|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
43-971 |
8.54e-139 |
|
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: 454.40 E-value: 8.54e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 43 PNPVDDAGLLSFATFSWLTPVMIRSYKHTLTVDTLPPLSPYDSSDVNAKRLQILWDEEIERVGPERASLGRVVWKFQRTR 122
Cdd:TIGR00957 201 PCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKQPVSAVYGKKDPSKPK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 123 VLMDVVAN------------------ILCIIMAALGPTVLIH---------------QILQHVTNISSGHIGIS---ICL 166
Cdd:TIGR00957 281 GSSQLDANeevealivksphkprkpsLFKVLYKTFGPYFLMSfcfkaihdlmmfigpQILSLLIRFVNDPMAPDwqgYFY 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 167 CLALFATEFTKVLFWALAWAINYRTAIRLKVALSTLIFKNLLSFKTLTHISA--GEVLNVLSSDSYSLFEAALFCPLPAT 244
Cdd:TIGR00957 361 TGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSStvGEIVNLMSVDAQRFMDLATYINMIWS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 245 IPiLMVVCAVYAFFI-LGSTALVGICVYLIFIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFM 323
Cdd:TIGR00957 441 AP-LQVILALYFLWLnLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 324 NTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTCHIFL--KRTLTAPVAFSVIAMFNVMKFSIAILPFSVKA 401
Cdd:TIGR00957 520 DKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVdeNNILDAEKAFVSLALFNILRFPLNILPMVISS 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 402 VAEASVSLRRMKKILvaksppsyiTQPE-DPDTI------------LLLANATLTWEQeinrkrgplktqdqrrhvfkkq 468
Cdd:TIGR00957 600 IVQASVSLKRLRIFL---------SHEElEPDSIerrtikpgegnsITVHNATFTWAR---------------------- 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 469 raelyseqslsdqgvasperqsGSPKSvLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAYVS 548
Cdd:TIGR00957 649 ----------------------DLPPT-LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVP 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 549 QQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYAN 628
Cdd:TIGR00957 706 QQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTE-------IGEKGVNLSGGQKQRVSLARAVYSN 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 629 RQLYLLDDPLSAVDAHVGKHVFEECI--KKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 706
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 707 IHN----------------LRGLQFKDPEHIYNVAMVETLKESQAQRDEDAvlASGDERDEGKEPETEEFVDI---KAPV 767
Cdd:TIGR00957 859 LRTyapdeqqghledswtaLVSGEGKEAKLIENGMLVTDVVGKQLQRQLSA--SSSDSGDQSRHHGSSAELQKaeaKEET 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 768 HQLIQIESPQEGIVTWKTYHTYIKASgGYLVSFLVLCLFFLMMGSSAFSTWWLGLWLDSgsqvicaPQSNETACNVNQTL 847
Cdd:TIGR00957 937 WKLMEADKAQTGQVELSVYWDYMKAI-GLFITFLSIFLFVCNHVSALASNYWLSLWTDD-------PMVNGTQNNTSLRL 1008
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 848 QdtkhhmyqlVYIAsmmsvltFGIIKGFTFTNTTL-------MASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDM 920
Cdd:TIGR00957 1009 S---------VYGA-------LGILQGFAVFGYSMavsiggiQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKEL 1072
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 921 DELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVLVVLAGLAILFFILLR 971
Cdd:TIGR00957 1073 DTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQR 1123
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
45-967 |
2.23e-132 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 438.40 E-value: 2.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 45 PVDDAGLLSFATFSWLTPVMIRSYKHTLTVDTLPPLSPYDSSDVNAKRLQILWDEEIERVGPE--RA---SLGRVVWKFQ 119
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKPWllRAlnnSLGGRFWLGG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 120 RTRVLMDVVANIlciimaalGPtVLIHQILQHVTNISSGHIGisiclcLALFATEFTKVLFWALAWAINY----RTAIRL 195
Cdd:PLN03130 308 FFKIGNDLSQFV--------GP-LLLNLLLESMQNGEPAWIG------YIYAFSIFVGVVLGVLCEAQYFqnvmRVGFRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 196 KVALSTLIFKNLLSfktLTHIS-----AGEVLNVLSSDSYSLFEaalFCPLPATI---PILMVVCAVYAFFILGSTALVG 267
Cdd:PLN03130 373 RSTLVAAVFRKSLR---LTHEGrkkftSGKITNLMTTDAEALQQ---ICQQLHTLwsaPFRIIIAMVLLYQQLGVASLIG 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 268 ICVYLIFIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGN 347
Cdd:PLN03130 447 SLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFN 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 348 SALAPIVSTIAIVSTFTCHIFLKRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRMKKILVAK------SP 421
Cdd:PLN03130 527 SFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEervllpNP 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 422 PsyiTQPEDPdtILLLANATLTWEqeinrkrgplktqdqrrhvfkkqraelyseqslsdqgvasperqSGSPKSVLHNIS 501
Cdd:PLN03130 607 P---LEPGLP--AISIKNGYFSWD--------------------------------------------SKAERPTLSNIN 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 502 FVVRKGKVLGICGNVGSGKSSLISALLGQM-QLQKGVVAVSGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVC 580
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVT 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 581 GLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKG 660
Cdd:PLN03130 718 ALQHDLDLLPGGDLTE-------IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRG 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 661 KTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNLRGLQfkdpehiynvAMVETLKESQAQRDED 740
Cdd:PLN03130 791 KTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKME----------EYVEENGEEEDDQTSS 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 741 AVLASGdeRDEGKEPETEEFVDIKAPVHQLIQIESPQEGIVTWKTYHTYIKASGGYLVsflVLCLFFLMMGSSAF---ST 817
Cdd:PLN03130 861 KPVANG--NANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGGAWV---VMILFLCYVLTEVFrvsSS 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 818 WWLGLWLDSGsqvicapqsnetacnvnqTLQDTKHHMYQLVYiasmmSVLTFG-----IIKGFTFTNTTLMASSSLHNRV 892
Cdd:PLN03130 936 TWLSEWTDQG------------------TPKTHGPLFYNLIY-----ALLSFGqvlvtLLNSYWLIMSSLYAAKRLHDAM 992
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 893 FNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVLVVLAGLAILFF 967
Cdd:PLN03130 993 LGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFY 1067
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
125-412 |
2.68e-129 |
|
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: 393.85 E-value: 2.68e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 125 MDVVANILCIIMAALGPTVLIHQILQHVTNiSSGHIGISICLCLALFATEFTKVLFWALAWAINYRTAIRLKVALSTLIF 204
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILIRKLLEYLED-SDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 205 KNLLSFKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGICVYLIFIPIQMFMAKL 284
Cdd:cd18592 80 KKILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 285 NSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFT 364
Cdd:cd18592 160 TGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1958746143 365 CHIFLKRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18592 240 AHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
45-967 |
3.72e-129 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 427.86 E-value: 3.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 45 PVDDAGLLSFATFSWLTPVMIRSYKHTLTVDTLPPLSPYDSSDVNAKRLQILWDEEIERVGP--ERA---SLGRVVWKFQ 119
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPKPwlLRAlnnSLGGRFWLGG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 120 RTRVLMDVVANIlciimaalGPTVLIHqILQHVTNISSGHIGISICLCLalfateFTKVLFWALAWAINY----RTAIRL 195
Cdd:PLN03232 308 IFKIGHDLSQFV--------GPVILSH-LLQSMQEGDPAWVGYVYAFLI------FFGVTFGVLCESQYFqnvgRVGFRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 196 KVALSTLIF-KNL-LSFKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGICVYLI 273
Cdd:PLN03232 373 RSTLVAAIFhKSLrLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 274 FIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGNSALAPI 353
Cdd:PLN03232 453 LIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNS 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 354 VSTIAIVSTFTCHIFLKRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRMKKILV------AKSPPsyiTQ 427
Cdd:PLN03232 533 IPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLseerilAQNPP---LQ 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 428 PEDPdtILLLANATLTWEqeinrkrgpLKTQdqrrhvfkkqraelyseqslsdqgvasperqsgspKSVLHNISFVVRKG 507
Cdd:PLN03232 610 PGAP--AISIKNGYFSWD---------SKTS-----------------------------------KPTLSDINLEIPVG 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 508 KVLGICGNVGSGKSSLISALLGQM-QLQKGVVAVSGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDL 586
Cdd:PLN03232 644 SLVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 587 NSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLV 666
Cdd:PLN03232 724 DLLPGRDLTE-------IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLV 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 667 THQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNLRglqfkdpehiynvAMVETLKESQAQRDED----AV 742
Cdd:PLN03232 797 TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAG-------------KMDATQEVNTNDENILklgpTV 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 743 LASGDERDEGKEPETEEFVDIkapvhqLIQIESPQEGIVTWKTYHTYIKASGG-YLVSFLVLCLFFLMMGSSAFSTWwLG 821
Cdd:PLN03232 864 TIDVSERNLGSTKQGKRGRSV------LVKQEERETGIISWNVLMRYNKAVGGlWVVMILLVCYLTTEVLRVSSSTW-LS 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 822 LWLDsgsqvicapQSnetacnvnqTLQDTKHHMYQLVYiasmmSVLTFGIIkGFTFTNT------TLMASSSLHNRVFNK 895
Cdd:PLN03232 937 IWTD---------QS---------TPKSYSPGFYIVVY-----ALLGFGQV-AVTFTNSfwlissSLHAAKRLHDAMLNS 992
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 896 IVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVLVVLAGLAILFF 967
Cdd:PLN03232 993 ILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFY 1064
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
106-970 |
4.82e-124 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 414.56 E-value: 4.82e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 106 PERASLGRVVWKFQRTRVLMDVVANILCIIMAALGPTVLihQILQHVTNISSGHIGISICLCLALFATEFTKVLFWALAW 185
Cdd:PTZ00243 229 PKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLL--KYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFY 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 186 AINYRTAIRLKVALSTLIFKNLL--SFKTLTH--ISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILG 261
Cdd:PTZ00243 307 YISIRCGLQYRSALNALIFEKCFtiSSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 262 STALVGICVYLIFIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKag 341
Cdd:PTZ00243 387 WCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRD-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 342 yVQSGNSAL------APIVsTIAIVstFTCHIFLKRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRMKKI 415
Cdd:PTZ00243 465 -VQLARVATsfvnnaTPTL-MIAVV--FTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTF 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 416 L---------VAKSPPSYITQPEDPDTILLLA---NATLT--------------------------WEQEINRKRGPLKT 457
Cdd:PTZ00243 541 LecdnatcstVQDMEEYWREQREHSTACQLAAvleNVDVTafvpvklprapkvktsllsralrmlcCEQCRPTKRHPSPS 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 458 -----------QDQRRHVFKKQRAELYSEQSLSDQGVASPERQSGS-----PKSVLHNISFVVRKGKVLGICGNVGSGKS 521
Cdd:PTZ00243 621 vvvedtdygspSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDffelePKVLLRDVSVSVPRGKLTVVLGATGSGKS 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 522 SLISALLGQMQLQKGVVAVSGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyph 601
Cdd:PTZ00243 701 TLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETE----- 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 602 lqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVIL 681
Cdd:PTZ00243 776 --IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVA 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 682 LEDGEICEKGTHKELMEergryAKLIHNLRGLQFKDPEhiynvamvetLKESQAQRDEDAV-----LASGDERDEGKEPE 756
Cdd:PTZ00243 854 LGDGRVEFSGSSADFMR-----TSLYATLAAELKENKD----------SKEGDADAEVAEVdaapgGAVDHEPPVAKQEG 918
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 757 TEEFVDIKA---PVHQLIQIESPQEGIVTWKTYHTYIKASGGYLVSFLVLCLFFLMMGSSAFSTWWLGLWldsgsqvica 833
Cdd:PTZ00243 919 NAEGGDGAAldaAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMW---------- 988
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 834 pQSNETACNvnqtlQDTKHHMYQLVYIASmmsvlTFGIIKGFTFTNTTL-MASSSLHNRVFNKIVSSPMSFFDTTPTGRL 912
Cdd:PTZ00243 989 -STRSFKLS-----AATYLYVYLGIVLLG-----TFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRI 1057
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 913 MNRFSKDMDELDVRLPFHAENFLQ-QFSMVVFILViMAASFPVVLVVLAGLAILFFILL 970
Cdd:PTZ00243 1058 LNRFSRDIDILDNTLPMSYLYLLQcLFSICSSILV-TSASQPFVLVALVPCGYLYYRLM 1115
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
487-686 |
4.93e-104 |
|
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: 324.04 E-value: 4.93e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 487 ERQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAYVSQQAWIFHGNVRENILFGE 566
Cdd:cd03250 11 DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 567 KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 646
Cdd:cd03250 91 PFDEERYEKVIKACALEPDLEILPDGDLTE-------IGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958746143 647 KHVFEECIKKTLK-GKTVVLVTHQLQFLESCDEVILLEDGE 686
Cdd:cd03250 164 RHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-997 |
2.09e-81 |
|
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: 291.04 E-value: 2.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 44 NPVDDAGLLSFATFSWLTPVMIRSYKHTLTVDTLPPLSPYDSSDVNAKRLQILWDEEI--ERVGPE--RASLGRVVWKFQ 119
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELasAKKNPKllNALRRCFFWRFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 120 RTRVLM-------DVVANILCIIMAALGPtvlihqilQHVTNISSG-HIGISICLclaLFATEFtkvLFWALAWAINYRT 191
Cdd:TIGR01271 84 FYGILLyfgeatkAVQPLLLGRIIASYDP--------FNAPEREIAyYLALGLCL---LFIVRT---LLLHPAIFGLHHL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 192 AIRLKVALSTLIFKNLL--SFKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGIC 269
Cdd:TIGR01271 150 GMQMRIALFSLIYKKTLklSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 270 VYLIFIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGNSA 349
Cdd:TIGR01271 230 FLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 350 LAPIVSTIAIVSTFTCHIFLKRTLTAPVaFSVIAMFNVMKFSIA-ILPFSVKAVAEASVSLRRMKKILVA---KSPPSYI 425
Cdd:TIGR01271 310 AFFFSGFFVVFLSVVPYALIKGIILRRI-FTTISYCIVLRMTVTrQFPGAIQTWYDSLGAITKIQDFLCKeeyKTLEYNL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 426 TQPEdpdtiLLLANATLTWEQEINRKRGPLKTQDQRRHVFKKQRAELYSEQSLSdqgvasperqsGSPksVLHNISFVVR 505
Cdd:TIGR01271 389 TTTE-----VEMVNVTASWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNFSLY-----------VTP--VLKNISFKLE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 506 KGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKD 585
Cdd:TIGR01271 451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEED 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 586 LNSLPYGDLTechyphlQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVL 665
Cdd:TIGR01271 531 IALFPEKDKT-------VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRIL 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 666 VTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNL----------------------------------- 710
Cdd:TIGR01271 604 VTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLeafdnfsaerrnsiltetlrrvsidgdstvfsgpe 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 711 -RGLQFKDPEHIYN-----------------VAMVE-TLKESQAQRDEDAVLASGD-------ERDEGKE--PETEEF-- 760
Cdd:TIGR01271 684 tIKQSFKQPPPEFAekrkqsiilnpiasarkFSFVQmGPQKAQATTIEDAVREPSErkfslvpEDEQGEEslPRGNQYhh 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 761 ------------------------------------------------VDIKA-PVHQLIQIESPQE------------- 778
Cdd:TIGR01271 764 glqhqaqrrqsvlqlmthsnrgenrreqlqtsfrkkssitqqnelaseLDIYSrRLSKDSVYEISEEineedlkecfade 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 779 -----GIVTWKTYHTYIKASGGyLVSFLVLCLFFLMMGSSAFstwWLGLWLDSGSQVICAPQSNETACNVNQTLQ----- 848
Cdd:TIGR01271 844 renvfETTTWNTYLRYITTNRN-LVFVLIFCLVIFLAEVAAS---LLGLWLITDNPSAPNYVDQQHANASSPDVQkpvii 919
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 849 -DTKHHMYQLVYIASMMSVLTFGIIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRL 927
Cdd:TIGR01271 920 tPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDML 999
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 928 PFHAENFLQQFSMVVFILVIMAASFPVVLVVLAGLAILfFILLRCGWTTCAEALRE-----SSPGL-HLVTLLDPL 997
Cdd:TIGR01271 1000 PLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVI-FIMLRAYFLRTSQQLKQleseaRSPIFsHLITSLKGL 1074
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
132-412 |
6.22e-72 |
|
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: 240.47 E-value: 6.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 132 LCIIMAALGPTVLIHQILQHVTNISSGHIGISICLCLALFATEFTKVLFWALAWAINYRTAIRLKVALSTLIF-KNL-LS 209
Cdd:cd18579 7 LLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYrKALrLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 210 FKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGICVYLIFIPIQMFMAKLNSAFR 289
Cdd:cd18579 87 SSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLISKLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 290 RSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTCHIFL 369
Cdd:cd18579 167 KKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFATYVLL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958746143 370 KRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18579 247 GNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
107-717 |
1.11e-71 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 249.31 E-value: 1.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 107 ERASLGRVVWKF---QRTRVLMDVVANILCIIMAALGPTVLIHQILQHVTNISSGHIGISICLCLALFateFTKVLFWAL 183
Cdd:COG1132 4 SPRKLLRRLLRYlrpYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLA---LLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 184 AWAINYRTAIRLKVALSTLIFKNL--LSFKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPA-TIPILMVVCAVYAFFI- 259
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLlrLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLvRSVVTLIGALVVLFVId 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 260 --LGSTALVGICVYLIFIPIqmFMAKLNSAFRRSAISVtDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLL 337
Cdd:COG1132 161 wrLALIVLLVLPLLLLVLRL--FGRRLRKLFRRVQEAL-AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 338 EKAGYVQSGNSALAPIVSTIAIVST--FTCHIFLKRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRMKKI 415
Cdd:COG1132 238 LRAARLSALFFPLMELLGNLGLALVllVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 416 LVAKSPpsyITQPEDPDtilllanatltweqeinrkrgPLKTQDQR---RHV-FKkqraelYSEQslsdqgvasperqsg 491
Cdd:COG1132 318 LDEPPE---IPDPPGAV---------------------PLPPVRGEiefENVsFS------YPGD--------------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 492 spKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------PL-------AYVSQQAWIFHGNV 558
Cdd:COG1132 353 --RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdlTLeslrrqiGVVPQDTFLFSGTI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTechyphlQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDP 637
Cdd:COG1132 431 RENIRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDT-------VVGERGVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 638 LSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHnlrgLQFKD 717
Cdd:COG1132 504 TSALDTETEALIQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR----LQFGE 578
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
795-972 |
1.88e-71 |
|
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: 240.16 E-value: 1.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 795 GYLVSFLVLCLFFLMMGSSAFSTWWLGLWLDSGSQVICAPQSNETaCNVNQTLQDTKHHMYQLVYIASMMSVLTFGIIKG 874
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNST-VDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 875 FTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPV 954
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170
....*....|....*...
gi 1958746143 955 VLVVLAGLAILFFILLRC 972
Cdd:cd18599 160 FLIALIPLAIIFVFLSKI 177
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
71-709 |
1.63e-56 |
|
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: 208.92 E-value: 1.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 71 TLTVDTLPPLSPYDSSDVNAKRLQILWDeeieRVGPERASLGRVVwkfqrtrvLMDVVANILciimaALGPTVLIHQILQ 150
Cdd:COG2274 122 TGVALLLEPTPEFDKRGEKPFGLRWFLR----LLRRYRRLLLQVL--------LASLLINLL-----ALATPLFTQVVID 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 151 HVTNISSGHIGISICLCLALFATeFTKVLFWALAWAINyRTAIRLKVALSTLIFKNLLSFKT--LTHISAGEVLN----- 223
Cdd:COG2274 185 RVLPNQDLSTLWVLAIGLLLALL-FEGLLRLLRSYLLL-RLGQRIDLRLSSRFFRHLLRLPLsfFESRSVGDLASrfrdv 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 224 -----VLSSDSYSLFEAALFcplpatIPILMVVCAVYAFFILGSTALVGICVYLIFIPIQMFMAKLNS-AFRRSAisvtd 297
Cdd:COG2274 263 esireFLTGSLLTALLDLLF------VLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSReESEASA----- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 298 KRVQTMNEFLTCIKLIKMYA--------WEKSFMNTIHDIRKREKKLLekagYVQSGNSALaPIVSTIAIVsTFTCHIFL 369
Cdd:COG2274 332 KRQSLLVETLRGIETIKALGaesrfrrrWENLLAKYLNARFKLRRLSN----LLSTLSGLL-QQLATVALL-WLGAYLVI 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 370 KRTLTAP--VAFSVIA-MFN--VMKFSIAILPFsvkavAEASVSLRRMKKILvaKSPPsyitqpedpdtilllanatltw 444
Cdd:COG2274 406 DGQLTLGqlIAFNILSgRFLapVAQLIGLLQRF-----QDAKIALERLDDIL--DLPP---------------------- 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 445 EQEINRKRGPLKTQDQR---RHV-FKkqraelYSEQSlsdqgvasperqsgspKSVLHNISFVVRKGKVLGICGNVGSGK 520
Cdd:COG2274 457 EREEGRSKLSLPRLKGDielENVsFR------YPGDS----------------PPVLDNISLTIKPGERVAIVGRSGSGK 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 521 SSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDL 586
Cdd:COG2274 515 STLLKLLLGLYEPTSGRILIDGiDLrqidpaslrrqiGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFI 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 587 NSLPYGdltechYpHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFeECIKKTLKGKTVVLV 666
Cdd:COG2274 595 EALPMG------Y-DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL-ENLRRLLKGRTVIII 666
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1958746143 667 THQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 709
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
491-685 |
1.51e-55 |
|
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: 192.16 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVS-----------------GPLAYVSQQAWI 553
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 554 FHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYL 633
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTE-------IGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 634 LDDPLSAVDAHVGKHVFEECIKKTLKG--KTVVLVTHQLQFLESCDEVILLEDG 685
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
131-412 |
2.37e-54 |
|
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: 191.94 E-value: 2.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 131 ILCIIMAAL--GPTVLIHQILQHVTNISSGHIGISICLCLALFATEFTKVLFWALAWAINYRTAIRLKVALSTLIFKNLL 208
Cdd:cd18596 4 LLAVLSSVLsfAPPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 209 SFKTLTHI---------------------SAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVG 267
Cdd:cd18596 84 RRRDKSGSsksseskkkdkeededekssaSVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 268 ICVYLIFIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGN 347
Cdd:cd18596 164 LAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLL 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 348 SALAPIVSTIAIVSTFTCHIFL-KRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18596 244 SLLWFLIPILVTVVTFATYTLVmGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
477-701 |
6.86e-53 |
|
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: 194.98 E-value: 6.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 477 SLSDQGVASPERqsgspKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP------------- 543
Cdd:COG4988 338 ELEDVSFSYPGG-----RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrq 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 544 LAYVSQQAWIFHGNVRENILFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGdltechyPHLQIGERGVNLSGGQRQRISLA 622
Cdd:COG4988 413 IAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDG-------LDTPLGEGGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 623 RAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 701
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
491-707 |
3.44e-52 |
|
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: 184.67 E-value: 3.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAYVSQQAWIFHGNVRENILFGEKYNH 570
Cdd:cd03291 49 GAP--VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 571 QRYQHTVHVCGLQKDLNSLPYGDLTechyphlQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVF 650
Cdd:cd03291 127 YRYKSVVKACQLEEDITKFPEKDNT-------VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIF 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 651 EECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 707
Cdd:cd03291 200 ESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
208-706 |
6.76e-51 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 189.21 E-value: 6.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 208 LSFKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFI----LGSTALVGICVYLIFIPIqmFMAK 283
Cdd:COG4987 101 LAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFfspaLALVLALGLLLAGLLLPL--LAAR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 284 LNSAF-RRSAISVTDKRVQTMnEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVST 362
Cdd:COG4987 179 LGRRAgRRLAAARAALRARLT-DLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 363 --FTCHIFLKRTLTAP----VAFSVIAMFNVmkfsIAILPFSVKAVAEASVSLRRMKKILVAK----SPPSYITQPEDPD 432
Cdd:COG4987 258 lwLAAPLVAAGALSGPllalLVLAALALFEA----LAPLPAAAQHLGRVRAAARRLNELLDAPpavtEPAEPAPAPGGPS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 433 tiLLLANATLTWEqeinrkrgplktqdqrrhvfkkqraelyseqslsdqgvasperqsGSPKSVLHNISFVVRKGKVLGI 512
Cdd:COG4987 334 --LELEDVSFRYP---------------------------------------------GAGRPVLDGLSLTLPPGERVAI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 513 CGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWIFHGNVRENILFGekynhqRYQHT--- 576
Cdd:COG4987 367 VGPSGSGKSTLLALLLRFLDPQSGSITLGGvDLrdldeddlrrriAVVPQRPHLFDTTLRENLRLA------RPDATdee 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 577 -VHVC---GLQKDLNSLPYGdLtechypHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEE 652
Cdd:COG4987 441 lWAALervGLGDWLAALPDG-L------DTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 653 cIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 706
Cdd:COG4987 514 -LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
127-412 |
6.45e-49 |
|
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: 175.72 E-value: 6.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 127 VVANILCIIMAALGPtVLIHQILQHVTN----ISSGHIGISICLCLALFATEFTKVLFWALAWAINYRTAIRLKVALSTL 202
Cdd:cd18597 3 GLLKLLADVLQVLSP-LLLKYLINFVEDaylgGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 203 IF-KNL-LSFKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGICVYLIFIPIQMF 280
Cdd:cd18597 82 IYrKSLrLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 281 MAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIV 360
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 361 STFTCHIFLKRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18597 242 LSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
190-412 |
4.74e-47 |
|
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: 170.09 E-value: 4.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 190 RTAIRLKVALSTLIFKNLL--SFKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVG 267
Cdd:cd18593 66 RIGMRLRVACSSLIYRKALrlSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 268 ICVYLIFIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGN 347
Cdd:cd18593 146 LAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALN 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 348 SALAPIVSTIAIVSTFTCHIFLKRTLTAPVAFSVIAMFNVMKFSIAI-LPFSVKAVAEASVSLRRM 412
Cdd:cd18593 226 MGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
166-412 |
6.38e-47 |
|
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: 169.96 E-value: 6.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 166 LCLALFATEFTKVLFWALAWAINYRTAIRLKVALSTLIFKnllsfKTLThIS--------AGEVLNVLSSDSYSLFEAAL 237
Cdd:cd18595 40 YAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYR-----KALR-LSnsarkkstVGEIVNLMSVDAQRIQDLVP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 238 FCPLPATIPILMVVCAVYAFFILGSTALVGICVYLIFIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYA 317
Cdd:cd18595 114 YLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 318 WEKSFMNTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTCHIFL--KRTLTAPVAFSVIAMFNVMKFSIAIL 395
Cdd:cd18595 194 WEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSdpDNVLDAEKAFVSLSLFNILRFPLSML 273
|
250
....*....|....*..
