|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-758 |
1.19e-149 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 477.31 E-value: 1.19e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 12 PLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAendaqKPSLTRAIIKCYWKS 91
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKP-----KPWLLRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 92 YLVLGIF-----------------------------------------------------------------TLIEA--- 103
Cdd:PLN03130 303 FWLGGFFkigndlsqfvgplllnlllesmqngepawigyiyafsifvgvvlgvlceaqyfqnvmrvgfrlrsTLVAAvfr 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 104 --LRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGK 181
Cdd:PLN03130 383 ksLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIIS 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 182 LFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNlaSFFSASkIIVFVT- 260
Cdd:PLN03130 463 KMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFN--SFILNS-IPVLVTv 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 261 --FTTYVLLGSVITASRVFVAVTLYGAVRLTvtLF-FPSAIERVSEAIVSIRRIQTFLLLDE-ISQRNRQLPSdGKKMVH 336
Cdd:PLN03130 540 vsFGVFTLLGGDLTPARAFTSLSLFAVLRFP--LFmLPNLITQAVNANVSLKRLEELLLAEErVLLPNPPLEP-GLPAIS 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 337 VQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP-SHGLVSVHGRIAYVSQQPWVFSGTLR 415
Cdd:PLN03130 617 IKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPQVSWIFNATVR 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 495
Cdd:PLN03130 697 DNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 496 RHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKKDNEESEQPPVPGTPTLR 575
Cdd:PLN03130 777 RQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVEENGEEEDD 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 576 NrtfsESSVWSQQSSRPSL-KDGALESQDTENVPVTLSEENRSEGKVGFQAYKNYFRA-GAHWIVFIfLILLNTAAQVAY 653
Cdd:PLN03130 857 Q----TSSKPVANGNANNLkKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNAlGGAWVVMI-LFLCYVLTEVFR 931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 654 VLQDWWLSYWANKQSmlnvtvngggnvTEKLDLNWYLGIYSGLTVATVLFGIARSllvfYVLVNSS----QTLHNKMFES 729
Cdd:PLN03130 932 VSSSTWLSEWTDQGT------------PKTHGPLFYNLIYALLSFGQVLVTLLNS----YWLIMSSlyaaKRLHDAMLGS 995
|
810 820
....*....|....*....|....*....
gi 685504970 730 ILKAPVLFFDRNPIGRILNRFSKDIGHLD 758
Cdd:PLN03130 996 ILRAPMSFFHTNPLGRIINRFAKDLGDID 1024
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-769 |
4.08e-143 |
|
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: 457.87 E-value: 4.08e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 3 PVYQE--VKPNPLQD--ANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKE----------- 67
Cdd:TIGR00957 190 PLFSEtnHDPNPCPEssASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKEckktrkqpvsa 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 68 -------------------------VLRAENDAQKPSLTRAIIKCY---------------------------------- 88
Cdd:TIGR00957 270 vygkkdpskpkgssqldaneevealIVKSPHKPRKPSLFKVLYKTFgpyflmsfcfkaihdlmmfigpqilsllirfvnd 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 89 -----WKSYLVLGIF-------TLI-------------------------EALRLSNMAMGKTTTGQIVNLLSNDVNKFD 131
Cdd:TIGR00957 350 pmapdWQGYFYTGLLfvcaclqTLIlhqyfhicfvsgmriktavmgavyrKALVITNSARKSSTVGEIVNLMSVDAQRFM 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 132 QVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRII 211
Cdd:TIGR00957 430 DLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 212 KMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLL--GSVITASRVFVAVTLYGAVRLT 289
Cdd:TIGR00957 510 KLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVdeNNILDAEKAFVSLALFNILRFP 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 290 VTLFfPSAIERVSEAIVSIRRIQTFLLLDEI---SQRNRQLPSDGKKMVHVQDFTAFWDKaSETPTLQGLSFTVRPGELL 366
Cdd:TIGR00957 590 LNIL-PMVISSIVQASVSLKRLRIFLSHEELepdSIERRTIKPGEGNSITVHNATFTWAR-DLPPTLNGITFSIPEGALV 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 367 AVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLE 446
Cdd:TIGR00957 668 AVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILP 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 447 DGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQ--ILHEKITILVTHQLQYLKA 524
Cdd:TIGR00957 748 SGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTHGISYLPQ 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 525 ASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKK--------DNEES----------EQPPVPGTPTLRN-------RTF 579
Cdd:TIGR00957 828 VDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTyapdeqqgHLEDSwtalvsgegkEAKLIENGMLVTDvvgkqlqRQL 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 580 SESSVWSQQSSRPSLKDGALESQDTENVPVTLSEENRSE-GKVGFQAYKNYFRAGAHWIVF--IFLILLNTAAQVAyvlQ 656
Cdd:TIGR00957 908 SASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQtGQVELSVYWDYMKAIGLFITFlsIFLFVCNHVSALA---S 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 657 DWWLSYWANkQSMLNVTVNgggNVTEKLDLNWYLGIYSGLTVatvlFGIARSLLVFYVLvnSSQTLHNKMFESILKAPVL 736
Cdd:TIGR00957 985 NYWLSLWTD-DPMVNGTQN---NTSLRLSVYGALGILQGFAV----FGYSMAVSIGGIQ--ASRVLHQDLLHNKLRSPMS 1054
|
890 900 910
....*....|....*....|....*....|...
gi 685504970 737 FFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFI 769
Cdd:TIGR00957 1055 FFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM 1087
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-758 |
3.39e-140 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 449.43 E-value: 3.39e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 12 PLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAendaqKPSLTRAIIKC---- 87
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRP-----KPWLLRALNNSlggr 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 88 YW--------------------------------------------------------------------KSYLVLGIFT 99
Cdd:PLN03232 303 FWlggifkighdlsqfvgpvilshllqsmqegdpawvgyvyafliffgvtfgvlcesqyfqnvgrvgfrlRSTLVAAIFH 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 100 liEALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCF 179
Cdd:PLN03232 383 --KSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 180 GKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFV 259
Cdd:PLN03232 461 VRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLV 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 260 TFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFfPSAIERVSEAIVSIRRIQTFLLLDE-ISQRNRQLpSDGKKMVHVQ 338
Cdd:PLN03232 541 SFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNML-PNLLSQVVNANVSLQRIEELLLSEErILAQNPPL-QPGAPAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 339 DFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH-GLVSVHGRIAYVSQQPWVFSGTLRSN 417
Cdd:PLN03232 619 NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVREN 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 497
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 498 LFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKKDNEESEQPPV-PGTPTLRN 576
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVnTNDENILK 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 577 RTFSESSVWSQQSSrpslkdgALESQDTENVPVTLSEENRSEGKVGFQAYKNYFRA-GAHWIVFIfLILLNTAAQVAYVL 655
Cdd:PLN03232 859 LGPTVTIDVSERNL-------GSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAvGGLWVVMI-LLVCYLTTEVLRVS 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 656 QDWWLSYWANKQSMlnvtvngggnvtEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPV 735
Cdd:PLN03232 931 SSTWLSIWTDQSTP------------KSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPM 998
|
810 820
....*....|....*....|...
gi 685504970 736 LFFDRNPIGRILNRFSKDIGHLD 758
Cdd:PLN03232 999 LFFHTNPTGRVINRFSKDIGDID 1021
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-770 |
7.82e-133 |
|
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: 429.72 E-value: 7.82e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 11 NPLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAEndaQKPSLTRAIIKCY-W 89
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAK---KNPKLLNALRRCFfW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 90 K----------------------------------------SYLVLGI-----------------------------FTL 100
Cdd:TIGR01271 81 RfvfygillyfgeatkavqplllgriiasydpfnapereiaYYLALGLcllfivrtlllhpaifglhhlgmqmrialFSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 101 I--EALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSC 178
Cdd:TIGR01271 161 IykKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 179 FGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVF 258
Cdd:TIGR01271 241 LGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 259 VTFTTYVLLGSVITaSRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRIQTFLLLDEISQRNRQLPSDGKKMVHVq 338
Cdd:TIGR01271 321 LSVVPYALIKGIIL-RRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNV- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 339 dfTAFWD--------KASE-----------------------TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL 387
Cdd:TIGR01271 399 --TASWDegigelfeKIKQnnkarkqpngddglffsnfslyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGEL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 388 APSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKAR 467
Cdd:TIGR01271 477 EPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRAR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 468 VNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 547
Cdd:TIGR01271 557 ISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 548 SGIDFGSLL----KKDNEESE---------------------------------QPP----------------------- 567
Cdd:TIGR01271 637 KRPDFSSLLlgleAFDNFSAErrnsiltetlrrvsidgdstvfsgpetikqsfkQPPpefaekrkqsiilnpiasarkfs 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 568 ----------------------------VP----GTPTL------------------------------------RNRTF 579
Cdd:TIGR01271 717 fvqmgpqkaqattiedavrepserkfslVPedeqGEESLprgnqyhhglqhqaqrrqsvlqlmthsnrgenrreqLQTSF 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 580 SESSVWSQQS---------SRPSLKDGALE--------------SQDTENVPVTLSeenrsegkvgFQAYKNYFRAGAHW 636
Cdd:TIGR01271 797 RKKSSITQQNelaseldiySRRLSKDSVYEiseeineedlkecfADERENVFETTT----------WNTYLRYITTNRNL 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 637 IVFIFLILLNTAAQVAYVLQDWWL----SYWANKQSMLNVTVNGGGNVTEKLDLN----WYLGIYSGLTVATVLFGIARS 708
Cdd:TIGR01271 867 VFVLIFCLVIFLAEVAASLLGLWLitdnPSAPNYVDQQHANASSPDVQKPVIITPtsayYIFYIYVGTADSVLALGFFRG 946
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 709 LLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:TIGR01271 947 LPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQ 1008
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
103-311 |
5.48e-120 |
|
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: 362.69 E-value: 5.48e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 103 ALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKL 182
Cdd:cd18593 83 ALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 183 FSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFT 262
Cdd:cd18593 163 FSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 685504970 263 TYVLLGSVITASRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRI 311
Cdd:cd18593 243 AYILLGNILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
335-535 |
3.80e-116 |
|
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: 349.46 E-value: 3.80e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTAFWDKASET--PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSG 412
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 685504970 493 EVSRHLFELCICQIL-HEKITILVTHQLQYLKAASQILILKDGK 535
Cdd:cd03250 161 HVGRHIFENCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
85-770 |
7.64e-108 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 361.40 E-value: 7.64e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 85 IKC--YWKSYLVLGIFTLIEALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISC 162
Cdd:PTZ00243 310 IRCglQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 163 LAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISkilrssCLR 242
Cdd:PTZ00243 390 LMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELR------YLR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 243 GMNLA----SFFS--ASKIIVFVTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFfPSAIERVSEAIVSIRRIQTFLL 316
Cdd:PTZ00243 464 DVQLArvatSFVNnaTPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMI-PWVFTTVLQFLVSIKRISTFLE 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 317 LDEIS-------------QRNR---------------------QLPSDGKKM--------------------------VH 336
Cdd:PTZ00243 543 CDNATcstvqdmeeywreQREHstacqlaavlenvdvtafvpvKLPRAPKVKtsllsralrmlcceqcrptkrhpspsVV 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 337 VQDF----------------TAFWDKASETPT---------------------LQGLSFTVRPGELLAVVGPVGAGKSSL 379
Cdd:PTZ00243 623 VEDTdygspssasrhiveggTGGGHEATPTSErsaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTL 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 380 LSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTT 459
Cdd:PTZ00243 703 LQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVN 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 460 LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQK 539
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFS 862
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 540 GTYTEFLKSGI--DFGSLLK---------KDNEESEQPPVPGTPTLRNRTFsessvwSQQSSRPSLKDGAleSQDTENVP 608
Cdd:PTZ00243 863 GSSADFMRTSLyaTLAAELKenkdskegdADAEVAEVDAAPGGAVDHEPPV------AKQEGNAEGGDGA--ALDAAAGR 934
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 609 VTLSEENRSeGKVGFQAYKNYFRA--GAHWIVFIFLI-----LLNTAAQVayvlqdwWLSYWANKQsmlnvtvngggnvt 681
Cdd:PTZ00243 935 LMTREEKAS-GSVPWSTYVAYLRFcgGLHAAGFVLATfavteLVTVSSGV-------WLSMWSTRS-------------- 992
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 682 EKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLL 761
Cdd:PTZ00243 993 FKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTL 1072
|
....*....
gi 685504970 762 PLTFLDFIQ 770
Cdd:PTZ00243 1073 PMSYLYLLQ 1081
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
98-312 |
5.79e-97 |
|
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: 303.02 E-value: 5.79e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 98 FTLI--EALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPL 175
Cdd:cd18594 75 SSLIykKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 176 QSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKI 255
Cdd:cd18594 155 QAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 256 IVFVTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRIQ 312
Cdd:cd18594 235 VSFATFVPYVLTGNTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
103-311 |
5.81e-85 |
|
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: 271.28 E-value: 5.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 103 ALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKL 182
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 183 FSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFT 262
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 685504970 263 TYVLLGSVITASRVFVAVTLYGAVRlTVTLFFPSAIERVSEAIVSIRRI 311
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLR-FPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
635-770 |
4.92e-70 |
|
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: 232.60 E-value: 4.92e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 635 HWIVFIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNV------TVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARS 708
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDttdrvqGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 709 LLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQ 142
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
105-549 |
1.41e-66 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 231.59 E-value: 1.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 105 RLSNMAMG---KTTTGQIVNLLSNDVNKFDQ-VTVFLHFLWAGPLQAIAVTALLWM---EIGISCLAGMAVLIILLPLqs 177
Cdd:COG1132 103 HLLRLPLSffdRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVidwRLALIVLLVLPLLLLVLRL-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 178 cFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKS----FSNLITNLRKKEISKILRSSCLrgMNLASFFSAS 253
Cdd:COG1132 181 -FGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSALF--FPLMELLGNL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 254 KIIVFVTFTTYVLLGSVITASrVFVAVTLYgavrlTVTLFFP-----SAIERVSEAIVSIRRIQTFLLL-DEISQRNRQL 327
Cdd:COG1132 258 GLALVLLVGGLLVLSGSLTVG-DLVAFILY-----LLRLFGPlrqlaNVLNQLQRALASAERIFELLDEpPEIPDPPGAV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 328 P-SDGKKMVHVQDFTAFWDKasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------L 393
Cdd:COG1132 332 PlPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrilidgvdirdltL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 394 VSVHGRIAYVSQQPWVFSGTLRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLAR 472
Cdd:COG1132 410 ESLRRQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIAR 489
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 473 AVYQDADIYLLDDPLSAVDAEVSRHLFElCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
350-556 |
1.57e-65 |
|
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: 219.34 E-value: 1.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERY 429
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 430 EKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHE 509
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMAN 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 685504970 510 KITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLL 556
Cdd:cd03291 210 KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
103-311 |
1.18e-60 |
|
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: 206.55 E-value: 1.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 103 ALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKL 182
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 183 FSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFT 262
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 685504970 263 TYVLLGS--VITASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 311
Cdd:cd18595 241 TYVLSDPdnVLDAEKAFVSLSLFNILRFPLS-MLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
103-311 |
8.66e-59 |
|
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: 201.53 E-value: 8.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 103 ALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKL 182
Cdd:cd18597 86 SLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLMKK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 183 FSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFT 262
Cdd:cd18597 166 LFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASMLSFI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 685504970 263 TYVLLGSVITASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 311
Cdd:cd18597 246 TYYATGHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
303-549 |
1.63e-56 |
|
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: 203.07 E-value: 1.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 303 EAIVSIRRIQTFLLLDE--ISQRNRQLPSDGKKMVHVQDFTAFWDkaSETPTLQGLSFTVRPGELLAVVGPVGAGKSSLL 380
Cdd:COG4988 303 NGIAAAEKIFALLDAPEpaAPAGTAPLPAAGPPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 381 SAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGK-KYEKERYEKVIKACALKKDLQLLE 446
Cdd:COG4988 381 NLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 447 DGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAAS 526
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQAD 539
|
250 260
....*....|....*....|...
