
1.82e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 443 NINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIK------HSGRVSFCSQFSWI--MPGtIK------ENIIF 508
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQDLLYLghQPG-IKteltalENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 509 gvsydeyryksvvkACQLQQDITKFAEQDntVLGEGGV---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK13538 98 --------------YQRLHGPGDDEALWE--ALAQVGLagfedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
.
gi 14141185 580 V 580
Cdd:PRK13538 162 K 162
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1219-1432 |
2.05e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.46 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1219 GNAVLENISFSISPGQRVGLLGRTGSGKSTllsAFLRMLNI----KGDIEIDGVSWNSVTLQE-WRKAFGVITQKVFIFS 1293
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIvprdAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1294 -----GTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLnftlvdgGYVLSHGHKQLMCLARSVLSKAKIILLDEP 1368
Cdd:PRK10895 92 rlsvyDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 1369 SAHLDPITYQVIRRVLKQAF-AGCTVILCEHRIEAMLD-CQRFLVIEESNVWQYDSLQALLSEKSI 1432
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1222-1432 |
2.06e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.45 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RMLNIKGDIEIDG---VSWNsvTLQEWRKAFGVITQKVFIFSG-TF 1296
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCgDPRATSGRIVFDGkdiTDWQ--TAKIMREAVAIVPEGRRVFSRmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1297 RQNLDPNGKWKDEEIWKVAdevgLKSVIEQFPgQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPIT 1376
Cdd:PRK11614 98 EENLAMGGFFAERDQFQER----IKWVYELFP-RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1377 YQVIRRVLKQAFA-GCTVILCEHRI-EAMLDCQRFLVIEESNVWQYDSLQALLSEKSI 1432
Cdd:PRK11614 173 IQQIFDTIEQLREqGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
439-628 |
2.23e-13 |
|
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: 70.27 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLIlgeleasegiikhSGRVSFCsqfswIMPGTIKENiifGVSYDEYRYK 518
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------------AGRRTGL-----GVSGEVLIN---GRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 519 SvvkacqlqqdITKFAEQDNTVLGEGGV-----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVF 587
Cdd:cd03213 82 K----------IIGYVPQDDILHPTLTVretlmfaaklrGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14141185 588 EScvckLMA----NKTRILVT----SKMEHLrkADKILILHQGSSYFYG 628
Cdd:cd03213 152 SL----LRRladtGRTIICSIhqpsSEIFEL--FDKLLLLSQGRVIYFG 194
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1206-1398 |
2.33e-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: 70.89 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLqewrKAFGV 1284
Cdd:TIGR03740 1 LETKNLSKRF--GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRpTSGEIIFDGHPWTRKDL----HKIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFIFSG-TFRQNLDPNGKW---KDEEIWKVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKA 1360
Cdd:TIGR03740 75 LIESPPLYENlTARENLKVHTTLlglPDSRIDEVLNIVDLTNTGKKKAKQF-----------SLGMKQRLGIAIALLNHP 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14141185 1361 KIILLDEPSAHLDPITYQVIRRVLKqAFA--GCTVILCEH 1398
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIR-SFPeqGITVILSSH 182
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1222-1412 |
2.34e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 70.77 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-MLNIKGDIEIDGVSWNSVT------LQEWR---KAFGVITQKVFI 1291
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEVLFDGKPLDIAArnrigyLPEERglyPKMKVIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1292 FS--GTFRQNLdpnGKWKDEEIWKVADEVGLKSVIEQfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPS 1369
Cdd:cd03269 95 AQlkGLKKEEA---RRRIDEWLERLELSEYANKRVEE---------------LSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14141185 1370 AHLDPITYQVIRRVL-KQAFAGCTVILCEHRIEAMLD-CQRFLVI 1412
Cdd:cd03269 157 SGLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLL 201
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
440-588 |
2.72e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-----------------RVSFCSQFSWIMPG-T 501
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENI-----IFGVSYDEYRYKS--VVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK11629 104 ALENVampllIGKKKPAEINSRAleMLAAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLVLADEP 172
|
170
....*....|....
gi 14141185 575 FGYLDVFTEEQVFE 588
Cdd:PRK11629 173 TGNLDARNADSIFQ 186
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
439-622 |
2.73e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.21 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFC----------------SQFSWIMP--- 499
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrrkkflrrigvvfgqkTQLWWDLPvid 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 --GTIKEniIFGVSYDEYRyKSVVKACQLqQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03267 115 sfYLLAA--IYDLPPARFK-KRLDELSEL-LDLEELLDTPVR-------QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14141185 578 LDVFTEEQV--FESCVCKLmaNKTRILVTSK-MEHLRK-ADKILILHQG 622
Cdd:cd03267 184 LDVVAQENIrnFLKEYNRE--RGTTVLLTSHyMKDIEAlARRVLVIDKG 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
437-579 |
2.95e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------VSFCSQFSWIMPG-TIKE 504
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrhVNTVFQSYALFPHmTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFG-----VSYDEY--RYKSVVKACQLQQditkFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK09452 106 NVAFGlrmqkTPAAEItpRVMEALRMVQLEE----FAQRKPH-------QLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
..
gi 14141185 578 LD 579
Cdd:PRK09452 175 LD 176
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1436 |
3.41e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDG--VSWNSVTLQEWRKAFGV 1284
Cdd:PRK13636 8 VEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGkpIDYSRKGLMKLRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKV--FIFSGTFRQNLD---PNGKWKDEEIWKVADEVGLKSVIEQFPGQLNftlvdggYVLSHGHKQLMCLARSVLSK 1359
Cdd:PRK13636 87 VFQDPdnQLFSASVYQDVSfgaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPT-------HCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1360 AKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEHRIEAM-LDCQRFLVIEESNVWQYDSLQALLSEKSIFQQA 1436
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKV 239
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1208-1403 |
3.77e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 71.62 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDG---NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGV--SWNSVTLQEWRKA 1281
Cdd:PRK13637 5 IENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVdiTDKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 FGVITQ--KVFIFSGTFRQNLD---PNGKWKDEEIWKVADE----VGLKsvIEQFPGQLNFTlvdggyvLSHGHKQLMCL 1352
Cdd:PRK13637 85 VGLVFQypEYQLFEETIEKDIAfgpINLGLSEEEIENRVKRamniVGLD--YEDYKDKSPFE-------LSGGQKRRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDP-----ITYQVirRVLKQAFaGCTVILCEHRIEAM 1403
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPkgrdeILNKI--KELHKEY-NMTIILVSHSMEDV 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1201-1417 |
3.88e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1201 PSGGEMVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRML-------------------NIKG 1261
Cdd:PRK11247 8 NQGTPLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLLagletpsagellagtaplaEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1262 DIEIdgvSWNSVTLQEWRKafgVITQkvfifsgtfrQNLDPNGKWKDEEIwKVADEVGLKSVIEQFPGqlnftlvdggyV 1341
Cdd:PRK11247 82 DTRL---MFQDARLLPWKK---VIDN----------VGLGLKGQWRDAAL-QALAAVGLADRANEWPA-----------A 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1342 LSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPIT----YQVIRRVLKQafAGCTVILCEHRI-EAMLDCQRFLVIEESN 1416
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTriemQDLIESLWQQ--HGFTVLLVTHDVsEAVAMADRVLLIEEGK 211
|
.
gi 14141185 1417 V 1417
Cdd:PRK11247 212 I 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
426-580 |
4.09e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLclvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG-IIKHSG-RVSFCSQFSWIMPG-TI 502
Cdd:COG0488 2 ENLSKSFG---GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGeVSIPKGlRIGYLPQEPPLDDDlTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 503 KENIIFGVS-----YDEYRY------KSVVKACQLQQDITKFAEQD--------NTVLGEGGV----------TLSGGQR 553
Cdd:COG0488 79 LDTVLDGDAelralEAELEEleaklaEPDEDLERLAELQEEFEALGgweaearaEEILSGLGFpeedldrpvsELSGGWR 158
|
170 180
....*....|....*....|....*..
gi 14141185 554 ARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1222-1386 |
4.15e-13 |
|
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: 70.65 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLlsaFLRMLNI----KGDIEIDGvswNSVTL----QEWRKAFGVITQKVFIFS 1293
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTT---FYMIVGLvkpdSGKILLDG---QDITKlpmhKRARLGIGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1294 G-TFRQNL--------DPNGKWKdEEIWKVADEVGLKSVIEQFpgqlnftlvdgGYVLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:cd03218 89 KlTVEENIlavleirgLSKKERE-EKLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEIARALATNPKFLL 156
|
170 180
....*....|....*....|..
gi 14141185 1365 LDEPSAHLDPITYQVIRRVLKQ 1386
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKI 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
428-628 |
5.26e-13 |
|
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: 74.21 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 428 VSFSHLCLVGNP----VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSF 490
Cdd:TIGR00957 1285 VEFRNYCLRYREdldlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 491 CSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYL 570
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 571 LDSPFGYLDVFTEEQV-------FESCVCKLMANK-------TRILVTSKMEhLRKADKILILHQGSSYFYG 628
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIqstirtqFEDCTVLTIAHRlntimdyTRVIVLDKGE-VAEFGAPSNLLQQRGIFYS 1515
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1208-1442 |
5.84e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 5.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDG--------VSWNSVTLQEWR 1279
Cdd:PRK14258 10 VNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqnIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1280 KAFGVITQKVFIFSGTFRQNLDPNGK---W--------------KDEEIWkvaDEVGLKsvieqfpgqLNFTLVDggyvL 1342
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKivgWrpkleiddivesalKDADLW---DEIKHK---------IHKSALD----L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1343 SHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAF--AGCTVILCEHRIEAMLDCQRFLVIEESNVWQY 1420
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
250 260
....*....|....*....|..
gi 14141185 1421 DSLQALLSEKSIFQQAISSSEK 1442
Cdd:PRK14258 232 GQLVEFGLTKKIFNSPHDSRTR 253
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
99-355 |
5.92e-13 |
|
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: 71.09 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 99 PVLLGRIIASYDPENKVERSIAIYLgIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLIYKKTLKLSSRVLDKISIG 178
Cdd:cd18559 17 PSNLWLLLWFDDPVNGPQEHGQVYL-SVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 179 QLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAILGKMMVKYRDQRAAKINER 258
Cdd:cd18559 96 ELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 259 LVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVFLSVLPYTVI---NGIVLRK 335
Cdd:cd18559 176 YKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRhslAGLVALK 255
|
250 260
....*....|....*....|
gi 14141185 336 IFTTISFCIVLRMSVtRQFP 355
Cdd:cd18559 256 VFYSLALTTYLNWPL-NMSP 274
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1218-1432 |
6.12e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.79 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1218 DGNAVLENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLniKGDIEIDGVSWNSVT-LQEWRKAFGVITQKVFI-F 1292
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQ--KGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPETqF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1293 SG-TFRQNL---DPNGKWKDEEIWKVAD----EVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:PRK13644 91 VGrTVEEDLafgPENLCLPPIEIRKRVDralaEIGLEKYRHRSPKT-----------LSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1365 LDEPSAHLDPITYQ-VIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSI 1432
Cdd:PRK13644 160 FDEVTSMLDPDSGIaVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
438-639 |
6.93e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLLM----LILGE------LEASEGIIKHSGRVS------------FCSQFS 495
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDksagshIELLGRTVQREGRLArdirksrantgyIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 496 WIMPGTIKENIIFGVSYDE------YRYKSVVKACQLQQDITK-----FAEQDNTvlgeggvTLSGGQRARISLARAVYK 564
Cdd:PRK09984 97 LVNRLSVLENVLIGALGSTpfwrtcFSWFTREQKQRALQALTRvgmvhFAHQRVS-------TLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 565 DADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVT-SKMEH-LRKADKILILHQGSSYFYGTFSELQSLRPD 639
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFD 246
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
404-588 |
7.45e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.92 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 404 GFGELLEKVQ--QSNGDRKHSSDENNVSFSHLCLV---GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEAS 478
Cdd:COG4178 337 GFEEALEAADalPEAASRIETSEDGALALEDLTLRtpdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 479 EGIIKH--SGRVSFCSQFSWIMPGTIKENIIF---GVSYDEYRYKSVVKACQLQQDITKFAEQDNTvlgegGVTLSGGQR 553
Cdd:COG4178 417 SGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGEQ 491
|
170 180 190
....*....|....*....|....*....|....*
gi 14141185 554 ARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFE 588
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
405-622 |
7.71e-13 |
|
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: 70.37 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 405 FGElleKVQQSNGDRKHSSDENNVSFSHLCLVGnpvLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKH 484
Cdd:cd03294 10 FGK---NPQKAFKLLAKGKSKEEILKKTGQTVG---VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 485 SG-----------------RVSFCSQFSWIMPG-TIKENIIF-----GVSYDEYRYKS--VVKACQLQQDITKFAEQdnt 539
Cdd:cd03294 84 DGqdiaamsrkelrelrrkKISMVFQSFALLPHrTVLENVAFglevqGVPRAEREERAaeALELVGLEGWEHKYPDE--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 540 vlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD--VFTEEQvfeSCVCKLMAN--KTRILVTSKM-EHLRKAD 614
Cdd:cd03294 161 --------LSGGMQQRVGLARALAVDPDILLMDEAFSALDplIRREMQ---DELLRLQAElqKTIVFITHDLdEALRLGD 229
|
....*...
gi 14141185 615 KILILHQG 622
Cdd:cd03294 230 RIAIMKDG 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1210-1398 |
8.27e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.26 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1210 DLTVKYMDdgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN------IKGDIEIDGVSWNS--VTLQEWRKA 1281
Cdd:PRK14267 9 NLRVYYGS--NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYSpdVDPIEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 FGVitqkVFIFSGTF---------------------RQNLDPNGKW--KDEEIWkvaDEVglKSVIEQFPGQLnftlvdg 1338
Cdd:PRK14267 87 VGM----VFQYPNPFphltiydnvaigvklnglvksKKELDERVEWalKKAALW---DEV--KDRLNDYPSNL------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1339 gyvlSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEH 1398
Cdd:PRK14267 151 ----SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
437-622 |
8.91e-13 |
|
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: 69.10 E-value: 8.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII------------------KHSGRVsFcSQFSWIM 498
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkkninelrQKVGMV-F-QQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 499 PGTIKENIIF------GVSYDEyrykSVVKACQLQQDItKFAEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLD 572
Cdd:cd03262 90 HLTVLENITLapikvkGMSKAE----AEERALELLEKV-GLADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 573 SPFGYLDvftEEQVFEscVCKLMAN-----KTRILVTSKMEHLRK-ADKILILHQG 622
Cdd:cd03262 161 EPTSALD---PELVGE--VLDVMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
437-662 |
9.26e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 9.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------VSFCSQFSWIMPG-TIKE 504
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFGVSYDEY-------RYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK11607 111 NIAFGLKQDKLpkaeiasRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 578 LD-----------VFTEEQVFESCVcklmanktriLVTSKMEH-LRKADKILILHQGSSYFYGTFSELQSlRPD--FSSK 643
Cdd:PRK11607 180 LDkklrdrmqlevVDILERVGVTCV----------MVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEIYE-HPTtrYSAE 248
|
250 260
....*....|....*....|
gi 14141185 644 LMG-YDTFDQFTEERRSSIL 662
Cdd:PRK11607 249 FIGsVNVFEGVLKERQEDGL 268
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
441-622 |
9.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 9.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-----------------RVSFCSQF--SWIMPGT 501
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFpeAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENII-----FGVSYDEYRYKSV--VKACQLQQDitkfaeqdntVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK13641 103 VLKDVEfgpknFGFSEDEAKEKALkwLKKVGLSED----------LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14141185 575 FGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEHLRK-ADKILILHQG 622
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHG 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
427-622 |
1.11e-12 |
|
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: 72.24 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 427 NVSFSHLCLVGNPV--LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII----------------KHSGRV 488
Cdd:COG1123 265 NLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklsrrslrELRRRV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 489 SFCSQ--FSWIMPG-TIKENIIFGVsydeyRYKSVVKACQLQQDITKFAEQ---DNTVLGEGGVTLSGGQRARISLARAV 562
Cdd:COG1123 345 QMVFQdpYSSLNPRmTVGDIIAEPL-----RLHGLLSRAERRERVAELLERvglPPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 563 YKDADLYLLDSPFGYLDVFTEEQVFEscvckLMA------NKTRILVT---SKMEHLrkADKILILHQG 622
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILN-----LLRdlqrelGLTYLFIShdlAVVRYI--ADRVAVMYDG 481
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1222-1401 |
1.17e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNI-----KGDIEIDGVSW------NSVTLQEWRKAFGVITQKVF 1290
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLL----RVLNLletpdSGQLNIAGHQFdfsqkpSEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1291 IFSG-TFRQNL--------DPNGKWKDEEIWKVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAK 1361
Cdd:COG4161 93 LWPHlTVMENLieapckvlGLSKEQAREKAMKLLARLRLTDKADRFPLHL-----------SGGQQQRVAIARALMMEPQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14141185 1362 IILLDEPSAHLDP-ITYQVIRRVLKQAFAGCTVILCEHRIE 1401
Cdd:COG4161 162 VLLFDEPTAALDPeITAQVVEIIRELSQTGITQVIVTHEVE 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1218-1386 |
1.27e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1218 DGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDGVS---WNSVTLQEWRKAFGVITQ------- 1287
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPlhnLNRRQLLPVRHRIQVVFQdpnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1288 -----KVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQ-FPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAK 1361
Cdd:PRK15134 377 prlnvLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAE-----------FSGGQRQRIAIARALILKPS 445
|
170 180
....*....|....*....|....*
gi 14141185 1362 IILLDEPSAHLDPITYQVIRRVLKQ 1386
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKS 470
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1205-1422 |
1.34e-12 |
|
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: 69.29 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1205 EMVVKDLTVKYmddGNAV-LENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRMLNiKGDIEIDGVSWNSVTLQEwrKA 1281
Cdd:cd03296 2 SIEVRNVSKRF---GDFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRliAGLERPD-SGTILFGGEDATDVPVQE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 FGVITQKVFIFSG-TFRQNL-----------DPNGKWKDEEIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQL 1349
Cdd:cd03296 76 VGFVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQ-----------LSGGQRQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 1350 MCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAF--AGCTVILCEH-RIEAMLDCQRFLVIEESNVWQYDS 1422
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1205-1417 |
1.44e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1205 EMVVKDLTVKYMDDgnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWNSVTLQEWRKAFG 1283
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQKVFIFSGTFRQNLDPNGK------W-----KDEEIWKVADEvglKSVIEQFPGQLnftLVDggyvLSHGHKQLMCL 1352
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRspwlslWgrlsaEDNARVNQAME---QTRINHLADRR---LTD----LSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDpITYQV----IRRVLKQafAGCTVILCEHRI-EAMLDCQRFLVIEESNV 1417
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLD-INHQVelmrLMRELNT--QGKTVVTVLHDLnQASRYCDHLVVLANGHV 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
439-622 |
1.51e-12 |
|
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: 69.55 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPGTIKEN 505
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTeEQ 585
Cdd:cd03288 115 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-EN 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 14141185 586 VFESCVCKLMANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRG 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1221-1414 |
1.75e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 69.33 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1221 AVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRML-----NIKGDieidgVSWNSVTL----QEWRKAFGVITQKVF- 1290
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTL----ARLLvglesPSQGN-----VSWRGEPLaklnRAQRKAFRRDIQMVFq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1291 --------------IFSGTFRQNLDPNGKWKDEEIWKVADEVGLK-SVIEQFPGQlnftlvdggyvLSHGHKQLMCLARS 1355
Cdd:PRK10419 97 dsisavnprktvreIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQ-----------LSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1356 VLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEHRIEAMLD-CQRFLVIEE 1414
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKklQQQFGTACLFITHDLRLVERfCQRVMVMDN 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
446-622 |
1.84e-12 |
|
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: 68.29 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 446 LNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------VSFCSQFSWIMPG-TIKENIIFGVSyd 513
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGLS-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 514 eyryKSVVKACQLQQDITKFAEQdntvLGEGGV------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQ-- 585
Cdd:cd03298 97 ----PGLKLTAEDRQAIEVALAR----VGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEml 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14141185 586 --VFESCVCKLMankTRILVTSKMEHLRK-ADKILILHQG 622
Cdd:cd03298 169 dlVLDLHAETKM---TVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1174-1413 |
1.88e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.24 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1174 IIKELPREGSSDVLVIKNEHVKKSDIWPSGG-EMVVKDLT-VKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLS 1251
Cdd:PRK13536 6 VAEEAPRRLELSPIERKHQGISEAKASIPGSmSTVAIDLAgVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1252 AFLRMLNI-KGDIEIDGVSWNSvTLQEWRKAFGVITQkvfiFSG-----TFRQNLDPNGKW---KDEEIwkvadEVGLKS 1322
Cdd:PRK13536 86 MILGMTSPdAGKITVLGVPVPA-RARLARARIGVVPQ----FDNldlefTVRENLLVFGRYfgmSTREI-----EAVIPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1323 VIE--QFPGQLNFTLVDggyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA-GCTVILCEHR 1399
Cdd:PRK13536 156 LLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHF 231
|
250
....*....|....*
gi 14141185 1400 I-EAMLDCQRFLVIE 1413
Cdd:PRK13536 232 MeEAERLCDRLCVLE 246
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
427-687 |
2.12e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.25 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 427 NVSFSHLclVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG----------------RVSF 490
Cdd:PRK13644 6 NVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqgirklvGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 491 CSQFSWIMPGTIKENIIFGVSydeyryksvvKACQLQQDITKFAEQdntVLGEGGV---------TLSGGQRARISLARA 561
Cdd:PRK13644 84 QNPETQFVGRTVEEDLAFGPE----------NLCLPPIEIRKRVDR---ALAEIGLekyrhrspkTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 562 VYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGtfsELQSLRPDFS 641
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEG---EPENVLSDVS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 14141185 642 SKLMGYdTFDQFTEerrssiLTETLRRFSVddsSAPWSKPK--QSFRQ 687
Cdd:PRK13644 228 LQTLGL-TPPSLIE------LAENLKMHGV---VIPWENTSspSSFAE 265
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
428-604 |
2.52e-12 |
|
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: 68.57 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 428 VSFSHLCLV--GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG-----------------IIKHSGRV 488
Cdd:COG1119 4 LELRNVTVRrgGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvweLRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 489 SfCSQFSWIMPGTIKENII----FGVS--YDEYRYKSVVKACQL--QQDITKFAEQDntvLGeggvTLSGGQRARISLAR 560
Cdd:COG1119 84 S-PALQLRFPRDETVLDVVlsgfFDSIglYREPTDEQRERARELleLLGLAHLADRP---FG----TLSQGEQRRVLIAR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14141185 561 AVYKDADLYLLDSPFGYLDVFTEEQVFEScVCKLMAN--KTRILVT 604
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLAL-LDKLAAEgaPTLVLVT 200
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
440-622 |
3.25e-12 |
|
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: 67.84 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-----------------RVSFCSQFSWIMPG-T 501
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararlrarHVGFVFQSFQLLPTlT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENI-----IFGVSYDEYRYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:COG4181 107 ALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14141185 577 YLDVFTEEQVFEscvckLM--ANKTR----ILVTSKMEHLRKADKILILHQG 622
Cdd:COG4181 176 NLDAATGEQIID-----LLfeLNRERgttlVLVTHDPALAARCDRVLRLRAG 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
440-628 |
3.33e-12 |
|
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: 67.31 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-VSFCSQ--FSWiMPG--------TIKENIIF 508
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpLDIAARnrIGY-LPEerglypkmKVIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 509 -----GVSYDEYRYksvvkacQLQQDITKF--AEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 581
Cdd:cd03269 94 laqlkGLKKEEARR-------RIDEWLERLelSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14141185 582 TEEqVFESCVCKLMAN-KTRILVTSKMEHL-RKADKILILHQGSSYFYG 628
Cdd:cd03269 163 NVE-LLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1222-1424 |
4.29e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.34 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRMLNiKGDIEIDGVSWNSVTLQEWRKAFgvitqkVFIFSGTFRQ- 1298
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRiiAGLEHQT-SGHIRFHGTDVSRLHARDRKVGF------VFQHYALFRHm 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1299 ----NLD-----------PNGKWKDEEIWKVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKII 1363
Cdd:PRK10851 90 tvfdNIAfgltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 1364 LLDEPSAHLDPITYQVIRRVLKQ---AFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQ 1424
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQlheELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1209-1401 |
4.39e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1209 KDLTVKYMDdgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM------LNIKGDIEIDGVSWNS--VTLQEWRK 1280
Cdd:PRK14243 14 ENLNVYYGS--FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVEGKVTFHGKNLYApdVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFGVITQKVFIFSGTFRQNL----DPNGKWKD-----EEIWKVA---DEVGLKsvieqfpgqlnftLVDGGYVLSHGHKQ 1348
Cdd:PRK14243 92 RIGMVFQKPNPFPKSIYDNIaygaRINGYKGDmdelvERSLRQAalwDEVKDK-------------LKQSGLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1349 LMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIE 1401
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
448-586 |
5.30e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 448 IEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSQFswIMP---GTIKENI-----IFGVSYdeyrYKS 519
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQY--IKPdydGTVEDLLrsitdDLGSSY----YKS 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 520 -VVKACQLQqditKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVftEEQV 586
Cdd:PRK13409 436 eIIKPLQLE----RLLDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRL 490
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1206-1428 |
5.32e-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: 67.36 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmddGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVswNSVTLQEWRKAFGV 1284
Cdd:cd03299 1 LKVENLSKDW---KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKpDSGKILLNGK--DITNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFIFSG-TFRQNLD-------PNGKWKDEEIWKVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSV 1356
Cdd:cd03299 76 VPQNYALFPHmTVYKNIAyglkkrkVDKKEIERKVLEIAEMLGIDHLLNRKPETL-----------SGGEQQRVAIARAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1357 LSKAKIILLDEPSAHLDPITYQVIRRVLKQAF--AGCTVILCEHR-IEAMLDCQRFLVIEESNVWQYDSLQALLS 1428
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1208-1405 |
5.86e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRML----NIKGDI----------------EIDG 1267
Cdd:TIGR03269 3 VKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMdqyePTSGRIiyhvalcekcgyverpSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1268 ----VSWNSVTLQE---W----------RKAFGVITQKVFIFSGTFR------QNLDPNGKWKDEEIWKVADevglksVI 1324
Cdd:TIGR03269 80 epcpVCGGTLEPEEvdfWnlsdklrrriRKRIAIMLQRTFALYGDDTvldnvlEALEEIGYEGKEAVGRAVD------LI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1325 EQFpgQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAF--AGCTVILCEHRIEA 1402
Cdd:TIGR03269 154 EMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEV 231
|
...