gi 1958746143 396 PFSVKAVAEASVSLRRM 412
Cdd:cd18595 274 PMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
131-411 |
1.23e-46 |
|
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: 168.97 E-value: 1.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 131 ILCIIMAALGPT--VLIHQILQHVTNISSGHIGISICLCLALFATEFTKVLFWALAWAINYRTAIRLKVALSTLIFKNLL 208
Cdd:cd18594 4 ILLFLEESLKIVqpLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 209 SFKT--LTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTALVGICVYLIFIPIQMFMAKLNS 286
Cdd:cd18594 84 KLSSsaLSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 287 AFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTCH 366
Cdd:cd18594 164 KYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1958746143 367 IFLKRTLTAPVAFSVIAMFNVMKFSIAI-LPFSVKAVAEASVSLRR 411
Cdd:cd18594 244 VLTGNTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKR 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
488-706 |
2.79e-44 |
|
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: 160.47 E-value: 2.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIF 554
Cdd:cd03251 9 RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 HGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGdltechYpHLQIGERGVNLSGGQRQRISLARAVYANRQLYL 633
Cdd:cd03251 89 NDTVAENIAYGrPGATREEVEEAARAANAHEFIMELPEG------Y-DTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 634 LDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 706
Cdd:cd03251 162 LDEATSALDT-ESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
494-701 |
2.96e-41 |
|
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: 151.22 E-value: 2.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVRE 560
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKYNHQ-RYQHTVHVCGLQKDLNSLPYGDLTechyphlQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:cd03254 96 NIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDT-------VLGENGGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 640 AVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 701
Cdd:cd03254 169 NIDTETEKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
490-686 |
3.92e-41 |
|
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: 148.69 E-value: 3.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 490 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWIFHG 556
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvDLrdldleslrkniAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENILfgekynhqryqhtvhvcglqkdlnslpygdltechyphlqigergvnlSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:cd03228 91 TIRENIL------------------------------------------------SGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958746143 637 PLSAVDAHvGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGE 686
Cdd:cd03228 123 ATSALDPE-TEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
491-687 |
2.48e-40 |
|
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: 148.51 E-value: 2.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------P------LAYVSQQAWIFHGN 557
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldPadlrrnIGYVPQDVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENILFGEKY-NHQRYQHTVHVCGLQKDLNSLPYGDltechypHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:cd03245 94 LRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGL-------DLQIGERGRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 637 PLSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:cd03245 167 PTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
496-709 |
4.05e-40 |
|
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: 148.46 E-value: 4.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-------------LAYVSQQAWIFHGNVRENI 562
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFGEKYNHQryQHTVHVCGL---QKDLNSLPYGDLTEChyphlqiGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:cd03249 98 RYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLV-------GERGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 640 AVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 709
Cdd:cd03249 169 ALDAESEKLV-QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
488-706 |
9.83e-39 |
|
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: 144.55 E-value: 9.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIF 554
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 HGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGdltechYPHLqIGERGVNLSGGQRQRISLARAVYANRQLYL 633
Cdd:cd03252 89 NRSIRDNIALAdPGMSMERVIEAAKLAGAHDFISELPEG------YDTI-VGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 634 LDDPLSAVDAHvGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 706
Cdd:cd03252 162 FDEATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
494-706 |
1.68e-38 |
|
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: 143.91 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVRE 560
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTechyphlQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:cd03253 94 NIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDT-------IVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 640 AVDAHVGKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 706
Cdd:cd03253 167 ALDTHTEREIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
799-971 |
2.40e-38 |
|
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: 145.34 E-value: 2.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 799 SFLVLCLFFLMMGSSAFSTWWLGLWLDSgsqvicapqsnetacnvNQTLQDTKHHMYQLVYIA-SMMSVLTFGIIKGFTF 877
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSD-----------------WSSSPNSSSGYYLGVYAAlLVLASVLLVLLRWLLF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 878 TNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVLV 957
Cdd:cd18580 64 VLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLI 143
|
170
....*....|....
gi 1958746143 958 VLAGLAILFFILLR 971
Cdd:cd18580 144 VLPPLLVVYYLLQR 157
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
496-682 |
2.83e-38 |
|
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: 150.90 E-value: 2.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWIFHGNVRENI 562
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvPLadadadswrdqiAWVPQHPFLFAGTIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFGEKY-NHQRYQHTVHVCGLQKDLNSLPYGdltechyPHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:TIGR02857 417 RLARPDaSDAEIREALERAGLDEFVAALPQG-------LDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958746143 642 DAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILL 682
Cdd:TIGR02857 490 DAETEAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
187-411 |
1.16e-37 |
|
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: 143.53 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 187 INYRTAIRLKVALSTLIFKNLLSFKTLT----HISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGS 262
Cdd:cd18591 79 IVIREGIRLKTALQAMIYEKALRLSSWNlssgSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 263 TALVGICVYLIFIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGY 342
Cdd:cd18591 159 SALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAV 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 343 VQSGNSALAPIVSTIAIVSTFTCHIFLKRT-LTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRR 411
Cdd:cd18591 239 YWSLMTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
799-971 |
5.59e-37 |
|
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: 141.46 E-value: 5.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 799 SFLVLCLFFLMMGSSAFSTWWLGLWldsgsqvicapqSNETACNVNQTLQDTkhHMYQLVYIASMMSVLTFGIIKGFTFT 878
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEW------------SDDPALNGTQDTEQR--DYRLGVYGALGLGQAIFVFLGSLALA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 879 NTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVLVV 958
Cdd:cd18603 67 LGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVV 146
|
170
....*....|...
gi 1958746143 959 LAGLAILFFILLR 971
Cdd:cd18603 147 IIPLAILYFFIQR 159
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
488-717 |
6.03e-37 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 147.56 E-value: 6.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIF 554
Cdd:TIGR02203 339 RYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlaslrrQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 HGNVRENILFGE--KYNHQRYQHTVHVCGLQKDLNSLPYGdltechyPHLQIGERGVNLSGGQRQRISLARAVYANRQLY 632
Cdd:TIGR02203 419 NDTIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLG-------LDTPIGENGVLLSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 633 LLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLiHNlrg 712
Cdd:TIGR02203 492 ILDEATSALDNESERLV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL-HN--- 566
|
....*
gi 1958746143 713 LQFKD 717
Cdd:TIGR02203 567 MQFRE 571
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
491-708 |
3.92e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 142.16 E-value: 3.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV-------------AVSGPLAYVSQQAWIFHGN 557
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENILFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:PRK10789 405 VANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTE-------VGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 637 PLSAVDAHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 708
Cdd:PRK10789 478 ALSAVDGRT-----EHQILHNLrqwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
494-709 |
4.30e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 142.29 E-value: 4.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQkGVVAVSG-------------PLAYVSQQAWIFHGNVRE 560
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEK-YNHQRYQHTVHVCGLQKDLNSLPYGdltechyPHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:PRK11174 442 NVLLGNPdASDEQLQQALENAWVSEFLPLLPQG-------LDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 640 AVDAHVGKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 709
Cdd:PRK11174 515 SLDAHSEQLVMQ-ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
496-706 |
1.36e-33 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 138.72 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISAL-------LGQMQLQKGVVAVSGP------LAYVSQQAWIFHGNVRENI 562
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLqrlytpqHGQVLVDGVDLAIADPawlrrqMGVVLQENVLFSRSIRDNI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:TIGR01846 552 ALCNpGAPFEHVIHAAKLAGAHDFISELPQGYNTE-------VGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSAL 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 642 DAHvGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 706
Cdd:TIGR01846 625 DYE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
496-720 |
7.32e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.90 E-value: 7.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICG-NvGSGKSSLISALLGQMQLQKGVVAVSGP--------LAYVSQQA---WIFHGNVRENIL 563
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGpN-GAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 FGekynhqRYQHTvhvcGLQKDLNSLPYGDLTEC-------HYPHLQIGErgvnLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:COG1121 100 MG------RYGRR----GLFRRPSRADREAVDEAlervgleDLADRPIGE----LSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 637 PLSAVDAHvGKHVFEECIKKtLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEkGTHKELMEErgryaKLIHNLRGL 713
Cdd:COG1121 166 PFAGVDAA-TEEALYELLRE-LRreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTP-----ENLSRAYGG 237
|
....*..
gi 1958746143 714 QFKDPEH 720
Cdd:COG1121 238 PVALLAH 244
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
479-707 |
7.36e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 136.78 E-value: 7.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 479 SDQGVASPERQSgspKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL------------A 545
Cdd:TIGR00958 482 QDVSFSYPNRPD---VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvPLvqydhhylhrqvA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 546 YVSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEChyphlqiGERGVNLSGGQRQRISLARA 624
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEV-------GEKGSQLSGGQKQRIAIARA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 625 VYANRQLYLLDDPLSAVDAHVGKHVFEEcikKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYA 704
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
...
gi 1958746143 705 KLI 707
Cdd:TIGR00958 709 HLV 711
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
496-682 |
8.33e-33 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 126.49 E-value: 8.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL-------AYVSQQA---WIFHGNVRENILF 564
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkPLekerkriGYVPQRRsidRDFPISVRDVVLM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 565 GekynhqRYQHTVHVCGLQKD-----LNSLPYGDLTecHYPHLQIGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:cd03235 94 G------LYGHKGLFRRLSKAdkakvDEALERVGLS--ELADRQIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958746143 640 AVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILL 682
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLLL 205
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
149-715 |
9.78e-33 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 134.83 E-value: 9.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 149 LQHVTNISSGHIGISICLCLALFATeftkvlFWALAWaINYR--TAIRLKValstliFKNLLSFKTLTH--ISAGEVLNV 224
Cdd:TIGR02204 54 SGLLNRYFAFLLVVALVLALGTAAR------FYLVTW-LGERvvADIRRAV------FAHLISLSPSFFdkNRSGEVVSR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 225 LSSDSySLFEAALFCPLP-ATIPILMVVCAVYAFFILGS--TALVGICVYLIFIPIQMFMAKLNSAFRRSAISVTDKrVQ 301
Cdd:TIGR02204 121 LTTDT-TLLQSVIGSSLSmALRNALMCIGGLIMMFITSPklTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADA-GS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 302 TMNEFLTCIKLIKMYAWEksfmntiHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAIVSTFTC---------HIFLKRT 372
Cdd:TIGR02204 199 YAGETLGAIRTVQAFGHE-------DAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAivgvlwvgaHDVIAGK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 373 LTAPV--AFSVIAMFNVMkfSIAILPFSVKAVAEASVSLRRMKKILVAKSPpsyITQPEDPDTIlllanatltweqeinr 450
Cdd:TIGR02204 272 MSAGTlgQFVFYAVMVAG--SIGTLSEVWGELQRAAGAAERLIELLQAEPD---IKAPAHPKTL---------------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 451 krgplktqdqrrhvfkkqRAELYSEQSLSDQGVASPERQSgspKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQ 530
Cdd:TIGR02204 331 ------------------PVPLRGEIEFEQVNFAYPARPD---QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 531 MQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVRENILFG-------EKYNHQRYQHTvhvcglQKDLNSLP 590
Cdd:TIGR02204 390 YDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVMENIRYGrpdatdeEVEAAARAAHA------HEFISALP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 591 YGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQL 670
Cdd:TIGR02204 464 EGYDTY-------LGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLV-QQALETLMKGRTTLIIAHRL 535
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1958746143 671 QFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHnlrgLQF 715
Cdd:TIGR02204 536 ATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLAR----LQF 576
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
465-709 |
1.05e-32 |
|
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: 136.02 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 465 FKKQRAELYSEQSLSDQGVASPERQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-P 543
Cdd:TIGR01193 458 FINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfS 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 544 LA------------YVSQQAWIFHGNVRENILFGEKYN--HQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGV 609
Cdd:TIGR01193 538 LKdidrhtlrqfinYLPQEPYIFSGSILENLLLGAKENvsQDEIWAACEIAEIKDDIENMPLGYQTE-------LSEEGS 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 610 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKktLKGKTVVLVTHQLQFLESCDEVILLEDGEICE 689
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
250 260
....*....|....*....|
gi 1958746143 690 KGTHKELMEERGRYAKLIHN 709
Cdd:TIGR01193 689 QGSHDELLDRNGFYASLIHN 708
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
800-969 |
1.95e-32 |
|
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: 127.97 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 800 FLVLCLFFLMMGSSAFSTWWLGLWLDSGSQVICAPQSNETAcnvnqtlqdtkhhMYQL-VYIASMMSVLTFGIIKGFTFT 878
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSV-------------LYYLgIYALISLLSVLLGTLRYLLFF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 879 NTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVLVV 958
Cdd:cd18604 69 FGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLP 148
|
170
....*....|.
gi 1958746143 959 LAGLAILFFIL 969
Cdd:cd18604 149 AVVLAALYVYI 159
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
496-692 |
2.13e-32 |
|
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: 125.68 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------PL-------AYVSQQAWIFHGNVRENI 562
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiGLhdlrsriSIIPQDPVLFSGTIRSNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 -LFGEKYNHQRYQhTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:cd03244 99 dPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTV-------VEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 642 DAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 692
Cdd:cd03244 171 DPETDALI-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
800-969 |
5.81e-31 |
|
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: 123.74 E-value: 5.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 800 FLVLCLFFLMMGSSAFSTWWLGLWLDsgsqvicapqsnetacnvnqtlqDTKH---HMYQLVYIASMMSVLTFGIIKGFT 876
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTE-----------------------DFFGlsqGFYIGIYAGLGVLQAIFLFLFGLL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 877 FTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVL 956
Cdd:cd18606 59 LAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFA 138
|
170
....*....|...
gi 1958746143 957 VVLAGLAILFFIL 969
Cdd:cd18606 139 IALPPLLVLYYFI 151
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
491-710 |
1.20e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 128.40 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLA------------YVSQQAWIFHGN 557
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqPIAdyseaalrqaisVVSQRVHLFSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLtechyphlQIGERGVNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:PRK11160 430 LRDNLLLAaPNASDEALIEVLQQVGLEKLLEDDKGLNA--------WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 637 PLSAVDAHVGKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNL 710
Cdd:PRK11160 502 PTEGLDAETERQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
491-715 |
1.73e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 128.21 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGN 557
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENILF--GEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLD 635
Cdd:PRK11176 433 IANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTV-------IGENGVLLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 636 DPLSAVDAHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLiHNlr 711
Cdd:PRK11176 506 EATSALDTES-----ERAIQAALdelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL-HK-- 577
|
....
gi 1958746143 712 gLQF 715
Cdd:PRK11176 578 -MQF 580
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
799-967 |
1.75e-30 |
|
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: 122.64 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 799 SFLVLCLFFLMMGSSAFSTWWLGLWLdsgsqvicapqSNETACNVNQTLQDTKHHMYQLVYIASMMSVLTFgiIKGFTFT 878
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWV-----------SHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTL--LRAFLFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 879 NTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVLVV 958
Cdd:cd18605 68 YGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLL 147
|
....*....
gi 1958746143 959 LAGLAILFF 967
Cdd:cd18605 148 LLPLAFIYY 156
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
481-699 |
8.67e-30 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 125.54 E-value: 8.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 481 QGVASPERQSGSP----KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP------------- 543
Cdd:TIGR01842 314 EGHLSVENVTIVPpggkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAdlkqwdretfgkh 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 544 LAYVSQQAWIFHGNVRENIL-FGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLA 622
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTV-------IGPGGATLSGGQRQRIALA 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 623 RAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKT-LKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDE-EGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
494-687 |
2.88e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.07 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWIFHGNVRE 560
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkPLsampppewrrqvAYVPQEPALWGGTVRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKYNHQRYQHTvHVCGLQKDLNsLPYGDL-TECHyphlqigergvNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:COG4619 93 NLPFPFQLRERKFDRE-RALELLERLG-LPPDILdKPVE-----------RLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 640 AVDAHvGKHVFEECIKKTL--KGKTVVLVTH-QLQFLESCDEVILLEDGEI 687
Cdd:COG4619 160 ALDPE-NTRRVEELLREYLaeEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
491-687 |
8.85e-29 |
|
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: 122.55 E-value: 8.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV-----AVS-------GP-LAYVSQQAWIFHGN 557
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgaDLSqwdreelGRhIGYLPQDVELFDGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENI-LFGEkynhqryqHT------------VHvcglqkDL-NSLPYGdltechYpHLQIGERGVNLSGGQRQRISLAR 623
Cdd:COG4618 422 IAENIaRFGD--------ADpekvvaaaklagVH------EMiLRLPDG------Y-DTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 624 AVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKtLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDD-EGEAALAAAIRA-LKarGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
488-684 |
1.20e-28 |
|
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: 114.88 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG--------PLAYVSQQAWIF-HGNV 558
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDALLpWLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENILFGEKYNH-------QRYQHTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAVYANRQL 631
Cdd:cd03293 91 LDNVALGLELQGvpkaearERAEELLELVGLSGFEN----------AYPH--------QLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 632 YLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLqflescDEVILLED 684
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEE-LLDIWRetGKTVLLVTHDI------DEAVFLAD 200
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
496-699 |
1.57e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.78 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------------PLAYVSQQAwIFHGN--VREN 561
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEP-ALYPDltVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILF-------GEKYNHQRYQHTVHVCGLQKDLNSLpygdltechyphlqIGergvNLSGGQRQRISLARAVYANRQLYLL 634
Cdd:COG1131 94 LRFfarlyglPRKEARERIDELLELFGLTDAADRK--------------VG----TLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 635 DDPLSAVDAhVGKHVFEECIKKtLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 699
Cdd:COG1131 156 DEPTSGLDP-EARRELWELLRE-LAaeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
494-687 |
1.68e-28 |
|
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: 112.88 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGplayvsQQAWIFHGNVRENI--LFGEKYnhq 571
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIgyLPEEPS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 572 ryqhtvhvcglqkdlnslPYGDLTechyphlqiGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFE 651
Cdd:cd03230 84 ------------------LYENLT---------VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958746143 652 ECIKK-TLKGKTVVLVTHQLQFLES-CDEVILLEDGEI 687
Cdd:cd03230 136 ELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
795-971 |
2.91e-28 |
|
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: 116.65 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 795 GYLVSFLVLCLFFLMMGSSAFSTWWLGLWLDSGSQVICAPQSNETACNVNQTLQDTKHHMYQLVYIASMMSVLTFGIIKG 874
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 875 FTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPV 954
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170
....*....|....*..