gi 685504970 527 QILILKDGKMVQKGTYTEFLKSG 549
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLAKN 562
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
104-547 |
2.49e-55 |
|
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: 199.99 E-value: 2.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 104 LRLSNMAMGKTTTGQIVNLLSNDVNKFDqvTVFLHFL------WAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLqs 177
Cdd:COG4987 99 EPLAPAGLARLRSGDLLNRLVADVDALD--NLYLRVLlpllvaLLVILAAVAFLAFFSPALALVLALGLLLAGLLLPL-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 178 cfgkLFSSL-----RSKTATFTDARIRTMnEVITGIRIIKMY----AWEKSFSNLITNLRKKEiskilrssclRGMNLAS 248
Cdd:COG4987 175 ----LAARLgrragRRLAAARAALRARLT-DLLQGAAELAAYgaldRALARLDAAEARLAAAQ----------RRLARLS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 249 FFSASKIIVFVTFTTYVLLGSVITASR------VFVAVtlygAVRLTVTLF-----FPSAIERVSEAIVSIRRIqtFLLL 317
Cdd:COG4987 240 ALAQALLQLAAGLAVVAVLWLAAPLVAagalsgPLLAL----LVLAALALFealapLPAAAQHLGRVRAAARRL--NELL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 318 DE---ISQRNRQLPSDGKKMVHVQDFTAFWDKASEtPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV 394
Cdd:COG4987 314 DAppaVTEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 395 -------------SVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKEryEKVIKACA---LKKDLQLLEDGDLTVIGDRGT 458
Cdd:COG4987 393 tlggvdlrdldedDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD--EELWAALErvgLGDWLAALPDGLDTWLGEGGR 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 459 TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQ 538
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
....*....
gi 685504970 539 KGTYTEFLK 547
Cdd:COG4987 550 QGTHEELLA 558
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
167-557 |
2.42e-54 |
|
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: 200.06 E-value: 2.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 167 AVLIILLPLQSCFGKLFSSLRSKTA--TFTDARIR--TMNEVITGIRIIKMYA--------WEKSFSNLI-TNLRKKEIS 233
Cdd:COG2274 299 LVVLLLIPLYVLLGLLFQPRLRRLSreESEASAKRqsLLVETLRGIETIKALGaesrfrrrWENLLAKYLnARFKLRRLS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 234 KILrssclrgMNLASFFSASKIIVFVTFTTYVLLGSVITASrVFVAVTLYgAVRLT---VTLFfpSAIERVSEAIVSIRR 310
Cdd:COG2274 379 NLL-------STLSGLLQQLATVALLWLGAYLVIDGQLTLG-QLIAFNIL-SGRFLapvAQLI--GLLQRFQDAKIALER 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 311 IQTFLLL--DEISQRNRQLPSDGKKMVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELA 388
Cdd:COG2274 448 LDDILDLppEREEGRSKLSLPRLKGDIELENVS-FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 389 PSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIG 454
Cdd:COG2274 527 PTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVG 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 455 DRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDG 534
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKG 685
|
410 420
....*....|....*....|...
gi 685504970 535 KMVQKGTYTEFLKSGIDFGSLLK 557
Cdd:COG2274 686 RIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
337-534 |
1.35e-51 |
|
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: 179.45 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 337 VQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-----------------SVHGR 399
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 400 IAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDAD 479
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 480 IYLLDDPLSAVDAEVSRHLFELCICQILHE--KITILVTHQLQYLKAASQILILKDG 534
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
96-311 |
2.89e-50 |
|
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: 178.14 E-value: 2.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 96 GIFTLI--EALRLSNMamGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILL 173
Cdd:cd18592 73 AVLGLLykKILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFY 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 174 PLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSAS 253
Cdd:cd18592 151 PLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVP 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 254 KIIVFVTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 311
Cdd:cd18592 231 VIASVVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLR-MLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
112-311 |
1.34e-48 |
|
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: 174.22 E-value: 1.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 112 GKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTA 191
Cdd:cd18596 110 SSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELM 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 192 TFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLL-GSV 270
Cdd:cd18596 190 KARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVmGQE 269
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 685504970 271 ITASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 311
Cdd:cd18596 270 LTASVAFTSLALFNMLRGPLN-VLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
79-311 |
4.48e-45 |
|
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: 163.49 E-value: 4.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 79 SLTRAIIKCYWKSYLVLGIFTliEALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEI 158
Cdd:cd18598 59 NFQMNKVSLKVRAALVTAVYR--KALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 159 GISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEIS----- 233
Cdd:cd18598 137 GVAFLAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKalkgr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 234 KILRSSClrgmnlaSFFSASK--IIVFVTFTTYVLLGSVITASRVFVAVTLYGavRLTVTL-FFPSAIERVSEAIVSIRR 310
Cdd:cd18598 217 KYLDALC-------VYFWATTpvLISILTFATYVLMGNTLTAAKVFTSLALFN--MLIGPLnAFPWVLNGLVEAWVSLKR 287
|
.
gi 685504970 311 I 311
Cdd:cd18598 288 L 288
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
103-311 |
3.29e-43 |
|
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: 158.94 E-value: 3.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 103 ALRLS--NMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFG 180
Cdd:cd18591 99 ALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 181 KLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEIsKILRSSCLRGMNLASFFSASKIIV-FV 259
Cdd:cd18591 179 RKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKEL-KLLLKDAVYWSLMTFLTQASPILVtLV 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 685504970 260 TFTTYVLL-GSVITASRVFVAVTLYGavRLTVTLF-FPSAIERVSEAIVSIRRI 311
Cdd:cd18591 258 TFGLYPYLeGEPLTAAKAFSSLALFN--QLTVPLFiFPVVIPILINAVVSTRRL 309
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
348-535 |
1.11e-42 |
|
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: 152.54 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-------------SVHGRIAYVSQQPWVFSGTL 414
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdldleSLRKNIAYVPQDPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 RSNIlfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 494
Cdd:cd03228 93 RENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 685504970 495 SRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGK 535
Cdd:cd03228 132 EALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
348-549 |
2.34e-42 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 153.92 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------LVSVHGRIAYVSQQPWVFSGTL 414
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirdisRKSLRSMIGVVLQDTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 RSNILFGKKYEKEryEKVIKACALKKDLQL---LEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:cd03254 94 MENIRLGRPNATD--EEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 492 AEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:cd03254 172 TE-TEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
346-540 |
2.57e-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: 147.74 E-value: 2.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 346 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG 412
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:cd03245 93 TLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 685504970 492 AEVSRHLFElCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKG 540
Cdd:cd03245 173 MNSEERLKE-RLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
311-562 |
4.28e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 156.54 E-value: 4.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 311 IQTFLLLDEISQRN--RQLPSDGKKMVHVQDFTAFwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELa 388
Cdd:PRK11174 324 LVTFLETPLAHPQQgeKELASNDPVTIEAEDLEIL--SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 389 PSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVIG 454
Cdd:PRK11174 401 PYQGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 455 DRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFElCICQILHEKITILVTHQLQYLKAASQILILKDG 534
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ-ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
250 260
....*....|....*....|....*...
gi 685504970 535 KMVQKGTYTEFLKSGIDFGSLLKKDNEE 562
Cdd:PRK11174 560 QIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
349-549 |
6.37e-40 |
|
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: 146.99 E-value: 6.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLR 415
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNILFGKKYE-KERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEv 494
Cdd:cd03251 94 ENIAYGRPGAtREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTE- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 495 SRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:cd03251 173 SERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
349-549 |
2.20e-39 |
|
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: 145.76 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 415
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlrwlrsQIGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNILFGKKYEK-ERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEv 494
Cdd:cd03249 95 ENIRYGKPDATdEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 495 SRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:cd03249 174 SEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
349-531 |
4.66e-39 |
|
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: 152.44 E-value: 4.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 415
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNILFGKKYEKE-RYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 494
Cdd:TIGR02857 414 ENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|....*....
gi 685504970 495 SRHLFE--LCICQilhEKITILVTHQLQYLKAASQILIL 531
Cdd:TIGR02857 494 EAEVLEalRALAQ---GRTVLLVTHRLALAALADRIVVL 529
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
349-549 |
1.74e-38 |
|
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: 151.39 E-value: 1.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 415
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVM 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNILFGKKYEKEryEKVIKACALKKD---LQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:TIGR02204 432 ENIRYGRPDATD--EEVEAAARAAHAhefISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 493 EvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG 565
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
333-534 |
4.80e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 4.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 333 KMVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------RIAYVS 404
Cdd:COG1121 5 PAIELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 405 QQ---PWVF---------SGTLRSNILFgKKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDR--GtTLSGGQKARVNL 470
Cdd:COG1121 82 QRaevDWDFpitvrdvvlMGRYGRRGLF-RRPSRADREAVDEA---------LERVGLEDLADRpiG-ELSGGQQQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 471 ARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITIL-VTHQLQYL-KAASQILILKDG 534
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYEL-LRELRREGKTILvVTHDLGAVrEYFDRVLLLNRG 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
328-536 |
2.29e-36 |
|
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: 136.83 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 328 PSDGKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV----------- 396
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpisqyehk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 397 --HGRIAYVSQQPWVFSGTLRSNILFG---KKYEKeryekvIKACALKKD----LQLLEDGDLTVIGDRGTTLSGGQKAR 467
Cdd:cd03248 85 ylHSKVSLVGQEPVLFARSLQDNIAYGlqsCSFEC------VKEAAQKAHahsfISELASGYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 468 VNLARAVYQDADIYLLDDPLSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKM 536
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
351-549 |
5.99e-36 |
|
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: 135.82 E-value: 5.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLRSN 417
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrraIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:cd03253 95 IRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 685504970 497 HLFElCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:cd03253 175 EIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
348-548 |
7.06e-36 |
|
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: 143.35 E-value: 7.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTL 414
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 RSNI-LFGKkyekERYEKVIKACALK--KDLQL-LEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 490
Cdd:COG4618 423 AENIaRFGD----ADPEKVVAAAKLAgvHEMILrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 491 DAEVSRHLFELcicqILHEK----ITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKS 548
Cdd:COG4618 499 DDEGEAALAAA----IRALKargaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
298-542 |
8.48e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 143.31 E-value: 8.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 298 IERVSEAIVSIRRiqtflLLDE---ISQRNRQLPsDGKKMVHVqDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGA 374
Cdd:PRK10789 280 VERGSAAYSRIRA-----MLAEapvVKDGSEPVP-EGRGELDV-NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 375 GKSSLLSAVLGELAPSHGLVSVH-------------GRIAYVSQQPWVFSGTLRSNILFGK-KYEKERYEKVIKACALKK 440
Cdd:PRK10789 353 GKSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHD 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 441 DLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRhlfelcicQILH-------EKITI 513
Cdd:PRK10789 433 DILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH--------QILHnlrqwgeGRTVI 504
|
250 260
....*....|....*....|....*....
gi 685504970 514 LVTHQLQYLKAASQILILKDGKMVQKGTY 542
Cdd:PRK10789 505 ISAHRLSALTEASEILVMQHGHIAQRGNH 533
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
639-770 |
9.46e-36 |
|
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: 137.25 E-value: 9.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 639 FIFLILLNTAAQVAYVLQDWWLSYWANKQSMlnvtvngggnvTEKLDLNWYLGIYSGLTV-ATVLFGIARSLLVFYVLVN 717
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSS-----------SPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLR 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 685504970 718 SSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd18580 70 ASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQ 122
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
294-519 |
1.57e-35 |
|
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: 142.11 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 294 FPSAIERVSEAIVSIRRIqTFLLLDEISQRNRQLPSDG-----KKMVHVQDFTAFWDKASetPTLQGLSFTVRPGELLAV 368
Cdd:TIGR02868 290 LPAAAQQLTRVRAAAERI-VEVLDAAGPVAEGSAPAAGavglgKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 369 VGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGKK-YEKERYEKVIK 434
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 435 ACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITIL 514
Cdd:TIGR02868 447 RVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVL 525
|
....*
gi 685504970 515 VTHQL 519
Cdd:TIGR02868 526 ITHHL 530
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
113-556 |
2.12e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 143.71 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 113 KTTTGQIVNLLSNDVNKF-----DQVTVFLHFLwagplqaIAVTALLWMEIGISCLAGMaVLIILLPL----QSCFGKLF 183
Cdd:TIGR00958 254 ENKTGELTSRLSSDTQTMsrslsLNVNVLLRNL-------VMLLGLLGFMLWLSPRLTM-VTLINLPLvflaEKVFGKRY 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 184 SSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKS----FSNLITNL----RKKEISKIL----RSSCLRGMNLASFFS 251
Cdd:TIGR00958 326 QLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETlqlnKRKALAYAGylwtTSVLGMLIQVLVLYY 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 252 ASKIIV--------FVTFTTYVLLgsviTASRVFVAVTLYGAVRLTVtlffpSAIERVseaivsirriqtFLLLDeisqR 323
Cdd:TIGR00958 406 GGQLVLtgkvssgnLVSFLLYQEQ----LGEAVRVLSYVYSGMMQAV-----GASEKV------------FEYLD----R 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 324 NRQLPSDGKKM-------VHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-- 394
Cdd:TIGR00958 461 KPNIPLTGTLAplnleglIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVll 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 395 -----------SVHGRIAYVSQQPWVFSGTLRSNILFG-KKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSG 462
Cdd:TIGR00958 541 dgvplvqydhhYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSG 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 463 GQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcicQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTY 542
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
490
....*....|....