gi 14141185 1403 MLD 1405
Cdd:TIGR03269 232 IED 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
411-637 |
7.59e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 411 KVQQSNgDRKHSSDENNVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLIL------------------ 472
Cdd:PTZ00265 1155 RIKNKN-DIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneht 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 473 ----------GELEASEG--------------------IIKHSGRV-------------------SFCSQFSWIMPGTIK 503
Cdd:PTZ00265 1234 ndmtneqdyqGDEEQNVGmknvnefsltkeggsgedstVFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLFNMSIY 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFGvsYDEYRYKSVVKACQ---LQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PTZ00265 1314 ENIKFG--KEDATREDVKRACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 581 FTEEQVFESCV-CKLMANKTRILVTSKMEHLRKADKILILH---QGSSYF--YGTFSELQSLR 637
Cdd:PTZ00265 1392 NSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFNnpdRTGSFVqaHGTHEELLSVQ 1454
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
441-622 |
7.66e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.73 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLML------------ILGELEASEGI--IKHSGR----VSFCSQFS--WIMPG 500
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliisetgqtIVGDYAIPANLkkIKEVKRlrkeIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENIIFGVSY----DEYRYKSV---VKACQLQQDITKfaeqdntvlgEGGVTLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK13645 107 TIEKDIAFGPVNlgenKQEAYKKVpelLKLVQLPEDYVK----------RSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14141185 574 PFGYLDVFTEEQvFESCVCKLMANKTR--ILVTSKMEH-LRKADKILILHQG 622
Cdd:PRK13645 177 PTGGLDPKGEED-FINLFERLNKEYKKriIMVTHNMDQvLRIADEVIVMHEG 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
426-622 |
8.13e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLCLVgNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-RVSFC------------- 491
Cdd:PRK13632 11 ENVSFSYPNSE-NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGiTISKEnlkeirkkigiif 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 492 ----SQFSWImpgTIKENIIFGVS---YDEYRYKSVVKACQLQQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYK 564
Cdd:PRK13632 90 qnpdNQFIGA---TVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQ-------NLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 565 DADLYLLDSPFGYLDVFTEEQVFescvcKLM------ANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIK-----KIMvdlrktRKKTLISITHDMDEAILADKVIVFSEG 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
437-579 |
8.21e-12 |
|
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: 66.28 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG---------RVSFCSQ--------FSWIMP 499
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRkigvvfqdFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 GTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
440-633 |
9.14e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG------------RVSFCSQFSWIMPG-TIKENI 506
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQFDNLDPDfTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 507 -IFGvsydeyRY--KSVVKACQLQQDITKFAEQDNTVLGEGGvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 583
Cdd:PRK13537 102 lVFG------RYfgLSAAAARALVPPLLEFAKLENKADAKVG-ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 584 EQVFESCVCKLMANKTRILVTSKMEHL-RKADKILILHQGSSYFYGTFSEL 633
Cdd:PRK13537 175 HLMWERLRSLLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
438-618 |
9.24e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.65 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLI-------LGEL----------EASEGIIKHSGRVSFcSQFSWIMPG 500
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdglkvndpKVDERLIRQEAGMVF-QQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENIIFGVSydEYRYKSVVKACQLQQDITK---FAEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK09493 93 TALENVMFGPL--RVRGASKEEAEKQARELLAkvgLAERAHHYPSE----LSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14141185 578 LDVFTEEQVFEscVCKLMANK--TRILVTSKMEHLRKADKILI 618
Cdd:PRK09493 167 LDPELRHEVLK--VMQDLAEEgmTMVIVTHEIGFAEKVASRLI 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1206-1398 |
1.19e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.47 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmddGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN------IKGDIEIDGVSWNSVTLQEW 1278
Cdd:PRK14247 4 IEIRDLKVSF---GQVeVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1279 RKAFGVITQ------KVFIFSGTF-----------RQNLDPNGKWKDE--EIWkvaDEVglKSVIEQFPGQLnftlvdgg 1339
Cdd:PRK14247 81 RRRVQMVFQipnpipNLSIFENVAlglklnrlvksKKELQERVRWALEkaQLW---DEV--KDRLDAPAGKL-------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1340 yvlSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEH 1398
Cdd:PRK14247 148 ---SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1220-1401 |
1.25e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1220 NAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNI-----KGDIEIDGVSW------NSVTLQEWRKAFGVITQK 1288
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLL----RVLNLlemprSGTLNIAGNHFdfsktpSDKAIRELRRNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1289 VFIFSG-TFRQNL--DP---NGKWKDEEIwKVADEV----GLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLS 1358
Cdd:PRK11124 91 YNLWPHlTVQQNLieAPcrvLGLSKDQAL-ARAEKLlerlRLKPYADRFPLHL-----------SGGQQQRVAIARALMM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14141185 1359 KAKIILLDEPSAHLDP-ITYQVIRRVLKQAFAGCTVILCEHRIE 1401
Cdd:PRK11124 159 EPQVLLFDEPTAALDPeITAQIVSIIRELAETGITQVIVTHEVE 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1208-1373 |
1.25e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMlnIKGDIEIDGvswNSVTLQE-WRkaFGVIT 1286
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTL----LKI--LAGELEPDS---GEVSIPKgLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFIFSG-TFRQN-LDPNGKWK----------------DEEIWKVA------DEVG---LKSVIEQFPGQLNFTLVDGG 1339
Cdd:COG0488 68 QEPPLDDDlTVLDTvLDGDAELRaleaeleeleaklaepDEDLERLAelqeefEALGgweAEARAEEILSGLGFPEEDLD 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 14141185 1340 Y---VLSHGHKQLMCLARSVLSKAKIILLDEPSAHLD 1373
Cdd:COG0488 148 RpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
428-619 |
1.28e-11 |
|
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: 64.48 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 428 VSFSHLCLV---GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMlILGEL-EASEG-IIKHSG-RVSFCSQFSWIMPGT 501
Cdd:cd03223 1 IELENLSLAtpdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLwPWGSGrIGMPEGeDLLFLPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENIIfgvsydeYRYKSVvkacqlqqditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 581
Cdd:cd03223 80 LREQLI-------YPWDDV---------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 14141185 582 TEEQVFESCVCKLMAnktrILVTSKMEHLRK-ADKILIL 619
Cdd:cd03223 126 SEDRLYQLLKELGIT----VISVGHRPSLWKfHDRVLDL 160
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1222-1398 |
1.51e-11 |
|
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: 65.76 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML----NIKGDIEIDGVswnSVTLQEWRKAFGVITQKVFIFSG-TF 1296
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVegggTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1297 RQNLD-------PNgKWKDEEIWKVADEVGLKsvieqfpgQLNFTLVDGGYV--LSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:cd03234 99 RETLTytailrlPR-KSSDAIRKKRVEDVLLR--------DLALTRIGGNLVkgISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 14141185 1368 PSAHLDPIT-YQVIRRVLKQAFAGCTVILCEH 1398
Cdd:cd03234 170 PTSGLDSFTaLNLVSTLSQLARRNRIVILTIH 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
437-655 |
1.93e-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: 68.29 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILG--ELEASEG-IIKHsgrVSFCSQFSWIMP------------GT 501
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGrIIYH---VALCEKCGYVERpskvgepcpvcgGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENIIFGVSYDEYRYKSVVK--ACQLQQDITKFAEQ---DNTV--LGEGGVT--------------------------- 547
Cdd:TIGR03269 89 LEPEEVDFWNLSDKLRRRIRKriAIMLQRTFALYGDDtvlDNVLeaLEEIGYEgkeavgravdliemvqlshrithiard 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 548 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSK----MEHLrkADKILILHQGS 623
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevIEDL--SDKAIWLENGE 246
|
250 260 270
....*....|....*....|....*....|...
gi 14141185 624 SYFYGTFSELqslrpdfSSKLM-GYDTFDQFTE 655
Cdd:TIGR03269 247 IKEEGTPDEV-------VAVFMeGVSEVEKECE 272
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
437-622 |
2.17e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.93 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLI------------LGELE--------ASEGIIKH-SGRVSFCSQ-F 494
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITidtarslsQQKGLIRQlRQHVGFVFQnF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 495 SWIMPGTIKENIIFG--VSYDEYRYKSVVKACQLQQDITKFAEQDNTVLgeggvTLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK11264 95 NLFPHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYPR-----RLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 573 SPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEHLRK-ADKILILHQG 622
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
437-623 |
2.43e-11 |
|
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: 65.59 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG-------IIKHSGRVSFCSQFSWIM--------PG- 500
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGevtfdgrPVTRRRRKAFRRRVQMVFqdpyaslhPRh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENI-----IFGVSYDEYRYKSVVKACQLQQDI-TKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:COG1124 97 TVDRILaeplrIHGLPDREERIAELLEQVGLPPSFlDRYPHQ-----------LSGGQRQRVAIARALILEPELLLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14141185 575 FGYLDVFTEEQVFEsCVCKLMA--NKTRILVT---SKMEHLrkADKILILHQGS 623
Cdd:COG1124 166 TSALDVSVQAEILN-LLKDLREerGLTYLFVShdlAVVAHL--CDRVAVMQNGR 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1225-1403 |
2.52e-11 |
|
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: 65.74 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1225 NISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN--IK---GDIEIDGVSWNSVT---LQEWR-KAFGVITQKVFIFSG- 1294
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTL----LRCINrlIEptsGKVLIDGQDIAAMSrkeLRELRrKKISMVFQSFALLPHr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 TFRQN----LDPNGKWKDEEIWK---VADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:cd03294 118 TVLENvafgLEVQGVPRAEREERaaeALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14141185 1368 PSAHLDPItyqvIRRVLK------QAFAGCTVILCEHR-IEAM 1403
Cdd:cd03294 187 AFSALDPL----IRREMQdellrlQAELQKTIVFITHDlDEAL 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1209-1417 |
2.58e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.26 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1209 KDLTVKYMDDGNA----VLENISFSISPGQRVGLLGRTGSGKSTL---LSAFLrmLNIKGDIEIDGVSW-NSVTLQEWRK 1280
Cdd:PRK13633 8 KNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL--IPSEGKVYVDGLDTsDEENLWDIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFGVitqkVFifsgtfrQNLD----------------PNGKWKDEEIWKVADEvGLKSV----IEQFPGQLnftlvdggy 1340
Cdd:PRK13633 86 KAGM----VF-------QNPDnqivativeedvafgpENLGIPPEEIRERVDE-SLKKVgmyeYRRHAPHL--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1341 vLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPI----TYQVIRRVLKQafAGCTVILCEHRIEAMLDCQRFLVIEESN 1416
Cdd:PRK13633 145 -LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSgrreVVNTIKELNKK--YGITIILITHYMEEAVEADRIIVMDSGK 221
|
.
gi 14141185 1417 V 1417
Cdd:PRK13633 222 V 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1208-1373 |
2.75e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 67.79 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYM----------DDGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDGVSWNSVT--- 1274
Cdd:COG4172 278 ARDLKVWFPikrglfrrtvGHVKAV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSrra 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1275 LQEWRKAFgvitQKVFifsgtfrQN----LDP-------------------NGKWKDEEIWKVADEVGLK-SVIEQFPGQ 1330
Cdd:COG4172 357 LRPLRRRM----QVVF-------QDpfgsLSPrmtvgqiiaeglrvhgpglSAAERRARVAEALEEVGLDpAARHRYPHE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14141185 1331 lnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEP-SAhLD 1373
Cdd:COG4172 426 -----------FSGGQRQRIAIARALILEPKLLVLDEPtSA-LD 457
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
440-635 |
3.46e-11 |
|
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: 64.77 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASegiikhSGRVSFCS--------------------QFSWIMP 499
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT------SGSVLFDGeditglppheiarlgigrtfQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 G-TIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGV------TLSGGQRARISLARAVYKDADLYLLD 572
Cdd:cd03219 89 ElTVLENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLadrpagELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 573 SPFGYLDVfTEEQVFESCVCKLMANKTRILVTskmEH-----LRKADKILILHQGSSYFYGTFSELQS 635
Cdd:cd03219 169 EPAAGLNP-EETEELAELIRELRERGITVLLV---EHdmdvvMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1208-1436 |
3.67e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.59 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTlLSAFLRML-----NIKGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:PRK13640 8 FKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKST-ISKLINGLllpddNPNSKITVDGITLTAKTVWDIREKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQ---KVFIfSGTFRQN----LDPNGKWKDEEIWKVADevglksVIEQFpGQLNFTLVDGGYvLSHGHKQLMCLARS 1355
Cdd:PRK13640 87 GIVFQnpdNQFV-GATVGDDvafgLENRAVPRPEMIKIVRD------VLADV-GMLDYIDSEPAN-LSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1356 VLSKAKIILLDEPSAHLDPI----TYQVIRRVLKQafAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKS 1431
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAgkeqILKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
....*
gi 14141185 1432 IFQQA 1436
Cdd:PRK13640 236 MLKEI 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
440-622 |
3.73e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG--------------------------RVSFCSQ 493
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 494 -FSWIMPGTIKENI------IFGVSYDEYRYKSVVKACQLqqDITKFAEqdntvlGEGGVTLSGGQRARISLARAVYKDA 566
Cdd:PRK10619 100 hFNLWSHMTVLENVmeapiqVLGLSKQEARERAVKYLAKV--GIDERAQ------GKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 567 DLYLLDSPFGYLDvftEEQVFEscVCKLMAN-----KTRILVTSKMEHLRK-ADKILILHQG 622
Cdd:PRK10619 172 EVLLFDEPTSALD---PELVGE--VLRIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQG 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1227-1401 |
3.80e-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: 64.44 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1227 SFSISPGQRVGLLGRTGSGKSTLL---SAFLrmLNIKGDIEIDGVswNSVTLQEWRKAFGVITQKVFIFSG-TFRQNLD- 1301
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLnliAGFE--TPQSGRVLINGV--DVTAAPPADRPVSMLFQENNLFAHlTVEQNVGl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1302 ---PNGKWKDEE---IWKVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPI 1375
Cdd:cd03298 94 glsPGLKLTAEDrqaIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180
....*....|....*....|....*...