gi 1958746143 955 VLVVLAGLAILFFILLR 971
Cdd:cd18601 161 VLIPVIPLVILFLFLRR 177
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
494-699 |
2.11e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 112.06 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWI-FHGNVR 559
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrDLaslsrrelarriAYVPQEPPApFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFGekynhqRYQHtvhvcglQKDLNSLPYGD-------LTECHYPHLQigERGVN-LSGGQRQRISLARAVYANRQL 631
Cdd:COG1120 94 ELVALG------RYPH-------LGLFGRPSAEDreaveeaLERTGLEHLA--DRPVDeLSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 632 YLLDDPLSAVDAHvgkHVFE--ECIKK--TLKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:COG1120 159 LLLDEPTSHLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
496-702 |
2.78e-27 |
|
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: 111.49 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------PLAYVSQQAWIFHGN-------VRENI 562
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkePREARRQIGVLPDERglydrltVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 -LFGEKY------NHQRYQHTVHVCGLQKDLNSLpygdltechyphlqIGErgvnLSGGQRQRISLARAVYANRQLYLLD 635
Cdd:COG4555 96 rYFAELYglfdeeLKKRIEELIELLGLEEFLDRR--------------VGE----LSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 636 DPLSAVDAhVGKHVFEECIKKTLK-GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGR 702
Cdd:COG4555 158 EPTNGLDV-MARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
496-687 |
3.30e-27 |
|
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: 111.02 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWIFHGNVRENI 562
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkPIsqyehkylhskvSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFGekynhqryqhtvhvcglqkdLNSLPYGDLTEC--------------HYPHLQIGERGVNLSGGQRQRISLARAVYAN 628
Cdd:cd03248 109 AYG--------------------LQSCSFECVKEAaqkahahsfiselaSGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 629 RQLYLLDDPLSAVDAHvGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:cd03248 169 PQVLILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
488-687 |
5.62e-27 |
|
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: 108.46 E-value: 5.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-------------LAYVSQQAWIF 554
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 HGNVRENILfgekynhqryqhtvhvcglqkdlnslpygdltechyphlqigergvnlSGGQRQRISLARAVYANRQLYLL 634
Cdd:cd03246 89 SGSIAENIL------------------------------------------------SGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 635 DDPLSAVDaHVGKHVFEECIKKT-LKGKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:cd03246 121 DEPNSHLD-VEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
131-412 |
8.12e-27 |
|
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: 111.49 E-value: 8.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 131 ILCIIMAALGPTVLiHQILQHVTNISSGHIgISICLCLALFATEFTKVLFWA-LAWAINyRTAIRLKVALSTLIFKNLLS 209
Cdd:cd18598 7 LLADVLGFAGPLLL-NKLVEFLEDSSEPLS-DGYLYALGLVLSSLLGALLSShYNFQMN-KVSLKVRAALVTAVYRKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 210 FKT--LTHISAGEVLNVLSSDS-------YSLFEAALfcpLPATIPIlmvvcavyAFFIL----GSTALVGICVYLIFIP 276
Cdd:cd18598 84 VRSssLSKFSTGEIVNLMSTDAdrivnfcPSFHDLWS---LPLQIIV--------ALYLLyqqvGVAFLAGLVFALVLIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 277 IQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGNSALAPIVST 356
Cdd:cd18598 153 INKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 357 IAIVSTFTCHIFLKRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18598 233 LISILTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
491-686 |
9.94e-27 |
|
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: 109.09 E-value: 9.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAW--------------IFH 555
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkDLTKLSLKELrrkvglvfqnpddqFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 556 GNVRENILFGEKyNHQRYQHTVhvcgLQKDLNSLPYGDLTEC--HYPHlqigergvNLSGGQRQRISLArAVYANR-QLY 632
Cdd:cd03225 91 PTVEEEVAFGLE-NLGLPEEEI----EERVEEALELVGLEGLrdRSPF--------TLSGGQKQRVAIA-GVLAMDpDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 633 LLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQFL-ESCDEVILLEDGE 686
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLE--LLKKLKaeGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
494-696 |
1.29e-26 |
|
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: 109.51 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------------PL----AYVSQQAWIFHG- 556
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyRLrrrmGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENILFGEKYNHQRYQHTV--------HVCGLQKDLNSLPYgdltechyphlqigergvNLSGGQRQRISLARAVYAN 628
Cdd:cd03261 93 TVFENVAFPLREHTRLSEEEIreivleklEAVGLRGAEDLYPA------------------ELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 629 RQLYLLDDPLSAVDAhVGKHVFEECI---KKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 696
Cdd:cd03261 155 PELLLYDEPTAGLDP-IASGVIDDLIrslKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
496-708 |
1.68e-26 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 116.58 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSS---LISALL----GQM--------QLQKGVVAVSgpLAYVSQQAWIFHGNVRE 560
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTiakLVAGLYqpwsGEIlfdgipreEIPREVLANS--VAMVDQDIFLFEGTVRD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NI-LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGdltechYpHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:TIGR03796 572 NLtLWDPTIPDADLVRACKDAAIHDVITSRPGG------Y-DAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATS 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 640 AVDAHVGKHVFEEcIKKtlKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 708
Cdd:TIGR03796 645 ALDPETEKIIDDN-LRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
494-686 |
2.80e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 105.79 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWifhgnvRENILfgekYNHQr 572
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEEL------RRRIG----YVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 573 yqhtvhvcglqkdlnslpygdltechyphlqigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEE 652
Cdd:cd00267 81 --------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....*
gi 1958746143 653 CIKKTLKGKTVVLVTHQLQFLE-SCDEVILLEDGE 686
Cdd:cd00267 123 LRELAEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
496-684 |
9.76e-26 |
|
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: 106.02 E-value: 9.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------PLAYVSQQAWIFHGN-------VRENI 562
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHADglkpeltVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LF-----GEKYNHQRYQHTVHVCGLQkdlnslpygdltecHYPHLQIGergvNLSGGQRQRISLARAVYANRQLYLLDDP 637
Cdd:COG4133 97 RFwaalyGLRADREAIDEALEAVGLA--------------GLADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958746143 638 LSAVDAHvGKHVFEECIKKTL-KGKTVVLVTHQLQFLESCdEVILLED 684
Cdd:COG4133 159 FTALDAA-GVALLAELIAAHLaRGGAVLLTTHQPLELAAA-RVLDLGD 204
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
496-708 |
1.34e-25 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 113.51 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV-------------AVSGPLAYVSQQAWIFHGNVRENI 562
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqdlagldvqAVRRQLGVVLQNGRLMSGSIFENI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGdltechyPHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 642
Cdd:TIGR03797 548 AGGAPLTLDEAWEAARMAGLAEDIRAMPMG-------MHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 643 AHVGKHVFEECikKTLKGkTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 708
Cdd:TIGR03797 621 NRTQAIVSESL--ERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
494-687 |
1.54e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 104.44 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-------------LAYVSQQawifhgnvre 560
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQA---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 nilfgekynhqryqhtVHVCGLQkdlnslpygdltechypHLqiGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:cd03214 82 ----------------LELLGLA-----------------HL--ADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958746143 640 AVDAHVGKHVFEECIK-KTLKGKTVVLVTHQL-QFLESCDEVILLEDGEI 687
Cdd:cd03214 127 HLDIAHQIELLELLRRlARERGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
496-700 |
3.02e-25 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 105.11 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------PLAYVSQ-----------QawIFHGNV 558
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRkvglvfqnpddQ--LFAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENILFG-------EKYNHQRYQHTVHVCGLQKdlnslpYGDltecHYPHlqigergvNLSGGQRQRISLArAVYANR-Q 630
Cdd:COG1122 94 EEDVAFGpenlglpREEIRERVEEALELVGLEH------LAD----RPPH--------ELSGGQKQRVAIA-GVLAMEpE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 631 LYLLDDPLSAVDAHvGKHVFEECIKK-TLKGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:COG1122 155 VLVLDEPTAGLDPR-GRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
496-687 |
7.55e-25 |
|
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: 103.72 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAW----------IF-------HGN 557
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtDISKLSEKELaafrrrhigfVFqsfnllpDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENILFGEKY-------NHQRYQHTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAVYANRQ 630
Cdd:cd03255 99 ALENVELPLLLagvpkkeRRERAEELLERVGLGDRLN----------HYPS--------ELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 631 LYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMEL-LRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
491-691 |
1.37e-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: 101.62 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV------------AVSGPLAYVSQQAWIFHGNV 558
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpvsdlekALSSLISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENIlfgekynhqryqhtvhvcglqkdlnslpygdltechyphlqiGERgvnLSGGQRQRISLARAVYANRQLYLLDDPL 638
Cdd:cd03247 92 RNNL------------------------------------------GRR---FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 639 SAVDAHVGKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKG 691
Cdd:cd03247 127 VGLDPITERQLLS-LIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
800-971 |
2.10e-24 |
|
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: 104.99 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 800 FLVLCLFFLMMGSSAFSTWWLGLWLDSGSQVicapqSNETACNVNQTLQDTKHHMYQLVYIASMMSVLTFGIIKGFTFTN 879
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDV-----ASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 880 TTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVLVVL 959
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170
....*....|..
gi 1958746143 960 AGLAILFFILLR 971
Cdd:cd18602 157 IPIIIVYYFLQK 168
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
495-692 |
2.76e-24 |
|
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: 101.72 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVREN 561
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 IlfgEKYNHqryqhtvhvcglqkdlnslpYGDltECHYPHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:cd03369 102 L---DPFDE--------------------YSD--EEIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 642 DAHVgKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 692
Cdd:cd03369 157 DYAT-DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
496-698 |
3.47e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 105.23 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------------PLAYVSQQAWIF-HGNVRENI 562
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlpprerRVGFVFQHYALFpHMTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFG-------EKYNHQRYQH---TVHVCGLQKdlnslpygdltecHYPHlqigergvNLSGGQRQRISLARAVYANRQLY 632
Cdd:COG1118 97 AFGlrvrppsKAEIRARVEElleLVQLEGLAD-------------RYPS--------QLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 633 LLDDPLSAVDAHVGKHVfEECIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELME 698
Cdd:COG1118 156 LLDEPFGALDAKVRKEL-RRWLRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
486-706 |
3.57e-24 |
|
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: 108.75 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 486 PERQsgspksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQ---AWI-------- 553
Cdd:COG5265 369 PERP------ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqDIRDVTQAslrAAIgivpqdtv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 554 -FHGNVRENILFG-------EKYNHQRYQHtvhvcgLQKDLNSLPYGDLTechyphlQIGERGVNLSGGQRQRISLARAV 625
Cdd:COG5265 443 lFNDTIAYNIAYGrpdaseeEVEAAARAAQ------IHDFIESLPDGYDT-------RVGERGLKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 626 YANRQLYLLDDPLSAVDAHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 701
Cdd:COG5265 510 LKNPPILIFDEATSALDSRT-----ERAIQAALrevaRGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGG 584
|
....*
gi 1958746143 702 RYAKL 706
Cdd:COG5265 585 LYAQM 589
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
488-685 |
5.61e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.48 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV-----AVSGP---LAYVSQQA----WIfh 555
Cdd:COG1116 18 PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkPVTGPgpdRGVVFQEPallpWL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 556 gNVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAVYAN 628
Cdd:COG1116 96 -TVLDNVALGlelrgvpKAERRERARELLELVGLAGFED----------AYPH--------QLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 629 RQLYLLDDPLSAVDAHVGKHVFEECIK---KTlkGKTVVLVTHQLQ---FLesCDEVILLEDG 685
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRlwqET--GKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
499-687 |
6.04e-24 |
|
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: 101.22 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVrKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPL-----------------AYVSQQAWIF-HGNVRE 560
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKYNH-----QRYQHTVHVCGLQKDLNSLPYGdltechyphlqigergvnLSGGQRQRISLARAVYANRQLYLLD 635
Cdd:cd03297 95 NLAFGLKRKRnredrISVDELLDLLGLDHLLNRYPAQ------------------LSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 636 DPLSAVDAHVGKHVFEEC--IKKTLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 687
Cdd:cd03297 157 EPFSALDRALRLQLLPELkqIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
496-687 |
3.85e-23 |
|
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: 98.75 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVRENIL 563
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDYALFpHLTVAENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 FGEKYNHQRYQHTVHVCGLQKDLNSLpygDLTECHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 643
Cdd:cd03259 95 FGLKLRGVPKAEIRARVRELLELVGL---EGLLNRYPH--------ELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958746143 644 HVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 687
Cdd:cd03259 164 KLREELREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
496-699 |
7.54e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 101.33 E-value: 7.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVRENIL 563
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppekrNVGMVFQDYALFpHLTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 FG---EKYN----HQRYQHTVHVCGLQKdlnslpYGDltecHYPHlqigergvNLSGGQRQRISLARAVyANR-QLYLLD 635
Cdd:COG3842 100 FGlrmRGVPkaeiRARVAELLELVGLEG------LAD----RYPH--------QLSGGQQQRVALARAL-APEpRVLLLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 636 DPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:COG3842 161 EPLSALDAKLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
497-639 |
8.05e-23 |
|
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: 95.79 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-------------LAYVSQQAWIF-HGNVRENI 562
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 563 LFGEkyNHQRYQHTVHVCGLQKDLNSLPYGDLtechyPHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDL-----ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
471-703 |
1.09e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 104.03 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 471 ELYSEQSLSDQGVASPER-------------------QSGS------------PKSVLHNISFVVRKGKVLGICGNVGSG 519
Cdd:PRK10790 300 ELTTQQSMLQQAVVAGERvfelmdgprqqygnddrplQSGRididnvsfayrdDNLVLQNINLSVPSRGFVALVGHTGSG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 520 KSSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDL 586
Cdd:PRK10790 380 KSTLASLLMGYYPLTEGEIRLDGrPLsslshsvlrqgvAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 587 NSLPYGdltechyPHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgkhvfEECIKKTL----KGKT 662
Cdd:PRK10790 460 RSLPDG-------LYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-----EQAIQQALaavrEHTT 527
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958746143 663 VVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRY 703
Cdd:PRK10790 528 LVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
494-686 |
1.70e-22 |
|
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: 95.72 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG---------------PLAYVSQQAWIF-HGN 557
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFpHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENILFGekynhqryqhtvhvcglqkdlnslpygdltechyphlqigergvnLSGGQRQRISLARAVYANRQLYLLDDP 637
Cdd:cd03229 93 VLENIALG---------------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 638 LSAVDAHVGKHVFEECikKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGE 686
Cdd:cd03229 128 TSALDPITRREVRALL--KSLQaqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
496-698 |
1.85e-22 |
|
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: 97.57 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAYVSQQAWiFHGNVRenILFGEKYN--HQRy 573
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA-FRRRVQ--MVFQDPYAslHPR- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 574 qHTV--------HVCGLQKD-------LNS--LPYGDLTEchYPHlQigergvnLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:COG1124 96 -HTVdrilaeplRIHGLPDReeriaelLEQvgLPPSFLDR--YPH-Q-------LSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 637 PLSAVDAHVGKHV---FEEcIKKTlKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 698
Cdd:COG1124 165 PTSALDVSVQAEIlnlLKD-LREE-RGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
497-707 |
2.00e-22 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 103.05 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVRENIL 563
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGidintvtreslrkSIATVFQDAGLFNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 FG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTechyphlQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 642
Cdd:TIGR01192 431 LGrEGATDEEVYEAAKAAAAHDFILKRSNGYDT-------LVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALD 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 643 AHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 707
Cdd:TIGR01192 504 VETEARV-KNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
496-709 |
2.25e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 104.29 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVRENI 562
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrrVLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGdltechyPHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 642
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDVIDRNPFG-------LDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 643 AHVGKhVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGR-YAKLIHN 709
Cdd:PLN03232 1404 VRTDS-LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFRMVHS 1470
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
496-670 |
2.49e-22 |
|
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: 102.44 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-------------LAYVSQQAWIFHGNVRENI 562
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:TIGR02868 430 RLArPDATDEELWAALERVGLADWLRALPDGLDTV-------LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*....
gi 1958746143 642 DAHVGKHVFEEcIKKTLKGKTVVLVTHQL 670
Cdd:TIGR02868 503 DAETADELLED-LLAALSGRTVVLITHHL 530
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
496-687 |
7.15e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 95.50 E-value: 7.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLA----------------YVSQqawiFHG-- 556
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqDISslserelarlrrrhigFVFQ----FFNll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 ---NVRENILF-------GEKYNHQRYQHTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAVY 626
Cdd:COG1136 99 pelTALENVALplllagvSRKERRERARELLERVGLGDRLD----------HRPS--------QLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 627 ANRQLYLLDDPLSAVDAHVGKHVFE---ECIKKTlkGKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLEllrELNREL--GTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
491-691 |
9.53e-22 |
|
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: 94.88 E-value: 9.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQ---------AWIF------ 554
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkDLLKLSRRlrkirrkeiQMVFqdpmss 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 -----------------HGNVRENilfgEKYNHQRYQHTVHVCGLQKDLNSlpygdltechYPHlqigergvNLSGGQRQ 617
Cdd:cd03257 95 lnprmtigeqiaeplriHGKLSKK----EARKEAVLLLLVGVGLPEEVLNR----------YPH--------ELSGGQRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 618 RISLARAVYANRQLYLLDDPLSAVDAHVgkhvfEECIKKTLK------GKTVVLVTHQLQFL-ESCDEVILLEDGEICEK 690
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSV-----QAQILDLLKklqeelGLTLLFITHDLGVVaKIADRVAVMYAGKIVEE 227
|
.
gi 1958746143 691 G 691
Cdd:cd03257 228 G 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
497-708 |
1.32e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.42 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVRENIL 563
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 FGekynhqRYQHT-VHVCGLQKDLNSLPYGDLTECHYpHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 642
Cdd:PRK13657 431 VG------RPDATdEEMRAAAERAQAHDFIERKPDGY-DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 643 AhvgkhVFEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 708
Cdd:PRK13657 504 V-----ETEAKVKAALdelmKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
123-388 |
1.68e-21 |
|
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: 95.79 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 123 VLMDVVANILCIIMAALGPtVLIHQILQHVTNISSGHIGISICLCLALFATEFTKVLFWALAWAINYRTAIRLKVALSTL 202
Cdd:pfam00664 1 LILAILLAILSGAISPAFP-LVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 203 IFKNLL--SFKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILG-STALVGICVYLIFIPIQM 279
Cdd:pfam00664 80 LFKKILrqPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGwKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 280 FMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQSGNSALAPIVSTIAI 359
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|.
gi 1958746143 360 VSTFTCHIFL--KRTLTAPVAFSVIAMFNVM 388
Cdd:pfam00664 240 ALALWFGAYLviSGELSVGDLVAFLSLFAQL 270
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
497-698 |
4.22e-21 |
|
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: 93.56 E-value: 4.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLA-----------YVSQQAWIF-HGNVRENILF 564
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHYALFrHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 565 G-------EKYNHQRYQHTVHvcglqkDLNSLPYGDLTECHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLLDDP 637
Cdd:cd03296 98 GlrvkprsERPPEAEIRAKVH------ELLKLVQLDWLADRYPA--------QLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 638 LSAVDAHVGKHvfeecIKKTLK------GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELME 698
Cdd:cd03296 164 FGALDAKVRKE-----LRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
491-697 |
8.20e-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: 92.75 E-value: 8.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSS---LISALL----------GQMQLQKGVVAVSGPLAYVSQQAWIF-HG 556
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTtmkMINRLIeptsgeifidGEDIREQDPVELRRKIGYVIQQIGLFpHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENI-----LfgEKYNHQRYQHTVHVCGLQKDLNSLPYGDltecHYPHlqigergvNLSGGQRQRISLARAVYANRQL 631
Cdd:cd03295 91 TVEENIalvpkL--LKWPKEKIRERADELLALVGLDPAEFAD----RYPH--------ELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 632 YLLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 697
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
493-696 |
8.59e-21 |
|
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: 92.24 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 493 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKG--------------------VVAVSGPLAYVSQQAW 552
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegevlldgkdiydldvdVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 IFHGNVRENILFGEKynhqryqhtVHVCGLQKDLNSLPYGDLTECHYP---HLQIGERGvnLSGGQRQRISLARAVYANR 629
Cdd:cd03260 92 PFPGSIYDNVAYGLR---------LHGIKLKEELDERVEEALRKAALWdevKDRLHALG--LSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 630 QLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKEL 696
Cdd:cd03260 161 EVLLLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
782-971 |
9.18e-21 |
|
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: 94.48 E-value: 9.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 782 TWKTYHTYIKASGGYLVsFLVLCLFFLMMGSSAFSTWwlgLW-LDSGSQVICAPQSNETACNVNQTLQDTKHHMYQLVYI 860
Cdd:cd18600 2 TWNTYLRYITSHKSLIF-VLILCLVIFAIEVAASLVG---LWlLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 861 ASMMSVLTFGIIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSM 940
Cdd:cd18600 78 GVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLI 157
|
170 180 190
....*....|....*....|....*....|.
gi 1958746143 941 VVFILVIMAASFPVVLVVLAGLAILfFILLR 971
Cdd:cd18600 158 VIGAITVVSILQPYIFLATVPVIIA-FIVLR 187
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
493-687 |
1.37e-20 |
|
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: 91.44 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 493 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG---------------PLAYVSQQAWIF-HG 556
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENILFGEKYNHQRYQHTVHVCGLQ--KDLNSLPYGDltecHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLL 634
Cdd:cd03262 92 TVLENITLAPIKVKGMSKAEAEERALEllEKVGLADKAD----AYPA--------QLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 635 DDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQF-LESCDEVILLEDGEI 687
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
494-698 |
1.59e-20 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 91.96 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWI---------FHG------- 556
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrrigmlFQGgalfdsl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENILFGEKynhqryQHT----------VHVC----GLQKDLNSLPygdltechyphlqiGErgvnLSGGQRQRISLA 622
Cdd:COG1127 98 TVFENVAFPLR------EHTdlseaeirelVLEKlelvGLPGAADKMP--------------SE----LSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 623 RAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 698
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDP-ITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
496-696 |
1.76e-20 |
|
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: 91.49 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG----------------PLAYVSQQAWIFHG-NV 558
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkarrRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENILF-------GEKYNHQRYQHTVHVCGLqkdlnslpyGDLTEcHYPHlqigergvNLSGGQRQRISLARAVYANRQL 631
Cdd:cd03258 100 FENVALpleiagvPKAEIEERVLELLELVGL---------EDKAD-AYPA--------QLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 632 YLLDDPLSAVDAHVGKHVFE--ECIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 696
Cdd:cd03258 162 LLCDEATSALDPETTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
494-687 |
1.83e-20 |
|
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: 90.78 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------P----LAYVSQQAWIF-HGNVREN 561
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlpPkdrdIAMVFQNYALYpHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGEKYNH-------QRYQHTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLL 634
Cdd:cd03301 93 IAFGLKLRKvpkdeidERVREVAELLQIEHLLD----------RKPK--------QLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 635 DDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 687
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAE-LKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
496-699 |
2.38e-20 |
|
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: 90.96 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------P-------LAYVSQQAWIFHG-NVRE 560
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglpPheraragIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKYNHQRyqhtvhvcGLQKDLNSLpYgDLtechYPHLQ--IGERGVNLSGGQRQRISLARAVYANRQLYLLDDP- 637
Cdd:cd03224 95 NLLLGAYARRRA--------KRKARLERV-Y-EL----FPRLKerRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPs 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 638 --LSAVdahVGKHVFeECIKKtLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:cd03224 161 egLAPK---IVEEIF-EAIRE-LRdeGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
496-722 |
4.71e-20 |
|
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: 94.97 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAW---------IF---------HG 556
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkDLTKLSRRSLrelrrrvqmVFqdpysslnpRM 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENI-----LFGEKYNHQRYQHTVHV---CGLQKDlnslpYGDLtechYPHlqigergvNLSGGQRQRISLARAVYAN 628
Cdd:COG1123 360 TVGDIIaeplrLHGLLSRAERRERVAELlerVGLPPD-----LADR----YPH--------ELSGGQRQRVAIARALALE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 629 RQLYLLDDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELmeergrya 704
Cdd:COG1123 423 PKLLILDEPTSALDVSVQAQIlnlLRD-LQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV-------- 492
|
250
....*....|....*...
gi 1958746143 705 klihnlrglqFKDPEHIY 722
Cdd:COG1123 493 ----------FANPQHPY 500
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
491-698 |
5.38e-20 |
|
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: 94.97 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLG---QMQLQKGVVAVSGP-------------LAYVSQQAW-- 552
Cdd:COG1123 16 GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMtq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 IFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAV 625
Cdd:COG1123 96 LNPVTVGDQIAEAlenlglsRAEARARVLELLEAVGLERRLD----------RYPH--------QLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 626 YANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELME 698
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDL-LRELQRerGTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
497-699 |
9.46e-20 |
|
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: 90.40 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQA----------WIF-------HGNV 558
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqDIAAMSRKElrelrrkkisMVFqsfallpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENILFG-------EKYNHQRYQHTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAVYANRQL 631
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEH----------KYPD--------ELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 632 YLLDDPLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
462-687 |
1.11e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.13 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 462 RHVFKKQRAELYSEQSLSDQGVASPERQSGsPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVS 541
Cdd:cd03220 4 ENVSKSYPTYKGGSSSLKKLGILGRKGEVG-EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 542 GplayvsQQAWI------FHGN--VRENILFG-------EKYNHQRYQHTVHVCGLQKDLNsLPYGdltechyphlqige 606
Cdd:cd03220 83 G------RVSSLlglgggFNPEltGRENIYLNgrllglsRKEIDEKIDEIIEFSELGDFID-LPVK-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 607 rgvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvgkhvF-EECIKK----TLKGKTVVLVTHQLQFLES-CDEVI 680
Cdd:cd03220 142 ---TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA-----FqEKCQRRlrelLKQGKTVILVSHDPSSIKRlCDRAL 213
|
....*..
gi 1958746143 681 LLEDGEI 687
Cdd:cd03220 214 VLEKGKI 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
491-700 |
1.57e-19 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 89.16 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPL----------AYVSQQAWIFHG---- 556
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrQLRRQIGMIFQQfnli 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 ---NVRENILFGekynhqR--YQHTVHVC-GL------QKDLNSLPYGDLTECHYphlqigERGVNLSGGQRQRISLARA 624
Cdd:cd03256 91 erlSVLENVLSG------RlgRRSTWRSLfGLfpkeekQRALAALERVGLLDKAY------QRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 625 VYANRQLYLLDDPLSAVD---AHVGKHVFEEcIKKTlKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:cd03256 159 LMQQPKLILADEPVASLDpasSRQVMDLLKR-INRE-EGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
490-696 |
3.49e-19 |
|
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: 87.56 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 490 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------------PLAYVSQQAWIFHG- 556
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENI-LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDlTECHyphlqigergvNLSGGQRQRISLARAVYANRQLYLLD 635
Cdd:cd03263 91 TVREHLrFYARLKGLPKSEIKEEVELLLRVLGLTDKAN-KRAR-----------TLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 636 DPLSAVDaHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 696
Cdd:cd03263 159 EPTSGLD-PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
496-698 |
6.96e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.07 E-value: 6.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSL---ISAL--LGQMQLQKGVVAVSGPLA----------YVSQQAWIF-HGNVR 559
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLeeITSGDLIVDGLKVNDPKVderlirqeagMVFQQFYLFpHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFGekynhqryqhTVHVCGLQK-DLNSLPYGDLTEC-------HYPHlqigergvNLSGGQRQRISLARAVYANRQL 631
Cdd:PRK09493 96 ENVMFG----------PLRVRGASKeEAEKQARELLAKVglaerahHYPS--------ELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 632 YLLDDPLSAVDAHVGKHVFEecIKKTL--KGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELME 698
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLK--VMQDLaeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
483-687 |
7.15e-19 |
|
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: 85.68 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 483 VASPERQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ--KGVVAVSGP----------LAYVSQQ 550
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRpldkrsfrkiIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 551 AwIFHGN--VRENILFGEKYnhqryqhtvhvcglqkdlnslpygdltechyphlqigeRGvnLSGGQRQRISLARAVYAN 628
Cdd:cd03213 91 D-ILHPTltVRETLMFAAKL--------------------------------------RG--LSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 629 RQLYLLDDPLSAVDAHVGKHVFeecikKTLK-----GKTVVLVTHQL--QFLESCDEVILLEDGEI 687
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVM-----SLLRrladtGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
462-708 |
8.72e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.06 E-value: 8.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 462 RHVFKKQRAELYSEQSLSDQgVASPERQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVS 541
Cdd:COG1134 8 ENVSKSYRLYHEPSRSLKEL-LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 542 G----PLAYvsqqAWIFHGN--VRENILFG-------EKYNHQRYQHTVHVCGLQKDLNsLPYGdltecHYphlqigerg 608
Cdd:COG1134 87 GrvsaLLEL----GAGFHPEltGRENIYLNgrllglsRKEIDEKFDEIVEFAELGDFID-QPVK-----TY--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 609 vnlSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvgkhvF-EECIKK----TLKGKTVVLVTHQLQFLES-CDEVILL 682
Cdd:COG1134 148 ---SSGMRARLAFAVATAVDPDILLVDEVLAVGDAA-----FqKKCLARirelRESGRTVIFVSHSMGAVRRlCDRAIWL 219
|
250 260
....*....|....*....|....*.