gi 685504970 543 TEFLKSGIDFGSLL 556
Cdd:TIGR00958 698 KQLMEDQGCYKHLV 711
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
348-532 |
7.43e-35 |
|
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: 131.89 E-value: 7.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------RIAYVSQQ---PWVFSGT--- 413
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRrsiDRDFPISvrd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 -----LRSNILFGKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:cd03235 90 vvlmgLYGHKGLFRRLSKADKAKV---------DEALERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 685504970 488 SAVDAEVSRHLFELcICQILHEKITIL-VTHQL-QYLKAASQILILK 532
Cdd:cd03235 161 AGVDPKTQEDIYEL-LRELRREGMTILvVTHDLgLVLEYFDRVLLLN 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
353-561 |
1.28e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.11 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSNIL 419
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 420 F-------GKKYEKERYEKVIKACALKKdlqlledgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTD-----------AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504970 493 EVSRHLFELcICQILHEKITILV-THQLQYL-KAASQILILKDGKMVQKGTYTEFLKSGID--FGSLLKKDNE 561
Cdd:COG1131 165 EARRELWEL-LRELAAEGKTVLLsTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLLEdvFLELTGEEAR 236
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
636-770 |
5.23e-33 |
|
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: 129.12 E-value: 5.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 636 WIVFIFLILLntaAQVAYVLQDWWLSYWANKQSMLNVTVNGGGNVtekldlNWYLGIYSGLTVATVLFGIARSLLVFYVL 715
Cdd:cd18604 1 WALLLLLFVL---SQLLSVGQSWWLGIWASAYETSSALPPSEVSV------LYYLGIYALISLLSVLLGTLRYLLFFFGS 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 716 VNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd18604 72 LRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLE 126
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
348-540 |
1.20e-32 |
|
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: 124.35 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSGTLR 415
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNIlfgkkyekeryekvikacalkkdlqlledgdltvigdrGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 495
Cdd:cd03247 93 NNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 685504970 496 RHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKG 540
Cdd:cd03247 135 RQLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
335-540 |
1.36e-31 |
|
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: 122.63 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYV 403
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 404 SQQPWVFSG-TLRSNILFG----KKYEKERYEKVIKAcalkkdLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQDA 478
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlklrGVPKAEIRARVREL------LELVGLEGL--LNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 479 DIYLLDDPLSAVDAEVSRHLFELcICQILHE--KITILVTH-QLQYLKAASQILILKDGKMVQKG 540
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREE-LKELQRElgITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-541 |
2.69e-31 |
|
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: 122.84 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFTAfwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RI 400
Cdd:COG1120 1 MLEAENLSV---GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 401 AYVSQQPWV-FSGTLRSNILFG--------KKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVNL 470
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphlglfGRPSAEDREAVEEA---------LERTGLEHLADRPvDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 471 ARAVYQDADIYLLDDPLSAVD----AEVSRHLFELCICQilhEKITILVTHQL-QYLKAASQILILKDGKMVQKGT 541
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARER---GRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGP 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
329-534 |
2.69e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.28 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 329 SDGKKMVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------R 399
Cdd:COG1116 2 SAAAPALELRGVSkRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 400 IAYVSQQ----PWVfsgTLRSNILFG----KKYEKERYEKVikacalkkdLQLLEDGDLTvigDRGT----TLSGGQKAR 467
Cdd:COG1116 82 RGVVFQEpallPWL---TVLDNVALGlelrGVPKAERRERA---------RELLELVGLA---GFEDayphQLSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 468 VNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KITIL-VTHQLQ---YLkaASQILILKDG 534
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDE-LLRLWQEtGKTVLfVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
335-541 |
3.56e-31 |
|
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: 121.83 E-value: 3.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTAFWDKASEtPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIA 401
Cdd:cd03244 3 IEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 402 YVSQQPWVFSGTLRSNI-LFGKKYEKERYEkVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADI 480
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 481 YLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGT 541
Cdd:cd03244 161 LVLDEATASVDPETDALIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
349-536 |
4.51e-31 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 119.63 E-value: 4.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 415
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnelgdHVGYLPQDDELFSGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNIlfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 495
Cdd:cd03246 94 ENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 685504970 496 RHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKM 536
Cdd:cd03246 133 RALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
353-540 |
6.18e-31 |
|
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: 119.46 E-value: 6.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQqpwvfsgtlrsnil 419
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 420 fgkkyekeryekvikacalkkdlqLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 498
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 685504970 499 FELcICQILHE--KITILVTHQL-QYLKAASQILILKDGKMVQKG 540
Cdd:cd03214 137 LEL-LRRLARErgKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
635-770 |
1.07e-30 |
|
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: 123.06 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 635 HWIVFIFLILLNTAAQVAYVLQDWWLSYW-----ANKQSMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSL 709
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 710 LVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQ 141
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
342-531 |
1.16e-30 |
|
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: 120.27 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 342 AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------IAYVSQQ----PWV 409
Cdd:cd03293 9 TYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQdallPWL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 fsgTLRSNILFG----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLD 484
Cdd:cd03293 89 ---TVLDNVALGlelqGVPKAEARERA---------EELLELVGLSGFENAyPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 685504970 485 DPLSAVDAEVSRHLFELcICQILHE--KITILVTHQLQ---YLkaASQILIL 531
Cdd:cd03293 157 EPFSALDALTREQLQEE-LLDIWREtgKTVLLVTHDIDeavFL--ADRVVVL 205
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
639-769 |
1.64e-30 |
|
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: 122.20 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 639 FIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNVTVNGggnvteklDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNS 718
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTE--------QRDYRLGVYGALGLGQAIFVFLGSLALALGCVRA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 685504970 719 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFI 769
Cdd:cd18603 73 SRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFL 123
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
353-488 |
1.73e-30 |
|
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: 117.36 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG-TLRSNI 418
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 419 LFGKkyEKERYEKVIKACALKKDLQLLEDGDL--TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLS 488
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
351-547 |
1.80e-30 |
|
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: 120.35 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSN 417
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 I-LFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeVSR 496
Cdd:COG4555 95 IrYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-----GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 685504970 497 HLFELCICQILHEKITILV-THQLQYLKA-ASQILILKDGKMVQKGTYTEFLK 547
Cdd:COG4555 169 RLLREILRALKKEGKTVLFsSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
639-769 |
3.21e-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: 121.10 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 639 FIFLILLNTAAQVAYVLQDWWLSYWANKQsmlnvtvNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNS 718
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHS-------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRA 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 685504970 719 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFI 769
Cdd:cd18605 74 ARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILL 124
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
351-572 |
7.21e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 125.46 E-value: 7.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSN 417
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGKK--YEKERYEKVIKACALkkDLQLL-EDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 494
Cdd:PRK13657 429 IRVGRPdaTDEEMRAAAERAQAH--DFIERkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 495 SRHLfELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLK-----KDNEESEQPPVP 569
Cdd:PRK13657 507 EAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRaqgmlQEDERRKQPAAE 585
|
...
gi 685504970 570 GTP 572
Cdd:PRK13657 586 GAN 588
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
343-549 |
7.56e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 118.36 E-value: 7.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 343 FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV 409
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 FSGTLRSNILFGKkyEKERYEKVIKACALKKD---LQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDP 486
Cdd:cd03252 88 FNRSIRDNIALAD--PGMSMERVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504970 487 LSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:cd03252 166 TSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
353-541 |
1.60e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 120.64 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQP------WVFSG-------TLRSNIL 419
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvgFVFQHyalfphmTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 420 FG----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA-- 492
Cdd:COG1118 98 FGlrvrPPSKAEIRARV---------EELLELVQLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkv 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 493 --EVSRHLFElcicqiLHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGT 541
Cdd:COG1118 169 rkELRRWLRR------LHDELggtTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
636-770 |
1.90e-29 |
|
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: 118.73 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 636 WIVFIFLILLntaAQVAYVLQDWWLSYWANKqsmlnvtvngggnvTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVL 715
Cdd:cd18606 1 LPLLLLLLIL---SQFAQVFTNLWLSFWTED--------------FFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLG 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 716 VNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd18606 64 IRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLY 118
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
348-546 |
1.96e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 124.17 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTL 414
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 RSNILFGK-KYEKERYEKVIKACALKKdlqLLEDGD-L-TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:PRK11160 431 RDNLLLAApNASDEALIEVLQQVGLEK---LLEDDKgLnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 492 AEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL 546
Cdd:PRK11160 508 AETERQILEL-LAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-535 |
2.46e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 116.03 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 337 VQDFTAFWDKaSETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYV 403
Cdd:cd03225 2 LKNLSFSYPD-GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 404 SQQP--WVFSGTLRSNILFGKKYEKERYEKVIkacalKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADI 480
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIE-----ERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 481 YLLDDPLSAVDAEVSRHLFELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGK 535
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLEL-LKKLKAEGKTIIiVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
346-536 |
1.47e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.76 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 346 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG 412
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGKKYEKERYEKViKACALKKDLQLledgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:COG4619 89 TVRDNLPFPFQLRERKFDRE-RALELLERLGL----PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 685504970 493 EVSRHLFELcICQILHEK-ITIL-VTH-QLQYLKAASQILILKDGKM 536
Cdd:COG4619 164 ENTRRVEEL-LREYLAEEgRAVLwVSHdPEQIERVADRVLTLEAGRL 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
349-544 |
1.82e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.48 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVF-SGTLRS 416
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQSYALYpHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 NILFG----KKYEKERYEKVIKACALkkdLQLLEdgdltvIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:COG3839 95 NIAFPlklrKVPKAEIDRRVREAAEL---LGLED------LLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 492 AEvSRHLFELCICQiLHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 544
Cdd:COG3839 166 AK-LRVEMRAEIKR-LHRRLgttTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
349-547 |
5.61e-28 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 112.81 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPW--VFSGT 413
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 LRSNILFGKKY----EKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLS 488
Cdd:COG1122 93 VEEDVAFGPENlglpREEIRERVEEA---------LELVGLEHLADRPPhELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 489 AVDAEVSRHLFELcICQILHEKIT-ILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLK 547
Cdd:COG1122 164 GLDPRGRRELLEL-LKRLNKEGKTvIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
351-531 |
7.87e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.17 E-value: 7.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQ---PWVFSGTLRSNI---LFGK 422
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 423 KYEKERY----EKVIKACALKKDLQLLEDGDLTvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 498
Cdd:NF040873 86 RGLWRRLtrddRAAVDDALERVGLADLAGRQLG-------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190
....*....|....*....|....*....|....
gi 685504970 499 FELcICQILHEKITIL-VTHQLQYLKAASQILIL 531
Cdd:NF040873 159 IAL-LAEEHARGATVVvVTHDLELVRRADPCVLL 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
348-545 |
5.49e-27 |
|
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: 110.35 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPW--- 408
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMIFQQFNlie 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 409 -------VFSG------TLRSniLFGKKYEKERYekviKACALKKDLQLLEDgdltvIGDRGTTLSGGQKARVNLARAVY 475
Cdd:cd03256 92 rlsvlenVLSGrlgrrsTWRS--LFGLFPKEEKQ----RALAALERVGLLDK-----AYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 476 QDADIYLLDDPLSAVDAEVSRHLFELC--ICQilHEKITILVT-HQLQYLKA-ASQILILKDGKMVQKGTYTEF 545
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLkrINR--EEGITVIVSlHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
103-311 |
5.98e-27 |
|
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: 111.54 E-value: 5.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 103 ALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKL 182
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 183 FSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFT 262
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 685504970 263 TYVLLGS--VITASRVFVAVTLYGAVRLTVTLfFPSAIERVSEAIVSIRRI 311
Cdd:cd18559 241 AYVSRHSlaGLVALKVFYSLALTTYLNWPLNM-SPEVITNIVAAEVSLERS 290
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
334-544 |
6.90e-27 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 109.59 E-value: 6.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 398
Cdd:cd03258 1 MIELKNVSkVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 --RIAYVSQQPWVFSG-TLRSNILF----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNL 470
Cdd:cd03258 81 rrRIGMIFQHFNLLSSrTVFENVALpleiAGVPKAEIEERV---------LELLELVGLEDKADAyPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 471 ARAVYQDADIYLLDDPLSAVDAEVSRHLFELcicqiLHE-----KITI-LVTHQLQYLKA-ASQILILKDGKMVQKGTYT 543
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILAL-----LRDinrelGLTIvLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
.