gi 14141185 1376 TYQVIRRVLKQAFA--GCTVILCEHRIE 1401
Cdd:cd03298 163 LRAEMLDLVLDLHAetKMTVLMVTHQPE 190
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1206-1417 |
4.12e-11 |
|
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: 64.60 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKST---LLSAFLRmlNIKGDIEIDGVSWNSVTLQE-WRKA 1281
Cdd:TIGR04406 2 LVAENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTsfyMIVGLVR--PDAGKILIDGQDITHLPMHErARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 FGVITQKVFIFSG-TFRQNL--------DPNGKWKDEEIWKVADEVGLKSVIEQfpgqlnftlvdGGYVLSHGHKQLMCL 1352
Cdd:TIGR04406 78 IGYLPQEASIFRKlTVEENImavleirkDLDRAEREERLEALLEEFQISHLRDN-----------KAMSLSGGERRRVEI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITYQVIRRV---LKQafAGCTVILCEHRIEAMLD-CQRFLVIEESNV 1417
Cdd:TIGR04406 147 ARALATNPKFILLDEPFAGVDPIAVGDIKKIikhLKE--RGIGVLITDHNVRETLDiCDRAYIISDGKV 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
448-586 |
4.17e-11 |
|
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: 67.50 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 448 IEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSQF-SWIMPGTIKENI------IFGVSYdeyrYKS- 519
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYiSPDYDGTVEEFLrsantdDFGSSY----YKTe 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 520 VVKACQL----QQDITkfaeqdntvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVftEEQV 586
Cdd:COG1245 439 IIKPLGLekllDKNVK---------------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRL 492
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1214-1426 |
4.79e-11 |
|
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: 65.49 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1214 KYMDDGNAVlENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN--IKGDIEIDGVSWNSVTLQ--EWRKAFGVITQKV 1289
Cdd:TIGR01188 1 KVYGDFKAV-DGVNFKVREGEVFGFLGPNGAGKTTTI----RMLTtlLRPTSGTARVAGYDVVREprKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1290 FIFSG-TFRQNLDPNGKWKDEEiWKVADEvGLKSVIEQFpgqlnfTLVD------GGYvlSHGHKQLMCLARSVLSKAKI 1362
Cdd:TIGR01188 76 SVDEDlTGRENLEMMGRLYGLP-KDEAEE-RAEELLELF------ELGEaadrpvGTY--SGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 1363 ILLDEPSAHLDPITYQVIRR-VLKQAFAGCTVILCEHRI-EAMLDCQRFLVIEESNVWQYDSLQAL 1426
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRRAIWDyIRALKEEGVTILLTTHYMeEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
441-633 |
4.87e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.19 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-----------------RVSFCSQF--SWIMPGT 501
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFpeSQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENIIFGVSYDEYRYKSV-VKACQLQQDItKFAEQdntVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVkNYAHRLLMDL-GFSRD---VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 581 FTEEQVFESC-VCKLMANKTRILVTSKMEHL-RKADKILILHQGSSYFYGTFSEL 633
Cdd:PRK13646 179 QSKRQVMRLLkSLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1219-1373 |
5.11e-11 |
|
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: 63.89 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1219 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RMLNIKGdieidGVSWNSVTLQEW---------RKAFGVITQK 1288
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEG-----KVHWSNKNESEPsfeatrsrnRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1289 VFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEP 1368
Cdd:cd03290 88 PWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
....*
gi 14141185 1369 SAHLD 1373
Cdd:cd03290 168 FSALD 172
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
426-648 |
5.21e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.79 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFShlcLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR------------------ 487
Cdd:PRK13548 6 RNLSVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelarrravlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 488 ----VSFcsqfswimPGTIKENIIFGVS---YDEYRYKSVVKACQLQQDITKFAEQDNTvlgeggvTLSGGQRARISLAR 560
Cdd:PRK13548 83 qhssLSF--------PFTVEEVVAMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYP-------QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 561 A---VYKDAD---LYLLDSPFGYLDVFTEEQVFEscVCKLMANKTRILVTSKMEHL----RKADKILILHQGSSYFYGTF 630
Cdd:PRK13548 148 VlaqLWEPDGpprWLLLDEPTSALDLAHQHHVLR--LARQLAHERGLAVIVVLHDLnlaaRYADRIVLLHQGRLVADGTP 225
|
250
....*....|....*...
gi 14141185 631 SElqSLRPDFSSKLMGYD 648
Cdd:PRK13548 226 AE--VLTPETLRRVYGAD 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
437-636 |
6.08e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.19 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVL-KNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFcSQFSwimpgtikENIIFGVS---- 511
Cdd:PLN03073 520 GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRM-AVFS--------QHHVDGLDlssn 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 512 ---YDEYRYKSVVKAcQLQQDITKFAEQDNTVLgEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVfteeQVFE 588
Cdd:PLN03073 591 pllYMMRCFPGVPEQ-KLRAHLGSFGVTGNLAL-QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL----DAVE 664
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 589 SCVCKLMANKTRILVTSKMEHL--RKADKILILHQGS-SYFYGTFSELQSL 636
Cdd:PLN03073 665 ALIQGLVLFQGGVLMVSHDEHLisGSVDELWVVSEGKvTPFHGTFHDYKKT 715
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
440-628 |
6.21e-11 |
|
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: 63.93 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG------------RVSFCSQFSWIMPG-TIKENI 506
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 507 IF-----GVSYDEY--RYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03266 100 EYfaglyGLKGDELtaRLEELADRLGMEELLDRRVGG-----------FSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 580 VFTEEQVFESCVCKLMANKTRILVTSKMEHL-RKADKILILHQGSSYFYG 628
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1207-1403 |
6.27e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.86 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRML----NI-KGDIEIDGVSWNSVTLQEwRK- 1280
Cdd:COG3839 5 ELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIagleDPtSGEILIGGRDVTDLPPKD-RNi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFgvitqkVFifsgtfrQN--LDP-------------NGKWKDEEIWK----VADEVGLKSVIEQFPGQlnftlvdggyv 1341
Cdd:COG3839 78 AM------VF-------QSyaLYPhmtvyeniafplkLRKVPKAEIDRrvreAAELLGLEDLLDRKPKQ----------- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1342 LSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEH-RIEAM 1403
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRrlGTTTIYVTHdQVEAM 198
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
439-633 |
7.62e-11 |
|
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: 63.75 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGeLEA-SEGIIKHSG----------------RVSFCSQ-FSWIMPG 500
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERpTSGSVLVDGtdltllsgkelrkarrRIGMIFQhFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENI-----IFGVSyDEYRYKSV---VKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLD 572
Cdd:cd03258 98 TVFENValpleIAGVP-KAEIEERVlelLELVGLEDKADAYPAQ-----------LSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 573 SPFGYLDVFTEEQVFE---SCVCKLmaNKTRILVTSKMEHLRK-ADKILILHQGSSYFYGTFSEL 633
Cdd:cd03258 166 EATSALDPETTQSILAllrDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1220-1430 |
7.68e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.26 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1220 NAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN--IKGD------IEIDGvswNSVT--------LQEWRKAFG 1283
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLL----RHLSglITGDksagshIELLG---RTVQregrlardIRKSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQ------KVFIFSGTFRQNLDPNGKWKDEEIW--KVADEVGLKSVIEQFPGQLNFTLVDggyVLSHGHKQLMCLARS 1355
Cdd:PRK09984 90 YIFQqfnlvnRLSVLENVLIGALGSTPFWRTCFSWftREQKQRALQALTRVGMVHFAHQRVS---TLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1356 VLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEHRIE-AMLDCQRFLVIEESNVWQYDSLQALLSEK 1430
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1206-1401 |
7.81e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYMDDgnAVLENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLniKGdieidGVSWNSVTLQEWRKAF 1282
Cdd:PRK13638 2 LATSDLWFRYQDE--PVLKGLNLDFSLSPVTGLVGANGCGKSTLfmnLSGLLRPQ--KG-----AVLWQGKPLDYSKRGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKV-FIFSG----TFRQNLDPNGKWK-------DEEIWKVADEVglksvieqfpgqlnFTLVDGGY-------VLS 1343
Cdd:PRK13638 73 LALRQQVaTVFQDpeqqIFYTDIDSDIAFSlrnlgvpEAEITRRVDEA--------------LTLVDAQHfrhqpiqCLS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1344 HGHKQLMCLARSVLSKAKIILLDEPSAHLDPI----TYQVIRRVLKQafaGCTVILCEHRIE 1401
Cdd:PRK13638 139 HGQKKRVAIAGALVLQARYLLLDEPTAGLDPAgrtqMIAIIRRIVAQ---GNHVIISSHDID 197
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
438-622 |
7.83e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-VSFCSQF---SWI-------MPGT----- 501
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYkraKYIgrvfqdpMMGTapsmt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENII------------FGVSydeyryksvvkacqlQQDITKFAEQDNTvLGEG---------GvTLSGGQRARISLAR 560
Cdd:COG1101 99 IEENLAlayrrgkrrglrRGLT---------------KKRRELFRELLAT-LGLGlenrldtkvG-LLSGGQRQALSLLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 561 AVYKDADLYLLDSPFGYLDVFTEEQVFEscvcklMANK-------TRILVTSKMEH-LRKADKILILHQG 622
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLE------LTEKiveennlTTLMVTHNMEQaLDYGNRLIMMHEG 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
441-639 |
9.04e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.62 E-value: 9.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------VSFCSQ----FSWImpgTIKEN 505
Cdd:COG3840 15 PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQennlFPHL---TVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIFGVSydeyryksvvKACQL----QQDITKFAEQdntvLGEGGV------TLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:COG3840 92 IGLGLR----------PGLKLtaeqRAQVEQALER----VGLAGLldrlpgQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 576 GYLD-------------VFTEEQVfescvcklmankTRILVTskmeH-----LRKADKILILHQGSSYFYGTFSELQSLR 637
Cdd:COG3840 158 SALDpalrqemldlvdeLCRERGL------------TVLMVT----HdpedaARIADRVLLVADGRIAADGPTAALLDGE 221
|
..
gi 14141185 638 PD 639
Cdd:COG3840 222 PP 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1206-1374 |
1.19e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN---------IK-GDIEIDGvswnSVTL 1275
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTL----LRCINlleqpeagtIRvGDITIDT----ARSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1276 QEWRKAFGVITQKV-FIFSGTfrqNLDPN---------------GKWKDEEIW---KVADEVGLKSVIEQFPGQlnftlv 1336
Cdd:PRK11264 74 SQQKGLIRQLRQHVgFVFQNF---NLFPHrtvleniiegpvivkGEPKEEATArarELLAKVGLAGKETSYPRR------ 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 14141185 1337 dggyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDP 1374
Cdd:PRK11264 145 -----LSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1206-1414 |
1.24e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 62.77 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTlQEWRKAFGV 1284
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPtSGRATVAGHDVVREP-REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQKVFIFSG-TFRQNLD--------PNGKWKdEEIWKVADEVGLKSVIEQfpgqlnftLVdGGYvlSHGHKQLMCLARS 1355
Cdd:cd03265 78 VFQDLSVDDElTGWENLYiharlygvPGAERR-ERIDELLDFVGLLEAADR--------LV-KTY--SGGMRRRLEIARS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1356 VLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEHRI-EAMLDCQRFLVIEE 1414
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklKEEFGMTILLTTHYMeEAEQLCDRVAIIDH 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1208-1417 |
1.51e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.97 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNikGDIEIDG--VSWNSVTLQEW-RKAFG- 1283
Cdd:COG4152 4 LKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTT----IRIIL--GILAPDSgeVLWDGEPLDPEdRRRIGy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 ------------VITQKVFIfsGTFRqNLDPNgkwkdeEIWKVADE----VGLKSV----IEQfpgqlnftlvdggyvLS 1343
Cdd:COG4152 76 lpeerglypkmkVGEQLVYL--ARLK-GLSKA------EAKRRADEwlerLGLGDRankkVEE---------------LS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1344 HGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLK-QAFAGCTVILCEHR---IEAMldCQRFLVIEESNV 1417
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIReLAAKGTTVIFSSHQmelVEEL--CDRIVIINKGRK 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1223-1401 |
1.63e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.44 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNI-----KGDIEIDGV---SWNSVTLQEWRKAFGVITQKVFIFSG 1294
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLlerptSGRVLVDGQdltALSEKELRKARRQIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 -TFRQN----LDPNGkWKDEEIWKVADE----VGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:PRK11153 97 rTVFDNvalpLELAG-TPKAEIKARVTEllelVGLSDKADRYPAQ-----------LSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 14141185 1366 DEPSAHLDPITYQVIRRVLKQ--AFAGCTVILCEHRIE 1401
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDinRELGLTIVLITHEMD 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
440-622 |
1.86e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKtSLLMLILGELE-ASEGIIKHSGR-VSfcsqfswimpgTIKENII-------FGV 510
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGK-STLMNILGCLDkPTSGTYRVAGQdVA-----------TLDADALaqlrrehFGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 511 SYDEYRYKSVVKACQLQQDITKFA--------EQDNTVLGEGGV---------TLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK10535 91 IFQRYHLLSHLTAAQNVEVPAVYAglerkqrlLRAQELLQRLGLedrveyqpsQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 574 PFGYLDVFTEEQVFesCVCKLMANK--TRILVTSKMEHLRKADKILILHQG 622
Cdd:PRK10535 171 PTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1222-1414 |
1.91e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.67 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEwRKAFGVITQkvfiFSgtfrqNL 1300
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVPSRARHA-RQRVGVVPQ----FD-----NL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1301 DPNGKWKdEEIWKVADEVGLKS--VIEQFPGQLNFTLVDGGY-----VLSHGHKQLMCLARSVLSKAKIILLDEPSAHLD 1373
Cdd:PRK13537 92 DPDFTVR-ENLLVFGRYFGLSAaaARALVPPLLEFAKLENKAdakvgELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14141185 1374 PITYQVIRRVLKQAFA-GCTVILCEHRI-EAMLDCQRFLVIEE 1414
Cdd:PRK13537 171 PQARHLMWERLRSLLArGKTILLTTHFMeEAERLCDRLCVIEE 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1208-1373 |
2.21e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.47 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVSWNSVTlqEWRKAF 1282
Cdd:PRK11607 22 IRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAgfeqpTAGQIMLDGVDLSHVP--PYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKVFIFSG-TFRQN----LDPNGKWKDEEIWKVADEVGLKSVIE---QFPGQlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:PRK11607 94 NMMFQSYALFPHmTVEQNiafgLKQDKLPKAEIASRVNEMLGLVHMQEfakRKPHQ-----------LSGGQRQRVALAR 162
|
170
....*....|....*....
gi 14141185 1355 SVLSKAKIILLDEPSAHLD 1373
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALD 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1208-1413 |
2.47e-10 |
|
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: 62.43 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmDDGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRML--NIK---GDIEIDGVSWnSVTLQEWRKAF 1282
Cdd:cd03237 1 YTYPTMKK-TLGEFTLEVEGGSISESEVIGILGPNGIGKTT----FIKMLagVLKpdeGDIEIELDTV-SYKPQYIKADY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GViTQKVFIFSGTFRQNLDPngKWKDEeiwkVADEVGLKSVIEQfpgQLNftlvdggyVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:cd03237 75 EG-TVRDLLSSITKDFYTHP--YFKTE----IAKPLQIEQILDR---EVP--------ELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 1363 ILLDEPSAHLDP----ITYQVIRRVLKQAFAGCTVIlcEHRIeAMLD--CQRFLVIE 1413
Cdd:cd03237 137 YLLDEPSAYLDVeqrlMASKVIRRFAENNEKTAFVV--EHDI-IMIDylADRLIVFE 190
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
445-579 |
2.63e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.29 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 445 NLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------VSFCSQ----FSWImpgTIKENIIFG 509
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQennlFSHL---TVAQNIGLG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 510 V-------SYDEYRYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK10771 96 LnpglklnAAQREKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
437-584 |
2.98e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR----VSFCSQFSWImpG---------TIK 503
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYL--GhrnamkpalTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFGVSY---DEYRYKSVVKACQLqQDIT--KFAEqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK13539 92 ENLEFWAAFlggEELDIAAALEAVGL-APLAhlPFGY------------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
....*.
gi 14141185 579 DVFTEE 584
Cdd:PRK13539 159 DAAAVA 164
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1215-1398 |
3.14e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1215 YMDDgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDG--VSWNSVTLQ----EWRKAFGVITQ 1287
Cdd:PRK14246 19 YIND-KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGkvLYFGKDIFQidaiKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1288 KVFIFS-----GTFRQNLDPNGKWKDEEIWKVADE----VGL-KSVIEQfpgqlnftLVDGGYVLSHGHKQLMCLARSVL 1357
Cdd:PRK14246 98 QPNPFPhlsiyDNIAYPLKSHGIKEKREIKKIVEEclrkVGLwKEVYDR--------LNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14141185 1358 SKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEH 1398
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
437-580 |
3.16e-10 |
|
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: 61.22 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIK------HSGRVSFCSQFSWI--MPG-----TIK 503
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngtplAEQRDEPHENILYLghLPGlkpelSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFgvsydeyryksvvkACQLQQDITKFAEQDNTVLGEGGVT------LSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:TIGR01189 92 ENLHF--------------WAAIHGGAQRTIEDALAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
...
gi 14141185 578 LDV 580
Cdd:TIGR01189 158 LDK 160
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
439-633 |
3.30e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.73 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRV---------------SFC---SQFswiMPG 500
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrrqvgmVFQnpdNQF---VGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENIIF-----GVSYDEY--RYKSVVKacqlQQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK13635 98 TVQDDVAFgleniGVPREEMveRVDQALR----QVGMEDFLNREPH-------RLSGGQKQRVAIAGVLALQPDIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 574 PFGYLDVFTEEQVFEscVCKLMANKTRILV---TSKMEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:PRK13635 167 ATSMLDPRGRREVLE--TVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
437-622 |
3.45e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.31 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG------------RVSFCSQFSWIMPG-TIK 503
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQFDNLDLEfTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFgvsYDEYRYKSVVKACQLQQDITKFAEQDNTVlgEGGVT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 582
Cdd:PRK13536 133 ENLLV---FGRYFGMSTREIEAVIPSLLEFARLESKA--DARVSdLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14141185 583 EEQVFESCVCKLMANKTRILVTSKMEHL-RKADKILILHQG 622
Cdd:PRK13536 208 RHLIWERLRSLLARGKTILLTTHFMEEAeRLCDRLCVLEAG 248
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
441-633 |
3.57e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.73 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII--------------------KHSGRVsFcsQF--SWIM 498
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagkknkklkplrKKVGIV-F--QFpeHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 499 PGTIKENIIFG-----VSYDE--YRYKSVVKACQLQQDitkfaeqdntVLGEGGVTLSGGQRARISLARAVYKDADLYLL 571
Cdd:PRK13634 100 EETVEKDICFGpmnfgVSEEDakQKAREMIELVGLPEE----------LLARSPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 572 DSPFGYLDVFTEEQVFEscvcklM-------ANKTRILVTSKMEHL-RKADKILILHQGSSYFYGTFSEL 633
Cdd:PRK13634 170 DEPTAGLDPKGRKEMME------MfyklhkeKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1222-1422 |
4.66e-10 |
|
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: 61.58 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKST---LLSAFLRmlNIKGDIEIDG-VSWnsvtlqEWRKAFgvITQKVFIFSGtfR 1297
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLLQ--PTSGEVRVAGlVPW------KRRKKF--LRRIGVVFGQ--K 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1298 QNLdpngkWKD----------EEIWKVaDEVGLKSVIEQFPGQLNFTLVDGGYV--LSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:cd03267 104 TQL-----WWDlpvidsfyllAAIYDL-PPARFKKRLDELSELLDLEELLDTPVrqLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1366 DEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEHR---IEAMldCQRFLVIEESNVwQYDS 1422
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYmkdIEAL--ARRVLVIDKGRL-LYDG 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
441-644 |
4.79e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.30 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEAS---EGIIKHSGRV----------SFCSQFSWIMPG-TIKENI 506
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPidakemraisAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 507 IF--------GVSYDEYRYKsvVKACQLQQDITKFAeqdNTVLGEGGVT--LSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:TIGR00955 121 MFqahlrmprRVTKKEKRER--VDEVLQALGLRKCA---NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 577 YLDVFTEEQVFEscVCKLMANKTRILVTS----KMEHLRKADKILILHQGSSYFYGTFSELqslrPDFSSKL 644
Cdd:TIGR00955 196 GLDSFMAYSVVQ--VLKGLAQKGKTIICTihqpSSELFELFDKIILMAEGRVAYLGSPDQA----VPFFSDL 261
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
440-628 |
4.94e-10 |
|
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: 61.05 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGeMLAITGSTGSGKTSLLMLILGELEASegiikhSGRVSFCSQFSWIMPGTIKENI-----IFGVsYDE 514
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS------SGTIRIDGQDVLKQPQKLRRRIgylpqEFGV-YPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 515 YRYKSVVKACQLQQDI--TKFAEQDNTVLGEGGV---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVftE 583
Cdd:cd03264 87 FTVREFLDYIAWLKGIpsKEVKARVDEVLELVNLgdrakkkigSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP--E 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14141185 584 EQV-FESCVCKLMANKTRILVTSKMEHLRK-ADKILILHQGSSYFYG 628
Cdd:cd03264 165 ERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
437-560 |
5.20e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPGTIK 503
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 504 ENIIFGVsydEYRYKSVVKAcQLQQDITKFaEQDNTVLGEGGVTLSGGQRARISLAR 560
Cdd:PRK10247 99 DNLIFPW---QIRNQQPDPA-IFLDDLERF-ALPDTILTKNIAELSGGEKQRISLIR 150
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
437-585 |
5.46e-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: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIK------HSGRVSFCSQFSWI--MPG-----TIK 503
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggplDFQRDSIARGLLYLghAPGikttlSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFgvsydeYRyksvvKACQLQQDITKFAEQDNTVLGEGGV-TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 582
Cdd:cd03231 92 ENLRF------WH-----ADHSDEQVEEALARVGLNGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
...