gi 1958746143 683 EDGEICEKGTHKELMEergRYAKLIH 708
Cdd:COG1134 220 EKGRLVMDGDPEEVIA---AYEALLA 242
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
495-707 |
1.00e-18 |
|
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: 87.60 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALL------GQMQLQkGVVAVSGPL-------AYVSQQAWIFHGNVREN 561
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQID-GVSWNSVPLqkwrkafGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGEKYNHQRYQHTVHVCGLQKDLNSLPyGDLtechypHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEEVGLKSVIEQFP-GQL------DFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 642 DAhvgkhVFEECIKKTLK----GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 707
Cdd:cd03289 170 DP-----ITYQVIRKTLKqafaDCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
499-687 |
1.91e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 88.23 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------------PLAYVSQQAWIF-HGNVRE 560
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFpHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKY-----NHQRYQHTVHVCGLqkdlnslpyGDLTEcHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLLD 635
Cdd:COG4148 97 NLLYGRKRapraeRRISFDEVVELLGI---------GHLLD-RRPA--------TLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 636 DPLSAVDAHVgKHvfeECIK--KTLKGKT---VVLVTHQLQFLES-CDEVILLEDGEI 687
Cdd:COG4148 159 EPLAALDLAR-KA---EILPylERLRDELdipILYVSHSLDEVARlADHVVLLEQGRV 212
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
189-412 |
2.45e-18 |
|
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: 86.88 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 189 YRTAIRLKVALSTLIFKNLL----SFKTLThiSAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFILGSTA 264
Cdd:cd18559 63 SIGGIFASRAVHLDLYHKALrspiSFFERT--PSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 265 LVGICVYLIFIPIQMFMAKLNSAFRRSAISVTDKRVQTMNEFLTCIKLIKMYAWEKSFMNTIHDIRKREKKLLEKAGYVQ 344
Cdd:cd18559 141 AVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLR 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 345 SGNSALAPIVSTIAIVSTFTCHIFLKRT--LTAPVAFSVIAMFNVMKFSIAILPFSVKAVAEASVSLRRM 412
Cdd:cd18559 221 ALAVRLWCVGPCIVLFASFFAYVSRHSLagLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
496-699 |
2.52e-18 |
|
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: 85.37 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVRENIL 563
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlpphkrPVNTVFQNYALFpHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 FG-------EKYNHQRYQHTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:cd03300 95 FGlrlkklpKAEIKERVAEALDLVQLEGYAN----------RKPS--------QLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 637 PLSAVDAHVGKHVFEEC--IKKTLkGKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:cd03300 157 PLGALDLKLRKDMQLELkrLQKEL-GITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
496-702 |
4.00e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 84.66 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL--------------AYVSQQAWIF-HGNVR 559
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGeDLtdskkdinklrrkvGMVFQQFNLFpHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFGekynhqryqhTVHVCGLQKD---------LNSLPYGDLTEcHYPHlqigergvNLSGGQRQRISLARAVYANRQ 630
Cdd:COG1126 96 ENVTLA----------PIKVKKMSKAeaeeramelLERVGLADKAD-AYPA--------QLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 631 LYLLDDPLSAVDAhvgkhvfeECIKKTLK--------GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELME--- 698
Cdd:COG1126 157 VMLFDEPTSALDP--------ELVGEVLDvmrdlakeGMTMVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFFEnpq 228
|
....*
gi 1958746143 699 -ERGR 702
Cdd:COG1126 229 hERTR 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
496-682 |
4.24e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.44 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG--PLAYVSQQ---AWIFHGNVRENILFGekynh 570
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMG----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 571 qRYQHTvhvcGLQKDLNSLPYGDLTEC-------HYPHLQIGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 643
Cdd:NF040873 82 -RWARR----GLWRRLTRDDRAAVDDAlervglaDLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958746143 644 HVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILL 682
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
496-696 |
6.30e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 86.67 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------P----LAYVSQQAWIF-HGNVRENIL 563
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdlpPkdrnIAMVFQSYALYpHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 FGEKYN-------HQRYQHTVHVCGLQKDLNSLPYgdltechyphlqigergvNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:COG3839 98 FPLKLRkvpkaeiDRRVREAAELLGLEDLLDRKPK------------------QLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 637 PLSAVDAHVgKHVFEECIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 696
Cdd:COG3839 160 PLSNLDAKL-RVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
495-683 |
1.41e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.16 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP----------LAYVSQQA---WIFHGNVREN 561
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGeKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchYPHLQIGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:PRK15056 101 VMMG-RYGHMGWLRRAKKRDRQIVTAALARVDMVE--FRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958746143 642 DAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLE 683
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTVMVK 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
494-687 |
1.84e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 81.32 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHG---------------- 556
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkPVTRRSPRDAIRAGiayvpedrkreglvld 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 -NVRENILfgekynhqryqhtvhvcglqkdLNSLpygdltechyphlqigergvnLSGGQRQRISLARAVYANRQLYLLD 635
Cdd:cd03215 93 lSVAENIA----------------------LSSL---------------------LSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 636 DPLSAVDahVG--KHVFEECIKKTLKGKTVVLVTHQLQ-FLESCDEVILLEDGEI 687
Cdd:cd03215 130 EPTRGVD--VGakAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
494-697 |
2.89e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.86 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWI-FHGNVR 559
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrPLaawspwelarrrAVLPQHSSLaFPFTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFGeKYNHQRY--------QHTVHVCGLQkdlnslpygDLTECHYPHLqigergvnlSGGQRQRISLARA------- 624
Cdd:COG4559 94 EVVALG-RAPHGSSaaqdrqivREALALVGLA---------HLAGRSYQTL---------SGGEQQRVQLARVlaqlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 625 VYANRQLYLLDDPLSAVD-AHVgKHVFEecIKKTL--KGKTVVLVTHQL----QFlesCDEVILLEDGEICEKGTHKELM 697
Cdd:COG4559 155 VDGGPRWLFLDEPTSALDlAHQ-HAVLR--LARQLarRGGGVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
496-687 |
3.18e-17 |
|
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: 80.17 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHGnVRenilfgekynhqryq 574
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkEVSFASPRDARRAG-IA--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 575 hTVHvcglqkdlnslpygdltechyphlQigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecI 654
Cdd:cd03216 79 -MVY------------------------Q-------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--V 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958746143 655 KKTLK--GKTVVLVTHQLQ-FLESCDEVILLEDGEI 687
Cdd:cd03216 125 IRRLRaqGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
496-698 |
3.25e-17 |
|
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: 82.00 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------P----LAYVSQQAWIF-HGNVRENIL 563
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlpPekrdISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 FGEKYN-------HQRYQHTVHVCGLQKDLNSLPygdltechyphlqigergVNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:cd03299 94 YGLKKRkvdkkeiERKVLEIAEMLGIDHLLNRKP------------------ETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 637 PLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 698
Cdd:cd03299 156 PFSALDVRTKEKLREE-LKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
496-701 |
3.79e-17 |
|
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: 87.31 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVRENI 562
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEChyphlqiGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 642
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEC-------AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 643 AHVgKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 701
Cdd:TIGR00957 1454 LET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
496-689 |
4.69e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 81.25 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLA---------------YVSQQAW-IFHGNV 558
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqDLSrlkrreipylrrrigVVFQDFRlLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENILFG---EKYNHQRYQHTVH-----VcGLQKDLNSLPYgdltechyphlqigergvNLSGGQRQRISLARAVyANR- 629
Cdd:COG2884 97 YENVALPlrvTGKSRKEIRRRVRevldlV-GLSDKAKALPH------------------ELSGGEQQRVAIARAL-VNRp 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 630 QLYLLDDPLSAVDAHVGK---HVFEEcIKKTlkGKTVVLVTHQLQFLESCDE-VILLEDGEICE 689
Cdd:COG2884 157 ELLLADEPTGNLDPETSWeimELLEE-INRR--GTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
496-719 |
5.24e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 86.72 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVRENI 562
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 -LFGEkYNHQRYQHTVHVCGLQKDLNSLPYGDLTEchyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:PLN03130 1334 dPFNE-HNDADLWESLERAHLKDVIRRNSLGLDAE-------VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 642 DahVGKHVF-EECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL-MEERGRYAKLIHN--------LR 711
Cdd:PLN03130 1406 D--VRTDALiQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQStgaanaqyLR 1483
|
....*...
gi 1958746143 712 GLQFKDPE 719
Cdd:PLN03130 1484 SLVFGGDE 1491
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
493-687 |
9.39e-17 |
|
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: 80.02 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 493 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIF----HG-----NVRENI 562
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkPLDIAARNRIGYlpeeRGlypkmKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 L-FGE--KYNHQRYQHTVhvcglQKDLNSLPYGDLTEchyphlqigERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:cd03269 92 VyLAQlkGLKKEEARRRI-----DEWLERLELSEYAN---------KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958746143 640 AVDAhVGKHVFEECIKKTL-KGKTVVLVTHQLQFLES-CDEVILLEDGEI 687
Cdd:cd03269 158 GLDP-VNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
491-699 |
1.08e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------PLAYVSQQAWIFHGN------ 557
Cdd:PRK13644 14 GTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsKLQGIRKLVGIVFQNpetqfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 ---VRENILFGEKyN--------HQRYQHTVHVCGLQKDLNSLPYgdltechyphlqigergvNLSGGQRQRISLARAVY 626
Cdd:PRK13644 92 grtVEEDLAFGPE-NlclppieiRKRVDRALAEIGLEKYRHRSPK------------------TLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 627 ANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
499-700 |
1.22e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.18 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVRENILFG- 565
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppaerPVSMLFQENNLFpHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 566 ---EKYN---HQRYQHTVHVCGLQKDLNSLPYgdltechyphlqigergvNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:COG3840 97 rpgLKLTaeqRAQVEQALERVGLAGLLDRLPG------------------QLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 640 AVD-------AHVGKHVFEEcikktlKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:COG3840 159 ALDpalrqemLDLVDELCRE------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
494-699 |
1.28e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.07 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVREN 561
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvpaenrHVNTVFQSYALFpHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGEKynhqryqhtvhvcgLQKdlnslpygdltechYPHLQIGERgV------------------NLSGGQRQRISLAR 623
Cdd:PRK09452 107 VAFGLR--------------MQK--------------TPAAEITPR-VmealrmvqleefaqrkphQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 624 AVYANRQLYLLDDPLSAVDAHVGKHVFEEcIK---KTLkGKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNE-LKalqRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
490-682 |
1.30e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.06 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 490 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV-----AVSGPLAyvsQQAWIF--HG-----N 557
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgvPVTGPGA---DRGVVFqkDAllpwlN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENILFGEKYN-------HQRYQHTVHVCGLQkdlnslpygdltecHYPHLQIGErgvnLSGGQRQRISLARAVYANRQ 630
Cdd:COG4525 93 VLDNVAFGLRLRgvpkaerRARAEELLALVGLA--------------DFARRRIWQ----LSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 631 LYLLDDPLSAVDAHVGKHVFE---ECIKKTlkGKTVVLVTHQLQ---FLEScdEVILL 682
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQElllDVWQRT--GKGVFLITHSVEealFLAT--RLVVM 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
500-697 |
1.68e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 82.47 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 500 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------------PLAYVSQQAWIF-HGNVREN 561
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGEK-----YNHQRYQHTVHVCGLQkdlnslpygdltechypHLQigERGVN-LSGGQRQRISLARAVYANRQLYLLD 635
Cdd:TIGR02142 96 LRYGMKrarpsERRISFERVIELLGIG-----------------HLL--GRLPGrLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 636 DPLSAVDAHVGKHV--FEECIKKTLkGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 697
Cdd:TIGR02142 157 EPLAALDDPRKYEIlpYLERLHAEF-GIPILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
494-707 |
2.37e-16 |
|
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: 84.58 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALL------GQMQLQkGVVAVSGPL-------AYVSQQAWIFHGNVRE 560
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLrllsteGEIQID-GVSWNSVTLqtwrkafGVIPQKVFIFSGTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPyGDLtechypHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSA 640
Cdd:TIGR01271 1311 NLDPYEQWSDEEIWKVAEEVGLKSVIEQFP-DKL------DFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 641 VDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 707
Cdd:TIGR01271 1384 LDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
494-689 |
3.05e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 79.85 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYV---SQQAW------IFHG-----NV 558
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqDLYQLdrkQRRAFrrdvqlVFQDspsavNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENI--LFGEKYNH----------QRYQHTVHVCGLQ-KDLNSLPygdltechyphlqigergVNLSGGQRQRISLARAV 625
Cdd:TIGR02769 104 RMTVrqIIGEPLRHltsldeseqkARIAELLDMVGLRsEDADKLP------------------RQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 626 YANRQLYLLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICE 689
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKlQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
495-687 |
3.07e-16 |
|
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: 79.01 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQA----------WIF-------HG 556
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqDLFALDEDArarlrarhvgFVFqsfqllpTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENI-----LFGEKYNHQRYQHTVHVCGLQKDLNslpygdltecHYPHlQigergvnLSGGQRQRISLARAVYANRQL 631
Cdd:COG4181 106 TALENVmlpleLAGRRDARARARALLERVGLGHRLD----------HYPA-Q-------LSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 632 YLLDDPLSAVDAHVGKHV----FEecIKKTlKGKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:COG4181 168 LFADEPTGNLDAATGEQIidllFE--LNRE-RGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
488-707 |
4.10e-16 |
|
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: 79.57 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIF 554
Cdd:cd03288 28 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 HGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPyGDLTEChyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLL 634
Cdd:cd03288 108 SGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLP-GGLDAV------VTEGGENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 635 DDPLSAVDAHVgKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM-EERGRYAKLI 707
Cdd:cd03288 181 DEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
512-699 |
9.64e-16 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 79.46 E-value: 9.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 512 ICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVRENILFGEKYNHQ-RYQHTVH 578
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvtnvpphlrHINMVFQSYALFpHMTVEENVAFGLKMRKVpRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 579 VCGLQKDLNSLPYGDltecHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECikKTL 658
Cdd:TIGR01187 81 VLEALRLVQLEEFAD----RKPH--------QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL--KTI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958746143 659 K---GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:TIGR01187 147 QeqlGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
496-715 |
9.72e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.13 E-value: 9.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-----------LAYVSQQAWIF-HGNVRENIL 563
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHYALFrHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 FGEKYNHQRYQHTVHVcgLQKDLNSLpygdLTECHYPHLqiGER-GVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 642
Cdd:PRK10851 97 FGLTVLPRRERPNAAA--IKAKVTQL----LEMVQLAHL--ADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 643 AHVGK-------HVFEEcikktLKgKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL---------MEERGRYAK 705
Cdd:PRK10851 169 AQVRKelrrwlrQLHEE-----LK-FTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepatrfvLEFMGEVNR 242
|
250
....*....|
gi 1958746143 706 LIHNLRGLQF 715
Cdd:PRK10851 243 LQGTIRGGQF 252
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
497-684 |
1.29e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.75 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQlqkGVVAVSG------------P-----LAYVSQQAWIF-HGNV 558
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLS---PAFSASGevllngrrltalPaeqrrIGILFQDDLLFpHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENILFG--EKYNHQRYQHTVhvcglQKDLNSLPYGDLtECHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:COG4136 94 GENLAFAlpPTIGRAQRRARV-----EQALEEAGLAGF-ADRDPA--------TLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 637 PLSAVDAH----VGKHVFEECIKKTLkgkTVVLVTHQLQFLESCDEVILLED 684
Cdd:COG4136 160 PFSKLDAAlraqFREFVFEQIRQRGI---PALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
801-968 |
1.69e-15 |
|
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: 78.07 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 801 LVLCLFFLMMGS--SAFSTWWLGLWLDSGSqvicaPQSNETACNVNQTLqdtkhhmYQLVYIASMMSVLTFgiIKGFTFT 878
Cdd:pfam00664 1 LILAILLAILSGaiSPAFPLVLGRILDVLL-----PDGDPETQALNVYS-------LALLLLGLAQFILSF--LQSYLLN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 879 NTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVV-LV 957
Cdd:pfam00664 67 HTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLV 146
|
170
....*....|.
gi 1958746143 958 VLAGLAILFFI 968
Cdd:pfam00664 147 LLAVLPLYILV 157
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
496-669 |
1.90e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP----LAYVSQQAWIFHGN-------VRENILF 564
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYLGHRNamkpaltVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 565 GEKYNHQRyQHTVHVC----GLQkDLNSLPYGdltechyphlqigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSA 640
Cdd:PRK13539 97 WAAFLGGE-ELDIAAAleavGLA-PLAHLPFG-----------------YLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|
gi 1958746143 641 VDAHvGKHVFEECIKKTLK-GKTVVLVTHQ 669
Cdd:PRK13539 158 LDAA-AVALFAELIRAHLAqGGIVIAATHI 186
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
487-696 |
2.18e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 487 ERQSgSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV----SGPLAYVSQQAW---------- 552
Cdd:PRK13631 33 EKQE-NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITnpyskkiknf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 -----------------IFHGNVRENILFG------EKYN-HQRYQHTVHVCGLQKD-LNSLPYGdltechyphlqiger 607
Cdd:PRK13631 112 kelrrrvsmvfqfpeyqLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLDDSyLERSPFG--------------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 608 gvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDG 685
Cdd:PRK13631 177 ---LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKAnNKTVFVITHTMeHVLEVADEVIVMDKG 252
|
250
....*....|.
gi 1958746143 686 EICEKGTHKEL 696
Cdd:PRK13631 253 KILKTGTPYEI 263
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
492-691 |
2.74e-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: 75.87 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 492 SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------PLAyVSQQAWIFHGN-------- 557
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkePAE-ARRRLGFVSDStglydrlt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENIL-FGEKYNHQRYQHTVHVCGLQKDLNSLPYGDltechyphlqigERGVNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:cd03266 95 ARENLEyFAGLYGLKGDELTARLEELADRLGMEELLD------------RRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 637 PLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 691
Cdd:cd03266 163 PTTGLDVMATRALRE--FIRQLRalGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
494-698 |
3.96e-15 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 76.04 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------P--------LAYVSQQAWIFHG-NV 558
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklPmhkrarlgIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENIL-------FGEKYNHQRyqhtvhvcglqkdLNSLpygdLTECHYPHLQiGERGVNLSGGQRQRISLARAVYANRQL 631
Cdd:cd03218 93 EENILavleirgLSKKEREEK-------------LEEL----LEEFHITHLR-KSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 632 YLLDDPLSAVDAhvgKHVFE-ECIKKTLKGKTV-VLVT-HQL-QFLESCDEVILLEDGEICEKGTHKELME 698
Cdd:cd03218 155 LLLDEPFAGVDP---IAVQDiQKIIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
496-697 |
4.08e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.55 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP--------------------------LAYVSQ 549
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlkvadknqlrllrtrLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 550 QAWIF-HGNVRENILfgekynhqryQHTVHVCGLQKD---------LNSLPYGDLTECHYPhlqigergVNLSGGQRQRI 619
Cdd:PRK10619 100 HFNLWsHMTVLENVM----------EAPIQVLGLSKQeareravkyLAKVGIDERAQGKYP--------VHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 620 SLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 697
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
482-691 |
4.71e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.36 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 482 GVASPERQ-----SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLayvsqqawifHG 556
Cdd:PRK15134 282 QVAFPIRKgilkrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPL----------HN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENILfgekynhqRYQHTVHVcgLQKDLNSLPYGDLT---------ECHYPHLQIGERG---------VNL------- 611
Cdd:PRK15134 352 LNRRQLL--------PVRHRIQV--VFQDPNSSLNPRLNvlqiieeglRVHQPTLSAAQREqqviavmeeVGLdpetrhr 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 612 -----SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGK---TVVLVTHQLQFLES-CDEVILL 682
Cdd:PRK15134 422 ypaefSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA--LLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVL 499
|
....*....
gi 1958746143 683 EDGEICEKG 691
Cdd:PRK15134 500 RQGEVVEQG 508
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
494-700 |
7.01e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-------------LAYVSQQAWIFHG-NVR 559
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFGekynhqRYQHTVHVCGLQKDLNSLPYGDLTECHYPHLqiGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPL 638
Cdd:PRK11231 95 ELVAYG------RSPWLSLWGRLSAEDNARVNQAMEQTRINHL--ADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 639 SAVDAHvgkHVFEecIKKTL-----KGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:PRK11231 167 TYLDIN---HQVE--LMRLMrelntQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
497-698 |
7.12e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.21 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGpLAYVSQQAW--------IFHG--------NVRE 560
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmVFQNpdnqfvgaTVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKyNHQ--------RYQHTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAVYANRQLY 632
Cdd:PRK13635 102 DVAFGLE-NIGvpreemveRVDQALRQVGMEDFLN----------REPH--------RLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 633 LLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 698
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLE--TVRQLKeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
496-698 |
8.32e-15 |
|
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: 75.02 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------P-------LAYVSQQAWIFHG-NVRE 560
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpPhriarlgIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGE--KYNHQRYQHTV-HVCGLqkdlnslpygdltechYPHLQ--IGERGVNLSGGQRQRISLARAVYANRQLYLLD 635
Cdd:COG0410 98 NLLLGAyaRRDRAEVRADLeRVYEL----------------FPRLKerRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 636 DP---LSAVdahVGKHVFeECIKKtLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELME 698
Cdd:COG0410 162 EPslgLAPL---IVEEIF-EIIRR-LNreGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
488-699 |
1.03e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.79 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHG---------- 556
Cdd:PRK13536 48 SKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvPVPARARLARARIGvvpqfdnldl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 --NVRENIL-FGekynhqRYqhtvhvCGLQKDLNSLPYGDLTECHYPHLQIGERGVNLSGGQRQRISLARAVYANRQLYL 633
Cdd:PRK13536 128 efTVRENLLvFG------RY------FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 634 LDDPLSAVDAHvGKHVFEECIKKTL-KGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 699
Cdd:PRK13536 196 LDEPTTGLDPH-ARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
494-686 |
1.35e-14 |
|
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: 71.71 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPL--AYVSQqawifhgnvrenilfgekynhq 571
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVkiGYFEQ---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 572 ryqhtvhvcglqkdlnslpygdltechyphlqigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFE 651
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALE 110
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958746143 652 ECIKKtLKGkTVVLVTHQLQFLES-CDEVILLEDGE 686
Cdd:cd03221 111 EALKE-YPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
489-682 |
1.65e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 489 QSGSPKsVLHNISFVVRKGKVLGICGNVGSGKS-------SLISALLGQMQLQKGVVAVSGPLAY---VS---QQAWIFH 555
Cdd:PRK10247 16 LAGDAK-ILNNISFSLRAGEFKLITGPSGCGKStllkivaSLISPTSGTLLFEGEDISTLKPEIYrqqVSycaQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 556 GNVRENILFGEKYNHQRYQHTVhvcgLQKDLN--SLPygdltechyphLQIGERGVN-LSGGQRQRISLARAVYANRQLY 632
Cdd:PRK10247 95 DTVYDNLIFPWQIRNQQPDPAI----FLDDLErfALP-----------DTILTKNIAeLSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 633 LLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQLQFLESCDEVILL 682
Cdd:PRK10247 160 LLDEITSALDES-NKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
494-702 |
1.86e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.40 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL------------LGQMQL--------QKGVV-AVSGPLAYVSQQAW 552
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIdtarslsqQKGLIrQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 IF-HGNVRENILFG--------EKYNHQRYQHTVHVCGLQKDLNSlpygdltechYPHlqigergvNLSGGQRQRISLAR 623
Cdd:PRK11264 96 LFpHRTVLENIIEGpvivkgepKEEATARARELLAKVGLAGKETS----------YPR--------RLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 624 AVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELM----E 698
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFadpqQ 237
|
....
gi 1958746143 699 ERGR 702
Cdd:PRK11264 238 PRTR 241
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
489-724 |
4.95e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 73.66 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 489 QSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------------PLAYVSQ 549
Cdd:PRK13646 13 QKGTPyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 550 --QAWIFHGNVRENILFGEKynhqRYQHTVhvcglqKDLNSLPYGDLTECHYPHLQIGERGVNLSGGQRQRISLARAVYA 627
Cdd:PRK13646 93 fpESQLFEDTVEREIIFGPK----NFKMNL------DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 628 NRQLYLLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERGRYA 704
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQ-SKRQVMRLLKSlqTDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLA 241
|
250 260
....*....|....*....|...