gi 685504970 544 E 544
Cdd:cd03258 227 E 227
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
636-784 |
1.22e-26 |
|
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: 111.16 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 636 WIVFIFLILLNTAAQVAyvlQDWWLSYWANKQSMLNVTVNGGGNVTEKLDLNW-YLGIYSGLTVATVLFGIARSLLVFYV 714
Cdd:cd18602 1 VALVLALALLKQGLRVA---TDFWLADWTEANHDVASVVFNITSSSLEDDEVSyYISVYAGLSLGAVILSLVTNLAGELA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 715 LVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQRWdLAVLSWLVSNS 784
Cdd:cd18602 78 GLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFL-LLCLSAIIVNA 146
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
349-541 |
1.71e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 111.73 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQqpwvfSGTL--- 414
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQ-----DYALfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 ---RSNILFG----KKYEKERYEKVIKACALkkdLQLledGDLtviGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDP 486
Cdd:COG3842 92 ltvAENVAFGlrmrGVPKAEIRARVAELLEL---VGL---EGL---ADRYpHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 487 LSAVDAEVSRHL-FELciCQILHE-KIT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 541
Cdd:COG3842 163 LSALDAKLREEMrEEL--RRLQRElGITfIYVTHdQEEALALADRIAVMNDGRIEQVGT 219
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
351-555 |
4.00e-26 |
|
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: 114.45 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLRSN 417
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGKKyEKERYEKVIKACAL---KKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 494
Cdd:TIGR01193 568 LLLGAK-ENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 495 SRHLFELCIcqILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSL 555
Cdd:TIGR01193 647 EKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
335-546 |
4.14e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 113.96 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL-------GE-LAPSHG-----LVSVHGRIA 401
Cdd:PRK11176 342 IEFRNVT-FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEiLLDGHDlrdytLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 402 YVSQQPWVFSGTLRSNILF--GKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDAD 479
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 480 IYLLDDPLSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL 546
Cdd:PRK11176 501 ILILDEATSALDTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
350-548 |
1.46e-25 |
|
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: 106.23 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG-TLR 415
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNI-LFGK--KYEKERYEKVIKacalkkdlQLLEDGDLTVIGDRG---TTLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:cd03295 94 ENIaLVPKllKWPKEKIRERAD--------ELLALVGLDPAEFADrypHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 490 VDAEVSRHLFE--LCICQILHEKItILVTHQLQ-YLKAASQILILKDGKMVQKGTYTEFLKS 548
Cdd:cd03295 166 LDPITRDQLQEefKRLQQELGKTI-VFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
351-544 |
1.64e-25 |
|
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: 105.88 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNI 418
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 LFGKKyEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 497
Cdd:cd03296 96 AFGLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 685504970 498 LFELciCQILHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 544
Cdd:cd03296 175 LRRW--LRRLHDELhvtTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
334-535 |
2.18e-25 |
|
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: 104.48 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIA 401
Cdd:COG4133 2 MLEAENLSCRRG---ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 402 YVSQQPWVFSG-TLRSNILFgkkyekeryekvikACALKKD-------LQLLEDGDLTVIGDR-GTTLSGGQKARVNLAR 472
Cdd:COG4133 79 YLGHADGLKPElTVRENLRF--------------WAALYGLradreaiDEALEAVGLAGLADLpVRQLSAGQKRRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504970 473 AVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAAsQILILKDGK 535
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
349-548 |
2.50e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 105.28 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWVFSG 412
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 -TLRSNILFGKKYEKERYEKVIKACALKKdlqlledgdLTVIGDRGTT------LSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:cd03261 92 lTVFENVAFPLREHTRLSEEEIREIVLEK---------LEAVGLRGAEdlypaeLSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 486 PLSAVDAEVSRHLFELcicqI--LHEKI---TILVTHQLQ-YLKAASQILILKDGKMVQKGTYTEFLKS 548
Cdd:cd03261 163 PTAGLDPIASGVIDDL----IrsLKKELgltSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
334-531 |
2.98e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.10 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP---SHGLVSVHG-----------R 399
Cdd:COG4136 1 MLSLENLTITLGG---RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltalpaeqrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 400 IAYVSQQPWVFSG-TLRSNILFG-----KKyeKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVNLAR 472
Cdd:COG4136 78 IGILFQDDLLFPHlSVGENLAFAlpptiGR--AQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 473 AVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKI-TILVTHQLQYLKAASQILIL 531
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
349-535 |
3.92e-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: 104.11 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------------IAYVSQQPWVFS 411
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 412 G-TLRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLtviGDRGT----TLSGGQKARVNLARAVYQDADIYLLDDP 486
Cdd:cd03255 96 DlTALENVELPL-----LLAGVPKKERRERAEELLERVGL---GDRLNhypsELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 685504970 487 LSAVDAEVSRHLFELcICQILHEKIT--ILVTHQLQYLKAASQILILKDGK 535
Cdd:cd03255 168 TGNLDSETGKEVMEL-LRELNKEAGTtiVVVTHDPELAEYADRIIELRDGK 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
353-536 |
4.15e-25 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 102.48 E-value: 4.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSNIl 419
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEEPSLYENlTVRENL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 420 fgkkyekeryekvikacalkkdlqlledgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 499
Cdd:cd03230 95 ---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 685504970 500 ELcICQILHEKITILV-THQLQYLKA-ASQILILKDGKM 536
Cdd:cd03230 136 EL-LRELKKEGKTILLsSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
349-535 |
8.15e-25 |
|
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: 101.17 E-value: 8.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQqpwvfsgtlr 415
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiaklpleelrrRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 snilfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvS 495
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-S 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 685504970 496 RHLFELCICQILHEKITIL-VTHQLQYL-KAASQILILKDGK 535
Cdd:cd00267 116 RERLLELLRELAEEGRTVIiVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
352-537 |
8.90e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 102.72 E-value: 8.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 352 TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------IAYVSQQP--WVFSGTLRSNIL 419
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrksIGYVMQDVdyQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 420 FGKKYEKERYEKVikACALKK-DLQLLEDgdltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 498
Cdd:cd03226 95 LGLKELDAGNEQA--ETVLKDlDLYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 685504970 499 FELcicqILH----EKITILVTHQLQYL-KAASQILILKDGKMV 537
Cdd:cd03226 166 GEL----IRElaaqGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
334-575 |
1.58e-24 |
|
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: 108.45 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPS---HGLVSVHG------------ 398
Cdd:COG1123 4 LLEVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelsealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 -RIAYVSQQPWV--FSGTLRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAV 474
Cdd:COG1123 83 rRIGMVFQDPMTqlNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPhQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 475 YQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKIT--ILVTHQLQY-LKAASQILILKDGKMVQKGTYTEFLKSGID 551
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDL-LRELQRERGTtvLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
250 260
....*....|....*....|....*.
gi 685504970 552 FGSL--LKKDNEESEQPPVPGTPTLR 575
Cdd:COG1123 237 LAAVprLGAARGRAAPAAAAAEPLLE 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
334-548 |
2.64e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 102.57 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFTA-FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------R 399
Cdd:COG1124 1 MLEVRNLSVsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 400 IAYVSQQP-----------WVFSGTLRsniLFGKKYEKERYEKVIKACALKKDLQlledgdltvigDR-GTTLSGGQKAR 467
Cdd:COG1124 81 VQMVFQDPyaslhprhtvdRILAEPLR---IHGLPDREERIAELLEQVGLPPSFL-----------DRyPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 468 VNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KIT-ILVTHQLQYLKA-ASQILILKDGKMVQKGTYTE 544
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNL-LKDLREErGLTyLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
....
gi 685504970 545 FLKS 548
Cdd:COG1124 226 LLAG 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
332-537 |
3.51e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.66 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 332 KKMVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------ 398
Cdd:COG1136 2 SPLLELRNLTkSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 -----RIAYVSQQPWVFSG-TLRSNI----LFGKKYEKERYEKVikacalkkdLQLLED-GdltvIGDRG----TTLSGG 463
Cdd:COG1136 82 rlrrrHIGFVFQFFNLLPElTALENValplLLAGVSRKERRERA---------RELLERvG----LGDRLdhrpSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 464 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKMV 537
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELgTTIVmVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
353-548 |
3.61e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 102.03 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------RIAYVSQQPWVFSG-TLRSNILF 420
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 421 GKKyeKERYEKVIKAcalKKDLQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 499
Cdd:cd03299 95 GLK--KRKVDKKEIE---RKVLEIAEMLGIDHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 685504970 500 ELcICQILHE-KITIL-VTHQLQYLKA-ASQILILKDGKMVQKGTYTEFLKS 548
Cdd:cd03299 170 EE-LKKIRKEfGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
335-540 |
7.14e-24 |
|
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: 100.41 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYV 403
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 404 SQQPWVFSG-TLRSNILFGKKYEKERY----EKVIKACALKKDLQLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDA 478
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGLKLRKVPKdeidERVREVAELLQIEHLLDR--------KPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 479 DIYLLDDPLSAVDAEVSRHL-FELCICQILHEKITILVTH-QLQYLKAASQILILKDGKMVQKG 540
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMrAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
353-545 |
1.37e-23 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 99.95 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAV-----LGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG 412
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGKKYEKERYEKVIKAcalkKDLQLLEDGDLT-VIGDR--GTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:cd03260 96 SIYDNVAYGLRLHGIKLKEELDE----RVEEALRKAALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 490 VDAeVSRHLFELCICQiLHEKITIL-VTHQL-QYLKAASQILILKDGKMVQKGTYTEF 545
Cdd:cd03260 172 LDP-ISTAKIEELIAE-LKKEYTIViVTHNMqQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
346-546 |
1.53e-23 |
|
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: 100.80 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 346 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQPW 408
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 409 VFSG-TLRSNILFG-------KKYEKERYEKVIKACALKKDLQLLEDgdltvigdrgtTLSGGQKARVNLARAVYQDADI 480
Cdd:cd03294 113 LLPHrTVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 481 YLLDDPLSAVD----AEVSRHLFELcicQILHEKITILVTHQL-QYLKAASQILILKDGKMVQKGTYTEFL 546
Cdd:cd03294 182 LLMDEAFSALDplirREMQDELLRL---QAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
353-548 |
2.13e-23 |
|
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: 99.67 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWVFSG-TLR 415
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGMLFQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNILF-----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGTT-LSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:COG1127 101 ENVAFplrehTDLSEAEIRELV---------LEKLELVGLPGAADKMPSeLSGGMRKRVALARALALDPEILLYDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 490 VDAEVSRHLFELcICQILHE-KIT-ILVTHQLQYLKA-ASQILILKDGKMVQKGTYTEFLKS 548
Cdd:COG1127 172 LDPITSAVIDEL-IRELRDElGLTsVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
334-540 |
3.57e-23 |
|
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: 98.73 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 398
Cdd:cd03257 1 LLEVKNLSvSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 --RIAYVSQQP-----------WVFSGTLRSNilfGKKYEKERYEKVIkaCALKKDLQLLEDgdltVIGDRGTTLSGGQK 465
Cdd:cd03257 81 rkEIQMVFQDPmsslnprmtigEQIAEPLRIH---GKLSKKEARKEAV--LLLLVGVGLPEE----VLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 466 ARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFEL--CICQILheKITIL-VTHQLQYLKA-ASQILILKDGKMVQKG 540
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkKLQEEL--GLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
357-546 |
5.86e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.29 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 357 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNILFGK-- 422
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQENNLFPHlTVAQNIGLGLrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 423 --KYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 499
Cdd:COG3840 99 glKLTAEQRAQVEQA---------LERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 685504970 500 ELcICQILHE-KITIL-VTHQLQ-YLKAASQILILKDGKMVQKGTYTEFL 546
Cdd:COG3840 170 DL-VDELCRErGLTVLmVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
353-535 |
1.29e-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: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG-TLRS 416
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 NILFGkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 685504970 497 HLFELciCQILHEK--IT-ILVTHQLQYL-KAASQILILKDGK 535
Cdd:cd03229 138 EVRAL--LKSLQAQlgITvVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
356-540 |
2.72e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 95.82 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTVrPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQPWVFSG-TLRSN 417
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYALFPHlNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGKKYeKERYEKVIKACALkkdLQLLedgDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:cd03297 96 LAFGLKR-KRNREDRISVDEL---LDLL---GLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 685504970 497 hlfelcICQILHEKI-------TILVTH---QLQYLkaASQILILKDGKMVQKG 540
Cdd:cd03297 169 ------QLLPELKQIkknlnipVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
334-540 |
7.19e-22 |
|
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: 94.74 E-value: 7.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGriAYVSQQPW---- 408
Cdd:cd03266 1 MITADALTkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAearr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 409 ---VFSG--------TLRSNIL-FGKKYEKERYEkvIKAcALKKDLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQ 476
Cdd:cd03266 79 rlgFVSDstglydrlTARENLEyFAGLYGLKGDE--LTA-RLEELADRLGMEEL--LDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 477 DADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILV-THQLQYLKA-ASQILILKDGKMVQKG 540
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREF-IRQLRALGKCILFsTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
103-546 |
8.45e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.56 E-value: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 103 ALRLSNMAMGKTTTGQIVNLLSND--VNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGM---AVLIILLPLQS 177
Cdd:PRK10790 108 ALRQPLSAFDTQPVGQLISRVTNDteVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMifpAVLVVMVIYQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 178 CFGKLFSSLRSKTATFTDArirtMNEVITGIRIIKMYAWEKSFSnlitnlrkKEISKILRSSCLRGMN-----------L 246
Cdd:PRK10790 188 YSTPIVRRVRAYLADINDG----FNEVINGMSVIQQFRQQARFG--------ERMGEASRSHYMARMQtlrldgfllrpL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 247 ASFFSAskiivfvtfttYVLLGSVITASrvFVAVtlyGAVRLTVTLFFPSAIERVSE--------------AIVSIRRIq 312
Cdd:PRK10790 256 LSLFSA-----------LILCGLLMLFG--FSAS---GTIEVGVLYAFISYLGRLNEplielttqqsmlqqAVVAGERV- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 313 tFLLLDEISQR----NRQLPSdGKkmVHVQDFTAFWDKasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELA 388
Cdd:PRK10790 319 -FELMDGPRQQygndDRPLQS-GR--IDIDNVSFAYRD--DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 389 PSHGLVSVHGR-------------IAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGD 455
Cdd:PRK10790 393 LTEGEIRLDGRplsslshsvlrqgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 456 RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA----EVSRHLfelcicQILHEKITILV-THQLQYLKAASQILI 530
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSgteqAIQQAL------AAVREHTTLVViAHRLSTIVEADTILV 546
|
490
....*....|....*.