gi 14141185 583 EEQ 585
Cdd:cd03231 161 VAR 163
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
441-636 |
5.64e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 61.69 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII----------------KHSGRVsFCSQFSWIMPGTIKE 504
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklrKHIGIV-FQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFG-----VSYDEyrYKSVVKACQLQQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK13648 104 DVAFGlenhaVPYDE--MHRRVSEALKQVDMLERADYEPN-------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 580 VFTEEQVFeSCVCKLMANK--TRILVTSKMEHLRKADKILILHQGSSYFYGT----FSELQSL 636
Cdd:PRK13648 175 PDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTpteiFDHAEEL 236
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
439-614 |
5.90e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG------------RVSFCSQFSWIMPG-TIKEN 505
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdlctyqkQLCFVGHRSGINPYlTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIFGVSYDEyryksvvKACQLQQDITKFAEQDNTVLGEGgvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfteEQ 585
Cdd:PRK13540 95 CLYDIHFSP-------GAVGITELCRLFSLEHLIDYPCG--LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD----EL 161
|
170 180 190
....*....|....*....|....*....|...
gi 14141185 586 VFESCVCKLMANKTR---ILVTSKME-HLRKAD 614
Cdd:PRK13540 162 SLLTIITKIQEHRAKggaVLLTSHQDlPLNKAD 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
437-628 |
5.93e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.06 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSQFSWI---------------MPGT 501
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENIIFG-----VSYDEY--RYKSVVKACQLQqditKFAEQdntvlgeGGVTLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK13647 97 VWDDVAFGpvnmgLDKDEVerRVEEALKAVRMW----DFRDK-------PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 575 FGYLDVFTEEQVFESCVCKLMANKTRILVTSKME-HLRKADKILILHQGSSYFYG 628
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1208-1399 |
6.21e-10 |
|
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: 63.80 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDdgNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMlnIKGDIEIDGvswNSVTLQEwrkafgviTQ 1287
Cdd:TIGR03719 325 AENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTL----FRM--ITGQEQPDS---GTIEIGE--------TV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1288 KVfIFSGTFRQNLDPNGK-WkdEEIWKVADEVGLKSVieQFP-----GQLNFTLVD-----GgyVLSHGHKQLMCLARSV 1356
Cdd:TIGR03719 386 KL-AYVDQSRDALDPNKTvW--EEISGGLDIIKLGKR--EIPsrayvGRFNFKGSDqqkkvG--QLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14141185 1357 LSKAKIILLDEPSAHLDPITYQVIRRVLkQAFAGCTVILCEHR 1399
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAGCAVVISHDR 500
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1208-1413 |
8.18e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 60.91 E-value: 8.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRmLNIKGDIEIDGVSWNsvTLQEWRKAfG 1283
Cdd:COG4181 11 LRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGllAGLD-RPTSGTVRLAGQDLF--ALDEDARA-R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQKV-FIFsgtfrQN--LDPN--------------GKWKDEEIWKVA-DEVGLKSVIEQFPGQlnftlvdggyvLSHG 1345
Cdd:COG4181 87 LRARHVgFVF-----QSfqLLPTltalenvmlplelaGRRDARARARALlERVGLGHRLDHYPAQ-----------LSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1346 HKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVL--KQAFAGCTVILCEHRIEAMLDCQRFLVIE 1413
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTHDPALAARCDRVLRLR 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
437-622 |
8.75e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.23 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG----------IIKHSGRVSFcsQFSWIMP-GTIKEN 505
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtaplaEAREDTRLMF--QDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIFGVSYDeYRYKSvvkacqLQQ-DITKFAEQDNtvlgEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE- 583
Cdd:PRK11247 102 VGLGLKGQ-WRDAA------LQAlAAVGLADRAN----EWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRi 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14141185 584 --EQVFESCVckLMANKTRILVTSKM-EHLRKADKILILHQG 622
Cdd:PRK11247 171 emQDLIESLW--QQHGFTVLLVTHDVsEAVAMADRVLLIEEG 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
427-622 |
9.10e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 427 NVSFSHLCLV--GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG---I-------IKHSGR-VSFCSQ 493
Cdd:PRK11000 3 SVTLRNVTKAygDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGdlfIgekrmndVPPAERgVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 494 FSWIMPG-TIKENIIFGVSYdeyrykSVVKACQLQQDITKFAE--QDNTVLGEGGVTLSGGQRARISLARAVYKDADLYL 570
Cdd:PRK11000 83 SYALYPHlSVAENMSFGLKL------AGAKKEEINQRVNQVAEvlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 571 LDSPFGYLDVFTEEQVfESCVCKLMA--NKTRILVT-SKMEHLRKADKILILHQG 622
Cdd:PRK11000 157 LDEPLSNLDAALRVQM-RIEISRLHKrlGRTMIYVThDQVEAMTLADKIVVLDAG 210
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
432-623 |
9.18e-10 |
|
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: 59.85 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 432 HLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILG--ELEASEGIIKHSGrvsfcsqfswimpgtikENIIFg 509
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKG-----------------EDITD- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 510 VSYDEYRYKSVVKACQLQQDIT--KFAEqdntVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVF 587
Cdd:cd03217 69 LPPEERARLGIFLAFQYPPEIPgvKNAD----FLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 14141185 588 EScVCKLMANKTRILVTSKMEHL---RKADKILILHQGS 623
Cdd:cd03217 145 EV-INKLREEGKSVLIITHYQRLldyIKPDRVHVLYDGR 182
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
426-642 |
1.39e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.44 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLClvgNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMlILGELEASEGIIKHSGRVSFCSQFSW--------- 496
Cdd:PRK14258 11 NNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVEFFNQNIYerrvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 497 ------------IMPGTIKENIIFGVSYDEYRYK--------SVVKACQLQQDItkfaeqdNTVLGEGGVTLSGGQRARI 556
Cdd:PRK14258 87 rrqvsmvhpkpnLFPMSVYDNVAYGVKIVGWRPKleiddiveSALKDADLWDEI-------KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 557 SLARAVYKDADLYLLDSPFGYLDVFTEEQVfESCV--CKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQ 634
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFG 238
|
....*...
gi 14141185 635 SLRPDFSS 642
Cdd:PRK14258 239 LTKKIFNS 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1222-1270 |
1.42e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 1.42e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDG-VSW 1270
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTL----LKLIAgilepTSGRVEVNGrVSA 91
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1206-1419 |
1.44e-09 |
|
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: 59.58 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVSWNSVTLQEwrK 1280
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGGRDVTDLPPKD--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 AFGVITQKVFIFSG-TFRQNLDPNGKWK-------DEEIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCL 1352
Cdd:cd03301 73 DIAMVFQNYALYPHmTVYDNIAFGLKLRkvpkdeiDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEH-RIEAMLDCQRFLVIEESNVWQ 1419
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1208-1414 |
1.73e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 58.60 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKymddgnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKA-FGVI 1285
Cdd:cd03215 7 VRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPaSGEITLDGKPVTRRSPRDAIRAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1286 TQkvfifsgtfrqnlDPngkwKDEEIwkvadeVGLKSVIEqfpgqlNFTLvdgGYVLSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:cd03215 81 PE-------------DR----KREGL------VLDLSVAE------NIAL---SSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1366 DEPSAHLDPITYQVIRRVLKQ-AFAGCTVILcehrI-----EAMLDCQRFLVIEE 1414
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRElADAGKAVLL----IsseldELLGLCDRILVMYE 179
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
440-622 |
1.76e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTS-------LLMLILGELE------------------ASEGIIKHS--------- 485
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIEwifkdeknkkktkekekvLEKLVIQKTrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 486 ---GRVSFCSQFS--WIMPGTIKENIIFG-VSYdeyrykSVVK--ACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARIS 557
Cdd:PRK13651 102 eirRRVGVVFQFAeyQLFEQTIEKDIIFGpVSM------GVSKeeAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 558 LARAVYKDADLYLLDSPFGYLD-VFTEE--QVFEscvcKLMAN-KTRILVTSKMEH-LRKADKILILHQG 622
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDpQGVKEilEIFD----NLNKQgKTIILVTHDLDNvLEWTKRTIFFKDG 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1209-1436 |
2.01e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1209 KDLTVKYMDDGNAvLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWNSVTLQEWRKAFGVITQ 1287
Cdd:PRK13652 7 RDLCYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTsGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1288 KV--FIFSGTFRQNL--DPNGKWKDEE-----IWKVADEVGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCLARSVLS 1358
Cdd:PRK13652 86 NPddQIFSPTVEQDIafGPINLGLDEEtvahrVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1359 KAKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEHRIEAMLDCQRFL-VIEESNVWQYDSLQALLSEKSIFQQ 1435
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEMADYIyVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
.
gi 14141185 1436 A 1436
Cdd:PRK13652 235 V 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
437-635 |
2.71e-09 |
|
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: 58.98 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR--------------VSFCSQFSWIMPG-T 501
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENIIFGvsydEYRYKSVVKACQLQQDITKFaeqdnTVLGE-----GGvTLSGGQRARISLARAVYKDADLYLLDSPfg 576
Cdd:cd03224 92 VEENLLLG----AYARRRAKRKARLERVYELF-----PRLKErrkqlAG-TLSGGEQQMLAIARALMSRPKLLLLDEP-- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 577 yldvfTE-------EQVFEsCVCKLMANKTRILVTSKMEH--LRKADKILILHQGSSYFYGTFSELQS 635
Cdd:cd03224 160 -----SEglapkivEEIFE-AIRELRDEGVTILLVEQNARfaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1208-1374 |
2.92e-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: 58.52 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKymDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLL---SAFLRMLniKGDIEIDGVSWNSVTLQEWRkafgv 1284
Cdd:TIGR01189 3 ARNLACS--RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLrilAGLLRPD--SGEVRWNGTPLAEQRDEPHE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 itqkVFIFSG---------TFRQNLD---PNGKWKDEEIWKVADEVGLKSvIEQFP-GQLnftlvdggyvlSHGHKQLMC 1351
Cdd:TIGR01189 74 ----NILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG-FEDLPaAQL-----------SAGQQRRLA 137
|
170 180
....*....|....*....|...
gi 14141185 1352 LARSVLSKAKIILLDEPSAHLDP 1374
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDK 160
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1218-1422 |
2.92e-09 |
|
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: 59.17 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1218 DGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVSWNSvtLQEWRKAFGVITQKVFIF 1292
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAgfetpTSGEILLDGKDITN--LPPHKRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1293 SG-TFRQN----LDPNGKWKDEEIWKVA---DEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:cd03300 85 PHlTVFENiafgLRLKKLPKAEIKERVAealDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1365 LDEPSAHLDPITYQVIRRVLK--QAFAGCTVILCEH-RIEAMLDCQRFLVIEESNVWQYDS 1422
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKrlQKELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
441-633 |
3.23e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.82 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-----------------RVSFCSQFSWIMPG-TI 502
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 503 KENIIFG-----VSYDEYRYKSVVKACQLQQDITKFAEQDNtvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK10070 124 LDNTAFGmelagINAEERREKALDALRQVGLENYAHSYPDE---------LSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 578 LDVFTEEQVFESCVcKLMANKTRILVTSKM---EHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:PRK10070 195 LDPLIRTEMQDELV-KLQAKHQRTIVFISHdldEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
437-629 |
3.53e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.95 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR------------VSFCSQFSWIMPG-TIK 503
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFgvsYDEYRYKSVVKAcQLQQDitkfAEQDNTVL----GEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:TIGR01257 1022 EHILF---YAQLKGRSWEEA-QLEME----AMLEDTGLhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 580 VFTEEQVFEsCVCKLMANKTRILVTSKMEHLR-KADKILILHQGSSYFYGT 629
Cdd:TIGR01257 1094 PYSRRSIWD-LLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-622 |
3.77e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLL-----MLILGELEASEGIIKHSGR---------------VSFCSQFSWI 497
Cdd:PRK14267 17 NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVRLFGRniyspdvdpievrreVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 498 MPG-TIKENIIFGVsydeyRYKSVVKACQLQQDITKFAEQDNTV-------LGEGGVTLSGGQRARISLARAVYKDADLY 569
Cdd:PRK14267 97 FPHlTIYDNVAIGV-----KLNGLVKSKKELDERVEWALKKAALwdevkdrLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14141185 570 LLDSPFGYLDVFTEEQVfESCVCKLMANKTRILVT-SKMEHLRKADKILILHQG 622
Cdd:PRK14267 172 LMDEPTANIDPVGTAKI-EELLFELKKEYTIVLVThSPAQAARVSDYVAFLYLG 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
439-633 |
4.44e-09 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 58.71 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR--------------VSFCSQFSWIMPG-TIK 503
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENI-----IFGVSYDEYRYKsvvkACQLQQD--ITKFAEQDntvlgegGVTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:cd03218 94 ENIlavleIRGLSKKEREEK----LEELLEEfhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 577 YLDVFTeeqVFE--SCVCKLMANKTRILVTSK--MEHLRKADKILILHQGSSYFYGTFSEL 633
Cdd:cd03218 163 GVDPIA---VQDiqKIIKILKDRGIGVLITDHnvRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
437-589 |
4.67e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.24 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQ-----FSWim 498
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQdtslsFEF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 499 pgTIKENIIFGVSYDEYRY-------KSVVKACQLQQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLL 571
Cdd:PRK09536 93 --DVRQVVEMGRTPHRSRFdtwtetdRAAVERAMERTGVAQFADRPVT-------SLSGGERQRVLLARALAQATPVLLL 163
|
170
....*....|....*...
gi 14141185 572 DSPFGYLDVFTEEQVFES 589
Cdd:PRK09536 164 DEPTASLDINHQVRTLEL 181
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
437-586 |
5.22e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.13 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR----------VSFCSQ---FSWIMPGTIK 503
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQseeVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFG-------VSYDEYRYKSVVKACQLQQDITKFAEQDntvLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170
....*....|
gi 14141185 577 YLDVFTEEQV 586
Cdd:PRK15056 172 GVDVKTEARI 181
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
448-648 |
5.89e-09 |
|
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: 57.20 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 448 IEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-RVSFCSQFswimpgtikeniifgvsydeyryksvvkacql 526
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 527 qqditkfaeqdntvlgeggVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVftEEQVFESCVCKLM---ANKTRILV 603
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI--EQRLNAARAIRRLseeGKKTALVV 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14141185 604 TSKMEHLRKADKILILHQGSSYFYGTFSELQSLRPDFSSKLMGYD 648
Cdd:cd03222 129 EHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYL 173
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1208-1394 |
5.97e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.63 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:PRK13548 5 ARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRALSgelspDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKV---FIFS-------GtfrqnLDPNGKWKDEE---IWKVADEVGLksviEQFPGQLnftlvdggY-VLSHGHKQ 1348
Cdd:PRK13548 79 AVLPQHSslsFPFTveevvamG-----RAPHGLSRAEDdalVAAALAQVDL----AHLAGRD--------YpQLSGGEQQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 1349 LMCLARsVL-------SKAKIILLDEPSAHLDPITYQVIRRVLKQaFA---GCTVI 1394
Cdd:PRK13548 142 RVQLAR-VLaqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQ-LAherGLAVI 195
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1209-1398 |
6.38e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1209 KDLTVKYMDDGNAVlENISFSISPGQRVGLLGRTGSGKSTlLSAFLRMLN--IKGDIEIDGVSWNSVTLQEWRKAFGVIT 1286
Cdd:PRK10522 326 RNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKST-LAMLLTGLYqpQSGEILLDGKPVTAEQPEDYRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFIFSgtfrQNLDPNGKWKDEEIwkvadevgLKSVIEQFPGQLNFTLVDGGYV---LSHGHKQLMCLARSVLSKAKII 1363
Cdd:PRK10522 404 TDFHLFD----QLLGPEGKPANPAL--------VEKWLERLKMAHKLELEDGRISnlkLSKGQKKRLALLLALAEERDIL 471
|
170 180 190
....*....|....*....|....*....|....*....
gi 14141185 1364 LLDEPSAHLDP----ITYQVIRRVLKQafAGCTVILCEH 1398
Cdd:PRK10522 472 LLDEWAADQDPhfrrEFYQVLLPLLQE--MGKTIFAISH 508
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-633 |
6.91e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 420 KHSSDENNVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSQ--FSWI 497
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdiFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 498 MPGTIKE-NIIFGVS--------YDEYRYKSVVKACQLQQDITKFAEQDNTVLG----------EGGVTLSGGQRARISL 558
Cdd:PRK14246 85 AIKLRKEvGMVFQQPnpfphlsiYDNIAYPLKSHGIKEKREIKKIVEECLRKVGlwkevydrlnSPASQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 559 ARAVYKDADLYLLDSPFGYLDVFTeEQVFESCVCKLMANKTRILVTSKMEHL-RKADKILILHQGSSYFYGTFSEL 633
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVN-SQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1223-1427 |
6.95e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.33 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-I----KGDIEIDGvswnsVTLQEWRKAF----GVitqkVFifs 1293
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTT----IKMLTgIlvptSGEVRVLG-----YVPFKRRKEFarriGV----VF--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1294 GTfRQNLdpngkWKD----------EEIWKVADEVgLKSVIEQFPGQLNFtlvdGGYV------LSHGHKQLMCLARSVL 1357
Cdd:COG4586 102 GQ-RSQL-----WWDlpaidsfrllKAIYRIPDAE-YKKRLDELVELLDL----GELLdtpvrqLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 1358 SKAKIILLDEPSAHLDPITYQVIRRVLKQ--AFAGCTVILCEHR---IEAMldCQRFLVIEESNVwQYD-SLQALL 1427
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDmddIEAL--CDRVIVIDHGRI-IYDgSLEELK 243
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
440-580 |
7.05e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG--RVSFCSQ--------------FSWIMPGTIK 503
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQklyldttlpltvnrFLRLRPGTKK 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 504 ENIIFGVsydeyryKSVVKACQLQQDITKfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK09544 99 EDILPAL-------KRVQAGHLIDAPMQK---------------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1219-1412 |
7.52e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1219 GNAVLENISFSISPGQRVGLLGRTGSGKSTLlsaflrmlnIK----------GDIEIDG--VSWNSvTLQEWRKAFGVIT 1286
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTL---------MKilsgvyqpdsGEILLDGepVRFRS-PRDAQAAGIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFIFSG-TFRQNL----DPNGK----WKdeEIWKVADEVgLKSVieqfpgQLNF---TLVDGgyvLSHGHKQLMCLAR 1354
Cdd:COG1129 86 QELNLVPNlSVAENIflgrEPRRGglidWR--AMRRRAREL-LARL------GLDIdpdTPVGD---LSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1355 SVLSKAKIILLDEPSAHLDP----ITYQVIRRvLKQafAGCTVILCEHRIEAMLD-CQRFLVI 1412
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEreveRLFRIIRR-LKA--QGVAIIYISHRLDEVFEiADRVTVL 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
439-628 |
9.69e-09 |
|
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: 56.89 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLI---LGELEASEGII------------KHSGRVSFCSQFSWIMPG-TI 502
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIhyngipykefaeKYPGEIIYVSEEDVHFPTlTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 503 KENIIFgvsydeyryksvvkACQLQQDitkfaeqdNTVLGeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 582
Cdd:cd03233 101 RETLDF--------------ALRCKGN--------EFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14141185 583 EEQvFESCVcKLMANKTR------ILVTSKmEHLRKADKILILHQGSSYFYG 628
Cdd:cd03233 154 ALE-ILKCI-RTMADVLKtttfvsLYQASD-EIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1206-1400 |
1.03e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYMDdGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQ-------- 1276
Cdd:PRK15056 7 IVVNDVTVTWRN-GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTRQALQKnlvayvpq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1277 ----EWrkAFGVITQKVFIFSGTFRQNLDPNGKWKDEEIwkVADEVGLKSVIEQFPGQLNftlvdggyVLSHGHKQLMCL 1352
Cdd:PRK15056 86 seevDW--SFPVLVEDVVMMGRYGHMGWLRRAKKRDRQI--VTAALARVDMVEFRHRQIG--------ELSGGQKKRVFL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA-GCTVILCEHRI 1400
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDeGKTMLVSTHNL 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
411-584 |
1.04e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 411 KVQQSNGDR--KHSSDENNVSFShlcLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASegiikhSGRV 488
Cdd:PRK11147 306 KMQVEEASRsgKIVFEMENVNYQ---IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQAD------SGRI 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 489 SfCsqfswimpGTIKEniifgVSY-DEYRY-----KSVV-KACQLQQDITkFAEQDNTVLG---------EGGVT----L 548
Cdd:PRK11147 377 H-C--------GTKLE-----VAYfDQHRAeldpeKTVMdNLAEGKQEVM-VNGRPRHVLGylqdflfhpKRAMTpvkaL 441
|
170 180 190
....*....|....*....|....*....|....*.