gi 1958746143 705 KL---IHNLRGLQfKDPEHIYNV 724
Cdd:PRK13646 242 DWhigLPEIVQLQ-YDFEQKYQT 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
494-689 |
8.43e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.80 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAW-IFHGNVRenILFGEKYNHQ 571
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGePLAKLNRAQRkAFRRDIQ--MVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 572 RYQHTV---------HVCGLQKD------LNSLPYGDLTECHyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:PRK10419 103 NPRKTVreiireplrHLLSLDKAerlaraSEMLRAVDLDDSV-----LDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 637 PLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGEICE 689
Cdd:PRK10419 178 AVSNLDLVLQAGVIR--LLKKLQqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
488-692 |
9.49e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.57 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGqmqLQK---GVVAVSG-PLAYVSQQAW---------IF 554
Cdd:COG1135 12 PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LERptsGSVLVDGvDLTALSERELraarrkigmIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 -HGN------VRENILF-------GEKYNHQRYQHTVHVCGLQKDLNSlpygdltechYPHlqigergvNLSGGQRQRIS 620
Cdd:COG1135 89 qHFNllssrtVAENVALpleiagvPKAEIRKRVAELLELVGLSDKADA----------YPS--------QLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 621 LARAVYANRQLYLLDDPLSAVDAHVGKHVFE---EcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 692
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDllkD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
496-669 |
1.03e-13 |
|
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: 70.85 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLA-----YVSQQAWIFHGN-------VRENI 562
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtPLAeqrdePHENILYLGHLPglkpelsALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 LFgekYN--HQRYQHTVHvcglqkdlNSLPYGDLTecHYPHLQIGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSA 640
Cdd:TIGR01189 95 HF---WAaiHGGAQRTIE--------DALAAVGLT--GFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|
gi 1958746143 641 VDAHvGKHVFEECIKKTL-KGKTVVLVTHQ 669
Cdd:TIGR01189 158 LDKA-GVALLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
494-692 |
1.09e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.11 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL------------AYVSQQAWI-FHGNVR 559
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrPLadwspaelarrrAVLPQHSSLsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFGekynhqRYQHTvhvcGLQKDLNSLP--YGDLTEC------HYPHlqigergvnLSGGQRQRISLARA------V 625
Cdd:PRK13548 95 EVVAMG------RAPHG----LSRAEDDALVaaALAQVDLahlagrDYPQ---------LSGGEQQRVQLARVlaqlweP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 626 YANRQLYLLDDPLSAVD-AHvGKHVFEecIKKTL---KGKTVVLVTHQL----QFlesCDEVILLEDGEICEKGT 692
Cdd:PRK13548 156 DGPPRWLLLDEPTSALDlAH-QHHVLR--LARQLaheRGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
494-699 |
1.56e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.65 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQawifhgN--- 557
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQE------Nhin 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 ----VRENILFGekynhqRYQHT---------VHVcglqkDlNSLPYGDLTEchYPHLQIGErgvnLSGGQRQRISLArA 624
Cdd:COG4604 88 srltVRELVAFG------RFPYSkgrltaedrEII-----D-EAIAYLDLED--LADRYLDE----LSGGQRQRAFIA-M 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 625 VYANRQLY-LLDDPLSAVDAhvgKHVFEecIKKTLK------GKTVVLVTHQLQFlESC--DEVILLEDGEICEKGTHKE 695
Cdd:COG4604 149 VLAQDTDYvLLDEPLNNLDM---KHSVQ--MMKLLRrladelGKTVVIVLHDINF-ASCyaDHIVAMKDGRVVAQGTPEE 222
|
....
gi 1958746143 696 LMEE 699
Cdd:COG4604 223 IITP 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
494-685 |
1.79e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.65 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGV-----VAVSGPLA---YVSQQ----AWIfhgNVREN 561
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgKPVEGPGAergVVFQNegllPWR---NVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGEKY----NHQRyqhtvhvcgLQKDLNSLPYGDLTEchyphlqIGERGV-NLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:PRK11248 91 VAFGLQLagveKMQR---------LEIAHQMLKKVGLEG-------AEKRYIwQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 637 PLSAVDAHVGKHVFEECIK---KTlkGKTVVLVTHQLQ---FLEScdEVILLEDG 685
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKlwqET--GKQVLLITHDIEeavFMAT--ELVLLSPG 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
496-692 |
3.17e-13 |
|
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: 70.54 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVA-----VSGPLAYVS---------QQAWIFHG-NVRE 560
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGLPPHEIarlgigrtfQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTECHYPHLQiGERGVNLSGGQRQRISLARAVYANRQLYLLDDP--- 637
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLA-DRPAGELSYGQQRRLEIARALATDPKLLLLDEPaag 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 638 LSAVDAHVGKHVFEEcIKKtlKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 692
Cdd:cd03219 174 LNPEETEELAELIRE-LRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
488-698 |
3.52e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.76 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHG---------- 556
Cdd:PRK13537 14 EKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGePVPSRARHARQRVGvvpqfdnldp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 --NVRENIL-FGEKYNHQRYQHTVHVCGLqkdlnsLPYGDLTEchYPHLQIGErgvnLSGGQRQRISLARAVYANRQLYL 633
Cdd:PRK13537 94 dfTVRENLLvFGRYFGLSAAAARALVPPL------LEFAKLEN--KADAKVGE----LSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 634 LDDPLSAVDAHvGKHVFEECIKKTL-KGKTVVLVTHqlqFLES----CDEVILLEDGEICEKGTHKELME 698
Cdd:PRK13537 162 LDEPTTGLDPQ-ARHLMWERLRSLLaRGKTILLTTH---FMEEaerlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
504-691 |
3.86e-13 |
|
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: 69.44 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 504 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVRENILFGE----K 567
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadrPVSMLFQENNLFaHLTVEQNVGLGLspglK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 568 YNHQRyQHTVHVC----GLQKDLNSLPygdltechyphlqiGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD- 642
Cdd:cd03298 101 LTAED-RQAIEVAlarvGLAGLEKRLP--------------GE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDp 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 643 ---AHVGKHVFEECIKktlKGKTVVLVTHQLQFLESCDE-VILLEDGEICEKG 691
Cdd:cd03298 162 alrAEMLDLVLDLHAE---TKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
496-687 |
3.99e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.60 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG---------PLAYVSQQ--AWIFHgnvRENILf 564
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvatldadALAQLRREhfGFIFQ---RYHLL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 565 gekyNHQRYQHTVHV----CGLQKD---------LNSLPYGDltechyphlQIGERGVNLSGGQRQRISLARAVYANRQL 631
Cdd:PRK10535 99 ----SHLTAAQNVEVpavyAGLERKqrllraqelLQRLGLED---------RVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 632 YLLDDPLSAVDAHVGKHVFeeCIKKTL--KGKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVM--AILHQLrdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
492-699 |
4.56e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.98 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 492 SPKSVLHNISFVVRKGKVLGICGNVGSGKSS---LISALLGQMQLQKGVVAVSGpLAYVSQQAW--------IFH----- 555
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWdirekvgiVFQnpdnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 556 ---GNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDltechyphlqigERGVNLSGGQRQRISLARAVYANRQL 631
Cdd:PRK13640 97 fvgATVGDDVAFGlENRAVPRPEMIKIVRDVLADVGMLDYID------------SEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 632 YLLDDPLSAVDAHvGKHVFEECIKKTLKGK--TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:PRK13640 165 IILDESTSMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
496-697 |
6.35e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 70.25 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQA------WIFHG-----NVRENIl 563
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhKLEYGDYKYrckhirMIFQDpntslNPRLNI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 564 fGE------KYN--------HQRYQHTVHVCGLQKDlnslpygdltecH---YPHLqigergvnLSGGQRQRISLARAVY 626
Cdd:COG4167 107 -GQileeplRLNtdltaeerEERIFATLRLVGLLPE------------HanfYPHM--------LSSGQKQRVALARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 627 ANRQLYLLDDPLSAVDAHVGKhvfeECIKKTLK-----GKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 697
Cdd:COG4167 166 LQPKIIIADEALAALDMSVRS----QIINLMLElqeklGISYIYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVF 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
499-722 |
6.38e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVRENILFGe 566
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshvppyqrPINMMFQSYALFpHMTVEQNIAFG- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 567 kynhqryqhtvhvcgLQKDlnSLPYGDLTE-----CHYPHLQ--IGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:PRK11607 116 ---------------LKQD--KLPKAEIASrvnemLGLVHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 640 AVDahvgkhvfeecikKTLKGKTvvlvthQLQFLEscdevILLEDGEICEKGTH--KELMEERGRYAklIHNlRG--LQF 715
Cdd:PRK11607 179 ALD-------------KKLRDRM------QLEVVD-----ILERVGVTCVMVTHdqEEAMTMAGRIA--IMN-RGkfVQI 231
|
....*..
gi 1958746143 716 KDPEHIY 722
Cdd:PRK11607 232 GEPEEIY 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
494-687 |
6.44e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKG-VVAVSGPLAYVS-------QQA----WifhGNVREN 561
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGeLLAGTAPLAEARedtrlmfQDArllpW---KKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGEKYN-HQRYQHTVHVCGLQKDLNSLPYGdltechyphlqigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSA 640
Cdd:PRK11247 102 VGLGLKGQwRDAALQALAAVGLADRANEWPAA------------------LSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958746143 641 VDAhVGKHVFEECIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEI 687
Cdd:PRK11247 164 LDA-LTRIEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
497-700 |
6.50e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLG----------QMQLQKGVVAVSGPLA-----YVSQQAWIFHG----- 556
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirkSRANTGYIFQQfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 --NVRENILFGEKYNHQRYQHTVH-VCGLQKDLNSLPYGDLTECHYPHlqigERGVNLSGGQRQRISLARAVYANRQLYL 633
Cdd:PRK09984 100 rlSVLENVLIGALGSTPFWRTCFSwFTREQKQRALQALTRVGMVHFAH----QRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 634 LDDPLSAVDAHVGKHVFEEC--IKKTlKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLrdINQN-DGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
491-710 |
7.50e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------------PLAYVSQ 549
Cdd:PRK13641 15 GTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 550 QAWIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDL-NSLPYgdltechyphlqigergvNLSGGQRQRISL 621
Cdd:PRK13641 95 EAQLFENTVLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSEDLiSKSPF------------------ELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 622 ARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
250
....*....|
gi 1958746143 701 GRYAKliHNL 710
Cdd:PRK13641 237 EWLKK--HYL 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
496-687 |
7.75e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQA------------WIFHG------ 556
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqPMSKLSSAAkaelrnqklgfiYQFHHllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 ---NVRENILFGEKYN---HQRYQHTVHVCGLQKDLNslpygdltechyphlqigERGVNLSGGQRQRISLARAVYANRQ 630
Cdd:PRK11629 104 aleNVAMPLLIGKKKPaeiNSRALEMLAAVGLEHRAN------------------HRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 631 LYLLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
501-687 |
8.93e-13 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 68.73 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 501 SFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVRENILFG--- 565
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqshtglapyqrPVSMLFQENNLFaHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 566 -EKYNHQRYQHTVHVC---GLQKDLNSLPYgdltechyphlqigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:TIGR01277 98 gLKLNAEQQEKVVDAAqqvGIADYLDRLPE------------------QLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958746143 642 DAHVGKHVFeeCIKKTL---KGKTVVLVTHQLQFL-ESCDEVILLEDGEI 687
Cdd:TIGR01277 160 DPLLREEML--ALVKQLcseRQRTLLMVTHHLSDArAIASQIAVVSQGKI 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
494-699 |
9.04e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------PL--------AYVSQQAWIFHgnvR 559
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllPLhararrgiGYLPQEASIFR---R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENIlfgekynhqrYQHTVHVCGLQKDLNSLPYGD-----LTECHYPHLQiGERGVNLSGGQRQRISLARAVYANRQLYLL 634
Cdd:PRK10895 93 LSV----------YDNLMAVLQIRDDLSAEQREDranelMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 635 DDPLSAVDAhvgKHVFEecIKKTLK-----GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:PRK10895 162 DEPFAGVDP---ISVID--IKRIIEhlrdsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
495-691 |
9.84e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.41 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-------------LAYVSQQAWI-FHGNVRE 560
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLsFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGekynhqRYQHTVHVCGLQKD-----LNSLPYGDLTechyphlQIGERGV-NLSGGQRQRISLARAVYANRQLYLL 634
Cdd:PRK09536 97 VVEMG------RTPHRSRFDTWTETdraavERAMERTGVA-------QFADRPVtSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 635 DDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 691
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
494-687 |
1.13e-12 |
|
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: 68.45 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQK---GVVAVSG-PL---------AYVSQQ-AWIFHGNVR 559
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGqPRkpdqfqkcvAYVRQDdILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILF------GEKYNHQRYQHTVHVCGLqKDLNSLPYGdltechyphlqiGERGVNLSGGQRQRISLARAVYANRQLYL 633
Cdd:cd03234 100 ETLTYtailrlPRKSSDAIRKKRVEDVLL-RDLALTRIG------------GNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 634 LDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ-----LQFLescDEVILLEDGEI 687
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQprsdlFRLF---DRILLLSSGEI 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
497-687 |
1.26e-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: 68.20 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQA----------------WIFHGNVR 559
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAipylrrkigvvfqdfrLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPYGdltechyphlqigergvnLSGGQRQRISLARAVYANRQLY 632
Cdd:cd03292 97 ENVAFalevtgvPPREIRKRVPAALELVGLSHKHRALPAE------------------LSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 633 LLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDE-VILLEDGEI 687
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
497-698 |
1.89e-12 |
|
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: 70.87 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGqMQLQKGVVAVSG-PLAYVSQQAWifhgnvrenilfgekynhQRYQH 575
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRAL------------------RPLRR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 576 TVHVCgLQkDlnslPYGDL----------TE---CHYPHLQIGER---------GVNL------------SGGQRQRISL 621
Cdd:COG4172 363 RMQVV-FQ-D----PFGSLsprmtvgqiiAEglrVHGPGLSAAERrarvaealeEVGLdpaarhryphefSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 622 ARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGK---TVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELM 697
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
.
gi 1958746143 698 E 698
Cdd:COG4172 515 D 515
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
494-696 |
3.07e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAY-------------------VSQQAWIF 554
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiklrkevgmVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 -HGNVRENILFGEKYN--------HQRYQHTVHVCGLQKDLnslpygdltechypHLQIGERGVNLSGGQRQRISLARAV 625
Cdd:PRK14246 103 pHLSIYDNIAYPLKSHgikekreiKKIVEECLRKVGLWKEV--------------YDRLNSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 626 YANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQ-LQFLESCDEVILLEDGEICEKGTHKEL 696
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
495-689 |
3.23e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQA----------WIFHG------- 556
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqPLHQMDEEAraklrakhvgFVFQSfmliptl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENI-----LFGEKYNHQRYQ--HTVHVCGLQKDLNSLPygdltechyphlqigergVNLSGGQRQRISLARAVYANR 629
Cdd:PRK10584 104 NALENVelpalLRGESSRQSRNGakALLEQLGLGKRLDHLP------------------AQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 630 QLYLLDDPLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQLQFLESCDEVILLEDGEICE 689
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
499-696 |
3.83e-12 |
|
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: 67.01 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------------PLAYVSQQAWIFHG-NVRENI-LF 564
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLyIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 565 GEKYNHQRYQHTvhvcglQKDLNSLPYGDLTEchyphlqIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 643
Cdd:cd03265 98 ARLYGVPGAERR------ERIDELLDFVGLLE-------AADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 644 HVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 696
Cdd:cd03265 165 QTRAHVWEY-IEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
489-730 |
3.84e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.19 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 489 QSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------PLAYVSQQAWIFHGN---- 557
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeeNLWDIRNKAGMVFQNpdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 -----VRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDltecHYPHLqigergvnLSGGQRQRISLARAVYANRQL 631
Cdd:PRK13633 98 ivatiVEEDVAFGpENLGIPPEEIRERVDESLKKVGMYEYRR----HAPHL--------LSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 632 YLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKE------LMEERG-- 701
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNT-IKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEifkeveMMKKIGld 244
|
250 260 270
....*....|....*....|....*....|..
gi 1958746143 702 --RYAKLIHNLRGLQFKDPEHIYNV-AMVETL 730
Cdd:PRK13633 245 vpQVTELAYELKKEGVDIPSDILTIdEMVNEL 276
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
494-698 |
4.42e-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: 69.83 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAYVSQQAWI----FHGN---------VRE 560
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCGYVerpsKVGEpcpvcggtlEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILF-----GEKYNHQR-----YQHTVHVCG----LQKDLNSLPygdltECHYP-------------HLQIGER----GV 609
Cdd:TIGR03269 93 EVDFwnlsdKLRRRIRKriaimLQRTFALYGddtvLDNVLEALE-----EIGYEgkeavgravdlieMVQLSHRithiAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 610 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEECIKKtlKGKTVVLVTHQLQFLES-CDEVILLEDG 685
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhnaLEEAVKA--SGISMVLTSHWPEVIEDlSDKAIWLENG 245
|
250
....*....|...
gi 1958746143 686 EICEKGTHKELME 698
Cdd:TIGR03269 246 EIKEEGTPDEVVA 258
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
496-693 |
4.94e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISAL-------LGQMQL------------QKGVVAVSGPLAYVSQQ--AWIf 554
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIagnhfdfsktpsDKAIRELRRNVGMVFQQynLWP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 HGNVRENILfgekynhqryQHTVHVCGLQKD---------LNSLPYGDLTEcHYPhLQigergvnLSGGQRQRISLARAV 625
Cdd:PRK11124 96 HLTVQQNLI----------EAPCRVLGLSKDqalaraeklLERLRLKPYAD-RFP-LH-------LSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 626 YANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTH 693
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVS--IIRELAetGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDA 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
468-697 |
5.16e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.91 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 468 QRAELYSEQSLSDQGVASPERQSGSPKsvlhNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG----- 542
Cdd:PRK10070 19 QRAFKYIEQGLSKEQILEKTGLSLGVK----DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiak 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 543 ------------PLAYVSQQ-AWIFHGNVRENILFGekynhqryqhtVHVCGL------QKDLNSLPYGDLTecHYPHLQ 603
Cdd:PRK10070 95 isdaelrevrrkKIAMVFQSfALMPHMTVLDNTAFG-----------MELAGInaeerrEKALDALRQVGLE--NYAHSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 604 IGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVIL 681
Cdd:PRK10070 162 PDE----LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKhQRTIVFISHDLdEAMRIGDRIAI 237
|
250
....*....|....*.
gi 1958746143 682 LEDGEICEKGTHKELM 697
Cdd:PRK10070 238 MQNGEVVQVGTPDEIL 253
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
494-696 |
5.73e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.69 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL----LGQMQLQkGVVAVSG-PL---------AYVsQQAWIFHGN-- 557
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGS-GSVLLNGmPIdakemraisAYV-QQDDLFIPTlt 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENILFGEKYNHQRYQHTVH----VCGLQKDLNslpygdLTECHYPHLQIGERGVNLSGGQRQRISLARAVYANRQLYL 633
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEkrerVDEVLQALG------LRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 634 LDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVILLEDGEICEKGTHKEL 696
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
547-707 |
7.01e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 547 VSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTechyphlQIGERGVNLSGGQRQRISLARAV 625
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDT-------NVGPYGKSLSGGQKQRIAIARAL 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 626 YANRQLYLLDDPLSAVDAHVgkhvfEECIKKTL------KGKTVVLVTHQLQFLESCDEVILLEDGE-----ICEKGTHK 694
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSNS-----EKLIEKTIvdikdkADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHE 1448
|
170
....*....|....
gi 1958746143 695 ELME-ERGRYAKLI 707
Cdd:PTZ00265 1449 ELLSvQDGVYKKYV 1462
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
488-692 |
1.00e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.52 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG---------PLAYVSQQ-AWIF-HG 556
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalsekELRKARRQiGMIFqHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 N------VRENILFG-EKYNHQRYQHTVHVCGLqkdlnsLPYGDLTECH--YPhlqigergVNLSGGQRQRISLARAVYA 627
Cdd:PRK11153 92 NllssrtVFDNVALPlELAGTPKAEIKARVTEL------LELVGLSDKAdrYP--------AQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 628 NRQLYLLDDPLSAVDAHVGKHVFE--ECIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 692
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILEllKDINREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
857-971 |
1.14e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.65 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 857 LVYIASMMSVLTFGIIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQ 936
Cdd:COG1132 65 LLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVR 144
|
90 100 110
....*....|....*....|....*....|....*.
gi 1958746143 937 QFSMVVFILVIMAA-SFPVVLVVLAGLAILFFILLR 971
Cdd:COG1132 145 SVVTLIGALVVLFViDWRLALIVLLVLPLLLLVLRL 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
494-700 |
1.80e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.74 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------P-------LAYVS----QQAWIFH 555
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvrirsPrdairagIAYVPedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 556 GNVRENILFGekyNHQRYQH---------TVHVCGLQKDLNslpygdlTECHYPHLQIGergvNLSGGQRQRISLARAVY 626
Cdd:COG1129 345 LSIRENITLA---SLDRLSRgglldrrreRALAEEYIKRLR-------IKTPSPEQPVG----NLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 627 ANRQLYLLDDPLSAVDahVG-KHVFEECIKK-TLKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:COG1129 411 TDPKVLILDEPTRGID--VGaKAEIYRLIRElAAEGKAVIVISSELPeLLGLSDRILVMREGRIVGELDREEATEEA 485
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
494-698 |
1.81e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISaLLGQMQ-LQKGVVAVSG-PL------------AYVSQQAWIFHG-NV 558
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQpPSEGEILLDAqPLeswsskafarkvAYLPQQLPAAEGmTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENILFGeKY------------NHQRYQHTVHVCGLQKdlnslpygdltechyphlqIGERGVN-LSGGQRQRISLARAV 625
Cdd:PRK10575 103 RELVAIG-RYpwhgalgrfgaaDREKVEEAISLVGLKP-------------------LAHRLVDsLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 626 YANRQLYLLDDPLSAVD-AHvgkHVFEECIKKTL---KGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 698
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDiAH---QVDVLALVHRLsqeRGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
496-669 |
1.82e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV--SGPLAYVSQQAWIFHGNVRENILF---GEKYNH 570
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSD 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 571 QRYQHTVHVCGLqkdlnslpyGDLTEchypHLQIGER-GVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV 649
Cdd:COG4178 458 AELREALEAVGL---------GHLAE----RLDEEADwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
170 180
....*....|....*....|
gi 1958746143 650 FEEcIKKTLKGKTVVLVTHQ 669
Cdd:COG4178 525 YQL-LREELPGTTVISVGHR 543
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
501-697 |
2.69e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.60 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 501 SFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-----------PLAYVSQQAWIF-HGNVRENILFG--- 565
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppsrrPVSMLFQENNLFsHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 566 ----EKYNHQRYQHTVHVCGLQKDLNSLPygdltechyphlqiGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAV 641
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP--------------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 642 D----AHVGKHVFEECIKKTLkgkTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 697
Cdd:PRK10771 161 DpalrQEMLTLVSQVCQERQL---TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
497-698 |
2.78e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.16 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV------AVSGPLAYVSQQAWIFHGN---------VREN 561
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRKHIGIVFQNpdnqfvgsiVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGEKyNHQRYQHTVH--VCGLQKDLNSLPYGDltecHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:PRK13648 105 VAFGLE-NHAVPYDEMHrrVSEALKQVDMLERAD----YEPN--------ALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 640 AVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 698
Cdd:PRK13648 172 MLDPDARQNLLDLVRKvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
497-717 |
3.32e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.25 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAY--------------VSQQA--WIFHGNVR 559
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkPIDYsrkglmklresvgmVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFG-------EKYNHQRYQHTVHVCGLQKdLNSLPygdlTEChyphlqigergvnLSGGQRQRISLARAVYANRQLY 632
Cdd:PRK13636 102 QDVSFGavnlklpEDEVRKRVDNALKRTGIEH-LKDKP----THC-------------LSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 633 LLDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQFLE-SCDEVILLEDGEICEKGTHKELMEERG-------R 702
Cdd:PRK13636 164 VLDEPTAGLDP-MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEmlrkvnlR 242
|
250
....*....|....*
gi 1958746143 703 YAKLIHNLRGLQFKD 717
Cdd:PRK13636 243 LPRIGHLMEILKEKD 257
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
489-718 |
3.34e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.43 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 489 QSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PL----AYVSQ 549
Cdd:PRK13634 13 QYKTPfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagkknkklkPLrkkvGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 550 --QAWIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKD-LNSLPYgdltechyphlqigergvNLSGGQRQRI 619
Cdd:PRK13634 93 fpEHQLFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEElLARSPF------------------ELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 620 SLARAVYANRQLYLLDDPLSAVDAHvGKH----VFEECIKKtlKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHK 694
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPK-GRKemmeMFYKLHKE--KGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPR 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958746143 695 EL------MEERG-------RYAKLIHNLRGLQFKDP 718
Cdd:PRK13634 232 EIfadpdeLEAIGldlpetvKFKRALEEKFGISFPKP 268
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
498-676 |
4.33e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 498 HNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL-----AYVSQQAWIFHGN-------VRENILF 564
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGePIrrqrdEYHQDLLYLGHQPgikteltALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 565 gekynhqryqhtvhVCGLQKDLnslpygDLTECHYPHLQIGERGV------NLSGGQRQRISLARAVYANRQLYLLDDPL 638
Cdd:PRK13538 98 --------------YQRLHGPG------DDEALWEALAQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958746143 639 SAVDAHvGKHVFEECIKKTL-KGKTVVLVTHQLQFLESC 676
Cdd:PRK13538 158 TAIDKQ-GVARLEALLAQHAeQGGMVILTTHQDLPVASD 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
494-669 |
4.73e-11 |
|
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: 63.28 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLA-----YVSQQAWIFHGN-------VRE 560
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgPLDfqrdsIARGLLYLGHAPgikttlsVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NIlfgekynhqRYQHTVHvcGLQKDLNSLPYGDLTEchYPHLQIGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSA 640
Cdd:cd03231 93 NL---------RFWHADH--SDEQVEEALARVGLNG--FEDRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*....