gi 685504970 531 LKDGKMVQKGTYTEFL 546
Cdd:PRK10790 547 LHRGQAVEQGTHQQLL 562
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
351-549 |
1.09e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 99.89 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-------------SVHGRIAYVSQQPWVFSGTLRSN 417
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvtqaSLRAAIGIVPQDTVLFNDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----- 491
Cdd:COG5265 452 IAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDsrter 531
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 492 ------AEVSRHlfelcicqilheKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:COG5265 532 aiqaalREVARG------------RTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQG 583
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
353-541 |
1.13e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRiAYVSQQPWV---------------FSGTLRSN 417
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLAAWSPWElarrravlpqhsslaFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGK---KYEKERYEKVIKACalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVNLARA---VYQDAD----IYLLDDP 486
Cdd:COG4559 96 VALGRaphGSSAAQDRQIVREA--------LALVGLAHLAGRSyQTLSGGEQQRVQLARVlaqLWEPVDggprWLFLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 487 LSAVDAevsRHlfELCICQIL----HEKITIL-VTHQL----QYlkaASQILILKDGKMVQKGT 541
Cdd:COG4559 168 TSALDL---AH--QHAVLRLArqlaRRGGGVVaVLHDLnlaaQY---ADRILLLHQGRLVAQGT 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
349-546 |
1.98e-21 |
|
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: 93.65 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-T 413
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 LRSNILFG-----KKYEKERYEKVikacalkkdLQL---LEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:cd03224 92 VEENLLLGayarrRAKRKARLERV---------YELfprLKE----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 486 P---LSAVdaeVSRHLFElCICQILHEKITILVTHqlQYLKAASQI----LILKDGKMVQKGTYTEFL 546
Cdd:cd03224 159 PsegLAPK---IVEEIFE-AIRELRDEGVTILLVE--QNARFALEIadraYVLERGRVVLEGTAAELL 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
353-535 |
4.31e-21 |
|
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: 92.21 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG-TLRS 416
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 NILFGKKYEKeryeKVIKACALKKDLQLLED-GDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 495
Cdd:cd03262 96 NITLAPIKVK----GMSKAEAEERALELLEKvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 685504970 496 RHLFELcICQILHEKIT-ILVTHQLQY-LKAASQILILKDGK 535
Cdd:cd03262 172 GEVLDV-MKDLAEEGMTmVVVTHEMGFaREVADRVIFMDDGR 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
353-540 |
6.38e-21 |
|
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: 92.21 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAyvsqqpWV------FSGTL--RSNILFG--- 421
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLlglgggFNPELtgRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 422 ----KKYEKERYEKVIKACALKKDLqlledgDLTVigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE---- 493
Cdd:cd03220 112 lglsRKEIDEKIDEIIEFSELGDFI------DLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqek 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 685504970 494 VSRHLFELcicqILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 540
Cdd:cd03220 181 CQRRLREL----LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
350-541 |
7.57e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------RIAYVSQQPWVFSG-TLRSN 417
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGKKYeKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:PRK10851 95 IAFGLTV-LPRRERPNAAAIKAKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 685504970 497 HLFELciCQILHE--KIT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 541
Cdd:PRK10851 174 ELRRW--LRQLHEelKFTsVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
353-544 |
9.66e-21 |
|
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: 91.73 E-value: 9.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 417
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFG--------------KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYL 482
Cdd:cd03219 96 VMVAaqartgsglllaraRREEREARERA---------EELLERVGLADLADRpAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 483 LDDPLSAVDAEVSRHLFELcICQILHEKITILVT-HQLQYLKA-ASQILILKDGKMVQKGTYTE 544
Cdd:cd03219 167 LDEPAAGLNPEETEELAEL-IRELRERGITVLLVeHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
301-541 |
1.18e-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: 96.13 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 301 VSEAIVSIRRIQTFLLLDEISQRNRQLPSDGKKMVHVQDFTA--FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSS 378
Cdd:COG1123 227 PEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKST 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 379 LLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPwvFSG-----TLRSNI-----LFGKKYEKERYEKV 432
Cdd:COG1123 307 LARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDP--YSSlnprmTVGDIIaeplrLHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 433 ikacalkkdLQLLEDGDL--TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcicqiLHE- 509
Cdd:COG1123 385 ---------AELLERVGLppDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL-----LRDl 450
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 685504970 510 ----KITIL-VTHQL---QYLkaASQILILKDGKMVQKGT 541
Cdd:COG1123 451 qrelGLTYLfISHDLavvRYI--ADRVAVMYDGRIVEDGP 488
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
100-538 |
1.53e-20 |
|
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: 97.67 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 100 LIEALRLSNMAMGKTTTGQIVNLLSNDVNKFDQ---VTVF-LHFLWAGPLQAIAVTALLWMEIgisCLAGMAVLIILLPL 175
Cdd:TIGR01271 965 LHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDmlpLTLFdFIQLTLIVLGAIFVVSVLQPYI---FIAAIPVAVIFIML 1041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 176 QSCFGKLFSSLRSKTAtftDARIRTMNEVITGIR---IIKMYAWEKSFSNLITN-LRKKEISKILRSSCLRgmnlasFFS 251
Cdd:TIGR01271 1042 RAYFLRTSQQLKQLES---EARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKaLNLHTANWFLYLSTLR------WFQ 1112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 252 ASKIIVFVTFTTYVLLGSVIT----ASRVFVAVTLYGAVRLTVTLFFPSAIErVSEAIVSIRRIQTFL------------ 315
Cdd:TIGR01271 1113 MRIDIIFVFFFIAVTFIAIGTnqdgEGEVGIILTLAMNILSTLQWAVNSSID-VDGLMRSVSRVFKFIdlpqeeprpsgg 1191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 316 ---------LLDEISQRNRQLPSDGKKMVhvQDFTAFWDKASETpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLgE 386
Cdd:TIGR01271 1192 ggkyqlstvLVIENPHAQKCWPSGGQMDV--QGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-R 1267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 387 LAPSHGLVSVHG-----------RIAY--VSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVI 453
Cdd:TIGR01271 1268 LLSTEGEIQIDGvswnsvtlqtwRKAFgvIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVL 1347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 454 GDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKD 533
Cdd:TIGR01271 1348 VDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEG 1426
|
....*
gi 685504970 534 GKMVQ 538
Cdd:TIGR01271 1427 SSVKQ 1431
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
353-546 |
1.81e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV-FSGTLRSNI 418
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 LFGkkyekeRYekvIKACALKKDLQL----LEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDAD------IYLLDDPL 487
Cdd:PRK13548 98 AMG------RA---PHGLSRAEDDALvaaaLAQVDLAHLAGRDyPQLSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 488 SAVD----AEVSRHLFELCICQILHekiTILVTHQL----QYlkaASQILILKDGKMVQKGTYTEFL 546
Cdd:PRK13548 169 SALDlahqHHVLRLARQLAHERGLA---VIVVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
328-541 |
2.61e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 89.78 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 328 PSDGKkmVHVQDFTAFWdkASETP-TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------- 398
Cdd:cd03369 2 PEHGE--IEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 -----RIAYVSQQPWVFSGTLRSNI-LFGKKYEKERYEkvikacALKkdlqlledgdltvIGDRGTTLSGGQKARVNLAR 472
Cdd:cd03369 78 edlrsSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIYG------ALR-------------VSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504970 473 AVYQDADIYLLDDPLSAVDAEvSRHLfelcICQILHE---KITIL-VTHQLQYLKAASQILILKDGKMVQKGT 541
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYA-TDAL----IQKTIREeftNSTILtIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
334-492 |
3.84e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.69 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFTAFWD-KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI--------AYVS 404
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 405 QQ----PWVfsgTLRSNILFGKKY----EKERYEKvikACALkkdLQL--LEDgdltVIGDRGTTLSGGQKARVNLARAV 474
Cdd:COG4525 83 QKdallPWL---NVLDNVAFGLRLrgvpKAERRAR---AEEL---LALvgLAD----FARRRIWQLSGGMRQRVGIARAL 149
|
170
....*....|....*...
gi 685504970 475 YQDADIYLLDDPLSAVDA 492
Cdd:COG4525 150 AADPRFLLMDEPFGALDA 167
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
346-547 |
4.06e-20 |
|
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: 89.49 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 346 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG- 412
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILF-------GKKYEKERYEKVIKACALKKdlqlledgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:cd03263 91 TVREHLRFyarlkglPKSEIKEEVELLLRVLGLTD-----------KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504970 486 PLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKGTYTEfLK 547
Cdd:cd03263 160 PTSGLDPASRRAIWDL-ILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQE-LK 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
353-548 |
6.21e-20 |
|
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: 89.52 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV----------SVHGR----IAYVSQQPWVFSG-TLRSN 417
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklPMHKRarlgIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD- 491
Cdd:cd03218 96 ILavleIRGLSKKEREEKLE---------ELLEEFHITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504970 492 ---AEVSRhlfelcICQILHEK-ITILVT-HQL-QYLKAASQILILKDGKMVQKGTYTEFLKS 548
Cdd:cd03218 167 iavQDIQK------IIKILKDRgIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
349-549 |
7.71e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV-FSGTL 414
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 RSNILFGKKYEKERYEKVIKACALKKDlQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDae 493
Cdd:PRK09536 95 RQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 494 VSRHLFELCICQILHE--KITILVTHQLQyLKA--ASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:PRK09536 172 INHQVRTLELVRRLVDdgKTAVAAIHDLD-LAAryCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
116-546 |
1.17e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 94.66 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 116 TGQIVNLLSNDVNKFDQ-----VTVFLHFLWagplQAIAVTALLWMEIGISCLAGMAVLIIL----LPLQSC---FGKLF 183
Cdd:PLN03232 1006 TGRVINRFSKDIGDIDRnvanlMNMFMNQLW----QLLSTFALIGTVSTISLWAIMPLLILFyaayLYYQSTsreVRRLD 1081
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 184 SSLRSKT-ATFTDArirtMNEvITGIRIIKMYAWE-----KSFSNlitNLRKKEISK------ILRSSCLRGMnlasffs 251
Cdd:PLN03232 1082 SVTRSPIyAQFGEA----LNG-LSSIRAYKAYDRMakingKSMDN---NIRFTLANTssnrwlTIRLETLGGV------- 1146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 252 askiIVFVTfTTYVLLGSVITASRVFVAVT--LYGAVRLTVTLFFPSAIERVSEA---IVSIRRIQTFLLL----DEISQ 322
Cdd:PLN03232 1147 ----MIWLT-ATFAVLRNGNAENQAGFASTmgLLLSYTLNITTLLSGVLRQASKAensLNSVERVGNYIDLpseaTAIIE 1221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 323 RNRQL---PSDGkkMVHVQDFTAFWdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL-------GEL----- 387
Cdd:PLN03232 1222 NNRPVsgwPSRG--SIKFEDVHLRY-RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFrivelekGRImiddc 1298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 388 -APSHGLVSVHGRIAYVSQQPWVFSGTLRSNI---------LFGKKYEKERYEKVIKACALKKDLQLLEDGDltvigdrg 457
Cdd:PLN03232 1299 dVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdpfsehndaDLWEALERAHIKDVIDRNPFGLDAEVSEGGE-------- 1370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 458 tTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRhLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMV 537
Cdd:PLN03232 1371 -NFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS-LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVL 1448
|
....*....
gi 685504970 538 QKGTYTEFL 546
Cdd:PLN03232 1449 EYDSPQELL 1457
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
353-541 |
1.75e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.60 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAyvsqqpWVF---SG-----TLRSNILFG--- 421
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLelgAGfhpelTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 422 ----KKYEKERYEKVIkacalkkdlqlledgDLTVIGD------RgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:COG1134 116 lglsRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 492 AE----VSRHLFELcicqILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKGT 541
Cdd:COG1134 179 AAfqkkCLARIREL----RESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
353-541 |
2.27e-19 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 87.68 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI-----AYVSQQPWVFSG-------TLRSNILF 420
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRPVNTVFQNyalfphlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 421 G----KKYEKERYEKVIKACALkkdLQLLEDGDltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:cd03300 96 GlrlkKLPKAEIKERVAEALDL---VQLEGYAN-----RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 685504970 497 HL-FELcicQILHEK--IT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 541
Cdd:cd03300 168 DMqLEL---KRLQKElgITfVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
267-518 |
2.75e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.18 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 267 LGSVITASRVFVAVTlyGAVRltvtlFFPSAIERVSEAIVSIRRIQTFL----LLDEISQRNRQLPSDGKKMVHVQDFTA 342
Cdd:COG4178 298 LGGLMQAASAFGQVQ--GALS-----WFVDNYQSLAEWRATVDRLAGFEealeAADALPEAASRIETSEDGALALEDLTL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 343 FwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPS-HGLVSV--HGRIAYVSQQPWVFSGTLRSNIL 419
Cdd:COG4178 371 R--TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARpaGARVLFLPQRPYLPLGTLREALL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 420 F---GKKYEKERYEKVIKACALKKDLQLLEDGDltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:COG4178 448 YpatAEAFSDAELREALEAVGLGHLAERLDEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
250 260
....*....|....*....|..