gi 14141185 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEE 584
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
418-622 |
1.24e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.26 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 418 DRKHSSDENNVSFSHLClvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR---------- 487
Cdd:COG1129 247 KRAAAPGEVVLEVEGLS--VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprda 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 488 ----VSFCS----QFSWIMPGTIKENIIFgVSYDEYRYKSVVKACQLQQDITKFAEQ--------DNTVlgeggVTLSGG 551
Cdd:COG1129 325 iragIAYVPedrkGEGLVLDLSIRENITL-ASLDRLSRGGLLDRRRERALAEEYIKRlriktpspEQPV-----GNLSGG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 552 QRARISLARAVYKDADLYLLDSPF-GyLDVFTEEQVFescvcKLMANKTR-----ILVTSKM-EHLRKADKILILHQG 622
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTrG-IDVGAKAEIY-----RLIRELAAegkavIVISSELpELLGLSDRILVMREG 470
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
420-675 |
1.32e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.79 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 420 KHSSDENNVSfshlclvgNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG-----------------II 482
Cdd:PRK13633 13 KYESNEESTE--------KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvyvdgldtsdeenlwdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 483 KHSGRVsFCSQFSWIMPGTIKENIIFG-----VSYDEYRYK--SVVKACQLQqDITKFAEQdntvlgeggvTLSGGQRAR 555
Cdd:PRK13633 85 NKAGMV-FQNPDNQIVATIVEEDVAFGpenlgIPPEEIRERvdESLKKVGMY-EYRRHAPH----------LLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 556 ISLARAVYKDADLYLLDSPFGYLDVFTEEQVFeSCVCKLmaNK----TRILVTSKMEHLRKADKILILHQGSSYFYGT-- 629
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVV-NTIKEL--NKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTpk 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 14141185 630 --FSELQSLrpdfssKLMGYDTfDQFTEerrssiLTETLRRFSVDDSS 675
Cdd:PRK13633 230 eiFKEVEMM------KKIGLDV-PQVTE------LAYELKKEGVDIPS 264
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1223-1398 |
1.37e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.29 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRMLNIK--GDIEIDGVswnSVTLQEWRKAFGVITQ-KVFI------ 1291
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNalAFRSPKGVKgsGSVLLNGM---PIDAKEMRAISAYVQQdDLFIptltvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1292 ----FSGTFRQNLDPNGKWKDEEIWKVADEVGLKS---VIEQFPGQLNftlvdggyVLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:TIGR00955 118 ehlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcanTRIGVPGRVK--------GLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*
gi 14141185 1365 LDEPSAHLDPIT-YQVIRRVLKQAFAGCTVILCEH 1398
Cdd:TIGR00955 190 CDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
441-615 |
1.55e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.09 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLI--LGELEAS---EGIIKHSGR---------------VSFCSQFSWIMPG 500
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtvdlrkeIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENIIFGVSYDEYRYKSVVKAC---QLQQdiTKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDEAvekSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 14141185 578 LDVFTEEQVfESCVCKLMANKTRILVTSKMEHL-RKADK 615
Cdd:PRK14239 179 LDPISAGKI-EETLLGLKDDYTMLLVTRSMQQAsRISDR 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1200-1413 |
1.65e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.35 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1200 WPSGGEMVvkdltvkymddgnAVLENISFSISPGQRVGLLGRTGSGKSTLlsaflrmLNIKG--DIEIDGV----SWNSV 1273
Cdd:PRK10535 14 YPSGEEQV-------------EVLKGISLDIYAGEMVAIVGASGSGKSTL-------MNILGclDKPTSGTyrvaGQDVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1274 TL------QEWRKAFGVITQKVFIFSG-TFRQNLD-P---NGKWKDEEIWKVAD---EVGLKSVIEQFPGQlnftlvdgg 1339
Cdd:PRK10535 74 TLdadalaQLRREHFGFIFQRYHLLSHlTAAQNVEvPavyAGLERKQRLLRAQEllqRLGLEDRVEYQPSQ--------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1340 yvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA-GCTVILCEHRIEAMLDCQRflVIE 1413
Cdd:PRK10535 145 --LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAER--VIE 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1208-1379 |
1.71e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 58.70 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDdgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVIT 1286
Cdd:PRK09536 6 VSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFI-FSGTFRQNLD----PN----GKWKDeeiwkvADEVGLKSVIE-----QFPGQlNFTlvdggyVLSHGHKQLMCL 1352
Cdd:PRK09536 84 QDTSLsFEFDVRQVVEmgrtPHrsrfDTWTE------TDRAAVERAMErtgvaQFADR-PVT------SLSGGERQRVLL 150
|
170 180
....*....|....*....|....*..
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDpITYQV 1379
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD-INHQV 176
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1208-1401 |
1.95e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.02 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWN------SVTLQE--- 1277
Cdd:PRK11248 4 ISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEgpgaerGVVFQNegl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1278 --WRK-----AFGvitqkvfifsgtfrqnLDPNGKWKDEEIWKVAD---EVGLKSVIEQFPGQlnftlvdggyvLSHGHK 1347
Cdd:PRK11248 82 lpWRNvqdnvAFG----------------LQLAGVEKMQRLEIAHQmlkKVGLEGAEKRYIWQ-----------LSGGQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 1348 QLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA--GCTVILCEHRIE 1401
Cdd:PRK11248 135 QRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITHDIE 190
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
435-622 |
2.00e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.42 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 435 LVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG---------RVSFC-SQFSWI------- 497
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrEVPFLrRQIGMIfqdhhll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 498 MPGTIKEN-----IIFGVSYDEYRYK--SVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYL 570
Cdd:PRK10908 92 MDRTVYDNvaiplIIAGASGDDIRRRvsAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 571 LDSPFGYLDVFTEE---QVFESC----VCKLMANKTRILVTskmehlRKADKILILHQG 622
Cdd:PRK10908 161 ADEPTGNLDDALSEgilRLFEEFnrvgVTVLMATHDIGLIS------RRSYRMLTLSDG 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
440-622 |
2.04e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSQFSWIMPG---------------TIKE 504
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFGVSYDEYRyksvvkacQLQQDITKFAE-----QDNTVLGEGgvTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK11614 100 NLAMGGFFAERD--------QFQERIKWVYElfprlHERRIQRAG--TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14141185 580 VFTEEQVFEScVCKLMANKTRILVTSK--MEHLRKADKILILHQG 622
Cdd:PRK11614 170 PIIIQQIFDT-IEQLREQGMTIFLVEQnaNQALKLADRGYVLENG 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1223-1398 |
2.25e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.77 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDGVSWNSVTLQEWRKAFGVITQ--------KVFIFSG 1294
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQqqsppfamPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 TFRQnldpngkwkdeeiwKVADEVGLKSVIEQFPGQLNFTLVDGGYV--LSHGHKQLMCLARSVL-------SKAKIILL 1365
Cdd:COG4138 92 LHQP--------------AGASSEAVEQLLAQLAEALGLEDKLSRPLtqLSGGEWQRVRLAAVLLqvwptinPEGQLLLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 14141185 1366 DEPSAHLDpITYQVI-RRVLKQ-AFAGCTVILCEH 1398
Cdd:COG4138 158 DEPMNSLD-VAQQAAlDRLLRElCQQGITVVMSSH 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
437-634 |
2.27e-08 |
|
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: 56.22 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEG--------IIKHSG----RVSFCSQFSWIMPG-TIK 503
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVREPRevrrRIGIVFQDLSVDDElTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENI-----IFGVSYDEYRYK--SVVKACQLqqditkfAEQDNTVLGeggvTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:cd03265 92 ENLyiharLYGVPGAERRERidELLDFVGL-------LEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 577 YLDVFTEEQVFEScVCKLMA--NKTRILVTSKMEHLRK-ADKILILHQGSSYFYGTFSELQ 634
Cdd:cd03265 161 GLDPQTRAHVWEY-IEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEELK 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
441-633 |
2.78e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-RVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKS 519
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 520 VVKACQL--------QQDITKFAEQDNTVLG-------EGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEE 584
Cdd:PRK13643 102 VLKDVAFgpqnfgipKEKAEKIAAEKLEMVGladefweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 585 QVFESCVCKLMANKTRILVTSKMEHLRK-ADKILILHQGSSYFYGTFSEL 633
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1208-1417 |
2.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNA-VLENISFSISPGQRVGLLGRTGSGKST---LLSAFLRmlNIKGDIEIDGVSWNSVTLQEWRKAFG 1283
Cdd:PRK13642 7 VENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQ---KVFIfSGTFRQNLD---PNGKWKDEEIWKVADEVGLKSvieqfpGQLNFTLVDGGYvLSHGHKQLMCLARSVL 1357
Cdd:PRK13642 85 MVFQnpdNQFV-GATVEDDVAfgmENQGIPREEMIKRVDEALLAV------NMLDFKTREPAR-LSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1358 SKAKIILLDEPSAHLDPITYQVIRRVLKQAFAG--CTVILCEHRIEAMLDCQRFLVIEESNV 1417
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
437-579 |
2.91e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEasegiiKHSGRVSFCSQFSWIMPgtIKENIIFGVSY---- 512
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP------RDAGNIIIDDEDISLLP--LHARARRGIGYlpqe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 513 -DEYR----YKSVVKACQLQQDITKFAEQD--NTVLGEG---------GVTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK10895 87 aSIFRrlsvYDNLMAVLQIRDDLSAEQREDraNELMEEFhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
...
gi 14141185 577 YLD 579
Cdd:PRK10895 167 GVD 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1214-1398 |
3.06e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1214 KYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAflrMLNIkgDIEIDGVSWNSVT-----------LQEWRKAF 1282
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGV--DKDFNGEARPQPGikvgylpqepqLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 GVITQKVfifsGTFRQNLDP----NGKWKDE--EIWKVADEVG-------------LKSVIEQF-------PGQLNFTlv 1336
Cdd:TIGR03719 87 ENVEEGV----AEIKDALDRfneiSAKYAEPdaDFDKLAAEQAelqeiidaadawdLDSQLEIAmdalrcpPWDADVT-- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1337 dggyVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQaFAGcTVILCEH 1398
Cdd:TIGR03719 161 ----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTH 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1206-1398 |
3.06e-08 |
|
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: 55.58 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKymDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNIKGDIEIDGVSWNSVTLQEWRKafgvI 1285
Cdd:cd03231 1 LEADELTCE--RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLL----RILAGLSPPLAGRVLLNGGPLDFQRD----S 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1286 TQKVFIFSG---------TFRQNL----DPNGkwkDEEIWKVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCL 1352
Cdd:cd03231 71 IARGLLYLGhapgikttlSVLENLrfwhADHS---DEQVEEALARVGLNGFEDRPVAQL-----------SAGQQRRVAL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14141185 1353 ARSVLSKAKIILLDEPSAHLDPITY-QVIRRVLKQAFAGCTVILCEH 1398
Cdd:cd03231 137 ARLLLSGRPLWILDEPTTALDKAGVaRFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
437-493 |
3.13e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 3.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHS--GRVSFCSQ 493
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIGYYAQ 389
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
427-611 |
4.25e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.50 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 427 NVSfSHLCLVGNPVLK---NINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII----------------KHSGR 487
Cdd:TIGR03269 284 NVS-KRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpDGRGR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 488 VS-----FCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAV 562
Cdd:TIGR03269 363 AKryigiLHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVL 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 563 YKDADLYLLDSPFGYLDVFTEEQVFESCV-CKLMANKTRILVTSKMEHLR 611
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILkAREEMEQTFIIVSHDMDFVL 492
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1219-1398 |
5.23e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.88 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1219 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSwnsvtlQEWRKAFGVITqkvfiFSG--- 1294
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPaAGTIKLDGGD------IDDPDVAEACH-----YLGhrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 ------TFRQNLDpngKWK------DEEIWKVADEVGLKSVIEqfpgqlnftlVDGGYvLSHGHKQLMCLARSVLSKAKI 1362
Cdd:PRK13539 83 amkpalTVAENLE---FWAaflggeELDIAAALEAVGLAPLAH----------LPFGY-LSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14141185 1363 ILLDEPSAHLDPITYQ----VIRRVLKQafaGCTVILCEH 1398
Cdd:PRK13539 149 WILDEPTAALDAAAVAlfaeLIRAHLAQ---GGIVIAATH 185
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
441-615 |
6.31e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.56 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLL-----MLILGELEASEGIIKHSG---------------RVSFCSQFSWIMPG 500
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFHGknlyapdvdpvevrrRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 TIKENIIFGV-------SYDEYRYKSVVKACQLQQDITKfaeqdntvLGEGGVTLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK14243 106 SIYDNIAYGAringykgDMDELVERSLRQAALWDEVKDK--------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14141185 574 PFGYLDVFTEEQVfESCVCKLMANKTRILVTSKMEHL-RKADK 615
Cdd:PRK14243 178 PCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQQAaRVSDM 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
441-656 |
7.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.48 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR---------------VSFCSQFSWIMPGTIKEN 505
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkigMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIFGVSYDEYRYKSVVKACQ---LQQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 582
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDealLAVNMLDFKTREPA-------RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 583 EEQVFEscVCKLMANK---TRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQSLRPD---------FSSKLM----- 645
Cdd:PRK13642 176 RQEIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDmveigldvpFSSNLMkdlrk 253
|
250
....*....|..
gi 14141185 646 -GYDTFDQFTEE 656
Cdd:PRK13642 254 nGFDLPEKYLSE 265
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1213-1373 |
9.13e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1213 VKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVITQKVFI 1291
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISpTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1292 FSGTFRQNL-----------DPNGKWKDEEIWKVADEVGLKSVIEqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKA 1360
Cdd:PRK10247 93 FGDTVYDNLifpwqirnqqpDPAIFLDDLERFALPDTILTKNIAE----------------LSGGEKQRISLIRNLQFMP 156
|
170
....*....|...
gi 14141185 1361 KIILLDEPSAHLD 1373
Cdd:PRK10247 157 KVLLLDEITSALD 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
439-622 |
9.38e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 55.02 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------------RVSFCSQFSWIMPG-TIKE 504
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFGVS-----------YDEYRyksVVKACQlQQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK11231 96 LVAYGRSpwlslwgrlsaEDNAR---VNQAME-QTRINHLADRRLT-------DLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 574 PFGYLDVftEEQVfEscVCKLM-----ANKTRILVTSKMEHL-RKADKILILHQG 622
Cdd:PRK11231 165 PTTYLDI--NHQV-E--LMRLMrelntQGKTVVTVLHDLNQAsRYCDHLVVLANG 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1222-1379 |
9.47e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNL 1300
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1301 DPNGKWKDEEI---WKVADEVGLKSVIeQFPG--QLNFTLVDggyVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDpI 1375
Cdd:PRK10253 102 VARGRYPHQPLftrWRKEDEEAVTKAM-QATGitHLADQSVD---TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD-I 176
|
....
gi 14141185 1376 TYQV 1379
Cdd:PRK10253 177 SHQI 180
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
423-623 |
1.07e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.19 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 423 SDENNVSFSHLCLV----GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGEL---EASEGIIKHSGrVSFCSQFS 495
Cdd:PRK13640 1 MKDNIVEFKHVSFTypdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDG-ITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 496 W----------------IMPGTIKENIIFGVsydEYR------YKSVVKACQLQQDITKFAEQDNTvlgeggvTLSGGQR 553
Cdd:PRK13640 80 WdirekvgivfqnpdnqFVGATVGDDVAFGL---ENRavprpeMIKIVRDVLADVGMLDYIDSEPA-------NLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 554 ARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFeSCVCKLMANK--TRILVTSKMEHLRKADKILILHQGS 623
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
440-635 |
1.17e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 55.11 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII---------KHSGRVSFcsqfswiMP---G-----TI 502
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgepldpEDRRRIGY-------LPeerGlypkmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 503 KENIIF-----GVSydeyryKSVVKAcQLQQDITKF--AEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:COG4152 89 GEQLVYlarlkGLS------KAEAKR-RADEWLERLglGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 576 GYLD-VFTEeqVFESCVCKLMAN-KTRILVTSKMEHL-RKADKILILHQGSSYFYGTFSELQS 635
Cdd:COG4152 158 SGLDpVNVE--LLKDVIRELAAKgTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
440-632 |
1.22e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEAS--EGIIKHSG---------RVSFCSQFSWIMPG-TIKENII 507
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNrkptkqilkRTGFVTQDDILYPHlTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 508 FgvsydeyryksvvkaCQL--------QQDITKFAEQ----------DNTVLGEGGVT-LSGGQRARISLARAVYKDADL 568
Cdd:PLN03211 163 F---------------CSLlrlpksltKQEKILVAESviselgltkcENTIIGNSFIRgISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 569 YLLDSPFGYLDVFTEEQVFESCVCklMANKTRILVTSKMEHLRKA----DKILILHQGSSYFYGTFSE 632
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGS--LAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1208-1399 |
1.50e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDdgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSwnsvtLQEWRKAFgvit 1286
Cdd:PRK13540 4 VIELDFDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPeKGEILFERQS-----IKKDLCTY---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1287 QKVFIFSGtFRQNLDPNGKWKDE---EIWKVADEVGLKSVIEQFpgQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKII 1363
Cdd:PRK13540 73 QKQLCFVG-HRSGINPYLTLRENclyDIHFSPGAVGITELCRLF--SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 14141185 1364 LLDEPSAHLDPITYQVI-RRVLKQAFAGCTVILCEHR 1399
Cdd:PRK13540 150 LLDEPLVALDELSLLTIiTKIQEHRAKGGAVLLTSHQ 186
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1211-1267 |
1.83e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 1.83e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1211 LTVKYMD---DGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL---------RMLNIKGDIEIDG 1267
Cdd:PRK13547 2 LTADHLHvarRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggapRGARVTGDVTLNG 70
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
450-613 |
2.17e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 450 KGEMLAITGSTGSGKTSLLMLILGELEASEGIIKhsgrvsfcsqfsWIMPGTIKENIIFgvsydeyryksvvkacqlqqd 529
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI------------YIDGEDILEEVLD--------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 530 itkfaEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTR------ILV 603
Cdd:smart00382 48 -----QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSeknltvILT 122
|
170
....*....|
gi 14141185 604 TSKMEHLRKA 613
Cdd:smart00382 123 TNDEKDLGPA 132
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
438-579 |
2.40e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.73 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 438 NPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-VS--------FCSQF-SW-IMPG-TIKEN 505
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdVThrsiqqrdICMVFqSYaLFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 I-----IFGVSYDEyRYKSVVKACQLqQDITKFAEQ--DNtvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK11432 99 VgyglkMLGVPKEE-RKQRVKEALEL-VDLAGFEDRyvDQ---------ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
.
gi 14141185 579 D 579
Cdd:PRK11432 168 D 168
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1222-1444 |
2.61e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAflrmlnIKGDIEIDGvswNSVTL-QEWRKAFgvITQKV---------FI 1291
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLAL------LKNEISADG---GSYTFpGNWQLAW--VNQETpalpqpaleYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1292 FSG--TFRQNldpngkwkdEEIWKVADEVGLKSVIEQFPGQLN----FTLVDGGYVLSHG----HKQL------------ 1349
Cdd:PRK10636 85 IDGdrEYRQL---------EAQLHDANERNDGHAIATIHGKLDaidaWTIRSRAASLLHGlgfsNEQLerpvsdfsggwr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1350 --MCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKqAFAGcTVILCEHRIEaMLD--CQRFLVIEESNVWQ----YD 1421
Cdd:PRK10636 156 mrLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK-SYQG-TLILISHDRD-FLDpiVDKIIHIEQQSLFEytgnYS 232
|
250 260
....*....|....*....|...
gi 14141185 1422 SLQALLSEKSIFQQAISSSEKMR 1444
Cdd:PRK10636 233 SFEVQRATRLAQQQAMYESQQER 255
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1206-1275 |
3.37e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 53.16 E-value: 3.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 1206 MVVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDG---VSWNSVTL 1275
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPdSGEVLVDGldvATTPSREL 73
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1218-1402 |
3.61e-07 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 52.24 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1218 DGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSwnsvtlqewRKAFgvITQKVFI---FS 1293
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRRAGGA---------RVAY--VPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1294 GTFRQnLDPNGKWKDEEIWK---------VA---DEVGLksviEQFPG-QLNftlvdggyVLSHGHKQLMCLARSVLSKA 1360
Cdd:NF040873 72 LTVRD-LVAMGRWARRGLWRrltrddraaVDdalERVGL----ADLAGrQLG--------ELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14141185 1361 KIILLDEPSAHLDPITYQVIRRVLKQAFA-GCTVILCEHRIEA 1402
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLEL 181
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1222-1401 |
4.20e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML---NIKGDIEIDGVSWNS-VTLQEWRKAFGVITQKVFIFSGtfr 1297
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgtPVAGCVDVPDNQFGReASLIDAIGRKGDFKDAVELLNA--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1298 qnldpngkwkdeeiwkvadeVGLKSVieqfpgQLNFTLVDggyVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITY 1377
Cdd:COG2401 122 --------------------VGLSDA------VLWLRRFK---ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|....*.