gi 1958746143 641 VDAHVGKHVFEECIKKTLKGKTVVLVTHQ 669
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
494-698 |
4.81e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.89 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------P--------LAYVSQQAWIFHG-NV 558
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlPmhkrarlgIGYLPQEASIFRKlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENIL----FGEKYNHQRyqhtvhvcglQKDLNSLpygdLTECHYPHLQiGERGVNLSGGQRQRISLARAVYANRQLYLL 634
Cdd:COG1137 96 EDNILavleLRKLSKKER----------EERLEEL----LEEFGITHLR-KSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 635 DDPLSAVD--AhvgkhVFEecIKK---TLKGKTV-VLVT-HQLQ-FLESCDEVILLEDGEICEKGTHKELME 698
Cdd:COG1137 161 DEPFAGVDpiA-----VAD--IQKiirHLKERGIgVLITdHNVReTLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
494-687 |
5.02e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVsGP---LAYVSQQAWIFHGN--VRENIlfgeky 568
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQHQEELDPDktVLDEL------ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 569 nhQRY---QHTVHVCGLQKDLNsLPYGDLTEchyphlQIGergvNLSGGQRQRISLARAVYANRQLYLLDDP-----LSA 640
Cdd:COG0488 401 --RDGapgGTEQEVRGYLGRFL-FSGDDAFK------PVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIET 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958746143 641 VDAhvgkhvFEECIKkTLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 687
Cdd:COG0488 468 LEA------LEEALD-DFPG-TVLLVSHDRYFLDRvATRILEFEDGGV 507
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
499-699 |
5.78e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------PL-------AYV--SQQAWIFHGN--VRE 560
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprsPLdavkkgmAYIteSRRDNGFFPNfsIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKYNHQRYQHTVhvcGL------------QKDLNSLpygdltECHYPHLQIGErgvnLSGGQRQRISLARAVYAN 628
Cdd:PRK09700 361 NMAISRSLKDGGYKGAM---GLfhevdeqrtaenQRELLAL------KCHSVNQNITE----LSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 629 RQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRDDMSE 499
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
489-699 |
6.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.37 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 489 QSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHGNVRENILFg 565
Cdd:PRK13643 12 QPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKPVRKKVGVVF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 566 EKYNHQRYQHTV--------HVCGLQKDLNSLPYGDLTECHYPHLQIGERG-VNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:PRK13643 91 QFPESQLFEETVlkdvafgpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 637 PLSAVD--AHVGKHVFEECIKKTlkGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:PRK13643 171 PTAGLDpkARIEMMQLFESIHQS--GQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
496-699 |
8.08e-11 |
|
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: 64.69 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGqmqLQKGVVAVSG-------PLAYVSQQAW----------IFHG-- 556
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILG---LLPPPGITSGeilfdgeDLLKLSEKELrkirgreiqmIFQDpm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 ---N--------VRENILFGEKYNH-QRYQHTVHV---CGL---QKDLNSlpygdltechYPHlqigergvNLSGGQRQR 618
Cdd:COG0444 97 tslNpvmtvgdqIAEPLRIHGGLSKaEARERAIELlerVGLpdpERRLDR----------YPH--------ELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 619 ISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHK 694
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQIlnlLKD-LQREL-GLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVE 236
|
....*
gi 1958746143 695 ELMEE 699
Cdd:COG0444 237 ELFEN 241
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
475-697 |
9.52e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 475 EQSLSDQGVASPERqsgspkSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQ---LQKGVVAVSGPLA------ 545
Cdd:PLN03211 68 KPKISDETRQIQER------TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKPTkqilkr 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 546 --YVSQQAWIF-HGNVRENILFgekynhqryqhtvhvCGLQKDLNSLPYGD-------------LTECHypHLQIGE--- 606
Cdd:PLN03211 142 tgFVTQDDILYpHLTVRETLVF---------------CSLLRLPKSLTKQEkilvaesviselgLTKCE--NTIIGNsfi 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 607 RGVnlSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVILLED 684
Cdd:PLN03211 205 RGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSE 282
|
250
....*....|...
gi 1958746143 685 GEICEKGTHKELM 697
Cdd:PLN03211 283 GRCLFFGKGSDAM 295
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
494-669 |
1.09e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.40 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV--AVSGPLAYVSQQAWIFHGNVRENILFgekynhq 571
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmPEGEDLLFLPQRPYLPLGTLREQLIY------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 572 ryqhtvhvcglqkdlnslPYGDltechyphlqigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE 651
Cdd:cd03223 87 ------------------PWDD----------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170
....*....|....*...
gi 1958746143 652 ECikkTLKGKTVVLVTHQ 669
Cdd:cd03223 133 LL---KELGITVISVGHR 147
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
497-735 |
1.25e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.22 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAYVSQQAWI---------------FHGNVREN 561
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdltechyphlqigergvNLSGGQRQRISLARAVYANRQLYLL 634
Cdd:PRK13647 101 VAFGpvnmgldKDEVERRVEEALKAVRMWDFRDKPPY------------------HLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 635 DDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKG-----THKELMEERGRYAKLIH 708
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLVA 242
|
250 260
....*....|....*....|....*..
gi 1958746143 709 NLrglqFKDPEHIYNVAMVETLKESQA 735
Cdd:PRK13647 243 QI----FEDLPELGQSKLPLTVKEAVQ 265
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
509-687 |
1.25e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.13 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 509 VLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPL-----------------AYVSQQAWIF-HGNVRENILFG-EKYN 569
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLFpHYKVRGNLRYGmAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 570 HQRYQHTVHVCGLQKDLNSLPygdltechyphlqigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV 649
Cdd:PRK11144 106 VAQFDKIVALLGIEPLLDRYP------------------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958746143 650 --FEECIKKTLKgKTVVLVTHQLQ-FLESCDEVILLEDGEI 687
Cdd:PRK11144 168 lpYLERLAREIN-IPILYVSHSLDeILRLADRVVVLEQGKV 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
494-687 |
1.41e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPL--AYVSQQAWIF-HGNVRENIL--FGEKY 568
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLriGYLPQEPPLDdDLTVLDTVLdgDAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 569 NHQRYQHTVHVCGLQKDLNSLPYGDLTEC-------HYPH--------LQIGERGVN-----LSGGQRQRISLARAVYAN 628
Cdd:COG0488 91 ALEAELEELEAKLAEPDEDLERLAELQEEfealggwEAEAraeeilsgLGFPEEDLDrpvseLSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 629 RQLYLLDDP-----LSAVDAhvgkhvFEECIKKtLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 687
Cdd:COG0488 171 PDLLLLDEPtnhldLESIEW------LEEFLKN-YPG-TVLVVSHDRYFLDRvATRILELDRGKL 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
490-706 |
1.41e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.09 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 490 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------PLAYVSQQAWIFHGN------ 557
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKKIGIIFQNpdnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 ---VRENILFG---EKYNHQRYQ----HTVHVCGLQKDLNslpygdltecHYPHlqigergvNLSGGQRQRISLARAVYA 627
Cdd:PRK13632 98 gatVEDDIAFGlenKKVPPKKMKdiidDLAKKVGMEDYLD----------KEPQ--------NLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 628 NRQLYLLDDPLSAVDAHvGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM--EERGRY 703
Cdd:PRK13632 160 NPEIIIFDESTSMLDPK-GKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILnnKEILEK 238
|
...
gi 1958746143 704 AKL 706
Cdd:PRK13632 239 AKI 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
494-699 |
2.72e-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: 61.00 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQM--QLQKGVVAVSGplayvsqqawifhgnvrENILFGEKYNHQ 571
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-----------------EDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 572 R------YQHTVHVCGLqKDLNSLpygdltechyphlqigeRGVN--LSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 643
Cdd:cd03217 76 RlgiflaFQYPPEIPGV-KNADFL-----------------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 644 HVGKHVFEEcIKKTL-KGKTVVLVTHQLQFLESC--DEVILLEDGEICEKGThKELMEE 699
Cdd:cd03217 138 DALRLVAEV-INKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGD-KELALE 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
496-687 |
3.23e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICG-NvGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHG--------------NVR 559
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGeN-GAGKSTLMKILSGVYQPDSGEILLDGePVRFRSPRDAQAAGiaiihqelnlvpnlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFGE------KYNHQR-YQHTVHVC---GLQKDlnslpygdltechyPHLQIGErgvnLSGGQRQRISLARAVYANR 629
Cdd:COG1129 98 ENIFLGReprrggLIDWRAmRRRARELLarlGLDID--------------PDTPVGD----LSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 630 QLYLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEI 687
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFR--IIRRLKaqGVAIIYISHRLdEVFEIADRVTVLRDGRL 218
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
856-968 |
3.23e-10 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 62.42 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 856 QLVYIASMMSVLtFGIIKGFTFTNTTLMASSS------LHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDvrlpf 929
Cdd:cd18547 43 GLLRILLLLLGL-YLLSALFSYLQNRLMARVSqrtvydLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNIS----- 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958746143 930 haeNFLQQ--------FSMVVFILVIMAA-SFPVVLVVLAGLAILFFI 968
Cdd:cd18547 117 ---QALSQsltqlissILTIVGTLIMMLYiSPLLTLIVLVTVPLSLLV 161
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
499-699 |
3.94e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.67 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV-----------SGP---------LAYVSQQAWIF-HGN 557
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPGPdgrgrakryIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENIL------FGEKYNHQRYQHTVHVCGL--QKDLNSLPygdltecHYPHlqigergvNLSGGQRQRISLARAVYANR 629
Cdd:TIGR03269 382 VLDNLTeaigleLPDELARMKAVITLKMVGFdeEKAEEILD-------KYPD--------ELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 630 QLYLLDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 699
Cdd:TIGR03269 447 RIVILDEPTGTMDP-ITKVDVTHSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
497-691 |
4.86e-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: 60.67 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVL------------GICGNVGSGKSSLISALLGQMQLQKGVVAVSGP------------LAYVSQQaw 552
Cdd:cd03264 3 LENLTKRYGKKRALdgvsltlgpgmyGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 iFhgNVRENILFGEKYNHQRYQHTVH-------VCGLQKDLNSLPYGDltechyphlqigERGVNLSGGQRQRISLARAV 625
Cdd:cd03264 81 -F--GVYPNFTVREFLDYIAWLKGIPskevkarVDEVLELVNLGDRAK------------KKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 626 YANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 691
Cdd:cd03264 146 VGDPSILIVDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
496-702 |
5.00e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.05 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWifhG------------NVRENI 562
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGePLDPEDRRRI---GylpeerglypkmKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 L-FGE-KynhqryqhtvhvcGLQKD--LNSLPYgdLTEchypHLQIGERG---V-NLSGGQRQRISLARAVYANRQLYLL 634
Cdd:COG4152 93 VyLARlK-------------GLSKAeaKRRADE--WLE----RLGLGDRAnkkVeELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 635 DDPLSAVDAhVGKHVFEECIK-KTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGR 702
Cdd:COG4152 154 DEPFSGLDP-VNVELLKDVIReLAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
497-685 |
6.61e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHG--------------NVREN 561
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGE--------KYNHQRYQHTVHVCGLQKDLNslpygdltechyPHLQIGErgvnLSGGQRQRISLARAVYANRQLYL 633
Cdd:PRK11288 100 LYLGQlphkggivNRRLLNYEAREQLEHLGVDID------------PDTPLKY----LSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 634 LDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDG 685
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFR--VIRELRaeGRVILYVSHRMeEIFALCDAITVFKDG 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
494-671 |
6.78e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.82 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVvAVSGPLAY---------------------VSQQAW 552
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGA-RVEGEILLdgediydpdvdvvelrrrvgmVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 IFHGNVRENILFGEKYNHQRYQHTVHV--------CGLQ---KD-LNslpygdltechyphlqigERGVNLSGGQRQRIS 620
Cdd:COG1117 103 PFPKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWdevKDrLK------------------KSALGLSGGQQQRLC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 621 LARAVYANRQLYLLDDPLSAVD----AHVgkhvfEECIKKtLKGK-TVVLVTHQLQ 671
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDpistAKI-----EELILE-LKKDyTIVIVTHNMQ 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
492-696 |
7.05e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 61.36 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 492 SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP---------------LAYVSQQAWIFHG 556
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdltechyphlqigergvNLSGGQRQRISLARAVYANR 629
Cdd:PRK13652 95 TVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH------------------HLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 630 QLYLLDDPLSAVDAHVGKHV--FEECIKKTLkGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKEL 696
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
854-971 |
7.50e-10 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 61.41 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 854 MYQLVYIASMMsVLTFGIIKGFTFTNTTLMASSSLH------NRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRL 927
Cdd:cd07346 35 LSLLLWIALLL-LLLALLRALLSYLRRYLAARLGQRvvfdlrRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLV 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958746143 928 PFHAENFLQQFSMVVFILVIMAA-SFPVVLVVLAGLAILFFILLR 971
Cdd:cd07346 114 SSGLLQLLSDVLTLIGALVILFYlNWKLTLVALLLLPLYVLILRY 158
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
497-686 |
7.98e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLG----------------QMQL-------QKGVVAVSGPLAYVSQQAwi 553
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifegeELQAsnirdteRAGIAIIHQELALVKELS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 554 fhgnVRENILFGEK--------YN--HQRYQHTVHvcGLQKDLNslpygdltechyPHLQIGergvNLSGGQRQRISLAR 623
Cdd:PRK13549 99 ----VLENIFLGNEitpggimdYDamYLRAQKLLA--QLKLDIN------------PATPVG----NLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 624 AVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGE 686
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLD--IIRDLKahGIACIYISHKLnEVKAISDTICVIRDGR 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
487-687 |
7.99e-10 |
|
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: 59.58 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 487 ERQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMqlqKGVVAVSGPLAYVSQQAWIFHgnvrenilfge 566
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYNGIPYKEFA----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 567 kynhQRYQHTVHVCGlQKDLnslpygdltecHYPHLQIGE--------------RGVnlSGGQRQRISLARAVYANRQLY 632
Cdd:cd03233 79 ----EKYPGEIIYVS-EEDV-----------HFPTLTVREtldfalrckgnefvRGI--SGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 633 LLDDPLSAVDAHVGKHvFEECIK---KTLKGKTVVLVTHQLQFLESC-DEVILLEDGEI 687
Cdd:cd03233 141 CWDNSTRGLDSSTALE-ILKCIRtmaDVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQ 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
497-686 |
8.05e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.53 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLG----------------QMQLQ-------KGVVAVSGPLAYVSQQAwi 553
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASnirdterAGIVIIHQELTLVPELS-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 554 fhgnVRENILFGEKYNHQ----RYQHTVHVC-------GLQKDLNSLPYGDltechyphlqigergvnLSGGQRQRISLA 622
Cdd:TIGR02633 95 ----VAENIFLGNEITLPggrmAYNAMYLRAknllrelQLDADNVTRPVGD-----------------YGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 623 RAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGKTV--VLVTHQLQFLES-CDEVILLEDGE 686
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
497-696 |
9.34e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.18 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG--------------------PLAYVSQQAWIFHG 556
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkikevkrlrkeiGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTECHYphlqigergvNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPF----------ELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 637 PLSAVDAHvGKHVFEECIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKEL 696
Cdd:PRK13645 177 PTGGLDPK-GEEDFINLFERLNKeyKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
494-692 |
1.07e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPL--AYVSQQAWIfhgnvrENILFGEKYNHQ 571
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYL------DTTLPLTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 572 RYQHTVhvcglqKDLNSLPYgdLTECHYPHLqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD--AHVGKHV 649
Cdd:PRK09544 91 RLRPGT------KKEDILPA--LKRVQAGHL-IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQVALYD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958746143 650 FEECIKKTLkGKTVVLVTHQLQF-LESCDEVILLeDGEICEKGT 692
Cdd:PRK09544 162 LIDQLRREL-DCAVLMVSHDLHLvMAKTDEVLCL-NHHICCSGT 203
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
605-696 |
1.17e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.27 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 605 GERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVI 680
Cdd:PRK11432 130 EDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREK-IRELQQqfNITSLYVTHdQSEAFAVSDTVI 208
|
90
....*....|....*.
gi 1958746143 681 LLEDGEICEKGTHKEL 696
Cdd:PRK11432 209 VMNKGKIMQIGSPQEL 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
860-968 |
2.41e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 59.86 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 860 IASMMSVLtFGIIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFS 939
Cdd:cd18572 44 LLSVLSGL-FSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLV 122
|
90 100 110
....*....|....*....|....*....|
gi 1958746143 940 MVVFILVIMAA-SFPVVLVVLAGLAILFFI 968
Cdd:cd18572 123 QLVGGLAFMFSlSWRLTLLAFITVPVIALI 152
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
799-968 |
2.56e-09 |
|
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: 59.54 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 799 SFLVLCLFFLMMGSSAFSTWWLGLWLDSGSQvicAPQSnetacnvnQTLqdtkhhMYQLVYIASMMS--VLTFGIikGFT 876
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVN---GPQE--------HGQ------VYLSVLGALAILqgITVFQY--SMA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 877 FTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFPVVL 956
Cdd:cd18559 62 VSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAA 141
|
170
....*....|..
gi 1958746143 957 VVLAGLAILFFI 968
Cdd:cd18559 142 VGIPLGLLYVPV 153
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
491-731 |
2.62e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 59.68 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG--------PLAYVSQQAWI------- 553
Cdd:PRK13637 15 GTPfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvKLSDIRKKVGLvfqypey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 554 --FHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDlnslPYGDLTEchyphlqigergVNLSGGQRQRISLARA 624
Cdd:PRK13637 95 qlFEETIEKDIAFGpinlglsEEEIENRVKRAMNIVGLDYE----DYKDKSP------------FELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 625 VYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLKGK--TVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERG 701
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNK-IKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKEVE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958746143 702 RYAK----------LIHNLRGLQFKDPEHIYNV--AMVETLK 731
Cdd:PRK13637 238 TLESiglavpqvtyLVRKLRKKGFNIPDDIFTIeeAKEEILK 279
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
800-973 |
2.65e-09 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 59.74 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 800 FLVLCLFFLMMGSSAFSTWWLGLWLDSGSQvicapqsnetacnvnqtlqdtKHHMYQLVYIASMMSVLTFgiIKG-FTFT 878
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDIFV---------------------EKDLEALLLVPLAIIGLFL--LRGlASYL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 879 NTTLMASSSLH------NRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAA-S 951
Cdd:cd18552 59 QTYLMAYVGQRvvrdlrNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYlD 138
|
170 180
....*....|....*....|..
gi 1958746143 952 FPVVLVVLAGLAILFFILLRCG 973
Cdd:cd18552 139 WKLTLIALVVLPLAALPIRRIG 160
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
499-697 |
2.75e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.42 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PL-----AYVSQQA-WIFHG-----NVRENI---- 562
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhPLhfgdySYRSQRIrMIFQDpstslNPRQRIsqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 ---------LFGEKYNHQRYQhTVHVCGLQKDLNSlpygdltecHYPHLqigergvnLSGGQRQRISLARAVYANRQLYL 633
Cdd:PRK15112 111 dfplrlntdLEPEQREKQIIE-TLRQVGLLPDHAS---------YYPHM--------LAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 634 LDDPLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELM 697
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
494-697 |
2.78e-09 |
|
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: 58.94 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGK---VLGicGNvGSGKSSLISALLGQM-QLQKGVVAVSG-------------PLAYVS---QQAWI 553
Cdd:COG1119 16 KTILDDISWTVKPGEhwaILG--PN-GAGKSTLLSLITGDLpPTYGNDVRLFGerrggedvwelrkRIGLVSpalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 554 FHGNVRENIL---FG-----EKYN---HQRYQHTVHVCGLQkDLNSLPYGDLtechyphlqigergvnlSGGQRQRISLA 622
Cdd:COG1119 93 RDETVLDVVLsgfFDsiglyREPTdeqRERARELLELLGLA-HLADRPFGTL-----------------SQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 623 RAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 697
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
857-981 |
2.88e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 59.37 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 857 LVYIASMMsvLTFGIIKG-FTFTNTTLMASSS------LHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPF 929
Cdd:cd18542 38 LWLLALLI--LGVALLRGvFRYLQGYLAEKASqkvaydLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAF 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 930 HAENFLQQFSMVVFILVIM--------AASFpVVLVVLAGLAILFFILLRCGWTTCAEAL 981
Cdd:cd18542 116 GLVELVRAVLLFIGALIIMfsinwkltLISL-AIIPFIALFSYVFFKKVRPAFEEIREQE 174
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
495-696 |
3.34e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.94 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 495 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAY-------VSQQAWI---------FHGN 557
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYdkkslleVRKTVGIvfqnpddqlFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 VRENILFGE---KYNHQRYQHTVhvcglqKDlnSLPYGDLT--ECHYPHlqigergvNLSGGQRQRISLARAVYANRQLY 632
Cdd:PRK13639 96 VEEDVAFGPlnlGLSKEEVEKRV------KE--ALKAVGMEgfENKPPH--------HLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 633 LLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 696
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
494-696 |
3.95e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.63 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALlGQMQLQKGVVAVSGPLAY---------------------VSQQAW 552
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 IFHGNVRENILFGEKYNHQRYQHTVHVcGLQKDLNSLPYGDLTECHyphlqIGERGVNLSGGQRQRISLARAVYANRQLY 632
Cdd:PRK14239 97 PFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDEVKDR-----LHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 633 LLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 696
Cdd:PRK14239 171 LLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
497-671 |
3.97e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.64 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLI------SALLGQMQLQKGV--------------VAVSGPLAYVSQQAWIFHG 556
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEGKVtfhgknlyapdvdpVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENILFGEKYNhqryqhtvhvcGLQKDLNSLPYGDLTECHY---PHLQIGERGVNLSGGQRQRISLARAVYANRQLYL 633
Cdd:PRK14243 106 SIYDNIAYGARIN-----------GYKGDMDELVERSLRQAALwdeVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958746143 634 LDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQ 671
Cdd:PRK14243 175 MDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
459-687 |
4.78e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.11 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 459 DQRRHVFKKQRAELYSEQSLsdQGVASPERQSgspKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV 538
Cdd:cd03267 4 SNLSKSYRVYSKEPGLIGSL--KSLFKRKYRE---VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 539 AVSGPLAYVSQQAWIfhgnVRENILFGekynhQRYQ-----HTVHVCGLQKDLNSLPYG-------DLTEChyphLQIGE 606
Cdd:cd03267 79 RVAGLVPWKRRKKFL----RRIGVVFG-----QKTQlwwdlPVIDSFYLLAAIYDLPPArfkkrldELSEL----LDLEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 607 ------RgvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKK--TLKGKTVVLVTHQLQFLES-CD 677
Cdd:cd03267 146 lldtpvR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV-VAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlAR 222
|
250
....*....|
gi 1958746143 678 EVILLEDGEI 687
Cdd:cd03267 223 RVLVIDKGRL 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
610-698 |
6.17e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.93 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 610 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQ-LQFLESCDEVILLEDGEIC 688
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
90
....*....|
gi 1958746143 689 EKGTHKELME 698
Cdd:PRK14267 228 EVGPTRKVFE 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
497-696 |
6.19e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.20 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLaYVSQQAWifhgNVRENI--LFGEKYNhQRYQ 574
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVW----DIRHKIgmVFQNPDN-QFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 575 HTVH---VCGLQKdlNSLPYGDLTECHYPHLQI-------GERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH 644
Cdd:PRK13650 97 ATVEddvAFGLEN--KGIPHEEMKERVNEALELvgmqdfkEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 645 vGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL 696
Cdd:PRK13650 175 -GRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
497-697 |
8.36e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHG-----------------NV 558
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhEVVTRSPQDGLANGivyisedrkrdglvlgmSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENI---------LFGEKYNHQRYQHTVHvcglqkdlnslPYGDLTECHYPHL--QIGergvNLSGGQRQRISLARAVYA 627
Cdd:PRK10762 348 KENMsltalryfsRAGGSLKHADEQQAVS-----------DFIRLFNIKTPSMeqAIG----LLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958746143 628 NRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEIC-----EKGTHKELM 697
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMpEVLGMSDRILVMHEGRISgeftrEQATQEKLM 488
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
496-697 |
1.08e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.20 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG--------------PLAYVSQQAWIF-HGNVRE 560
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVFsRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKY-NHQRYQHTV-HVCGLqkdlnslpygdltechYPHLQ--IGERGVNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:PRK11614 100 NLAMGGFFaERDQFQERIkWVYEL----------------FPRLHerRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 637 PLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELM 697
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
496-669 |
1.30e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGvvavsgplayvsqqawifhgnvrENILFGEKYNHQR--Y 573
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKG-----------------------EILFERQSIKKDLctY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 574 QHTVHVCGLQKDLNslPYGDLTE-CHYP-HLQIGERGVN------------------LSGGQRQRISLARAVYANRQLYL 633
Cdd:PRK13540 73 QKQLCFVGHRSGIN--PYLTLREnCLYDiHFSPGAVGITelcrlfslehlidypcglLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958746143 634 LDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ 669
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
611-703 |
1.64e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 611 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICE 689
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
90
....*....|....*....