gi 685504970 497 HLFELcICQILHEKITILVTHQ 518
Cdd:COG4178 523 ALYQL-LREELPGTTVISVGHR 543
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
334-572 |
3.25e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.15 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RI 400
Cdd:PRK11231 2 TLRTENLTVGYGT---KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 401 AYVSQQPWVFSG-TLRS---------NILFGKKYEKERyEKVIKAcalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVN 469
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRElvaygrspwLSLWGRLSAEDN-ARVNQA---------MEQTRINHLADRRlTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 470 LARAVYQDADIYLLDDPLSAVDAEvsrHLFELC-ICQILHE--KITILVTHQL-QYLKAASQILILKDGKMVQKGTYTEF 545
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDIN---HQVELMrLMRELNTqgKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEV 225
|
250 260 270
....*....|....*....|....*....|
gi 685504970 546 LKSGidfgsLLKKD---NEESEQPPVPGTP 572
Cdd:PRK11231 226 MTPG-----LLRTVfdvEAEIHPEPVSGTP 250
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
626-770 |
3.74e-19 |
|
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: 89.48 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 626 YKNYFRAGAHWIVFIFLILLNTAAQVAYVLQDWWL---SYWANKQSMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVL 702
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLlrsQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVADSLLA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 703 FGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd18600 86 MGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQ 153
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
350-537 |
4.78e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 86.64 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWVFSGt 413
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRLLPD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 lRS---NILF-----GKKyEKERYEKVIKacALKKdLQLLEDGDLTVIgdrgtTLSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:COG2884 94 -RTvyeNVALplrvtGKS-RKEIRRRVRE--VLDL-VGLSDKAKALPH-----ELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 685504970 486 PLSAVDAEVSRHLFELcICQILHEKITILV-THQLQYL-KAASQILILKDGKMV 537
Cdd:COG2884 164 PTGNLDPETSWEIMEL-LEEINRRGTTVLIaTHDLELVdRMPKRVLELEDGRLV 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
353-548 |
6.60e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 6.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQPWVFSG-TLRSNILFG-------- 421
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLDGdaelrale 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 422 KKYEK------------ERYEKVI-------------KACALKKDLQL-LEDGDLTVigdrgTTLSGGQKARVNLARAVY 475
Cdd:COG0488 94 AELEEleaklaepdedlERLAELQeefealggweaeaRAEEILSGLGFpEEDLDRPV-----SELSGGWRRRVALARALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 476 QDADIYLLDDP---LsavDAEvSRHLFElcicQILHE-KIT-ILVTHQLQYL-KAASQILILKDGKMVQ-KGTYTEFLKS 548
Cdd:COG0488 169 SEPDLLLLDEPtnhL---DLE-SIEWLE----EFLKNyPGTvLVVSHDRYFLdRVATRILELDRGKLTLyPGNYSAYLEQ 240
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
356-540 |
6.93e-19 |
|
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: 86.01 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNILFGK- 422
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGLs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 423 ---KYEKERYEKVIKACAlKKDLQLLEDgdltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 499
Cdd:cd03298 97 pglKLTAEDRQAIEVALA-RVGLAGLEK-------RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 685504970 500 ELC--ICQilHEKITIL-VTHQLQYLKAASQILI-LKDGKMVQKG 540
Cdd:cd03298 169 DLVldLHA--ETKMTVLmVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
353-540 |
7.61e-19 |
|
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: 85.71 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGeLLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPwvfsgTLRSNIlf 420
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEF-----GVYPNF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 421 gKKYEKERYEKVIKACALKKD----LQLLEDGDLT-VIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvS 495
Cdd:cd03264 88 -TVREFLDYIAWLKGIPSKEVkarvDEVLELVNLGdRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE-E 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 685504970 496 RHLFELCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 540
Cdd:cd03264 166 RIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
353-537 |
1.26e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 83.63 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQqpwvfsgtlrsni 418
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevsfasprdarragIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 lfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 498
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 685504970 499 FELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGKMV 537
Cdd:cd03216 122 FKV-IRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
330-549 |
1.80e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.22 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 330 DGKKMVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------- 398
Cdd:PRK13635 1 MKEEIIRVEHIS-FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 --RIAYVSQQP-WVFSG-TLRSNILFGKKYE----KERYEKVIKACALKKDLQLLEdgdltvigDRGTTLSGGQKARVNL 470
Cdd:PRK13635 80 rrQVGMVFQNPdNQFVGaTVQDDVAFGLENIgvprEEMVERVDQALRQVGMEDFLN--------REPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 471 ARAVYQDADIYLLDDPLSAVD----AEVsrhlfeLCICQILHEK--ITIL-VTHQLQYLKAASQILILKDGKMVQKGTYT 543
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDprgrREV------LETVRQLKEQkgITVLsITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....*.
gi 685504970 544 EFLKSG 549
Cdd:PRK13635 226 EIFKSG 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
351-520 |
1.89e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.91 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI--------AYVSQQ----PWVfsgTLRSNI 418
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNegllPWR---NVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 LFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 497
Cdd:PRK11248 92 AFGL-----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*
gi 685504970 498 LFELcICQILHE--KITILVTHQLQ 520
Cdd:PRK11248 167 MQTL-LLKLWQEtgKQVLLITHDIE 190
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
357-546 |
2.69e-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: 87.46 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 357 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQPWVFSG-TLRSNI 418
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFPHlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 LFGKKYE-----KERYEKVIkacalkkdlQLLEDGDLTvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:COG4148 99 LYGRKRApraerRISFDEVV---------ELLGIGHLL---DRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 493 EvSRHlfelcicQIL------HEKITI---LVTHQL---QYLkaASQILILKDGKMVQKGTYTEFL 546
Cdd:COG4148 167 A-RKA-------EILpylerlRDELDIpilYVSHSLdevARL--ADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
639-770 |
3.73e-18 |
|
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: 85.39 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 639 FIFLILLNTAAQVAYVLQDWWLSYWANkqsmlnvtVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNS 718
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD--------VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERL 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 685504970 719 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:pfam00664 73 SRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQ 124
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
357-556 |
4.97e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.86 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 357 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---RIAYVSQQPW--------VFSG-TLRSNILFG--- 421
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRPVsmlfqennLFSHlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 422 ----KKYEKERYEKVIKACALKKDLQLLEdgdltvigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 497
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 498 LFELcICQILHEK-ITIL-VTHQLQ-YLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLL 556
Cdd:PRK10771 168 MLTL-VSQVCQERqLTLLmVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
349-548 |
5.56e-18 |
|
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: 84.37 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGL-VSVHG-------------RIAYVS---QQPWVFS 411
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGerrggedvwelrkRIGLVSpalQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 412 GTLRSNIL---FG-----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYL 482
Cdd:COG1119 95 ETVLDVVLsgfFDsiglyREPTDEQRERA---------RELLELLGLAHLADRPfGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 483 LDDPLSAVDAEvSRHLFELCICQILHEKIT--ILVTHQLQYLKAA-SQILILKDGKMVQKGTYTEFLKS 548
Cdd:COG1119 166 LDEPTAGLDLG-ARELLLALLDKLAAEGAPtlVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-535 |
8.41e-18 |
|
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: 80.57 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQqpwvfsg 412
Cdd:cd03221 1 IELENLSKTYGG---KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 tlrsnilfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 685504970 493 EvSRHLFElcicQIL--HEKITILVTHQLQYLKA-ASQILILKDGK 535
Cdd:cd03221 104 E-SIEALE----EALkeYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
186-594 |
1.17e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.16 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 186 LRSKTAT-FTDARIRTMNEVITGIRIIKMYAWEKSFSNLItNLRKKEISK-ILRSS--------CLRGMNLAS----FFS 251
Cdd:PTZ00265 223 INKKTSLlYNNNTMSIIEEALVGIRTVVSYCGEKTILKKF-NLSEKLYSKyILKANfmeslhigMINGFILASyafgFWY 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 252 ASKIIVFVTFTTY----VLLGSVITasrVFVAVtLYGAVRLTVTLffPSAIERVS--EAIVSIRRIQTFLLLDEISQRNR 325
Cdd:PTZ00265 302 GTRIIISDLSNQQpnndFHGGSVIS---ILLGV-LISMFMLTIIL--PNITEYMKslEATNSLYEIINRKPLVENNDDGK 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 326 QLPsDGKKmVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVH-------- 397
Cdd:PTZ00265 376 KLK-DIKK-IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdi 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 398 ------GRIAYVSQQPWVFSGTLRSNI---LFGKK---YEKERYEK--------------VIKACA-------------- 437
Cdd:PTZ00265 454 nlkwwrSKIGVVSQDPLLFSNSIKNNIkysLYSLKdleALSNYYNEdgndsqenknkrnsCRAKCAgdlndmsnttdsne 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 438 ---LKKDLQLLEDGDL---------------------TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 493
Cdd:PTZ00265 534 lieMRKNYQTIKDSEVvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 494 vSRHLFELCICQIL--HEKITILVTHQLQYLKAASQILILKDGkmvQKGTYTEFLKSGIDFGSLLKKDNEESEQPPVPGT 571
Cdd:PTZ00265 614 -SEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNR---ERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNN 689
|
490 500
....*....|....*....|....
gi 685504970 572 PTLRNRTFS-ESSVWSQQSSRPSL 594
Cdd:PTZ00265 690 NNNNNNKINnAGSYIIEQGTHDAL 713
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
315-547 |
1.41e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 315 LLLDEISQRNR----QLPSD---GKKMVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL 387
Cdd:COG0488 289 LEREEPPRRDKtveiRFPPPerlGKKVLELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 388 APSHGLVsVHG---RIAYVSQQPWVFSG--TLRSNIlfgKKYEKERYEKVIKacalkkdlQLLED----GD--LTVIGDr 456
Cdd:COG0488 366 EPDSGTV-KLGetvKIGYFDQHQEELDPdkTVLDEL---RDGAPGGTEQEVR--------GYLGRflfsGDdaFKPVGV- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 457 gttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvSRHL-------FELCIcqilhekitILVTHQLQYLKA-ASQI 528
Cdd:COG0488 433 ---LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE-TLEAleealddFPGTV---------LLVSHDRYFLDRvATRI 499
|
250 260
....*....|....*....|
gi 685504970 529 LILKDGKMVQK-GTYTEFLK 547
Cdd:COG0488 500 LEFEDGGVREYpGGYDDYLE 519
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
353-547 |
2.07e-17 |
|
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: 81.65 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSNI- 418
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 LFGKKY------EKERYEKVIKAcalkkdLQLLEDGDLTVigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:cd03265 96 IHARLYgvpgaeRRERIDELLDF------VGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 493 EVSRHLFELcICQILHEK-ITILVThqLQYLKAASQ----ILILKDGKMVQKGTYTEfLK 547
Cdd:cd03265 165 QTRAHVWEY-IEKLKEEFgMTILLT--THYMEEAEQlcdrVAIIDHGRIIAEGTPEE-LK 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
353-540 |
2.40e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 81.49 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------RIAYVSQQPWVFSG-TLRSNILF 420
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkniealrRIGALIEAPGFYPNlTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 421 GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 499
Cdd:cd03268 96 LARLLGIRKKRI---------DEVLDVVGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 685504970 500 ELcICQILHEKITILV-THQLQYL-KAASQILILKDGKMVQKG 540
Cdd:cd03268 167 EL-ILSLRDQGITVLIsSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
353-533 |
2.52e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.89 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLsAVLGELAPSH-GLVSVHGR--IAYVSQQPWVFSGTLRSNILfgkkYEKERy 429
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLWPWGsGRIGMPEGedLLFLPQRPYLPLGTLREQLI----YPWDD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 430 ekvikacalkkdlqlledgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCicqiLHE 509
Cdd:cd03223 91 -----------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KEL 137
|
170 180
....*....|....*....|....*
gi 685504970 510 KITIL-VTHQLQYLKAASQILILKD 533
Cdd:cd03223 138 GITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
335-540 |
5.70e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTAFWDKAseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPW------ 408
Cdd:PRK13647 5 IEVEDLHFRYKDG--TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskvg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 409 ---------VFSGTLRSNILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGTT-LSGGQKARVNLA 471
Cdd:PRK13647 83 lvfqdpddqVFSSTVWDDVAFGpvnmgldKDEVERRVEEALKAVRMWD------------FRDKPPYhLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 472 RAVYQDADIYLLDDPLSAVDAEVSRHLFElcICQILHE--KITILVTHQLQY-LKAASQILILKDGKMVQKG 540
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
345-541 |
7.32e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.04 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 345 DKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVSVHGRI-------------AYVSQQpwvfs 411
Cdd:COG4138 4 NDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPlsdwsaaelarhrAYLSQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 412 gTLRSNILFGKKY------EKERYEKVIKACAlkkdlQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQ-------D 477
Cdd:COG4138 78 -QSPPFAMPVFQYlalhqpAGASSEAVEQLLA-----QLAEALGLEDKLSRPlTQLSGGEWQRVRLAAVLLQvwptinpE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 478 ADIYLLDDPLSAVD----AEVSRHLFELCICQilhekITILV-THQLQY-LKAASQILILKDGKMVQKGT 541
Cdd:COG4138 152 GQLLLLDEPMNSLDvaqqAALDRLLRELCQQG-----ITVVMsSHDLNHtLRHADRVWLLKQGKLVASGE 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
356-545 |
1.16e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.06 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTVRPGELLAVVGPVGAGKSSLLSaVLGEL-APSHGLVSVHGRIAYVSQQPWVFSG-TLRSNIlfGKKYEK------- 426
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLeMPRSGTLNIAGNHFDFSKTPSDKAIrELRRNV--GMVFQQynlwphl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 427 -------ERYEKVI---KACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 495
Cdd:PRK11124 98 tvqqnliEAPCRVLglsKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 496 RHlfelcICQILHE----KIT-ILVTHQLQYL-KAASQILILKDGKMVQKGTYTEF 545
Cdd:PRK11124 178 AQ-----IVSIIRElaetGITqVIVTHEVEVArKTASRVVYMENGHIVEQGDASCF 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
344-540 |
1.38e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 78.75 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 344 WDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHglvsvhgriayvsqqpwvFSGTLRSNilfGKK 423
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG------------------VSGEVLIN---GRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 424 YEKERYEKVIkaCALKKDLQLLedGDLTV-------IGDRGttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:cd03213 75 LDKRSFRKII--GYVPQDDILH--PTLTVretlmfaAKLRG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 685504970 497 HLFELcICQILHEKITILVT-HQLQYL--KAASQILILKDGKMVQKG 540
Cdd:cd03213 149 QVMSL-LRRLADTGRTIICSiHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
337-581 |
1.50e-16 |
|
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: 80.67 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 337 VQDFTAFWDKASETpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLgELAPSHGLVSVHG-----------RIAY--V 403
Cdd:cd03289 5 VKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFgvI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 404 SQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLL 483
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 484 DDPLSAVDA-------EVSRHLFELCicqilhekITILVTHQLQYLKAASQILILKDGKMVQKGTY------TEFLKSGI 550
Cdd:cd03289 163 DEPSAHLDPityqvirKTLKQAFADC--------TVILSEHRIEAMLECQRFLVIEENKVRQYDSIqkllneKSHFKQAI 234
|
250 260 270
....*....|....*....|....*....|....*
gi 685504970 551 DFGSLLK----KDNEESEQPPVPGTPTLRNRTFSE 581
Cdd:cd03289 235 SPSDRLKlfprRNSSKSKRKPRPQIQALQEETEEE 269
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
353-518 |
1.62e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 79.24 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVS----VHG----------RIAYVSQ-----------QP 407
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTSgqilFNGqprkpdqfqkCVAYVRQddillpgltvrET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 408 WVFSGTLRSNILFGKKYEKERYEkvikacalkkDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVE----------DVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|..