gi 14141185 1378 QVIRRVLKQAF--AGCTVILCEHRIE 1401
Cdd:COG2401 173 KRVARNLQKLArrAGITLVVATHHYD 198
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1208-1428 |
4.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKY-MDDGNAVLENISFSISPGQRVGLLGRTGSGKST---LLSAFLRMLNikGDIEIDGVSWNSVTLQEWRKAFG 1283
Cdd:PRK13650 7 VKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAES--GQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1284 VITQKV-FIFSGTFRQN-----LDPNGKWKDEEIWKVADE---VGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDdvafgLENKGIPHEEMKERVNEAlelVGMQDFKEREPAR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1355 SVLSKAKIILLDEPSAHLDPI----TYQVIRRVLKQafAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLS 1428
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEgrleLIKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1218-1398 |
4.70e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.11 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1218 DGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNIKGDIEIDGVSWNSVTLQEWRKAFGvitQKVFiFSG--- 1294
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSL----LRILAGLARPDAGEVLWQGEPIRRQRDEYH---QDLL-YLGhqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 ------TFRQNLDPN----GKWKDEEIWKVADEVGLKSViEQFPGQlnftlvdggyVLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:PRK13538 84 giktelTALENLRFYqrlhGPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 14141185 1365 LDEPSAHLDPI-TYQVIRRVLKQAFAGCTVILCEH 1398
Cdd:PRK13538 153 LDEPFTAIDKQgVARLEALLAQHAEQGGMVILTTH 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1223-1414 |
4.72e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.20 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQE----WRKAFGVITQ--KVFIFSGT 1295
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1296 FRQNL---DPNGKWKDEEIWKVADE----VGL-KSVIEQFPgqlnftlvdggYVLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:PRK13643 102 VLKDVafgPQNFGIPKEKAEKIAAEklemVGLaDEFWEKSP-----------FELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14141185 1368 PSAHLDPITYQVIRRVLKQAF-AGCTVILCEHRIEAMLDCQRFLVIEE 1414
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHqSGQTVVLVTHLMDDVADYADYVYLLE 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1221-1419 |
6.77e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1221 AVLENISFSISPGQRVGLLGRTGSGKSTLLsAFLRMLNIKGDIEIDGVSWNSVTLQEWRKA------FGVITQKvFIFSG 1294
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLL-AILAGLDDGSSGEVSLVGQPLHQMDEEARAklrakhVGFVFQS-FMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 TF--RQNLD-------PNGKWKDEEIWKVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:PRK10584 102 TLnaLENVElpallrgESSRQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1366 DEPSAHLDPITYQVIRRVLkqaFA-----GCTVILCEHRIEAMLDCQRFLVIEESNVWQ 1419
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLL---FSlnrehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
426-622 |
7.97e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.43 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 426 NNVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII---------------KHSGRVSF 490
Cdd:PRK13650 8 KNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenvwdiRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 491 CSQFSWIMPGTIKENIIFG-----VSYDEYRyKSVVKACQLQqDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKD 565
Cdd:PRK13650 88 QNPDNQFVGATVEDDVAFGlenkgIPHEEMK-ERVNEALELV-GMQDFKEREPA-------RLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 566 ADLYLLDS------PFGYLDVF-TEEQVFEScvcklmANKTRILVTSKMEHLRKADKILILHQG 622
Cdd:PRK13650 159 PKIIILDEatsmldPEGRLELIkTIKGIRDD------YQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
437-579 |
8.45e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.39 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR-----------------VSFCSQFSWIMP 499
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevrktvgIVFQNPDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 GTIKENIIFG-----VSYDEY--RYKSVVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK13639 94 PTVEEDVAFGplnlgLSKEEVekRVKEALKAVGMEGFENKPPHH-----------LSGGQKKRVAIAGILAMKPEIIVLD 162
|
....*..
gi 14141185 573 SPFGYLD 579
Cdd:PRK13639 163 EPTSGLD 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1218-1401 |
8.57e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1218 DGNAVLENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLNIKGDIEIDGVSWNSVTLQEW-RKAFGVITQKVF--- 1290
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTlvp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1291 -------IFSGtfRQNLDPNGKWKDEEIWKVADEVgLKSVieQFPGqLNFTLVDGGYVLshGHKQLMCLARSVLSKAKII 1363
Cdd:TIGR02633 92 elsvaenIFLG--NEITLPGGRMAYNAMYLRAKNL-LREL--QLDA-DNVTRPVGDYGG--GQQQLVEIAKALNKQARLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14141185 1364 LLDEPSAHLDPITYQV---IRRVLKQAFAGCTVIlcEHRIE 1401
Cdd:TIGR02633 164 ILDEPSSSLTEKETEIlldIIRDLKAHGVACVYI--SHKLN 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1222-1270 |
8.61e-07 |
|
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: 51.76 E-value: 8.61e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLlsafLRML-NI----KGDIEIDG-VSW 1270
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTL----LRLLaGIyppdSGTVTVRGrVSS 87
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
440-629 |
1.12e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.16 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGII-----------------------------KHSGRVSF 490
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhelitnpyskkiknfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 491 CSQFS--WIMPGTIKENIIFG-VSYDEYRYKSVVKAcqlqqdiTKFAEQ---DNTVLGEGGVTLSGGQRARISLARAVYK 564
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGpVALGVKKSEAKKLA-------KFYLNKmglDDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 565 DADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEH-LRKADKILILHQGSSYFYGT 629
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGT 259
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
1218-1412 |
1.23e-06 |
|
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: 51.74 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1218 DGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWRKAFGVITQKVfifsgtf 1296
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpDAGTVDLAGVDLHGLSRRARARRVALVEQDS------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1297 rqNLDPN---------GKWKDEEIWKvADEVGLKSVIEQFPGQLNFT-LVDGGY-VLSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:TIGR03873 85 --DTAVPltvrdvvalGRIPHRSLWA-GDSPHDAAVVDRALARTELShLADRDMsTLSGGERQRVHVARALAQEPKLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14141185 1366 DEPSAHLDpITYQ--VIRRVLKQAFAGCTVILCEHRIE-AMLDCQRFLVI 1412
Cdd:TIGR03873 162 DEPTNHLD-VRAQleTLALVRELAATGVTVVAALHDLNlAASYCDHVVVL 210
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1206-1419 |
1.37e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.68 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWNSVTLQEWRKAFGV 1284
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQK--------VFIFSGTF--RQNLDPNGKWKdEEIWKVADEVGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCLAR 1354
Cdd:PRK13648 88 VFQNpdnqfvgsIVKYDVAFglENHAVPYDEMH-RRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1355 SVLSKAKIILLDEPSAHLDPITYQ----VIRRVlkQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQ 1419
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1202-1413 |
1.45e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1202 SGGEMVVK--DLTVKYmddGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRMLniKGDIEIDGvswnsvtlqewr 1279
Cdd:PRK13409 335 SERETLVEypDLTKKL---GDFSLEVEGGEIYEGEVIGIVGPNGIGKTT----FAKLL--AGVLKPDE------------ 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1280 kafGVITQKVFI----------FSGTFRQNLDPNGKWKDEEIWK--VADEVGLKSVIEQfpgqlnftLVDGgyvLSHGHK 1347
Cdd:PRK13409 394 ---GEVDPELKIsykpqyikpdYDGTVEDLLRSITDDLGSSYYKseIIKPLQLERLLDK--------NVKD---LSGGEL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1348 QLMCLARSVLSKAKIILLDEPSAHLDP----ITYQVIRRVLKQafAGCTVILCEHRIeAMLD--CQRFLVIE 1413
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRIAEE--REATALVVDHDI-YMIDyiSDRLMVFE 528
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1223-1403 |
1.52e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLlsaflrMlNI--------KGDIEIDGvswNSVTLQEWRKAF----GVITQ--- 1287
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL------M-KIlyglyqpdSGEILIDG---KPVRIRSPRDAIalgiGMVHQhfm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1288 --KVFifsgTFRQNL-----DPNGKWKD-----EEIWKVADEVGLK----SVIEQfpgqlnftlvdggyvLSHGHKQ--- 1348
Cdd:COG3845 91 lvPNL----TVAENIvlglePTKGGRLDrkaarARIRELSERYGLDvdpdAKVED---------------LSVGEQQrve 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1349 -LMCLARsvlsKAKIILLDEPSAHLDP----ITYQVIRRvLKQafAGCTVILCEHRI-EAM 1403
Cdd:COG3845 152 iLKALYR----GARILILDEPTAVLTPqeadELFEILRR-LAA--EGKSIIFITHKLrEVM 205
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1232-1405 |
1.59e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1232 PGQRVGLLGRTGSGKSTLLsaflRML--NIK---GDIEiDGVSWNSVtLQEWRkafGVITQKVF---------------- 1290
Cdd:COG1245 98 KGKVTGILGPNGIGKSTAL----KILsgELKpnlGDYD-EEPSWDEV-LKRFR---GTELQDYFkklangeikvahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1291 ------IFSGTFRQNL---DPNGKWKDeeiwkVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAK 1361
Cdd:COG1245 169 vdlipkVFKGTVRELLekvDERGKLDE-----LAEKLGLENILDRDISEL-----------SGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14141185 1362 IILLDEPSAHLDpiTYQVIR--RVLKQ-AFAGCTVILCEHRIeAMLD 1405
Cdd:COG1245 233 FYFFDEPSSYLD--IYQRLNvaRLIRElAEEGKYVLVVEHDL-AILD 276
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1208-1280 |
1.68e-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: 52.38 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNA--VLENISFSISPGQRVGLLGRTGSGKS-TLLSAfLRML-----NIKGDIEIDGVSWNSVTLQEWR 1279
Cdd:COG4172 9 VEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvTALSI-LRLLpdpaaHPSGSILFDGQDLLGLSERELR 87
|
.
gi 14141185 1280 K 1280
Cdd:COG4172 88 R 88
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1207-1373 |
1.74e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLniKGDIEIDG--VSW-------------- 1270
Cdd:PRK15064 321 EVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTL----LRTL--VGELEPDSgtVKWsenanigyyaqdha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1271 ----NSVTLQEWrkafgvITQkvfifsgtfrqnldpngkWKDEEiwkvADEVGLKSVIeqfpGQLNFTLVDGG---YVLS 1343
Cdd:PRK15064 393 ydfeNDLTLFDW------MSQ------------------WRQEG----DDEQAVRGTL----GRLLFSQDDIKksvKVLS 440
|
170 180 190
....*....|....*....|....*....|
gi 14141185 1344 HGHKQLMCLARSVLSKAKIILLDEPSAHLD 1373
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1219-1398 |
1.98e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.64 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1219 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWNSVTLQE---WRKAFGVITQKV-FIFS 1293
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSaGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHhLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1294 GTFRQN----LDPNGKWKDEEIWKVA---DEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:PRK10908 94 RTVYDNvaipLIIAGASGDDIRRRVSaalDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190
....*....|....*....|....*....|...
gi 14141185 1367 EPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEH 1398
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEfNRVGVTVLMATH 195
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1222-1373 |
2.07e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.58 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRMLN--IKGDIEIDGVSWNSVTLQ---EWR-KAFGVITQkvFifsgt 1295
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDtpTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQ--F----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1296 frQNLDPN-------------GKWKDEEIWKVADE----VGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLS 1358
Cdd:PRK11629 96 --HHLLPDftalenvamplliGKKKPAEINSRALEmlaaVGLEHRANHRPSE-----------LSGGERQRVAIARALVN 162
|
170
....*....|....*
gi 14141185 1359 KAKIILLDEPSAHLD 1373
Cdd:PRK11629 163 NPRLVLADEPTGNLD 177
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
439-572 |
2.51e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.34 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGiikhSGRVSfcsqfswimpgtIKENIIfgvsydeYRYK 518
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV----AGCVD------------VPDNQF-------GREA 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 519 SVVKACQLQQDITKFAEqdntVLGEGGV-----------TLSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG2401 101 SLIDAIGRKGDFKDAVE----LLNAVGLsdavlwlrrfkELSTGQKFRFRLALLLAERPKLLVID 161
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1206-1398 |
3.36e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1206 MVVKDLTVKymddgnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDGVS---WNSVTL------- 1275
Cdd:PRK03695 1 MQLNDVAVS------TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPleaWSAAELarhrayl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1276 -QEWRKAFGVitqKVFIFSGTFRQNLDPNGKWKDeEIWKVADEVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:PRK03695 75 sQQQTPPFAM---PVFQYLTLHQPDKTRTEAVAS-ALNEVAEALGLDDKLGRSVNQ-----------LSGGEWQRVRLAA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1355 SVL-------SKAKIILLDEPSAHLDpITYQVI-RRVLKQ-AFAGCTVILCEH 1398
Cdd:PRK03695 140 VVLqvwpdinPAGQLLLLDEPMNSLD-VAQQAAlDRLLSElCQQGIAVVMSSH 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1078-1404 |
3.77e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1078 NLHTANWFMYLATLRWFQMRIDMIFVLFFiVVTFISILTTGEGEGTAGIILTLAMnimSTLQWAVNSSIDTDSLMRSVSR 1157
Cdd:TIGR00956 654 DDYLKLSFQYYNSHKWRNFGIIIGFTVFF-FFVYILLTEFNKGAKQKGEILVFRR---GSLKRAKKAGETSASNKNDIEA 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1158 --VFKFIDIQTEESMYTQIiKELPREGSSDVLviknehvkksdIWpsggemvvKDLT--VKYMDDGNAVLENISFSISPG 1233
Cdd:TIGR00956 730 geVLGSTDLTDESDDVNDE-KDMEKESGEDIF-----------HW--------RNLTyeVKIKKEKRVILNNVDGWVKPG 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1234 QRVGLLGRTGSGKSTLLSAFLRMLNIkGDIEIDGVSWNSVTLQE-WRKAFGVITQK-----------VFIFSGTFRQNLD 1301
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLAERVTT-GVITGGDRLVNGRPLDSsFQRSIGYVQQQdlhlptstvreSLRFSAYLRQPKS 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1302 PNGKWKDEEIWKVADEVGLKSVIEQFPGQlnftlvdGGYVLSHGHKQLMCLARSVLSKAKIIL-LDEPSAHLDPIT-YQV 1379
Cdd:TIGR00956 869 VSKSEKMEYVEEVIKLLEMESYADAVVGV-------PGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTaWSI 941
|
330 340
....*....|....*....|....*.
gi 14141185 1380 IRRVLKQAFAGCTvILCE-HRIEAML 1404
Cdd:TIGR00956 942 CKLMRKLADHGQA-ILCTiHQPSAIL 966
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1223-1372 |
3.94e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLNIKGDIEIDG--VSWNSVTLQEwRKAFGVITQKVF------- 1290
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTYEGEIIFEGeeLQASNIRDTE-RAGIAIIHQELAlvkelsv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1291 ---IFSGtfrQNLDPNGKWKDEEIWKVAD----EVGLKSVIEQFPGQLnftlvdGGyvlshGHKQLMCLARSVLSKAKII 1363
Cdd:PRK13549 100 lenIFLG---NEITPGGIMDYDAMYLRAQkllaQLKLDINPATPVGNL------GL-----GQQQLVEIAKALNKQARLL 165
|
....*....
gi 14141185 1364 LLDEPSAHL 1372
Cdd:PRK13549 166 ILDEPTASL 174
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
427-575 |
4.34e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.15 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 427 NVSFSHlclvGN-PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG----------------RVS 489
Cdd:PRK11831 12 GVSFTR----GNrCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrsrlytvrkRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 490 FCSQFSWIMPG-TIKENIIFGVsydeyRYKSVVKACQLQQDITKFAEqdntVLGEGGVT------LSGGQRARISLARAV 562
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAYPL-----REHTQLPAPLLHSTVMMKLE----AVGLRGAAklmpseLSGGMARRAALARAI 158
|
170
....*....|...
gi 14141185 563 YKDADLYLLDSPF 575
Cdd:PRK11831 159 ALEPDLIMFDEPF 171
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1223-1428 |
5.54e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.42 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDGVSWNSVTLQEWR-----------KAFGVITQKVF 1290
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1291 IFSGTFRQNLdpNGKWKDEEIWKVAD---EVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:PRK10070 124 LDNTAFGMEL--AGINAEERREKALDalrQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 1368 PSAHLDPITYQVIRRVLK--QAFAGCTVILCEHRI-EAMLDCQRFLVIEESNVWQYDSLQALLS 1428
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
385-628 |
5.61e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 385 YNLMTTGIIMENVTAF-------WEEGFGELLEKVQqSNGDRKHSSDENNVSFShlclvgnpVLKNINLNIEKGEMLAIT 457
Cdd:TIGR00956 23 YKPYKLGVAYKNLSAYgvaadsdYQPTFPNALLKIL-TRGFRKLKKFRDTKTFD--------ILKPMDGLIKPGELTVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 458 GSTGSGKTSLLMLILGELEAS---------------EGIIKH-SGRVSFCSQFSWIMPG-TIKENIIF------------ 508
Cdd:TIGR00956 94 GRPGSGCSTLLKTIASNTDGFhigvegvitydgitpEEIKKHyRGDVVYNAETDVHFPHlTVGETLDFaarcktpqnrpd 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 509 GVSYDEYRYKSV-VKACQLQQDITKfaeqdNTVLGEGGVT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQv 586
Cdd:TIGR00956 174 GVSREEYAKHIAdVYMATYGLSHTR-----NTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALE- 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 14141185 587 FESCVcKLMAN--KTRILVT---SKMEHLRKADKILILHQGSSYFYG 628
Cdd:TIGR00956 248 FIRAL-KTSANilDTTPLVAiyqCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
432-473 |
5.75e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.64 E-value: 5.75e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 14141185 432 HLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILG 473
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1223-1384 |
6.56e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWNSVT---LQEWRKAFGvitqkvFIFSGTFrQ 1298
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSpgkLQALRRDIQ------FIFQDPY-A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1299 NLDP------------------NGKWKDEEIWKVADEVGLKSVIE-QFPgqlnftlvdggYVLSHGHKQLMCLARSVLSK 1359
Cdd:PRK10261 413 SLDPrqtvgdsimeplrvhgllPGKAAAARVAWLLERVGLLPEHAwRYP-----------HEFSGGQRQRICIARALALN 481
|
170 180
....*....|....*....|....*.
gi 14141185 1360 AKIILLDEPSAHLD-PITYQVIRRVL 1384
Cdd:PRK10261 482 PKVIIADEAVSALDvSIRGQIINLLL 507
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
441-622 |
6.94e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSlLMLIL-GELEASEGIIKHSGR-VSFCS-------------Q-FSWIMPGTIKE 504
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKST-LMKILyGLYQPDSGEILIDGKpVRIRSprdaialgigmvhQhFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 505 NIIFGVsydEYRYKSVVKACQLQQDITKFAEQ-------DNTVlgeggVTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:COG3845 100 NIVLGL---EPTKGGRLDRKAARARIRELSERygldvdpDAKV-----EDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 578 LdvfT--E-EQVFEscVCKLMAN--KTRILVTSKM-EHLRKADKILILHQG 622
Cdd:COG3845 172 L---TpqEaDELFE--ILRRLAAegKSIIFITHKLrEVMAIADRVTVLRRG 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1222-1399 |
8.77e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIdgvswnsvtlqewrkAFGvitqkvfIFSGTFRQNl 1300
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELApVSGEIGL---------------AKG-------IKLGYFAQH- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1301 dpngkwkDEEIWKvADEVGLKSVIEQFPGQLNFTLVD--GGY------------VLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:PRK10636 384 -------QLEFLR-ADESPLQHLARLAPQELEQKLRDylGGFgfqgdkvteetrRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|....*.
gi 14141185 1367 EPSAHLDpityQVIRRVLKQA---FAGCTVILCEHR 1399
Cdd:PRK10636 456 EPTNHLD----LDMRQALTEAlidFEGALVVVSHDR 487
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1208-1403 |
9.96e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.52 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDGVSWNSVTL-----QEWRK 1280
Cdd:COG4170 6 IRNLTIEIDTPQGRVkaVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLlklspRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1281 afgVITQKV-FIFsgtfrQN----LDPNGK-----------------------WKDEEIWKVADEVGLKS---VIEQFPg 1329
Cdd:COG4170 86 ---IIGREIaMIF-----QEpsscLDPSAKigdqlieaipswtfkgkwwqrfkWRKKRAIELLHRVGIKDhkdIMNSYP- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14141185 1330 qlnftlvdggYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQ--AFAGCTVILCEHRIEAM 1403
Cdd:COG4170 157 ----------HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlnQLQGTSILLISHDLESI 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
437-647 |
1.24e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEAS--EGIIKHSGRVSF------------CSQFSWIMPGTI 502
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGDVTLngeplaaidaprLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 503 KENiiFGVSYDEY----RYKSVVKACQLQQDITKFAEQ------DNTVLGEGGVTLSGGQRARISLARAVYK-------- 564
Cdd:PRK13547 93 QPA--FAFSAREIvllgRYPHARRAGALTHRDGEIAWQalalagATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 565 -DADLYLLDSPFGYLDVFTEEQVFEScvCKLMANKTRILVTSKMEHL----RKADKILILHQGSSYFYGTFSELqsLRPD 639
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDT--VRRLARDWNLGVLAIVHDPnlaaRHADRIAMLADGAIVAHGAPADV--LTPA 246
|
....*...