gi 1958746143 690 KGTHKELME-----ERGRY 703
Cdd:PRK14271 243 EGPTEQLFSspkhaETARY 261
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
496-687 |
1.72e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICG-NvGSGKSSLISALLGQMQLQKGVVAVSG-------P-------LAYVSQQAWIFHG-NVR 559
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGpN-GAGKTTLFNLITGFYRPTSGRILFDGrditglpPhriarlgIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFGekynhqryQHTVHVCGLQKDLNSLPYGDLTE----------------CHYPHLQIGergvNLSGGQRQRISLAR 623
Cdd:COG0411 98 ENVLVA--------AHARLGRGLLAALLRLPRARREEreareraeellervglADRADEPAG----NLSYGQQRRLEIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 624 AVYANRQLYLLDDPLSAVdAHVGKHVFEECIKK--TLKGKTVVLVTHQLQFLES-CDEVILLEDGEI 687
Cdd:COG0411 166 ALATEPKLLLLDEPAAGL-NPEETEELAELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
855-969 |
2.79e-08 |
|
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: 56.41 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 855 YQLVYIASMMSVLTFgiIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENF 934
Cdd:cd18557 40 LILLAIYLLQSVFTF--VRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958746143 935 LQQFSMVVFILVIMAAS----FPVVLVVLAGLAILFFIL 969
Cdd:cd18557 118 LRNILQVIGGLIILFILswklTLVLLLVIPLLLIASKIY 156
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
555-696 |
2.81e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.96 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 HGNVRENILFGEKYN-------HQRYQHTVHVCGLQKDLNSLPYGdltechyphlqigergvnLSGGQRQRISLARAVYA 627
Cdd:PRK11000 89 HLSVAENMSFGLKLAgakkeeiNQRVNQVAEVLQLAHLLDRKPKA------------------LSGGQRQRVAIGRTLVA 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 628 NRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 696
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIE-ISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
499-700 |
3.45e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ-KGVVAVSG-PLAYVSQQAWIFHGNV-------RENIL--FGEK 567
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkPVDIRNPAQAIRAGIAmvpedrkRHGIVpiLGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 568 YN-----HQRYQhTVHVCGLQKDLNSLPYGdLTECH----YPHLQIGergvNLSGGQRQRISLARAVYANRQLYLLDDPL 638
Cdd:TIGR02633 358 KNitlsvLKSFC-FKMRIDAAAELQIIGSA-IQRLKvktaSPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 639 SAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
488-705 |
4.14e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAYVSQQAWIfHGNVR--ENIlfg 565
Cdd:PRK13545 31 SKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGL-NGQLTgiENI--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 566 ekynhqryqhtvHVCGLQKDLNSLPYGDLTECHYPHLQIGeRGVN-----LSGGQRQRISLARAVYANRQLYLLDDPLSa 640
Cdd:PRK13545 107 ------------ELKGLMMGLTKEKIKEIIPEIIEFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALS- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958746143 641 vdahVGKHVF-EECIKK----TLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGRYAK 705
Cdd:PRK13545 173 ----VGDQTFtKKCLDKmnefKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
496-700 |
4.67e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-------------PLAYVSQQAWIFHGNVRENI 562
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreigayglrelrrQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 563 -LFGEKYNHQRYQhTVHVCGLQKDLNSLPYGdLTEChyphlqIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSA- 640
Cdd:PTZ00243 1405 dPFLEASSAEVWA-ALELVGLRERVASESEG-IDSR------VLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEATAn 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 641 VDAHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:PTZ00243 1477 IDPALDRQI-QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
857-968 |
4.92e-08 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 55.86 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 857 LVYIASMMSVLTFGIIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhAE---- 932
Cdd:cd18544 45 LLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL-------NElfts 117
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958746143 933 ---NFLQQFSMVVFILVIMAA-SFPVVLVVLAGLAILFFI 968
Cdd:cd18544 118 glvTLIGDLLLLIGILIAMFLlNWRLALISLLVLPLLLLA 157
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
850-948 |
5.21e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 55.59 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 850 TKHHMYQLVYIASMM---SVLTFGIIKGFTFTNTTLMA--SSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELD 924
Cdd:cd18563 35 PGGNTSLLLLLVLGLagaYVLSALLGILRGRLLARLGEriTADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQ 114
|
90 100
....*....|....*....|....
gi 1958746143 925 VRLPFHAENFLQQFSMVVFILVIM 948
Cdd:cd18563 115 DFLSDGLPDFLTNILMIIGIGVVL 138
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
496-700 |
5.48e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.86 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLI---SALL--------------------GQMQLQKGVVAVSGP--------- 543
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtgtiewifkdeknkkktKEKEKVLEKLVIQKTrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 544 -----LAYVSQQA--WIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKD-LNSLPYgdltechyphlqigerg 608
Cdd:PRK13651 102 eirrrVGVVFQFAeyQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGLDESyLQRSPF----------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 609 vNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEI 687
Cdd:PRK13651 165 -ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKI 243
|
250
....*....|....
gi 1958746143 688 CEKG-THKELMEER 700
Cdd:PRK13651 244 IKDGdTYDILSDNK 257
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
490-684 |
5.77e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 490 SGSPKSVLHNISFVvrKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------------PLAYVSQQAWIFHG- 556
Cdd:TIGR01257 941 SGRPAVDRLNITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 NVRENILFgekynhqryqhTVHVCGLQKDLNSLPYGDLTECHYPHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDD 636
Cdd:TIGR01257 1019 TVAEHILF-----------YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958746143 637 PLSAVDAHVGKHVFEECIKKTlKGKTVVLVTHQLqflescDEVILLED 684
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHM------DEADLLGD 1128
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
497-680 |
6.21e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.48 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLgqmqlqkgvvAVSGPLAYVSqqawifhgnvrenilFGEKYNHQRyqhT 576
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------YASGKARLIS---------------FLPKFSRNK---L 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 577 VHVCGLQKdlnslpygdLTECHYPHLQIGERGVNLSGGQRQRISLARAVYAN--RQLYLLDDPLSAVDaHVGKHVFEECI 654
Cdd:cd03238 63 IFIDQLQF---------LIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLH-QQDINQLLEVI 132
|
170 180
....*....|....*....|....*..
gi 1958746143 655 KKTL-KGKTVVLVTHQLQFLESCDEVI 680
Cdd:cd03238 133 KGLIdLGNTVILIEHNLDVLSSADWII 159
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
494-700 |
6.52e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQK-GVVAVSG-PLAYVSQQAWIFHG--------------- 556
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGkPVKIRNPQQAIAQGiamvpedrkrdgivp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 --NVRENIL--------FGEKYNHQRYQHTVhvcglQKDLNSLPYGDLTechyPHLQIGergvNLSGGQRQRISLARAVY 626
Cdd:PRK13549 355 vmGVGKNITlaaldrftGGSRIDDAAELKTI-----LESIQRLKVKTAS----PELAIA----RLSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 627 ANRQLYLLDDPLSAVDahVG-KHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 700
Cdd:PRK13549 422 LNPKILILDEPTRGID--VGaKYEIYKLINQLVQqGVAIIVISSELpEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
491-732 |
7.61e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.52 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 491 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVS-----GPLAYVSQQ----------AWIFH 555
Cdd:PRK11022 17 SAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKlefngQDLQRISEKerrnlvgaevAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 556 G---------NVRENILFGEKYnHQ------RYQHTVhvcglqkDLNSL-----PYGDLTEchYPHlqigergvNLSGGQ 615
Cdd:PRK11022 97 DpmtslnpcyTVGFQIMEAIKV-HQggnkktRRQRAI-------DLLNQvgipdPASRLDV--YPH--------QLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 616 RQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE---ECIKKtlKGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKG 691
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIElllELQQK--ENMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958746143 692 THKELmeergryaklihnlrglqFKDPEHIYNVAMVETLKE 732
Cdd:PRK11022 237 KAHDI------------------FRAPRHPYTQALLRALPE 259
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
496-669 |
9.23e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.30 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV--SGPLAYVSQQAWIFHGNVRENILFGEKYNHQRY 573
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 574 QhtvhvcGL-QKDLNSLpygdLTECHYPHlqIGERGVN----------LSGGQRQRISLARAVYANRQLYLLDDPLSAVD 642
Cdd:TIGR00954 547 R------GLsDKDLEQI----LDNVQLTH--ILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*..
gi 1958746143 643 AHVGKHVFEECIKktlKGKTVVLVTHQ 669
Cdd:TIGR00954 615 VDVEGYMYRLCRE---FGITLFSVSHR 638
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
497-732 |
1.71e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.94 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPlAYVSQQAW--------IFH--------GNVRE 560
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrkigmVFQnpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDltechyphlqigERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:PRK13642 102 DVAFGmENQGIPREEMIKRVDEALLAVNMLDFKT------------REPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 640 AVDAhVGKHVFEECIKKtLKGK---TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL------MEERGR----YAKL 706
Cdd:PRK13642 170 MLDP-TGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELfatsedMVEIGLdvpfSSNL 247
|
250 260
....*....|....*....|....*..
gi 1958746143 707 IHNLRGLQFKDPE-HIYNVAMVETLKE 732
Cdd:PRK13642 248 MKDLRKNGFDLPEkYLSEDELVELLAD 274
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
494-670 |
1.93e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALlGQMQLQKGVVAVSGPLAYVSQQAW--------------------- 552
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYerrvnlnrlrrqvsmvhpkpn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 IFHGNVRENILFGEKYNHQRYQhtVHVCGLQKdlNSLPYGDLTEcHYPHlQIGERGVNLSGGQRQRISLARAVYANRQLY 632
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVGWRPK--LEIDDIVE--SALKDADLWD-EIKH-KIHKSALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958746143 633 LLDDPLSAVDAHVGKHVFEECIKKTLKGK-TVVLVTHQL 670
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
468-759 |
2.49e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 468 QRAELYSEQSLSDQGVASPERQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALL------------GQMQLQK 535
Cdd:PRK10261 3 HSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqagglvqcDKMLLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 536 ---GVVAVSGPLAYVSQQ------AWIFHGNVRE-NILF--GEKYN-----HQRYQHTVHVCGLQK--DLNSLPYGDLTE 596
Cdd:PRK10261 83 rsrQVIELSEQSAAQMRHvrgadmAMIFQEPMTSlNPVFtvGEQIAesirlHQGASREEAMVEAKRmlDQVRIPEAQTIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 597 CHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGKT---VVLVTHQLQFL 673
Cdd:PRK10261 163 SRYPH--------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMsmgVIFITHDMGVV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 674 -ESCDEVILLEDGEICEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAMVETLKESQAQRDEDA----VLASGDE 748
Cdd:PRK10261 233 aEIADRVLVMYQGEAVETGSVEQI------------------FHAPQHPYTRALLAAVPQLGAMKGLDYprrfPLISLEH 294
|
330
....*....|.
gi 1958746143 749 RDEgKEPETEE 759
Cdd:PRK10261 295 PAK-QEPPIEQ 304
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
478-700 |
3.01e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 478 LSDQGVASPerqsgspksvlhnISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHG 556
Cdd:PRK11288 263 LKGPGLREP-------------ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 557 -----------------NVRENILFGEKYNHQRYqhtvhvcGLQkdLNSLPYGDLTECHYPHLQIGERG-----VNLSGG 614
Cdd:PRK11288 330 imlcpedrkaegiipvhSVADNINISARRHHLRA-------GCL--INNRWEAENADRFIRSLNIKTPSreqliMNLSGG 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 615 QRQRISLARAVYANRQLYLLDDPLSAVDahVG-KHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKG 691
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGID--VGaKHEIYNVIYELAAqGVAVLFVSSDLpEVLGVADRIVVMREGRIAGEL 478
|
....*....
gi 1958746143 692 THKELMEER 700
Cdd:PRK11288 479 AREQATERQ 487
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
494-714 |
3.88e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP--LAYVSQQAWIFHGNVREN------ILFG 565
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLLAQNattpgdITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 566 EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTECHYPHLQiGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHV 645
Cdd:PRK10253 100 ELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLA-DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 646 GKHVFE--ECIKKTlKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEergryAKLIHNLRGLQ 714
Cdd:PRK10253 179 QIDLLEllSELNRE-KGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT-----AELIERIYGLR 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
497-686 |
5.79e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHG--------------NVREN 561
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkEIDFKSSKEALENGismvhqelnlvlqrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFGekynhqRYQHTvhvcGLQKDLNSLpYGDlTECHYPHLQIG----ERGVNLSGGQRQRISLARAVYANRQLYLLDDP 637
Cdd:PRK10982 94 MWLG------RYPTK----GMFVDQDKM-YRD-TKAIFDELDIDidprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958746143 638 LSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGE 686
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRDGQ 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
500-701 |
5.95e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 500 ISFVVRKGKVLGICGNVGSGKSSLISALLGqMQLQKGVVAVSG-PL------------AYVSQQAwifhgnvreNILFGE 566
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGqPLeawsaaelarhrAYLSQQQ---------TPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 567 KYNH--QRYQHT-VHVCGLQKDLNslpygDLTEchypHLQIG---ERGVN-LSGGQRQRISLA-------RAVYANRQLY 632
Cdd:PRK03695 85 PVFQylTLHQPDkTRTEAVASALN-----EVAE----ALGLDdklGRSVNqLSGGEWQRVRLAavvlqvwPDINPAGQLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 633 LLDDPLSAVDahVGKHVFEECIKKTL--KGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERG 701
Cdd:PRK03695 156 LLDEPMNSLD--VAQQAALDRLLSELcqQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
599-727 |
6.00e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.66 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 599 YPHLqigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVF-------EECikktlkGKTVVLVTHQLQ 671
Cdd:PRK11308 151 YPHM--------FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLnlmmdlqQEL------GLSYVFISHDLS 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 672 FLES-CDEVILLEDGEICEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAMV 727
Cdd:PRK11308 217 VVEHiADEVMVMYLGRCVEKGTKEQI------------------FNNPRHPYTQALL 255
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
504-686 |
6.77e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 51.64 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 504 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-LAYVSQQAWI-FHGNVREnILFG---EKYNHQRYQHTVh 578
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYIKAdYEGTVRD-LLSSitkDFYTHPYFKTEI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 579 VCGLQKDlnslpygdltechyphlQIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVF 650
Cdd:cd03237 100 AKPLQIE-----------------QILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaSKVIRRFA 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958746143 651 EEcikktlKGKTVVLVTHQLQFLESCDEVILLEDGE 686
Cdd:cd03237 163 EN------NEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
851-970 |
8.62e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 52.08 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 851 KHHMYQLVYIASMMSVLTFgIIKGFTFTNTTLMAS------SSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELD 924
Cdd:cd18545 33 NGDLSGLLIIALLFLALNL-VNWVASRLRIYLMAKvgqrilYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLS 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958746143 925 VRLPFHAENFLQQFSMVVFILVIMAA-SFPVVLVVLAGLAILFFILL 970
Cdd:cd18545 112 DLLSNGLINLIPDLLTLVGIVIIMFSlNVRLALVTLAVLPLLVLVVF 158
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
496-701 |
8.68e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.55 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAY-------VSQQA---------WIFHGNV 558
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkPLDYskrgllaLRQQVatvfqdpeqQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 559 RENILF-------GEKYNHQRYQHTVHVCGLQkdlnslpygdltecHYPHLQIGergvNLSGGQRQRISLARAVYANRQL 631
Cdd:PRK13638 96 DSDIAFslrnlgvPEAEITRRVDEALTLVDAQ--------------HFRHQPIQ----CLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 632 YLLDDPLSAVDAhVGKHVFEECIKKTL-KGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKG------THKELMEERG 701
Cdd:PRK13638 158 LLLDEPTAGLDP-AGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
842-965 |
9.90e-07 |
|
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: 51.71 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 842 NVNQTLQDTKHHMYQLVYIASMMSVLTFgiIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMD 921
Cdd:cd18577 38 SPDEFLDDVNKYALYFVYLGIGSFVLSY--IQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTN 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 922 ELDV----RLPFhaenFLQQFSMVV------FI------LVIMaASFPVVLVVLAGLAIL 965
Cdd:cd18577 116 LIQDgigeKLGL----LIQSLSTFIagfiiaFIyswkltLVLL-ATLPLIAIVGGIMGKL 170
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
178-411 |
9.93e-07 |
|
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: 51.78 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 178 VLFWALAWAINY-------RTAIRLKVALSTLIFKNL--LSFKTLTHISAGEVLNVLSSDSYS---LFEAALFCPLPATI 245
Cdd:cd07346 46 LLLALLRALLSYlrrylaaRLGQRVVFDLRRDLFRHLqrLSLSFFDRNRTGDLMSRLTSDVDAvqnLVSSGLLQLLSDVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 246 piLMVVCAVYAFFILGSTALVGICVY-LIFIPIQMFMAKLNSAFRRSAISVtDKRVQTMNEFLTCIKLIKMYAWEKSFMN 324
Cdd:cd07346 126 --TLIGALVILFYLNWKLTLVALLLLpLYVLILRYFRRRIRKASREVRESL-AELSAFLQESLSGIRVVKAFAAEEREIE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 325 TIHDIRKREKKLLEKAGYVQSGNSALAPIVSTI--AIVSTFTCHIFLKRTLTAPVAFSVIAMFNVMKFSIAILPFSVKAV 402
Cdd:cd07346 203 RFREANRDLRDANLRAARLSALFSPLIGLLTALgtALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQL 282
|
....*....
gi 1958746143 403 AEASVSLRR 411
Cdd:cd07346 283 QQALASLER 291
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
496-687 |
1.03e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAY-------------VSQQAWIFHG-NVRE 560
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnPCARltpakahqlgiylVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 NILFGEKYNHQRYQhtvHVCGLQKDLNslpygdlteCHY-PHLQIGergvNLSGGQRQRISLARAVYANRQLYLLDDPLS 639
Cdd:PRK15439 106 NILFGLPKRQASMQ---KMKQLLAALG---------CQLdLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958746143 640 AVDAHVGKHVFEEcIKKTL-KGKTVVLVTHQL-QFLESCDEVILLEDGEI 687
Cdd:PRK15439 170 SLTPAETERLFSR-IRELLaQGVGIVFISHKLpEIRQLADRISVMRDGTI 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
113-687 |
1.10e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 52.49 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 113 RVVWKFQRTRVLMDVVANILC-IIMAALgpTVLIHQILQHVTNISSGHIGISICLCLALFATefTKVLFWALAWAINyRT 191
Cdd:COG4615 5 RLLLRESRWLLLLALLLGLLSgLANAGL--IALINQALNATGAALARLLLLFAGLLVLLLLS--RLASQLLLTRLGQ-HA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 192 AIRLKVALStlifKNLLS--FKTLTHISAGEVLNVLSSDSYSLFEAALFCPLPATIPILMVVCAVYAFFI-----LGSTA 264
Cdd:COG4615 80 VARLRLRLS----RRILAapLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWLspplfLLTLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 265 LVGICVYLIFIPIQMFMA--------------------------KLNS----AFRRSAISVTDKRVQTMNefltcIKLIK 314
Cdd:COG4615 156 LLGLGVAGYRLLVRRARRhlrrareaedrlfkhfrallegfkelKLNRrrrrAFFDEDLQPTAERYRDLR-----IRADT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 315 MYAWEKSFMNTIhdirkrekkllekagyvqsgnsALAPIVSTIAIVSTFTchiflkrTLTAPVAFSVIAMFNVMKFSIAI 394
Cdd:COG4615 231 IFALANNWGNLL----------------------FFALIGLILFLLPALG-------WADPAVLSGFVLVLLFLRGPLSQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 395 LPFSVKAVAEASVSLRRMKKILVAksppsyITQPEDPDTILLLANATLTWeqeinrkrgplktqdqrrhvfkkqraelys 474
Cdd:COG4615 282 LVGALPTLSRANVALRKIEELELA------LAAAEPAAADAAAPPAPADF------------------------------ 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 475 eQSLSDQGVA-SPERQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAW 552
Cdd:COG4615 326 -QTLELRGVTyRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqPVTADNREAY 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 ifhgnvRENI--------LFGEKYNhqryqhtVHVCGLQKDLNSLpygdLTEchyphLQIG-----ERG----VNLSGGQ 615
Cdd:COG4615 405 ------RQLFsavfsdfhLFDRLLG-------LDGEADPARAREL----LER-----LELDhkvsvEDGrfstTDLSQGQ 462
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 616 RQRISLARAVYANRQLYLLD------DPlsavdahVGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 687
Cdd:COG4615 463 RKRLALLVALLEDRPILVFDewaadqDP-------EFRRVFYTELLPELKarGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
492-691 |
1.18e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.24 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 492 SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQmqLQKGVVAVSGPL-----------------AYVSQQ---A 551
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGI--LPAGVRQTAGRVlldgkpvapcalrgrkiATIMQNprsA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 552 W----IFHGNVRENIL-FGEKYNHQRYQHTVHVCGLQKDLNSLPYgdltechYPhlqigergVNLSGGQRQRISLARAVY 626
Cdd:PRK10418 92 FnplhTMHTHARETCLaLGKPADDATLTAALEAVGLENAARVLKL-------YP--------FEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 627 ANRQLYLLDDPLSAVDAHVGKHVFE--ECIKKTlKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKG 691
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDllESIVQK-RALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
488-722 |
1.22e-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: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSslISALlGQMQLqkgvvaVSGPLAYVSQQAWiFHGnvrENIL-FGE 566
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKS--VTAL-SILRL------LPDPAAHPSGSIL-FDG---QDLLgLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 567 KY-NHQR-------YQ---------HTV----------HVcGLQKD---------------------LNSlpygdltech 598
Cdd:COG4172 84 RElRRIRgnriamiFQepmtslnplHTIgkqiaevlrlHR-GLSGAaararalellervgipdperrLDA---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 599 YPHlQigergvnLSGGQRQRISLARAVyANR-QLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQL---- 670
Cdd:COG4172 153 YPH-Q-------LSGGQRQRVMIAMAL-ANEpDLLIADEPTTALDVTVQAQILD--LLKDLQrelGMALLLITHDLgvvr 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958746143 671 QFlesCDEVILLEDGEICEKGTHKELmeergryaklihnlrglqFKDPEHIY 722
Cdd:COG4172 222 RF---ADRVAVMRQGEIVEQGPTAEL------------------FAAPQHPY 252
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
488-699 |
1.26e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 51.66 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVlHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAW---------IF--- 554
Cdd:COG4608 26 RTVGVVKAV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDITGLSGRELrplrrrmqmVFqdp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 HG--N----VRENILFGEKYNH--------QRYQHTVHVCGLQKDlnslpygdltecH---YPHlqigErgvnLSGGQRQ 617
Cdd:COG4608 105 YAslNprmtVGDIIAEPLRIHGlaskaerrERVAELLELVGLRPE------------HadrYPH----E----FSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 618 RISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTH 693
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVlnlLED-LQDEL-GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPR 242
|
....*.
gi 1958746143 694 KELMEE 699
Cdd:COG4608 243 DELYAR 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
611-696 |
1.26e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.07 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 611 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTH-QLQFLESCDEVILLEDGEICE 689
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDP-ENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
....*..