gi 685504970 488 SAVDAEVSRHLFELcICQILHEKITILVT-HQ 518
Cdd:cd03234 172 SGLDSFTALNLVST-LSQLARRNRIVILTiHQ 202
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
353-502 |
2.21e-16 |
|
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: 83.26 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSaVLGELAPSHG---LVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEkERY 429
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSE-DMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 430 EKVIKACALKKDLQLL-------EDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELC 502
Cdd:TIGR00954 546 RRGLSDKDLEQILDNVqlthileREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
346-531 |
2.55e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.60 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 346 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG 412
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGKKYEKERYEKVikacALKKDLQLLEDgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPDPA----IFLDDLERFAL-PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 685504970 493 EVSRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILIL 531
Cdd:PRK10247 171 SNKHNVNEI-IHRYVREQnIAVLwVTHDKDEINHADKVITL 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
353-515 |
5.44e-16 |
|
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: 78.54 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 417
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFG-------------------KKYEKERYEKVikacalkkdLQLLEDGDLT-VIGDRGTTLSGGQKARVNLARAVYQD 477
Cdd:COG0411 100 VLVAaharlgrgllaallrlpraRREEREARERA---------EELLERVGLAdRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 685504970 478 ADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KITILV 515
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAEL-IRRLRDErGITILL 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-516 |
5.86e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQqpwvFSG-----T 413
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQ----FDNldlefT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 LRSNIL-FGKKY--EKERYEKVIKAcalkkdlqLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:PRK13536 131 VRENLLvFGRYFgmSTREIEAVIPS--------LLEFARLESKADaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180
....*....|....*....|....*..
gi 685504970 490 VDAEvSRHLFELCICQILHEKITILVT 516
Cdd:PRK13536 203 LDPH-ARHLIWERLRSLLARGKTILLT 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
332-528 |
7.39e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.89 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 332 KKMVHVQDFTAFWDKASetpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPShglVSVHGRIAY------- 402
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPE---VTITGSIVYnghniys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 403 --------------VSQQPWVFSGTLRSNILFGKKYEKERYEKVIKAcALKKDLQ--LLEDGDLTVIGDRGTTLSGGQKA 466
Cdd:PRK14239 77 prtdtvdlrkeigmVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKgaSIWDEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 467 RVNLARAVYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQylkAASQI 528
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQ---QASRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
334-541 |
8.03e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.35 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 398
Cdd:COG1135 1 MIELENLSkTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalserelraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 --RIAYVSQQpwvF----SGTLRSNILF-----GKKyEKERYEKVikacalkkdLQLLEdgdLTVIGDRGTT----LSGG 463
Cdd:COG1135 81 rrKIGMIFQH---FnllsSRTVAENVALpleiaGVP-KAEIRKRV---------AELLE---LVGLSDKADAypsqLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 464 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRhlfelcicQIL------HEK--ITI-LVTHQLQYLKA-ASQILILKD 533
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTR--------SILdllkdiNRElgLTIvLITHEMDVVRRiCDRVAVLEN 216
|
....*...
gi 685504970 534 GKMVQKGT 541
Cdd:COG1135 217 GRIVEQGP 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
349-547 |
1.06e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.17 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQP--WVFS 411
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 412 GTLRSNILFGKK----YEKERYEKVIKACALKKDlqlledgDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDP 486
Cdd:PRK13637 99 ETIEKDIAFGPInlglSEEEIENRVKRAMNIVGL-------DYEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 487 LSAVDAEVSRHLFELciCQILHEK---ITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLK 547
Cdd:PRK13637 172 TAGLDPKGRDEILNK--IKELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
353-498 |
1.28e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------RIAYVSQQ----PwvfSGTLRSNI 418
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRnamkP---ALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 LFGKKYeKERYEKVIKACALKKDLQLLEDgdltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE----- 493
Cdd:PRK13539 95 EFWAAF-LGGEELDIAAALEAVGLAPLAH-------LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAavalf 166
|
....*...
gi 685504970 494 ---VSRHL 498
Cdd:PRK13539 167 aelIRAHL 174
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
353-491 |
1.28e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.99 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 417
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 418 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:COG1137 99 ILavleLRKLSKKEREERLE---------ELLEEFGITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
350-544 |
1.69e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAY--------------VSQQP--WVFSG 412
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYdkksllevrktvgiVFQNPddQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGK---KYEKERYEKVIKAcALKKdlqlledgdltvIGDRGTT------LSGGQKARVNLARAVYQDADIYLL 483
Cdd:PRK13639 95 TVEEDVAFGPlnlGLSKEEVEKRVKE-ALKA------------VGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 484 DDPLSAVD----AEVSRHLFELCicqilHEKITILV-THQLQYL-KAASQILILKDGKMVQKGTYTE 544
Cdd:PRK13639 162 DEPTSGLDpmgaSQIMKLLYDLN-----KEGITIIIsTHDVDLVpVYADKVYVMSDGKIIKEGTPKE 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
350-541 |
1.79e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.84 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIayVSQQP-------WVFSG-------TLR 415
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--ITHVPaenrhvnTVFQSyalfphmTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNILFGKKYEK----ERYEKVIKACALkkdLQLLEDGDltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:PRK09452 105 ENVAFGLRMQKtpaaEITPRVMEALRM---VQLEEFAQ-----RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 492 AEVSRHL-FELcicQILHEK--IT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 541
Cdd:PRK09452 177 YKLRKQMqNEL---KALQRKlgITfVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-540 |
2.04e-15 |
|
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: 75.78 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFT-AFWDKASetptLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------RIAYVS 404
Cdd:cd03269 1 LEVENVTkRFGRVTA----LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 405 QQPWVfsgtlrsnilfgkkYEKERYEKVI----------KACALKKDLQLLEDGDLTVIGD-RGTTLSGGQKARVNLARA 473
Cdd:cd03269 77 EERGL--------------YPKMKVIDQLvylaqlkglkKEEARRRIDEWLERLELSEYANkRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 474 VYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKIT-ILVTHQLQYLKA-ASQILILKDGKMVQKG 540
Cdd:cd03269 143 VIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTvILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
348-550 |
2.14e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 76.66 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG-T 413
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQENHINSRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 LRSNILFGK------KYEKERYEKVIKAcalkkdLQLLedgDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDP 486
Cdd:COG4604 92 VRELVAFGRfpyskgRLTAEDREIIDEA------IAYL---DLEDLADRYlDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 487 LSAVD----AEVSRHLFELCicqilHE--KITILVTHQLQYLKA-ASQILILKDGKMVQKGTYTEFLKSGI 550
Cdd:COG4604 163 LNNLDmkhsVQMMKLLRRLA-----DElgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPEV 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
328-520 |
2.31e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.61 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 328 PSDGKKMVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPS---HGLVSVHG---- 398
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLDGediy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 -----------RIAYVSQQPWVFSGTLRSNILFG--------KKYEKERYEKVIKACAL----KKDLQlledgdltvigD 455
Cdd:COG1117 82 dpdvdvvelrrRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSELDEIVEESLRKAALwdevKDRLK-----------K 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 456 RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQiLHEKITI-LVTHQLQ 520
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEEL-ILE-LKKDYTIvIVTHNMQ 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
353-545 |
2.51e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLL----SAVLGELAP-SH-----GLVSVHGRIA-----------YVSQQ-PWVF 410
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAgSHiellgRTVQREGRLArdirksrantgYIFQQfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 411 SGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDgdLTVIG------DRGTTLSGGQKARVNLARAVYQDADIYLLD 484
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504970 485 DPLSAVDAEVSRHLFELCICQILHEKITILVT-HQLQY-LKAASQILILKDGKMVQKGTYTEF 545
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
349-518 |
2.65e-15 |
|
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: 75.09 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------------IAYVSQQPWVfSGTLRS 416
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGL-KPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 nilfgkkYEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 495
Cdd:TIGR01189 91 -------LENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|...
gi 685504970 496 RHLFELCICQILHEKITILVTHQ 518
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHQ 186
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
335-519 |
3.31e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTAFWDKASETptLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------IAYVS 404
Cdd:PRK15056 7 IVVNDVTVTWRNGHTA--LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 405 QQP---WVFSGTLRSNILFGK-------KYEKERYEKVIKACALKKDLQLLEDGDltvIGDrgttLSGGQKARVNLARAV 474
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 685504970 475 YQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILV-THQL 519
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISL-LRELRDEGKTMLVsTHNL 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
356-563 |
4.37e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVS--QQP--WVFSG-------TLRSNILFGKK 423
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPpyQRPinMMFQSyalfphmTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 424 yeKERYEKVIKACALKKDLQLLEDGDLTviGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVsRHLFELCI 503
Cdd:PRK11607 118 --QDKLPKAEIASRVNEMLGLVHMQEFA--KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL-RDRMQLEV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 504 CQILhEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGT------------YTEFLKSGIDFGSLLKKDNEES 563
Cdd:PRK11607 193 VDIL-ERVgvtCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEpeeiyehpttrySAEFIGSVNVFEGVLKERQEDG 267
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
356-548 |
4.64e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 76.03 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPwvfSGTL--RSNI-- 418
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrckHIRMIFQDP---NTSLnpRLNIgq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 -------LFGKKYEKERYEKVIKAcaLKKdLQLLEDGDLTVIgdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:COG4167 109 ileeplrLNTDLTAEEREERIFAT--LRL-VGLLPEHANFYP----HMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 492 AEVSRHLFELCIcqILHEKIT---ILVTHQLQYLKAAS-QILILKDGKMVQKGTYTEFLKS 548
Cdd:COG4167 182 MSVRSQIINLML--ELQEKLGisyIYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
353-546 |
4.98e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.42 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG-TLRS 416
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltdskkdinklrrKVGMVFQQFNLFPHlTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 NILFGKKYEKeryeKVIKACALKKDLQLLEdgdlTV-IGDRG----TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:COG1126 97 NVTLAPIKVK----KMSKAEAEERAMELLE----RVgLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 492 ----AEVsrhlfeL-CICQILHEKIT-ILVTHQLQY-LKAASQILILKDGKMVQKGTYTEFL 546
Cdd:COG1126 169 pelvGEV------LdVMRDLAKEGMTmVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
334-538 |
7.12e-15 |
|
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: 74.78 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 334 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 398
Cdd:COG4181 8 IIELRGLTkTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 RIAYVSqqpWVF-------SGTLRSNI-----LFGKKYEKERYEKVIKACALkkdlqlledgdltviGDRGT----TLSG 462
Cdd:COG4181 88 RARHVG---FVFqsfqllpTLTALENVmlpleLAGRRDARARARALLERVGL---------------GHRLDhypaQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 463 GQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH----LFELCicqilHEKIT--ILVTHQLQYLKAASQILILKDGKM 536
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidlLFELN-----RERGTtlVLVTHDPALAARCDRVLRLRAGRL 224
|
..
gi 685504970 537 VQ 538
Cdd:COG4181 225 VE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
333-559 |
7.20e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.51 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 333 KMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------R 399
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrrK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 400 IAYVSQQP--WVFSGTLRSNILFGKKYEKERYEKVIKacalKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQD 477
Cdd:PRK13642 83 IGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 478 ADIYLLDDPLSAVDAEVSRHlfelcICQILHE-----KITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKS--- 548
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQE-----IMRVIHEikekyQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATsed 233
|
250
....*....|....*..
gi 685504970 549 ----GID--FGSLLKKD 559
Cdd:PRK13642 234 mveiGLDvpFSSNLMKD 250
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
349-550 |
9.13e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.00 E-value: 9.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQqpwvFSG---- 412
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQ----FDNldpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 -TLRSNIL-FGkkyekeRYEKVIKACALKKDLQLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:PRK13537 95 fTVRENLLvFG------RYFGLSAAAARALVPPLLEFAKLENKADaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 490 VDAEvSRHLFELCICQILHEKITILVThqLQYLKAASQ----ILILKDGKMVQKGTYTEFLKSGI 550
Cdd:PRK13537 169 LDPQ-ARHLMWERLRSLLARGKTILLT--THFMEEAERlcdrLCVIEEGRKIAEGAPHALIESEI 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
327-545 |
9.35e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 9.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 327 LPSDGKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------- 399
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 400 -------IAYVSQQPWVFSG-TLRSNILFGKKYEKERYEKVIK-----ACALKKDLQ--LLEdgdltvIGDRGTtlsggq 464
Cdd:PRK15439 81 akahqlgIYLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQllaalGCQLDLDSSagSLE------VADRQI------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 465 karVNLARAVYQDADIYLLDDPLSAVD-AEVSRhLFELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGKMVQKGT 541
Cdd:PRK15439 149 ---VEILRGLMRDSRILILDEPTASLTpAETER-LFSR-IRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGK 223
|
....
gi 685504970 542 YTEF 545
Cdd:PRK15439 224 TADL 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
113-553 |
1.14e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 78.45 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 113 KTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPL-QAIAVTALLWMEIGISclagmAVLIILLPLQSCFGKLFSSLRSKTA 191
Cdd:TIGR00957 1058 RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLfNVIGALIVILLATPIA-----AVIIPPLGLLYFFVQRFYVASSRQL 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 192 TFTDARIRT-----MNEVITGIRIIKMYAWEKSFSnLITNLRKKEISKILRSSCL--RGMNLASFFSASKIIVFVTFTTy 264
Cdd:TIGR00957 1133 KRLESVSRSpvyshFNETLLGVSVIRAFEEQERFI-HQSDLKVDENQKAYYPSIVanRWLAVRLECVGNCIVLFAALFA- 1210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 265 VLLGSVITASRVFVAVTLygavRLTVTLFFPSAIERVSEA---IVSIRRIQTFLLLD-------EISQRNRQLPSDGKkm 334
Cdd:TIGR00957 1211 VISRHSLSAGLVGLSVSY----SLQVTFYLNWLVRMSSEMetnIVAVERLKEYSETEkeapwqiQETAPPSGWPPRGR-- 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTAFWDKASETpTLQGLSFTVRPGELLAVVGPVGAGKSSL-------LSAVLGEL------APSHGLVSVHGRIA 401
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLtlglfriNESAEGEIiidglnIAKIGLHDLRFKIT 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 402 YVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIY 481
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKIL 1443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 482 LLDDPLSAVDAEVS-------RHLFELCicqilhekiTIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKS-GIDF 552
Cdd:TIGR00957 1444 VLDEATAAVDLETDnliqstiRTQFEDC---------TVLtIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQrGIFY 1514
|
.