gi 14141185 640 FSSKLMGY 647
Cdd:PRK13547 247 HIARCYGF 254
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1208-1277 |
1.24e-05 |
|
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: 47.91 E-value: 1.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1208 VKDLTVKymDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL---RMLNIKGDIEIDGVSWNSVTLQE 1277
Cdd:cd03217 3 IKDLHVS--VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGEDITDLPPEE 73
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1202-1401 |
1.58e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.04 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1202 SGGEMVVKDLTVKYMDdgNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRMLNI-----KGDIEIDGVSWNSV--- 1273
Cdd:PRK10619 2 SENKLNVIDLHKRYGE--HEVLKGVSLQANAGDVISIIGSSGSGKST----FLRCINFlekpsEGSIVVNGQTINLVrdk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1274 ----------TLQEWRKAFGVITQKVFIFSG-TFRQN--------LDPNGKWKDEEIWKVADEVGL-KSVIEQFPGQLnf 1333
Cdd:PRK10619 76 dgqlkvadknQLRLLRTRLTMVFQHFNLWSHmTVLENvmeapiqvLGLSKQEARERAVKYLAKVGIdERAQGKYPVHL-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1334 tlvdggyvlSHGHKQLMCLARSVLSKAKIILLDEPSAHLDP-ITYQVIRRVLKQAFAGCTVILCEHRIE 1401
Cdd:PRK10619 154 ---------SGGQQQRVSIARALAMEPEVLLFDEPTSALDPeLVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1220-1382 |
1.67e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.16 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1220 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGvswNSVT-LQEWRKAFGVItqKVF--IFSGT 1295
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPdSGSILIDG---KDVTkLPEYKRAKYIG--RVFqdPMMGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1296 F-----RQNL---DPNGKWKdeeiwkvadevGL-----KSVIEQFPGQLNfTLVDG---------GYvLSHGHKQLMCLA 1353
Cdd:COG1101 94 ApsmtiEENLalaYRRGKRR-----------GLrrgltKKRRELFRELLA-TLGLGlenrldtkvGL-LSGGQRQALSLL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 14141185 1354 RSVLSKAKIILLDEPSAHLDP--------ITYQVIRR 1382
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPktaalvleLTEKIVEE 197
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
424-590 |
2.12e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.98 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 424 DENNVSFSHLCLV---GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMlILGELEASEG---IIKHSGRVSFCSQFSWI 497
Cdd:TIGR00954 448 QDNGIKFENIPLVtpnGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 498 MPGTIKENIIFGVSYDEYRYKSVVKAcQLQQdITKFAEQDNTVLGEGGVT--------LSGGQRARISLARAVYKDADLY 569
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLSDK-DLEQ-ILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFA 604
|
170 180
....*....|....*....|.
gi 14141185 570 LLDSPFGYLDVFTEEQVFESC 590
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRLC 625
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1210-1413 |
2.13e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.01 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1210 DLTVKYmddGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRMLNikGDIEIDGvswnsvtlqewrkafGVITQKV 1289
Cdd:COG1245 346 DLTKSY---GGFSLEVEGGEIREGEVLGIVGPNGIGKTT----FAKILA--GVLKPDE---------------GEVDEDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1290 FI----------FSGTFRQNL-DPNGKWKDEEIWK--VADEVGLKSVIEQfpgqlnftLVDGgyvLSHGHKQ----LMCL 1352
Cdd:COG1245 402 KIsykpqyispdYDGTVEEFLrSANTDDFGSSYYKteIIKPLGLEKLLDK--------NVKD---LSGGELQrvaiAACL 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 1353 ARsvlsKAKIILLDEPSAHLDP----ITYQVIRRVLKQafAGCTVILCEHRIeAMLD--CQRFLVIE 1413
Cdd:COG1245 471 SR----DADLYLLDEPSAHLDVeqrlAVAKAIRRFAEN--RGKTAMVVDHDI-YLIDyiSDRLMVFE 530
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1230-1405 |
2.30e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1230 ISPGQRVGLLGRTGSGKST---LLSAFLrMLNIkGDIEiDGVSWNSV-------TLQEWRK--AFGVIT-----QKV-FI 1291
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTavkILSGEL-IPNL-GDYE-EEPSWDEVlkrfrgtELQNYFKklYNGEIKvvhkpQYVdLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1292 ---FSGTFRQNL---DPNGKWKDeeiwkVADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:PRK13409 173 pkvFKGKVRELLkkvDERGKLDE-----VVERLGLENILDRDISEL-----------SGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14141185 1366 DEPSAHLDpiTYQVIR--RVLKQAFAGCTVILCEHRIeAMLD 1405
Cdd:PRK13409 237 DEPTSYLD--IRQRLNvaRLIRELAEGKYVLVVEHDL-AVLD 275
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1207-1420 |
2.30e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKYMDdgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAflrmlnIKGDiEIDGVSwNSVTLQEWRKAFGV-- 1284
Cdd:PRK10938 262 VLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL------ITGD-HPQGYS-NDLTLFGRRRGSGEti 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 --ITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGL--------KSVIEQFPGQLNFT--LVDGGY-VLSHGHKQLMC 1351
Cdd:PRK10938 332 wdIKKHIGYVSSSLHLDYRVSTSVRNVILSGFFDSIGIyqavsdrqQKLAQQWLDILGIDkrTADAPFhSLSWGQQRLAL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1352 LARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFA-GCTVIL-CEHRIEAMLDC--QRFLVIEESNVWQY 1420
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQLLfVSHHAEDAPACitHRLEFVPDGDIYRY 484
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1208-1384 |
2.45e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.20 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYMDDG---NAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDGVSWNSVTLQ-----EWR 1279
Cdd:PRK11022 6 VDKLSVHFGDESapfRAV-DRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQrisekERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1280 KAFGVITQKVFIFSGTfrqNLDP------------------NGKWKDEEIWKVADEVGL---KSVIEQFPGQlnftlvdg 1338
Cdd:PRK11022 85 NLVGAEVAMIFQDPMT---SLNPcytvgfqimeaikvhqggNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQ-------- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14141185 1339 gyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLD-PITYQVIRRVL 1384
Cdd:PRK11022 154 ---LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLL 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1208-1414 |
2.75e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.29 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKYmdDGNAVLENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLNikGDI-----EIDGVSWNSV------ 1273
Cdd:PRK11300 8 VSGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVfncLTGFYKPTG--GTIllrgqHIEGLPGHQIarmgvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1274 -TLQEWR--KAFGVITQ---------KVFIFSGTF---------RQNLDPNGKWkdeeiwkvADEVGLKSVIEQFPGQLn 1332
Cdd:PRK11300 84 rTFQHVRlfREMTVIENllvaqhqqlKTGLFSGLLktpafrraeSEALDRAATW--------LERVGLLEHANRQAGNL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1333 ftlvdggyvlSHGHKQLMCLARSVLSKAKIILLDEPSAHLDP---ITYQVIRRVLKQAFaGCTVILCEHRIEAMLD-CQR 1408
Cdd:PRK11300 155 ----------AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPketKELDELIAELRNEH-NVTVLLIEHDMKLVMGiSDR 223
|
....*.
gi 14141185 1409 FLVIEE 1414
Cdd:PRK11300 224 IYVVNQ 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1223-1373 |
3.82e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.09 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGDIEIDG-------VSWNSvtlQEWRKAF----------GV 1284
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDhplhfgdYSYRS---QRIRMIFqdpstslnprQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1285 ITQkvfIFSGTFRQNLDPNGKWKDEEIWKVADEVGLksvieqFPGQLNFTlvdgGYVLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:PRK15112 106 ISQ---ILDFPLRLNTDLEPEQREKQIIETLRQVGL------LPDHASYY----PHMLAPGQKQRLGLARALILRPKVII 172
|
....*....
gi 14141185 1365 LDEPSAHLD 1373
Cdd:PRK15112 173 ADEALASLD 181
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
437-579 |
3.92e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGeLEA-SEGIIKHSGRV-------------SFcsQFSWIMPG-T 501
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LERiTSGEIWIGGRVvnelepadrdiamVF--QNYALYPHmS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 502 IKENIIFGVsydeyRYKSVVKAcQLQQDITKFAeqdnTVLGEGGV------TLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:PRK11650 93 VRENMAYGL-----KIRGMPKA-EIEERVAEAA----RILELEPLldrkprELSGGQRQRVAMGRAIVREPAVFLFDEPL 162
|
....
gi 14141185 576 GYLD 579
Cdd:PRK11650 163 SNLD 166
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
858-1024 |
5.03e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 47.04 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 858 LIWCVLVFLVEVAASLFVLWLLKNnPVNSGNNGTkiSNSSYVVIITSTsfyyifyiyvgvadtLLALSLFRGLPLVHTLI 937
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKN-LIDALSAGG--SSGGLLALLVAL---------------FLLQAVLSALSSYLLGR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 938 TASKI---LHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLAT 1014
Cdd:cd18551 63 TGERVvldLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVT 142
|
170
....*....|
gi 14141185 1015 VPGLVVFILL 1024
Cdd:cd18551 143 LAVVPLAFLI 152
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1218-1419 |
5.34e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.33 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1218 DGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRML----NI-KGDIEIDGVSWNSVTLQEwrKAFGVITQKVFIF 1292
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLL----RMIagleDItSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1293 SgtfRQNLDPN-------GKWKDEEIWK----VADEVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAK 1361
Cdd:PRK11000 88 P---HLSVAENmsfglklAGAKKEEINQrvnqVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1362 IILLDEPSAHLDP-ITYQV---IRRVLKQafAGCTVILCEH-RIEAMLDCQRFLVIEESNVWQ 1419
Cdd:PRK11000 154 VFLLDEPLSNLDAaLRVQMrieISRLHKR--LGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQ 214
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1223-1396 |
6.31e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.31 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLsaflrmlnikgDIeidgvswnsvtLQEwRKAFGVITQKVFIfsgtfrqnldp 1302
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLL-----------DV-----------LAG-RKTAGVITGEILI----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1303 NGKWKDEEIWKVADEV-------GLKSVIEqfpgQLNFTLVDGGyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPI 1375
Cdd:cd03232 69 NGRPLDKNFQRSTGYVeqqdvhsPNLTVRE----ALRFSALLRG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180
....*....|....*....|..
gi 14141185 1376 T-YQVIRRVLKQAFAGCTvILC 1396
Cdd:cd03232 143 AaYNIVRFLKKLADSGQA-ILC 163
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1203-1405 |
7.37e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1203 GGEMVVKDLTVKYMDdgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAF---LRMLNIKGDIEIDGVSWNSVTLqewr 1279
Cdd:PLN03211 66 GHKPKISDETRQIQE--RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagrIQGNNFTGTILANNRKPTKQIL---- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1280 KAFGVITQKVFIFSG-TFRQNLD-------PNGKWKDEEIW---KVADEVGLKSVIEQFPGQlnfTLVDGgyvLSHGHKQ 1348
Cdd:PLN03211 140 KRTGFVTQDDILYPHlTVRETLVfcsllrlPKSLTKQEKILvaeSVISELGLTKCENTIIGN---SFIRG---ISGGERK 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14141185 1349 LMCLARSVLSKAKIILLDEPSAHLDPIT-YQVIRRVLKQAFAGCTVILCEH----RIEAMLD 1405
Cdd:PLN03211 214 RVSIAHEMLINPSLLILDEPTSGLDATAaYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMFD 275
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1223-1374 |
7.52e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.54 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML------NIKGDIEIDGVSWNSVTLQEWRKAFGVITQ--KVFIFSG 1294
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgqTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 TFRQNLDPN----GKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLvdggyvlSHGHKQLMCLARSVLSKAKIILLDEPSA 1370
Cdd:PRK13645 107 TIEKDIAFGpvnlGENKQEAYKKVPELLKLVQLPEDYVKRSPFEL-------SGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
....
gi 14141185 1371 HLDP 1374
Cdd:PRK13645 180 GLDP 183
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1232-1405 |
8.71e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.82 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1232 PGQRVGLLGRTGSGKSTLLsaflRMLNIK-----GDIEiDGVSWNSVtLQEWRkafGVITQKVF--IFSGTFR-----QN 1299
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTAL----KILAGKlkpnlGKFD-DPPDWDEI-LDEFR---GSELQNYFtkLLEGDVKvivkpQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1300 LD--PNG-KWKDEEIWKVADEVG-LKSVIEQFpgQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDpi 1375
Cdd:cd03236 96 VDliPKAvKGKVGELLKKKDERGkLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD-- 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 14141185 1376 TYQ------VIRRVLKQAFAgctVILCEHRIeAMLD 1405
Cdd:cd03236 172 IKQrlnaarLIRELAEDDNY---VLVVEHDL-AVLD 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1223-1403 |
8.95e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-------MLNIKGDIEI----------------DGVSWNSVTLQEWR 1279
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgRIIYEQDLIVarlqqdpprnvegtvyDFVAEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1280 KAFGVITQKVFIFS--------GTFRQNLDPNGKWK-DEEIWKVADEVGLKSvieqfpgqlNFTLVDggyvLSHGHKQLM 1350
Cdd:PRK11147 99 KRYHDISHLVETDPseknlnelAKLQEQLDHHNLWQlENRINEVLAQLGLDP---------DAALSS----LSGGWLRKA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1351 CLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKqAFAGCTVILCEHR--IEAM 1403
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK-TFQGSIIFISHDRsfIRNM 219
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1219-1373 |
9.05e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1219 GNAVLENISFSISPGQRVGLLGRTGSGKSTLL----------------SAFLRMLnIKGDIEIDGVSWNSVTLQEWRKAF 1282
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILklisgelqpssgtvfrSAKVRMA-VFSQHHVDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1283 -GVITQKVFIFSGTFrqnldpngkwkdeeiwKVADEVGLKSVieqfpgqlnftlvdggYVLSHGHKQLMCLARSVLSKAK 1361
Cdd:PLN03073 600 pGVPEQKLRAHLGSF----------------GVTGNLALQPM----------------YTLSGGQKSRVAFAKITFKKPH 647
|
170
....*....|..
gi 14141185 1362 IILLDEPSAHLD 1373
Cdd:PLN03073 648 ILLLDEPSNHLD 659
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
547-657 |
1.00e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 547 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVfESCVCKLmaNKTRILVTSKMEHLRK-ADKILILHQgssy 625
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ETYLLKW--PKTFIVVSHAREFLNTvVTDILHLHG---- 416
|
90 100 110
....*....|....*....|....*....|..
gi 14141185 626 fygtfSELQSLRPDfssklmgYDTFDQFTEER 657
Cdd:PLN03073 417 -----QKLVTYKGD-------YDTFERTREEQ 436
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
437-622 |
1.13e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.56 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR--------------VSF---------Csq 493
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYipedrlgrgL-- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 494 fswIMPGTIKENIIFGvsydEYRYKSVVKACQLQQD-ITKFAEQdntVLGEGGV----------TLSGG--QRArIsLAR 560
Cdd:COG3845 348 ---VPDMSVAENLILG----RYRRPPFSRGGFLDRKaIRAFAEE---LIEEFDVrtpgpdtparSLSGGnqQKV-I-LAR 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 561 AVYKDADLYLLDSP-FGyLDVFTEEQVFEscvcKLMANKTR----ILVTSKMEHLRK-ADKILILHQG 622
Cdd:COG3845 416 ELSRDPKLLIAAQPtRG-LDVGAIEFIHQ----RLLELRDAgaavLLISEDLDEILAlSDRIAVMYEG 478
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1222-1398 |
1.15e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1222 VLENISFSISPGQRVGLLGRTGSGKSTLlsafLR-MLNIkgDIEIDGVSWnsvtLQEwrkafGVitqKVfifsGTFRQN- 1299
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTL----LRiMAGV--DKEFEGEAR----PAP-----GI---KV----GYLPQEp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1300 -LDPN-----------GKWKD-----EEIW-----------KVADEVG-------------LKSVIEQF-------PGQL 1331
Cdd:PRK11819 80 qLDPEktvrenveegvAEVKAaldrfNEIYaayaepdadfdALAAEQGelqeiidaadawdLDSQLEIAmdalrcpPWDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 1332 NFTlvdggyVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQaFAGcTVILCEH 1398
Cdd:PRK11819 160 KVT------KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD-YPG-TVVAVTH 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
441-572 |
1.19e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.50 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG-------RVSFCSQFS------WIMPGTIKENii 507
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpvtaeqPEDYRKLFSavftdfHLFDQLLGPE-- 416
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 508 fGVSYDEYRYKSVVKACQLQQditKFAEQDNTVLgegGVTLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK10522 417 -GKPANPALVEKWLERLKMAH---KLELEDGRIS---NLKLSKGQKKRLALLLALAEERDILLLD 474
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
443-487 |
1.32e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 45.30 E-value: 1.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 14141185 443 NINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR 487
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR 68
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
441-666 |
1.59e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR--------------VSFCSQ-FSWIMPGTIKEN 505
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQeLSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IIFG------------VSYDEYRYKS--VVKACQLQQDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLL 571
Cdd:PRK09700 101 LYIGrhltkkvcgvniIDWREMRVRAamMLLRVGLKVDLDEKVAN-----------LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 572 DSPFGYLDVFTEEQVFescvckLMANKTR------ILVTSKMEHLRK-ADKILILHQGSSYFYGTFSELQSlrPDFSSKL 644
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF------LIMNQLRkegtaiVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSN--DDIVRLM 241
|
250 260
....*....|....*....|....
gi 14141185 645 MGYDTFDQFT--EERRSSILTETL 666
Cdd:PRK09700 242 VGRELQNRFNamKENVSNLAHETV 265
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
437-574 |
1.61e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.16 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKtSLLMLIL-GELEASEGIIKHSGR-VSFCS-------------Q-FSwIMPG 500
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGK-STLMKILsGVYQPDSGEILLDGEpVRFRSprdaqaagiaiihQeLN-LVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 501 -TIKENIIFGvsyDEYRYKSVVKACQLQQDITKFAEQ-----D-NTVLGEggvtLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:COG1129 94 lSVAENIFLG---REPRRGGLIDWRAMRRRARELLARlgldiDpDTPVGD----LSVAQQQLVEIARALSRDARVLILDE 166
|
.
gi 14141185 574 P 574
Cdd:COG1129 167 P 167
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1201-1395 |
1.65e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.16 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1201 PSGGEMV--VKDLTVKymddgnAVLENISFSISPGQRVGLLGRTGSGKSTLLSA-FLRMLNIKGDIEIDG--VSWNSVT- 1274
Cdd:COG1129 250 AAPGEVVleVEGLSVG------GVVRDVSFSVRAGEILGIAGLVGAGRTELARAlFGADPADSGEIRLDGkpVRIRSPRd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1275 --------LQEWRKAFGVITQKvfifsgTFRQN-----LDPNGKWK-------DEEIWKVADEVGLK-SVIEQFPGQlnf 1333
Cdd:COG1129 324 airagiayVPEDRKGEGLVLDL------SIRENitlasLDRLSRGGlldrrreRALAEEYIKRLRIKtPSPEQPVGN--- 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14141185 1334 tlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPS------AHLDpItYQVIRRVLKQafaGCTVIL 1395
Cdd:COG1129 395 --------LSGGNQQKVVLAKWLATDPKVLILDEPTrgidvgAKAE-I-YRLIRELAAE---GKAVIV 449
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1215-1384 |
1.67e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1215 YMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGvswNSVTLQEWRKAFGVITQkvfifS 1293
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVeSGQIQIDG---KTATRGDRSRFMAYLGH-----L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1294 GTFRQNLDpngkwKDEEIWKVADEVGLKSviEQFPGQLnFTLVD-GGYV------LSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:PRK13543 91 PGLKADLS-----TLENLHFLCGLHGRRA--KQMPGSA-LAIVGlAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLD 162
|
170
....*....|....*...
gi 14141185 1367 EPSAHLDPITYQVIRRVL 1384
Cdd:PRK13543 163 EPYANLDLEGITLVNRMI 180
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
427-579 |
1.71e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.12 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 427 NVSFSHLclVGNP----VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG---------------- 486
Cdd:PRK13649 7 NVSYTYQ--AGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdikqir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 487 -RVSFCSQF--SWIMPGTIKENII-----FGVSYDEyryksvvkACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISL 558
Cdd:PRK13649 85 kKVGLVFQFpeSQLFEETVLKDVAfgpqnFGVSQEE--------AEALAREKLALVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180
....*....|....*....|.
gi 14141185 559 ARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLD 177
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1206-1252 |
1.88e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.92 E-value: 1.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 14141185 1206 MVVKDLTvKYMDDGNAvLENISFSISPGQRVGLLGRTGSGKSTLLSA 1252
Cdd:PRK11701 7 LSVRGLT-KLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNA 51
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
441-574 |
2.05e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.91 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLIL---------------GELEASEGiIKHSGRVSFCSQfSWI------MP 499
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEG-LEHIDKVIVIDQ-SPIgrtprsNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 GT-------IKEniIF-----GVSYD----EYRYK----------SVVKACQLQQDITKFAEQDNTV---------LGEG 544
Cdd:cd03271 89 ATytgvfdeIRE--LFcevckGKRYNretlEVRYKgksiadvldmTVEEALEFFENIPKIARKLQTLcdvglgyikLGQP 166
|
170 180 190
....*....|....*....|....*....|...