gi 1958746143 690 KGTHKEL 696
Cdd:PRK14247 226 WGPTREV 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
500-726 |
1.38e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.63 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 500 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-LAYVSQQAWIfhgNVRENI--LFgekynhqryqht 576
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWR---AVRSDIqmIF------------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 577 vhvcglQKDLNSL-P---YGDLT----ECHYPHL---QIGER--------GV--NL--------SGGQRQRISLARAVYA 627
Cdd:PRK15079 105 ------QDPLASLnPrmtIGEIIaeplRTYHPKLsrqEVKDRvkammlkvGLlpNLinryphefSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 628 NRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELmeergry 703
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVN--LLQQLQremGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV------- 249
|
250 260
....*....|....*....|...
gi 1958746143 704 aklihnlrglqFKDPEHIYNVAM 726
Cdd:PRK15079 250 -----------YHNPLHPYTKAL 261
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
604-971 |
1.55e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 604 IGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgkhvfEECIKKT---LKG---KTVVLVTHQLQFLESCD 677
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-----EYLVQKTinnLKGnenRITIIIAHRLSTIRYAN 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 678 EVILLEDGE-----------------------------------------------ICEKGTHKELMEER-GRYAKLIHN 709
Cdd:PTZ00265 648 TIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTMINN 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 710 ------------------LRGLQFKDPEHIYNVAMVETL-----KESQAQRDEDAVLASGDERD-EGKEPETEEFVDIKA 765
Cdd:PTZ00265 728 qkvsskkssnndndkdsdMKSSAYKDSERGYDPDEMNGNskhenESASNKKSCKMSDENASENNaGGKLPFLRNLFKRKP 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 766 pvhqliqiESPQEGIVTWKTYHTYIKASGGYLVSFLV---LCLFFLMMGSSAFSTWWLGLWLDSGSQvicapqsnetacn 842
Cdd:PTZ00265 808 --------KAPNNLRIVYREIFSYKKDVTIIALSILVaggLYPVFALLYAKYVSTLFDFANLEANSN------------- 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 843 vnqtlqdtKHHMYQLVYIASMMSVLTfgiIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDT---TPtGRLMNRFSKD 919
Cdd:PTZ00265 867 --------KYSLYILVIAIAMFISET---LKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRD 934
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 920 MDELDVRLpfhAENFLQQFSMVVFILVIMAASF---PVVLVVLAGlaiLFFILLR 971
Cdd:PTZ00265 935 VHLLKTGL---VNNIVIFTHFIVLFLVSMVMSFyfcPIVAAVLTG---TYFIFMR 983
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
506-673 |
1.69e-06 |
|
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: 48.91 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 506 KGKVLGICGNVGSGKSSLISALLGQMQLQ-KGVVAVSGPLAYVSQQAWIFhgnvrenilfgekynhqryqhtvhvcglqk 584
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 585 dlnslpygdltechypHLQIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEC------IKKTL 658
Cdd:smart00382 51 ----------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllLLKSE 114
|
170
....*....|....*
gi 1958746143 659 KGKTVVLVTHQLQFL 673
Cdd:smart00382 115 KNLTVILTTNDEKDL 129
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
611-680 |
1.73e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 1.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 611 LSGGQRQRISLARAV----YANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVI 680
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
858-968 |
1.92e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.03 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 858 VYIASMMSVLT--FGIIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFL 935
Cdd:TIGR00958 204 IFFMCLLSIASsvSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110
....*....|....*....|....*....|....
gi 1958746143 936 QQFSMVVFILVIM-AASFPVVLVVLAGLAILFFI 968
Cdd:TIGR00958 284 RNLVMLLGLLGFMlWLSPRLTMVTLINLPLVFLA 317
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
860-970 |
4.74e-06 |
|
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: 50.60 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 860 IASMMSVLtFGIIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSkDMDELdvrlpfhaENFLQQFS 939
Cdd:COG2274 204 LALLFEGL-LRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESI--------REFLTGSL 273
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958746143 940 --------MVVFILVIMAA-SFPVVLVVLAGLAILFFILL 970
Cdd:COG2274 274 ltalldllFVLIFLIVLFFySPPLALVVLLLIPLYVLLGL 313
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
497-686 |
4.95e-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: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWIFHG--------------NVREN 561
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkPVRIRSPRDAIALGigmvhqhfmlvpnlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 562 ILFG-EKYNH----------------QRYqhtvhvcGLQKDLNSLpygdltechyphlqIGErgvnLSGGQRQRISLARA 624
Cdd:COG3845 101 IVLGlEPTKGgrldrkaararirelsERY-------GLDVDPDAK--------------VED----LSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 625 VYANRQLYLLDDPlSAV--DAHVgKHVFEecIKKTLK--GKTVVLVTHQLQ-FLESCDEVILLEDGE 686
Cdd:COG3845 156 LYRGARILILDEP-TAVltPQEA-DELFE--ILRRLAaeGKSIIFITHKLReVMAIADRVTVLRRGK 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
496-685 |
5.25e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 48.97 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 496 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP---------------------LAYVSQ----- 549
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaqaspreilalrrrtIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 550 ----------QAWIFHGnvrenilFGEKYNHQRYQHTVHVCGLQKDLNSLpygdltechYPhlqigergVNLSGGQRQRI 619
Cdd:COG4778 106 prvsaldvvaEPLLERG-------VDREEARARARELLARLNLPERLWDL---------PP--------ATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 620 SLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDG 685
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
497-691 |
5.42e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.15 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG------PLAYVSQQ--------AWIF-HGNVRE- 560
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrDLYALSEAerrrllrtEWGFvHQHPRDg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 561 ---------NIlfGEKYNHQRYQHtvhvcglqkdlnslpYGD--------LTECHYPHLQIGERGVNLSGGQRQRISLAR 623
Cdd:PRK11701 102 lrmqvsaggNI--GERLMAVGARH---------------YGDiratagdwLERVEIDAARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 624 AVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTL---KGKTVVLVTHQL---QFLesCDEVILLEDGEICEKG 691
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLD--LLRGLvreLGLAVVIVTHDLavaRLL--AHRLLVMKQGRVVESG 234
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
601-686 |
7.99e-06 |
|
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: 48.76 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 601 HLQIGERGVNLSGGQRQRISLARAVyANRQ----LYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC 676
Cdd:cd03271 160 YIKLGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCA 238
|
90
....*....|..
gi 1958746143 677 DEVILL--EDGE 686
Cdd:cd03271 239 DWIIDLgpEGGD 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
499-696 |
1.25e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQlQKGVVAVSGplayvsqqawIFHG----NVRENILfgekyNHQRYQ 574
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIGGSA----------TFNGreilNLPEKEL-----NKLRAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 575 HTVHVcgLQKDLNSL-PY---GD-LTEC---H------------------------------YPHlqigergvNLSGGQR 616
Cdd:PRK09473 98 QISMI--FQDPMTSLnPYmrvGEqLMEVlmlHkgmskaeafeesvrmldavkmpearkrmkmYPH--------EFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 617 QRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLE-SCDEVILLEDGEICEKGT 692
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT--LLNELKrefNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGN 245
|
....
gi 1958746143 693 HKEL 696
Cdd:PRK09473 246 ARDV 249
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
489-716 |
1.39e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 489 QSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGP-------------------LAYV 547
Cdd:PRK13649 13 QAGTPfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkvgLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 548 SQQAWIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDL-NSLPYgdltechyphlqigergvNLSGGQRQRI 619
Cdd:PRK13649 93 FPESQLFEETVLKDVAFGpqnfgvsQEEAEALAREKLALVGISESLfEKNPF------------------ELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 620 SLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHK---- 694
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGKPKdifq 234
|
250 260 270
....*....|....*....|....*....|
gi 1958746143 695 --ELMEERG----RYAKLIHNL--RGLQFK 716
Cdd:PRK13649 235 dvDFLEEKQlgvpKITKFAQRLadRGISFS 264
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
887-970 |
1.67e-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: 47.81 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 887 SLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAA-SFPVVLVVLAGLAIL 965
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLlDWVLTLVTLAVVPLA 149
|
....*
gi 1958746143 966 FFILL 970
Cdd:cd18551 150 FLIIL 154
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
504-686 |
2.33e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 504 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSGPLAYVSQqaWI---FHGNVRENIlfgekynhqrYQHTvhvc 580
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLL----------RSIT---- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 581 glqKDLNSLPYgdLTECHYPhLQIG---ERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHV 649
Cdd:PRK13409 426 ---DDLGSSYY--KSEIIKP-LQLErllDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRI 499
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958746143 650 FEEcikktlKGKTVVLVTHQLQFLESCDEVILLEDGE 686
Cdd:PRK13409 500 AEE------REATALVVDHDIYMIDYISDRLMVFEGE 530
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
611-698 |
2.64e-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: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 611 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 687
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-IQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
90
....*....|.
gi 1958746143 688 CEKGTHKELME 698
Cdd:PRK11650 214 EQIGTPVEVYE 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
601-696 |
2.69e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 601 HLQIGERGVNLSGGQRQRISLARAVYA---NRQLYLLDDPLSavdahvGKHvFEEcIKKTL--------KGKTVVLVTHQ 669
Cdd:TIGR00630 820 YIRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTT------GLH-FDD-IKKLLevlqrlvdKGNTVVVIEHN 891
|
90 100 110
....*....|....*....|....*....|...
gi 1958746143 670 LQFLESCDEVILL------EDGEICEKGTHKEL 696
Cdd:TIGR00630 892 LDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
493-542 |
3.17e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 3.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958746143 493 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG 542
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
864-968 |
3.64e-05 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 864 MSVLTFGI-----IKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQF 938
Cdd:cd18784 42 MGLLAIASsvaagIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSL 121
|
90 100 110
....*....|....*....|....*....|.
gi 1958746143 939 SMVVFILVIMAA-SFPVVLVVLAGLAILFFI 968
Cdd:cd18784 122 VKAIGVIVFMFKlSWQLSLVTLIGLPLIAIV 152
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
500-696 |
4.05e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 500 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG-PLAYVSQQAWI---------FHgnvreniLF----- 564
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkPVTAEQPEDYRklfsavftdFH-------LFdqllg 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 565 --GEKYNHQRYQHTVHVCGLQKDLnSLPYGDLTEchyphlqigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 642
Cdd:PRK10522 415 peGKPANPALVEKWLERLKMAHKL-ELEDGRISN------------LKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958746143 643 AHVgKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICE-KGTHKEL 696
Cdd:PRK10522 482 PHF-RREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
846-971 |
4.69e-05 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 46.64 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 846 TLQDTKHHMYQLVYIASMMSVLTFGIIKGFTFTNTTLMASS-----SLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDM 920
Cdd:cd18541 28 ALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASrrieyDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958746143 921 DEldVR--LPFHAENFLQQFSMVVFILVIMAA-SFPVVLVVLAGLAILFFILLR 971
Cdd:cd18541 108 NA--VRmaLGPGILYLVDALFLGVLVLVMMFTiSPKLTLIALLPLPLLALLVYR 159
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
887-968 |
5.88e-05 |
|
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: 46.33 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 887 SLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAA-SFPVVLVVLAGLAIL 965
Cdd:cd18546 73 DLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVlDPRLALVALAALPPL 152
|
...
gi 1958746143 966 FFI 968
Cdd:cd18546 153 ALA 155
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
853-971 |
6.59e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 46.02 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 853 HMYQLVYIASMMsVLTFGIIKGFTFTNTTLM---ASSSLHN-RV--FNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVR 926
Cdd:cd18565 49 PRGQLWLLGGLT-VAAFLLESLFQYLSGVLWrrfAQRVQHDlRTdtYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERF 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1958746143 927 LPFHAENFLQQFSMVVFILVIMAA-SFPVVLVVLAGLAILFFILLR 971
Cdd:cd18565 128 LDDGANSIIRVVVTVLGIGAILFYlNWQLALVALLPVPLIIAGTYW 173
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
601-682 |
6.97e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 601 HLQIGERGVNLSGGQRQRISLARAVYA---NRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCD 677
Cdd:PRK00635 800 YLPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVAD 879
|
....*
gi 1958746143 678 EVILL 682
Cdd:PRK00635 880 YVLEL 884
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
499-645 |
7.33e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 499 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVSG----PLAYVSQQAwifhgnVRENI--LFGEKYNHQR 572
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridTLSPGKLQA------LRRDIqfIFQDPYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 573 YQHTV--------HVCGL-QKDLNSLPYGDLTE---------CHYPHlqigergvNLSGGQRQRISLARAVYANRQLYLL 634
Cdd:PRK10261 416 PRQTVgdsimeplRVHGLlPGKAAAARVAWLLErvgllpehaWRYPH--------EFSGGQRQRICIARALALNPKVIIA 487
|
170
....*....|.
gi 1958746143 635 DDPLSAVDAHV 645
Cdd:PRK10261 488 DEAVSALDVSI 498
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
865-966 |
8.22e-05 |
|
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: 45.55 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 865 SVLTFgiIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSM---- 940
Cdd:cd18576 50 AVFSF--FRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTligg 127
|
90 100 110
....*....|....*....|....*....|...
gi 1958746143 941 VVFILVI-------MAASFPVVLVVlaglAILF 966
Cdd:cd18576 128 VVLLFFIswkltllMLATVPVVVLV----AVLF 156
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
503-670 |
9.18e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 503 VVRKGKVLGICGNVGSGKSSLISALLGQM------------------------------QLQKGVVAVSGPLAYVSQQAW 552
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELipnlgdyeeepswdevlkrfrgtelqnyfkKLYNGEIKVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 553 IFHGNVREnILfgEKYNhQRyqhtvhvcGLQKDLNSLPygDLTEchyphlqIGERGV-NLSGGQRQRISLARAVYANRQL 631
Cdd:PRK13409 175 VFKGKVRE-LL--KKVD-ER--------GKLDEVVERL--GLEN-------ILDRDIsELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958746143 632 YLLDDPLSAVDahvgkhVFE-----ECIKKTLKGKTVVLVTHQL 670
Cdd:PRK13409 234 YFFDEPTSYLD------IRQrlnvaRLIRELAEGKYVLVVEHDL 271
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
488-696 |
1.08e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 488 RQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSslISALlGQMQLQKgvvavSGPLAYvSQQAWIFHGN---------- 557
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKS--VTAL-SILRLLP-----SPPVVY-PSGDIRFHGEsllhaseqtl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 558 --VREN---ILFGEKYNHQRYQHTVH-----VCGLQKDLNSLP-YGDLTEC--------------HYPHlqigergvNLS 612
Cdd:PRK15134 87 rgVRGNkiaMIFQEPMVSLNPLHTLEkqlyeVLSLHRGMRREAaRGEILNCldrvgirqaakrltDYPH--------QLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 613 GGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGK---TVVLVTHQLQFLES-CDEVILLEDGEIC 688
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQ--LLRELQQElnmGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
....*...
gi 1958746143 689 EKGTHKEL 696
Cdd:PRK15134 237 EQNRAATL 244
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
843-919 |
1.11e-04 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 45.20 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 843 VNQTLQDTKHHMYQLVYIASMMSVLtFGIIKGFTFTNTTLMASSS------LHNRVFNKIVSSPMSFFDTTPTGRLMNRF 916
Cdd:cd18573 26 ASKESGDIEIFGLSLKTFALALLGV-FVVGAAANFGRVYLLRIAGerivarLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
...
gi 1958746143 917 SKD 919
Cdd:cd18573 105 SSD 107
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
854-957 |
1.15e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 45.32 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 854 MYQLVYIASMMSVLTFgiIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELD----VRLPF 929
Cdd:cd18780 45 VLILLGVVLIGSIATF--LRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQnavtVNLSM 122
|
90 100 110
....*....|....*....|....*....|....*
gi 1958746143 930 HAENFLQQFSMVVFILV-------IMAASFPVVLV 957
Cdd:cd18780 123 LLRYLVQIIGGLVFMFTtswkltlVMLSVVPPLSI 157
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
497-700 |
1.52e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKG-------VVAVSGPLAyvSQQAW--IFHG--------NVR 559
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkEVTFNGPKS--SQEAGigIIHQelnlipqlTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 560 ENILFG-EKYNH-------QRYQHTVhvcGLQKDLNsLPYGdltechyPHLQIGErgvnLSGGQRQRISLARAVYANRQL 631
Cdd:PRK10762 98 ENIFLGrEFVNRfgridwkKMYAEAD---KLLARLN-LRFS-------SDKLVGE----LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958746143 632 YLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQ-FLESCDEVILLEDGE-ICEKGThKELMEER 700
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFR--VIRELKsqGRGIVYISHRLKeIFEICDDVTVFRDGQfIAEREV-ADLTEDS 232
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
857-970 |
1.52e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 44.89 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 857 LVYIASMMSVLT-----FGIIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSkdmdELD-VRlpfh 930
Cdd:cd18782 41 LYVIGVVMLVAAlleavLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS----ELDtIR---- 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1958746143 931 aeNFLQQFS---------MVVFILVIMAASFPVVLVVLAGLAILFFILL 970
Cdd:cd18782 113 --GFLTGTAlttlldvlfSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF 159
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
605-752 |
1.75e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 605 GERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLE 683
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVID 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 684 DGEICEKGTHKELMEERGRyaklihnlRGLQFKdPEHiynVAMVETLKESQAQRDEDAVLASGDERDEG 752
Cdd:NF000106 219 RGRVIADGKVDELKTKVGG--------RTLQIR-PAH---AAELDRMVGAIAQAGLDGIAGATADHEDG 275
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
486-687 |
1.76e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 486 PERQsgspksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQK--GVV--------------AVSGPLAYVS- 548
Cdd:NF040905 271 PERK------VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVfkdgkevdvstvsdAIDAGLAYVTe 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 549 ---QQAWIFHGNVRENI--------------------LFGEKYnhqryqhtvhvcglQKDLNslpygdlTECHyphlQIG 605
Cdd:NF040905 345 drkGYGLNLIDDIKRNItlanlgkvsrrgvideneeiKVAEEY--------------RKKMN-------IKTP----SVF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 606 ERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDahVG-KhvFE-ECIKKTL--KGKTVVLVTHQL-QFLESCDEVI 680
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID--VGaK--YEiYTIINELaaEGKGVIVISSELpELLGMCDRIY 475
|
....*..
gi 1958746143 681 LLEDGEI 687
Cdd:NF040905 476 VMNEGRI 482
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
610-687 |
1.86e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 44.31 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 610 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFE---ECIKKtlKGKTVVLVTHQLQF-LESCDEVILLEDG 685
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLElteKIVEE--NNLTTLMVTHNMEQaLDYGNRLIMMHEG 225
|
..
gi 1958746143 686 EI 687
Cdd:COG1101 226 RI 227
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
609-686 |
2.39e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 609 VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikktlKGKTVVLVTHQLQFLESCDEVIL 681
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKKTALVVEHDLAVLDYLSDRIH 143
|
....*
gi 1958746143 682 LEDGE 686
Cdd:cd03222 144 VFEGE 148
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
888-968 |
2.98e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 44.04 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 888 LHNRVFNKIVSSPMSFFDTTPTGRLMnrfsKDMDELD-VRlpfhaeNFLQQ---------FSMVVFILVIMAASFPVVLV 957
Cdd:cd18783 77 LALRTFDRLLSLPIDFFERTPAGVLT----KHMQQIErIR------QFLTGqlfgtlldaTSLLVFLPVLFFYSPTLALV 146
|
90
....*....|....*.
gi 1958746143 958 VLA-----GLAILFFI 968
Cdd:cd18783 147 VLAfsaliALIILAFL 162
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
604-685 |
3.05e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 604 IGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVI 680
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELL 1091
|
....*
gi 1958746143 681 LLEDG 685
Cdd:PLN03140 1092 LMKRG 1096
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
612-686 |
3.56e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 3.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 612 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTlkgKTVVLVTHQLQFLESCDEVILLEDGE 686
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNTVVTDILHLHGQ 417
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
888-971 |
3.96e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 43.63 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 888 LHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDEldVR-----LPFhaenFLQQFSMVVFILVIMAA-SFPVVLVVLAG 961
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSL--VQrflafGPF----LLGNLLTLVVGLVVMLVlSPPLALVALAS 147
|
90
....*....|
gi 1958746143 962 LAILFFILLR 971
Cdd:cd18543 148 LPPLVLVARR 157
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
888-966 |
4.26e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 43.62 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 888 LHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMAASFP-------VVLVVLA 960
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWklalivlAVVPVLA 156
|
....*.
gi 1958746143 961 GLAILF 966
Cdd:cd18540 157 VVSIYF 162
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
600-698 |
4.59e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 600 PHLQIGERGVNLSGGQRQRISLARAVYANRQ--LYLLDDPlsavdaHVGKHVFE-ECIKKTLK-----GKTVVLVTHQLQ 671
Cdd:TIGR00630 478 DYLSLSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEP------SIGLHQRDnRRLINTLKrlrdlGNTLIVVEHDED 551
|
90 100 110
....*....|....*....|....*....|...
gi 1958746143 672 FLESCDEVILL------EDGEICEKGTHKELME 698
Cdd:TIGR00630 552 TIRAADYVIDIgpgageHGGEVVASGTPEEILA 584
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
874-922 |
7.50e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 42.92 E-value: 7.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958746143 874 GFTFTNTTLMA------SSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDE 922
Cdd:cd18574 57 LLTFAYISLLSvvgervAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQE 111
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
494-637 |
9.20e-04 |
|
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: 43.00 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 494 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVsGP---LAYVSQQawifhgnvRENIlfgekynh 570
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvkLAYVDQS--------RDAL-------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 571 qryqhtvhvcglqkDLNSLPYGDLTECHyPHLQIGERGVN---------------------LSGGQRQRISLARAVYANR 629
Cdd:TIGR03719 398 --------------DPNKTVWEEISGGL-DIIKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGG 462
|
....*...
gi 1958746143 630 QLYLLDDP 637
Cdd:TIGR03719 463 NVLLLDEP 470
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
888-965 |
1.08e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 42.14 E-value: 1.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958746143 888 LHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDvRLPFHAenfLQQFSMVVFILVIMAASFPVVLVVLAGLAIL 965
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVE-RLIADG---IPQGITNVLTLVGVAIILFSINPKLALLTLI 148
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
876-968 |
1.10e-03 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 42.07 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 876 TFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFSMVVFILVIMA-ASFPV 954
Cdd:cd18589 59 IYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLwLSPKL 138
|
90
....*....|....
gi 1958746143 955 VLVVLAGLAILFFI 968
Cdd:cd18589 139 ALLTALGLPLLLLV 152
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
497-680 |
1.59e-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: 41.09 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 497 LHNISFVVRKGKVLGICGNVGSGKSSL----------------ISA----LLGQMQLQKgVVAVSG--PLAYVSQQAwiF 554
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAyarqFLGQMDKPD-VDSIEGlsPAIAIDQKT--T 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 555 HGNVRENIlfG---EKYNHQR--YQHTvhvcGLQKDLNSLpygdlTECHYPHLQIGERGVNLSGGQRQRISLARAVYANR 629
Cdd:cd03270 88 SRNPRSTV--GtvtEIYDYLRllFARV----GIRERLGFL-----VDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958746143 630 Q--LYLLDDPlsavdaHVGKHVFE-ECIKKTLK-----GKTVVLVTHQLQFLESCDEVI 680
Cdd:cd03270 157 TgvLYVLDEP------SIGLHPRDnDRLIETLKrlrdlGNTVLVVEHDEDTIRAADHVI 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
610-686 |
1.79e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.23 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 610 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH----VGKHVFEecikktLKGkTVVLVTHQLQFLESCDEVIL-LED 684
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHLQE------YPG-TVVAVTHDRYFLDNVAGWILeLDR 233
|
..
gi 1958746143 685 GE 686
Cdd:TIGR03719 234 GR 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
609-687 |
3.20e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 40.24 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 609 VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEECIKktlKGKTVVLVTHQLQFLESCD-EVILLED 684
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNR---VGVTVLMATHDIGLISRRSyRMLTLSD 212
|
...
gi 1958746143 685 GEI 687
Cdd:PRK10908 213 GHL 215
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
860-968 |
7.18e-03 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 39.79 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 860 IASMMSVLTFGIIKGFTFTNTTLMASSSLHNRVFNKIVSSPMSFFDTTPTGRLMNRfskdMDELD-VRlpfhaeNFLQQ- 937
Cdd:cd18588 49 LVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVAR----VRELEsIR------QFLTGs 118
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958746143 938 --------FSMVVFILVIMAASFPVVLVVLAGLAILFFI 968
Cdd:cd18588 119 altlvldlVFSVVFLAVMFYYSPTLTLIVLASLPLYALL 157
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| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
890-973 |
9.13e-03 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 39.36 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958746143 890 NRVFNKIVSSPMSFFDTTPTGRLMNRFSKDMDELdVRLPFHA-ENFLqqFSMVVFI--LVIMA-ASFPVVLVVLAGLAIL 965
Cdd:cd18549 79 RDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDI-SELAHHGpEDLF--ISIITIIgsFIILLtINVPLTLIVFALLPLM 155
|
....*...
gi 1958746143 966 FFILLRCG 973
Cdd:cd18549 156 IIFTIYFN 163
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