gi 14141185 545 GVTLSGGQRARISLARAVYKDAD---LYLLDSP 574
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKRSTgktLYILDEP 199
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
433-622 |
2.16e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.09 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 433 LCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMlILGELEASEGIIKHSG--------------------RVSFCS 492
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLR-TLNRMNDKVSGYRYSGdvllggrsifnyrdvlefrrRVGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 493 QFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQlQQDITKFAEQD--NTVLGEGGVTLSGGQRARISLARAVYKDADLYL 570
Cdd:PRK14271 108 QRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVA-QARLTEVGLWDavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14141185 571 LDSPFGYLDVFTEEQVfESCVCKLMANKTRILVTSKM-EHLRKADKILILHQG 622
Cdd:PRK14271 187 LDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDG 238
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
547-581 |
2.37e-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: 45.55 E-value: 2.37e-04
10 20 30
....*....|....*....|....*....|....*
gi 14141185 547 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 581
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
441-700 |
2.39e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCS---------------QFSWIMPGTIKEN 505
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAissglngqltgieniELKGLMMGLTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 506 IifgvsydeyryKSVVKACQLQQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLD-VFTEE 584
Cdd:PRK13545 120 I-----------KEIIPEIIEFADIGKFIYQPVK-------TYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 585 qvfesCVCKL----MANKTRILVTSKMEHLRK-ADKILILHQGSSYFYGTFSELQSLRPDFsskLMGYdtfDQFTEERRS 659
Cdd:PRK13545 182 -----CLDKMnefkEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEF---LKKY---NQMSVEERK 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 14141185 660 SILTETLRRFS----VDDSSAPWSKPKQSFRQTGEvgEKRKNSIL 700
Cdd:PRK13545 251 DFREEQISQFQhgllQEDQTGRERKRKKGKKTSRK--FKKKRVLI 293
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
429-633 |
2.51e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 429 SFShlclvGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR--------------VSFCSQF 494
Cdd:PRK15439 20 QYS-----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 495 SWIMPG-TIKENIIFGVSYDEYRYKSVVK-----ACQLQQDITkfaeqdntvlgegGVTLSGGQRARISLARAVYKDADL 568
Cdd:PRK15439 95 PLLFPNlSVKENILFGLPKRQASMQKMKQllaalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 569 YLLDSPFGYLDVFTEEQVFeSCVCKLMANKTRILVTS-KMEHLRK-ADKILILHQGSSYFYGTFSEL 633
Cdd:PRK15439 162 LILDEPTASLTPAETERLF-SRIRELLAQGVGIVFIShKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
441-633 |
2.70e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.69 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFC----------------SQFSWIMP----- 499
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKrrkefarrigvvfgqrSQLWWDLPaidsf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 500 GTIKEniIFGVSYDEYRyksvvkacqlqQDITKFAEqdntVLGEGGV------TLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:COG4586 118 RLLKA--IYRIPDAEYK-----------KRLDELVE----LLDLGELldtpvrQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 574 P-FGyLDVFTEEQV--FESCVCKlmANKTRILVTSK-M---EHLrkADKILILHQGSSYFYGTFSEL 633
Cdd:COG4586 181 PtIG-LDVVSKEAIreFLKEYNR--ERGTTILLTSHdMddiEAL--CDRVIVIDHGRIIYDGSLEEL 242
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
437-633 |
3.38e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 44.45 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 437 GNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASegiikhSGRVSFCSQ-FSWIMPGTIK------------ 503
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS------SGRILFDGKpIDYSRKGLMKlresvgmvfqdp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFGVS-YDEYRYKSVvkACQLQQDitKFAEQDNTVLGEGGVT---------LSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK13636 92 DNQLFSASvYQDVSFGAV--NLKLPED--EVRKRVDNALKRTGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14141185 574 PFGYLDVFTEEQVFEscVCKLMANK---TRILVTSKMEHLR-KADKILILHQGSSYFYGTFSEL 633
Cdd:PRK13636 168 PTAGLDPMGVSEIMK--LLVEMQKElglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1208-1437 |
3.80e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1208 VKDLTVKymDDGNAvlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GDIEIDGVSWN-SVTLQEWRKAFGVI 1285
Cdd:PRK09700 268 VRNVTSR--DRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAgGEIRLNGKDISpRSPLDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1286 TQKV----FIFSGTFRQNLD-----PNGKWKDeeIWKVADEVGLKSVIEQFPGQLNF---TLVDGGYVLSHGHKQLMCLA 1353
Cdd:PRK09700 344 TESRrdngFFPNFSIAQNMAisrslKDGGYKG--AMGLFHEVDEQRTAENQRELLALkchSVNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1354 RSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQ-AFAGCTVILCEHRI-EAMLDCQRFLVIEESNVWQYDSLQALLSEKS 1431
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRDDMSEEE 501
|
....*.
gi 14141185 1432 IFQQAI 1437
Cdd:PRK09700 502 IMAWAL 507
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
910-1135 |
3.83e-04 |
|
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: 44.39 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 910 IFYIYVGVA---DTLLALSLFRglplvhtlITASKILHR---KMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLP 983
Cdd:cd18577 51 LYFVYLGIGsfvLSYIQTACWT--------ITGERQARRirkRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 984 LTIFDFIQLVFIVIGAIIV---VS---ALqpyIFLATVPGLVVFILLRAYFLHTAQQlKQLESEGR-SPIFTHLVTSLKg 1056
Cdd:cd18577 123 EKLGLLIQSLSTFIAGFIIafiYSwklTL---VLLATLPLIAIVGGIMGKLLSKYTK-KEQEAYAKaGSIAEEALSSIR- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1057 lwTLRAFRRQTYFETLFHKALNlHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFI--SILTTgEGEGTAGIILTLAMNI 1134
Cdd:cd18577 198 --TVKAFGGEEKEIKRYSKALE-KARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWygSRLVR-DGEISPGDVLTVFFAV 273
|
.
gi 14141185 1135 M 1135
Cdd:cd18577 274 L 274
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1196-1412 |
4.42e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1196 KSDIWPSGGEMVVKDLTVKYMDDGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKG-DIEIDG----- 1267
Cdd:PRK10261 3 HSDELDARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGgLVQCDKmllrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1268 -----VSWNSVTLQEWRKAFGVITQKVFIFSGTfrqNLDP---------------NGKWKDE---EIWKVADEVGL---K 1321
Cdd:PRK10261 83 rsrqvIELSEQSAAQMRHVRGADMAMIFQEPMT---SLNPvftvgeqiaesirlhQGASREEamvEAKRMLDQVRIpeaQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1322 SVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHLD-PITYQVIR--RVLKQAFAgCTVILCEH 1398
Cdd:PRK10261 160 TILSRYPHQ-----------LSGGMRQRVMIAMALSCRPAVLIADEPTTALDvTIQAQILQliKVLQKEMS-MGVIFITH 227
|
250
....*....|....*
gi 14141185 1399 RIEAMLD-CQRFLVI 1412
Cdd:PRK10261 228 DMGVVAEiADRVLVM 242
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
441-640 |
4.49e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSqfswIMPG-----TIKENIIFGVSYDEY 515
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIA----ISAGlsgqlTGIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 516 RYKSVVKacqLQQDITKFAEqdntvLGE----GGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfteeQVF-ESC 590
Cdd:PRK13546 116 KRKEIKA---MTPKIIEFSE-----LGEfiyqPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD-----QTFaQKC 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 591 VCKLM----ANKTRILVTSKMEHLRK-ADKILILHQGssyFYGTFSELQSLRPDF 640
Cdd:PRK13546 183 LDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGG---KLKDYGELDDVLPKY 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1223-1401 |
4.83e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGDIEIDGVswnSVTLQEWRKAFG----VITQKVfifs 1293
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTL----LKILSgnyqpDAGSILIDGQ---EMRFASTTAALAagvaIIYQEL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1294 gtfrqNLDPNgkwkdeeiWKVADEVGLKsvieQFPGQlnFTLVDGGYV-----------------------LSHGHKQLM 1350
Cdd:PRK11288 89 -----HLVPE--------MTVAENLYLG----QLPHK--GGIVNRRLLnyeareqlehlgvdidpdtplkyLSIGQRQMV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1351 CLARSVLSKAKIILLDEPSAHLDP----ITYQVIRRVLKQafaGCTVILCEHRIE 1401
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAreieQLFRVIRELRAE---GRVILYVSHRME 201
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
441-623 |
5.48e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.31 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILgeleASEGIIKHSGRVSFCSQFSWIMPGTIKENIIFGVSYdeyryksv 520
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 521 vkacqlqqdITkfaeqdntvLGEGGVTLSGGQRARISLARAVYKDAD--LYLLDSPFGYLDVFTEEQVFESCVCKLMANK 598
Cdd:cd03238 79 ---------LT---------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN 140
|
170 180
....*....|....*....|....*
gi 14141185 599 TRILVTSKMEHLRKADKILILHQGS 623
Cdd:cd03238 141 TVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
439-490 |
5.93e-04 |
|
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: 44.29 E-value: 5.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 14141185 439 PVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELeaSEGIIKHSGRVSF 490
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL--PDPAAHPSGSILF 73
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
81-302 |
6.39e-04 |
|
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: 43.31 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 81 FLFYGILLYLGEVTKAVQPVLLGRIIASYDPENKVerSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLI 160
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDL--SLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLqvtllmgllwdllqFSAFCGLGLL---------- 230
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDV--------------LTLIGALVILfylnwkltlv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 231 ------IILVIFQAILGKMMVKYRDQR--AAKINERLVitsEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYM 302
Cdd:cd07346 145 allllpLYVLILRYFRRRIRKASREVResLAELSAFLQ---ESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARL 221
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
858-1117 |
6.79e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 43.25 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 858 LIWCVLVFLVEVAASLFVLWLLKNNpVNSGnngtkISNSSYVVIITSTSfyyifyIYVGVAdtlLALSLFRGLPLVHTLI 937
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYG-IDSG-----VRAGDLGVLLLAAA------AYLAVV---LAGWVAQRAQTRLTGR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 938 TASKILHRKMLHSILHA---PMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLAT 1014
Cdd:cd18546 66 TGERLLYDLRLRVFAHLqrlSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1015 VPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLF------HKALNLHTANwfmyl 1088
Cdd:cd18546 146 LAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFaelsddYRDARLRAQR----- 220
|
250 260
....*....|....*....|....*....
gi 14141185 1089 atlrwfqmridmIFVLFFIVVTFISILTT 1117
Cdd:cd18546 221 ------------LVAIYFPGVELLGNLAT 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
441-574 |
8.48e-04 |
|
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: 43.66 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKtSLLMLIL----------GELEASEGIIKHSG-------RVSFCSQFSWIMPG-TI 502
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGK-STLMKILsgvyphgtwdGEIYWSGSPLKASNirdteraGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14141185 503 KENIIFG--VSYDEYR--YKSVVKACQ-LQQDITKFAEQDNTVLGEGGvtlsGGQRARISLARAVYKDADLYLLDSP 574
Cdd:TIGR02633 96 AENIFLGneITLPGGRmaYNAMYLRAKnLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1232-1298 |
8.74e-04 |
|
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: 41.20 E-value: 8.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14141185 1232 PGQRVGLLGRTGSGKSTLLSAFLRMLNIKGD--IEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQ 1298
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgvIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL 69
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1224-1375 |
9.98e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.76 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1224 ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-----NIKGDIEIDGVSWNSVTL---------QEWRKAFgvitQKV 1289
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPVAPCALrgrkiatimQNPRSAF----NPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1290 FIFSGTFRQNLDPNGKWKDEE-IWKVADEVGL---KSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:PRK10418 96 HTMHTHARETCLALGKPADDAtLTAALEAVGLenaARVLKLYPFEM-----------SGGMLQRMMIALALLCEAPFIIA 164
|
170
....*....|
gi 14141185 1366 DEPSAHLDPI 1375
Cdd:PRK10418 165 DEPTTDLDVV 174
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
547-581 |
1.02e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....*
gi 14141185 547 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 581
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
441-586 |
1.04e-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: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLILgeleaseGIIKHSGRVSFCSQfswimpgtikenIIFGVSYDEYR-YKS 519
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALL-------RLIPSEGEIRFDGQ------------DLDGLSRRALRpLRR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 520 vvkacQLQ---QD-------------------------ITKfAEQDNTV---LGEGGVT----------LSGGQRARISL 558
Cdd:COG4172 363 -----RMQvvfQDpfgslsprmtvgqiiaeglrvhgpgLSA-AERRARVaeaLEEVGLDpaarhrypheFSGGQRQRIAI 436
|
170 180
....*....|....*....|....*...
gi 14141185 559 ARAVYKDADLYLLDSPFGYLDVFTEEQV 586
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQI 464
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
440-471 |
1.07e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.14 E-value: 1.07e-03
10 20 30
....*....|....*....|....*....|..
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLI 471
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI 51
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
441-467 |
1.66e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 1.66e-03
10 20
....*....|....*....|....*..
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSL 467
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
441-467 |
1.74e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 1.74e-03
10 20
....*....|....*....|....*..
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSL 467
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL 37
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1208-1267 |
1.90e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.57 E-value: 1.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14141185 1208 VKDLTVKYMD-DGNAVLENISFSISPGQRVGLLGRTGSGKSTL--LSAFLRMLNiKGDIEIDG 1267
Cdd:PRK13545 24 LKDLFFRSKDgEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLsnLIAGVTMPN-KGTVDIKG 85
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
945-1024 |
2.24e-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: 41.70 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 945 RKMLHSILHA-PMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQP---YIFLATVPGLVV 1020
Cdd:cd18576 72 RKDLYRHLQRlPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLLMLATVPVVVL 151
|
....
gi 14141185 1021 FILL 1024
Cdd:cd18576 152 VAVL 155
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
549-586 |
2.60e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.87 E-value: 2.60e-03
10 20 30
....*....|....*....|....*....|....*...
gi 14141185 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQV 586
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQV 193
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1223-1251 |
3.16e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 3.16e-03
10 20
....*....|....*....|....*....
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLS 1251
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLS 45
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1207-1412 |
3.55e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.55 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1207 VVKDLTVKyMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGDIEIDGVSWNSVTLQEWRKA---- 1281
Cdd:COG3845 259 EVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPaSGSIRLDGEDITGLSPRERRRLgvay 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1282 -------FGVITQkvfiFS-------GTFRQNLDPNGKWKDeeiWKVADEVGlKSVIEQF---PGQLNfTLVDGgyvLSH 1344
Cdd:COG3845 338 ipedrlgRGLVPD----MSvaenlilGRYRRPPFSRGGFLD---RKAIRAFA-EELIEEFdvrTPGPD-TPARS---LSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14141185 1345 GHKQLMCLARSVLSKAKIILLDEPSAHLDpI--TYQVIRRVLKQAFAGCTVILcehrIEAMLD-----CQRFLVI 1412
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLD-VgaIEFIHQRLLELRDAGAAVLL----ISEDLDeilalSDRIAVM 475
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
901-1078 |
3.84e-03 |
|
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: 40.89 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 901 IITSTSFYYIFYIYVGVADTLLA---LSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSkDIAI 977
Cdd:cd18570 32 IIPSGDINLLNIISIGLILLYLFqslLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 978 LDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGL 1057
Cdd:cd18570 111 IREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGI 190
|
170 180
....*....|....*....|....*
gi 14141185 1058 WTLRAFRRQTYF----ETLFHKALN 1078
Cdd:cd18570 191 ETIKSLNAEEQFlkkiEKKFSKLLK 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1223-1417 |
4.57e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 39.94 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFlrMLNIKGDIEIDG-VSWNSVTLQEwrkaFGVITQKVFIFSG------- 1294
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL--ANRTEGNVSVEGdIHYNGIPYKE----FAEKYPGEIIYVSeedvhfp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1295 --TFRQNLDPNGKWKDEEIwkvadevglksvieqfpgqlnftlVDGgyvLSHGHKQLMCLARSVLSKAKIILLDEPSAHL 1372
Cdd:cd03233 97 tlTVRETLDFALRCKGNEF------------------------VRG---ISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14141185 1373 DPIT----YQVIRRVLKQAFAGCTVIL--CEHRIEAMLDcqRFLVIEESNV 1417
Cdd:cd03233 150 DSSTaleiLKCIRTMADVLKTTTFVSLyqASDEIYDLFD--KVLVLYEGRQ 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
442-623 |
5.83e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.92 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 442 KNINLNIEKGEMLAITGSTGSGKTSLLMLILG-ELEASEGIIKHSGRVSFCSQFSWIMPG-----------------TIK 503
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGvDKRAGGEIRLNGKDISPRSPLDAVKKGmayitesrrdngffpnfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 504 ENIIFGVSYDEYRYKSVVKACQlQQDITKFAEQDNTVLG------EGGVT-LSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMGLFH-EVDEQRTAENQRELLAlkchsvNQNITeLSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14141185 577 YLDVFTEEQVFescvcKLM-----ANKTRILVTSKM-EHLRKADKILILHQGS 623
Cdd:PRK09700 439 GIDVGAKAEIY-----KVMrqladDGKVILMVSSELpEIITVCDRIAVFCEGR 486
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
904-1078 |
6.56e-03 |
|
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: 40.24 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 904 STSFYYIFYIYVGVAdtllALSLFRGLPLVhtlITASKI---LHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDD 980
Cdd:cd18557 36 NELALILLAIYLLQS----VFTFVRYYLFN---IAGERIvarLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 981 FLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTL 1060
Cdd:cd18557 109 AVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTV 188
|
170
....*....|....*...
gi 14141185 1061 RAFRRQTYFETLFHKALN 1078
Cdd:cd18557 189 RSFSAEEKEIRRYSEALD 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
441-471 |
6.60e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.55 E-value: 6.60e-03
10 20 30
....*....|....*....|....*....|.
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLI 471
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI 51
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
959-1138 |
6.66e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 40.16 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 959 ISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILLRAYFLH-----TAQ 1033
Cdd:cd18585 86 LQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYrlgkkIGQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 1034 QLKQLESEGRspifTHLVTSLKGLWTLRAFRR-QTYFETLFHKALNLHTANWFMylATLRWFQMRIdMIFVLFFIVVTFI 1112
Cdd:cd18585 166 QLVQLRAELR----TELVDGLQGMAELLIFGAlERQRQQLEQLSDALIKEQRRL--ARLSGLSQAL-MILLSGLTVWLVL 238
|
170 180
....*....|....*....|....*..
gi 14141185 1113 SILTTGEGEGT-AGIIltLAMNIMSTL 1138
Cdd:cd18585 239 WLGAPLVQNGAlDGAL--LAMLVFAVL 263
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
548-580 |
6.98e-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: 40.04 E-value: 6.98e-03
10 20 30
....*....|....*....|....*....|...
gi 14141185 548 LSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
441-467 |
7.89e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 7.89e-03
10 20
....*....|....*....|....*..
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSL 467
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
440-574 |
7.99e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 440 VLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGEleaSEG------IIKHSGRVSFCS-----------------QFSW 496
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SYGrnisgtVFKDGKEVDVSTvsdaidaglayvtedrkGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 497 IMPGTIKENI----IFGVSY-------------DEYRYKSVVKACQLQQDItkfaeqdntvlgeggVTLSGGQRARISLA 559
Cdd:NF040905 352 NLIDDIKRNItlanLGKVSRrgvideneeikvaEEYRKKMNIKTPSVFQKV---------------GNLSGGNQQKVVLS 416
|
170
....*....|....*
gi 14141185 560 RAVYKDADLYLLDSP 574
Cdd:NF040905 417 KWLFTDPDVLILDEP 431
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
448-624 |
8.20e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.56 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 448 IEKGEMLAITGSTGSGKTSLLMLI----LGELEA-----SEGIIKHSG----RVSFCSQFSWIMPGTIKEniiFGVSYDE 514
Cdd:cd03279 25 LDNNGLFLICGPTGAGKSTILDAItyalYGKTPRygrqeNLRSVFAPGedtaEVSFTFQLGGKKYRVERS---RGLDYDQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14141185 515 YRyKSVVKAcqlQQDITKFAEQDNTvlgeggvTLSGGQRARISLARAVY----------KDADLYLLDSPFGYLDVFTEE 584
Cdd:cd03279 102 FT-RIVLLP---QGEFDRFLARPVS-------TLSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEALE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14141185 585 QVFEscVCKLMANKTR-ILVTSKMEHL--RKADKILI--LHQGSS 624
Cdd:cd03279 171 AVAT--ALELIRTENRmVGVISHVEELkeRIPQRLEVikTPGGSR 213
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
441-472 |
9.92e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 9.92e-03
10 20 30
....*....|....*....|....*....|..
gi 14141185 441 LKNINLNIEKGEMLAITGSTGSGKTSLLMLIL 472
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTL 655
|
|
| |