gi 685504970 553 G 553
Cdd:TIGR00957 1515 S 1515
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
403-546 |
1.48e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 403 VSQQPWVFSGTLRSNILFGKkyEKERYEKVIKAC---ALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDAD 479
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 480 IYLLDDPLSAVDAEvSRHLFELCICQILH--EKITILVTHQLQYLKAASQILIL----KDGKMVQ-KGTYTEFL 546
Cdd:PTZ00265 1379 ILLLDEATSSLDSN-SEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELL 1451
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
349-540 |
2.96e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 73.14 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIayvsqqPWVFSGTLRSNI--LFGKK--- 423
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV------PWKRRKKFLRRIgvVFGQKtql 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 424 ----------------Y--EKERYEKVIKACAlkkdlQLLEDGDLTVIGDRgtTLSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:cd03267 107 wwdlpvidsfyllaaiYdlPPARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 486 PLSAVDAEVSRHLFE-LCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 540
Cdd:cd03267 180 PTIGLDVVAQENIRNfLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
353-540 |
3.31e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.25 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV--------------HGRIAYVSQQ-PWVFSG----- 412
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQLRQHvGFVFQNfnlfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 --TLRSNILFGKKYEKeryeKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:PRK11264 99 hrTVLENIIEGPVIVK----GEPKEEATARARELLAKVGLAGKETSyPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 685504970 490 VDAEVSRHLFElCICQILHEKIT-ILVTHQLQYLK-AASQILILKDGKMVQKG 540
Cdd:PRK11264 175 LDPELVGEVLN-TIRQLAQEKRTmVIVTHEMSFARdVADRAIFMDQGRIVEQG 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
353-518 |
3.54e-14 |
|
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: 72.14 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------------IAYVSQQPWVfSGTL--RSNI 418
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGI-KTTLsvLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 LFGKKYekeryekvikaCALKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 497
Cdd:cd03231 95 RFWHAD-----------HSDEQVEEALARVGLNGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|.
gi 685504970 498 LFELCICQILHEKITILVTHQ 518
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
337-558 |
4.16e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.97 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 337 VQDFTAFWDK--ASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-------------------- 394
Cdd:PRK13651 5 VKNIVKIFNKklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 395 -----------------SVHGRIAYVSQ--QPWVFSGTLRSNILFG-------KKYEKERYEKVIKACALkkDLQLLEDG 448
Cdd:PRK13651 85 eklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 449 DLTvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFElcICQILHE--KITILVTHQLQY-LKAA 525
Cdd:PRK13651 163 PFE--------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKqgKTIILVTHDLDNvLEWT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 685504970 526 SQILILKDGKMVQKG-TY-----TEFLKSG-------IDFGSLLKK 558
Cdd:PRK13651 233 KRTIFFKDGKIIKDGdTYdilsdNKFLIENnmeppklLNFVNKLEK 278
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
113-290 |
4.21e-14 |
|
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: 73.45 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 113 KTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGIS-CLAGMAVLIILLPLQSCFGKLFSSLRSKTA 191
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 192 TFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVT--FTTYVLLGS 269
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALAlwFGAYLVISG 253
|
170 180
....*....|....*....|.
gi 685504970 270 VITASRVFVAVTLYGAVRLTV 290
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
353-562 |
1.01e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPS---HGLVSVHG---------------RIAYVSQQPWVFSG 412
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGknlyapdvdpvevrrRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGKK---YE---KERYEKVIKACAL----KKDLQlledgdltvigDRGTTLSGGQKARVNLARAVYQDADIYL 482
Cdd:PRK14243 106 SIYDNIAYGARingYKgdmDELVERSLRQAALwdevKDKLK-----------QSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 483 LDDPLSAVDAEVSRHLFELciCQILHEKITI-LVTHQLQYLKAASQILILKDGKMVQKGTYT----EFLKSGIDFGSLLK 557
Cdd:PRK14243 175 MDEPCSALDPISTLRIEEL--MHELKEQYTIiIVTHNMQQAARVSDMTAFFNVELTEGGGRYgylvEFDRTEKIFNSPQQ 252
|
....*
gi 685504970 558 KDNEE 562
Cdd:PRK14243 253 QATRD 257
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
354-518 |
1.09e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 354 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIayVSQQPWVFsgtlRSNILF-----GKKYEKER 428
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDEY----HQDLLYlghqpGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 429 YEKVIKACALKkdlQLLEDGD----LTVIGDRGT------TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEV 494
Cdd:PRK13538 92 LENLRFYQRLH---GPGDDEAlweaLAQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvARL 168
|
170 180
....*....|....*....|....*.
gi 685504970 495 SRHLFELCicqilhEK--ITILVTHQ 518
Cdd:PRK13538 169 EALLAQHA------EQggMVILTTHQ 188
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
356-541 |
1.16e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.22 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNILFGKK 423
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHmSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 424 YEK----ERYEKVIKACALKkdlqlledgDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 498
Cdd:PRK11432 105 MLGvpkeERKQRVKEALELV---------DLAGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 685504970 499 FElcicQI--LHEK--ITIL-VTH-QLQYLKAASQILILKDGKMVQKGT 541
Cdd:PRK11432 176 RE----KIreLQQQfnITSLyVTHdQSEAFAVSDTVIVMNKGKIMQIGS 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
351-546 |
1.41e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSN 417
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 I-LFGKKYEKERYEK--------VIKACALKKDLQLLEDGDltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLS 488
Cdd:PLN03130 1333 LdPFNEHNDADLWESlerahlkdVIRRNSLGLDAEVSEAGE---------NFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 489 AVDAEVS-------RHLFELCicqilhekiTILV-THQLQYLKAASQILILKDGKMVQKGTYTEFL 546
Cdd:PLN03130 1404 AVDVRTDaliqktiREEFKSC---------TMLIiAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
332-555 |
1.48e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.69 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 332 KKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------- 398
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 RIAYVSQQP-WVFSG-TLRSNILFGKKYE----KERYEKVIKAcalkkdLQLLedgDLTVIGDRGTT-LSGGQKARVNLA 471
Cdd:PRK13650 82 KIGMVFQNPdNQFVGaTVEDDVAFGLENKgiphEEMKERVNEA------LELV---GMQDFKEREPArLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 472 RAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKT-IKGIRDDyQMTVIsITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
....*.
gi 685504970 550 IDFGSL 555
Cdd:PRK13650 232 NDLLQL 237
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
308-548 |
1.49e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.16 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 308 IRRIQtfllLDEISQRNRQLPS----DGKKM----VHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSL 379
Cdd:PRK15064 289 IDKIK----LEEVKPSSRQNPFirfeQDKKLhrnaLEVENLTKGFD---NGPLFKNLNLLLEAGERLAIIGENGVGKTTL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 380 LSAVLGELAPSHGLV--SVHGRIAYVSQQPwvfsgtlrsnilfgkkyekeryekvikACALKKDLQLLE---------DG 448
Cdd:PRK15064 362 LRTLVGELEPDSGTVkwSENANIGYYAQDH---------------------------AYDFENDLTLFDwmsqwrqegDD 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 449 DLTVigdRGT----------------TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLfelcicQILHEKIT 512
Cdd:PRK15064 415 EQAV---RGTlgrllfsqddikksvkVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL------NMALEKYE 485
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 685504970 513 ---ILVTHQLQYLKA-ASQILILKDGKMVQ-KGTYTEFLKS 548
Cdd:PRK15064 486 gtlIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYLRS 526
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
351-559 |
1.79e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 71.09 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSN 417
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeVSRH 497
Cdd:cd03288 115 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM-ATEN 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 498 LFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL--KSGIdFGSLLKKD 559
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaqEDGV-FASLVRTD 256
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
328-541 |
2.09e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.81 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 328 PSDGKKMVHVQDFTAFWDKASETP--TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------- 398
Cdd:PRK13631 15 PLSDDIILRVKNLYCVFDEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 ----------------------RIAYVSQQP--WVFSGTLRSNILFG------KKYE-KERYEKVIKACALKKDLqlLED 447
Cdd:PRK13631 95 nnhelitnpyskkiknfkelrrRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLDDSY--LER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 448 GDLTvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQL-QYLKAAS 526
Cdd:PRK13631 173 SPFG--------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVAD 244
|
250
....*....|....*
gi 685504970 527 QILILKDGKMVQKGT 541
Cdd:PRK13631 245 EVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
349-538 |
2.14e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP--WV 409
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFPeaQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 FSGTLRSNILFGKK----YEKERYEKVIKacALKKdLQLLEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:PRK13641 99 FENTVLKDVEFGPKnfgfSEDEAKEKALK--WLKK-VGLSED----LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 685504970 486 PLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYL-KAASQILILKDGKMVQ 538
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
350-536 |
2.91e-13 |
|
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: 69.74 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------RIAYVSQQPWVfsgTLRSNILF 420
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKIGV---VFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 421 gkkYEKERYEKVikACAL-----------KKDLQLLEDGDLT-VIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLS 488
Cdd:cd03292 91 ---PDRNVYENV--AFALevtgvppreirKRVPAALELVGLShKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 685504970 489 AVDAEVSRHLFELcICQILHEKITILV-THQLQYLKAAS-QILILKDGKM 536
Cdd:cd03292 166 NLDPDTTWEIMNL-LKKINKAGTTVVVaTHAKELVDTTRhRVIALERGKL 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
351-493 |
3.78e-13 |
|
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: 69.39 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVH---------------------GRIAYVSQ---- 405
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 406 -----------QPWVFSGTlrsnilfgkkyekERYEKVIKACALKKDLQLLEdgdltvigdR-----GTTLSGGQKARVN 469
Cdd:COG4778 105 iprvsaldvvaEPLLERGV-------------DREEARARARELLARLNLPE---------RlwdlpPATFSGGEQQRVN 162
|
170 180
....*....|....*....|....
gi 685504970 470 LARAVYQDADIYLLDDPLSAVDAE 493
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAA 186
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
349-549 |
4.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP--WV 409
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 FSGTLRSNILFGKKYEKERYEKViKACALKKDLQLLEDGDltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:PRK13646 99 FEDTVEREIIFGPKNFKMNLDEV-KNYAHRLLMDLGFSRD--VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 490 VDAEVSRHLFELCI-CQILHEKITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:PRK13646 176 LDPQSKRQVMRLLKsLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
350-543 |
5.74e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRiaYVSQQPWVFSGTLRSN------------ 417
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQklgfiyqfhhll 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ------------ILFGKKYEKERYEK---VIKACALKKDLQlledgdltvigDRGTTLSGGQKARVNLARAVYQDADIYL 482
Cdd:PRK11629 100 pdftalenvampLLIGKKKPAEINSRaleMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 483 LDDPLSAVDAEVSRHLFELC-ICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYT 543
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLM 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
332-548 |
7.49e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 69.63 E-value: 7.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 332 KKMVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------- 398
Cdd:PRK13632 5 SVMIKVENVS-FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 399 RIAYVSQQP-WVFSG-TLRSNILFG---KKYEKERYEKVIKACALKKDLQLLEDGDltvigdrGTTLSGGQKARVNLARA 473
Cdd:PRK13632 84 KIGIIFQNPdNQFIGaTVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDYLDKE-------PQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 474 VYQDADIYLLDDPLSAVDAEVSRHlfelcICQILHE------KITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 547
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKRE-----IKKIMVDlrktrkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
.
gi 685504970 548 S 548
Cdd:PRK13632 232 N 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
367-544 |
7.53e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.67 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 367 AVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------------IAYVSQQPWVFSG-TLRSNILFG-KKYEKE 427
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLFPHyKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 428 RYEKVIKACALKKdlqLLedgdltvigDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLfeLCICQI 506
Cdd:PRK11144 108 QFDKIVALLGIEP---LL---------DRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL--LPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 685504970 507 LHE--KITIL-VTHQLQ-YLKAASQILILKDGKMVQKGTYTE 544
Cdd:PRK11144 174 LAReiNIPILyVSHSLDeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
349-546 |
8.05e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.97 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPSHGLV---SVHGRIA----------YVSQQPWVFSG- 412
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDLIVdglKVNDPKVderlirqeagMVFQQFYLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGKKyekeRYEKVIKACALKKDLQLLEDGDLtviGDRG----TTLSGGQKARVNLARAVYQDADIYLLDDPLS 488
Cdd:PRK09493 93 TALENVMFGPL----RVRGASKEEAEKQARELLAKVGL---AERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 489 AVDAEVsRHlfE-LCICQILHEK--ITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFL 546
Cdd:PRK09493 166 ALDPEL-RH--EvLKVMQDLAEEgmTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
353-524 |
8.64e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQ-------PWVFS-------GTLRS 416
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQKlyldttlPLTVNrflrlrpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 NILfgkkyekERYEKVIKACALKKDLQlledgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:PRK09544 100 DIL-------PALKRVQAGHLIDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|
gi 685504970 497 HLFELcICQILHEK--ITILVTHQLQYLKA 524
Cdd:PRK09544 158 ALYDL-IDQLRRELdcAVLMVSHDLHLVMA 186
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
354-546 |
9.80e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 9.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 354 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQ----------QPWVF 410
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLAQnattpgditvQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 411 SGTLRSNILFgKKYEKERYEKVIKAcalkkdlqLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 490
Cdd:PRK10253 104 RGRYPHQPLF-TRWRKEDEEAVTKA--------MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 491 DAEVSRHLFELcICQILHEKITIL--VTHQL-QYLKAASQILILKDGKMVQKGTYTEFL 546
Cdd:PRK10253 175 DISHQIDLLEL-LSELNREKGYTLaaVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-537 |
9.84e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.96 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV----------SVHGRIAYVSQqpwVF-------- 410
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklPEYKRAKYIGR---VFqdpmmgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 411 -SGTLRSNILF----GKKY---------EKERY-EKVikacalkKDLQL-LEDGDLTVIGdrgtTLSGGQKARVNLARAV 474
Cdd:COG1101 95 pSMTIEENLALayrrGKRRglrrgltkkRRELFrELL-------ATLGLgLENRLDTKVG----LLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 475 YQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEK--ITILVTHQLQY-LKAASQILILKDGKMV 537
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLEL-TEKIVEENnlTTLMVTHNMEQaLDYGNRLIMMHEGRII 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
349-540 |
1.00e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.84 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------------------------RIAY 402
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 403 VSQQ--PWVFSgTLRSNIL--------FGKKYEKERYEKVIKACALKKDLQlledgdltviGDRGTTLSGGQKARVNLAR 472
Cdd:PRK10619 97 VFQHfnLWSHM-TVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 473 AVYQDADIYLLDDPLSAVDAEVSRHLfeLCICQILHE--KITILVTHQLQYLK-AASQILILKDGKMVQKG 540
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEV--LRIMQQLAEegKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEG 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
353-575 |
1.08e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 417
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFG----------KKYEKERYEKVIKACALKKDLQlledgdlTVIGDrgttLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:COG1129 100 IFLGreprrgglidWRAMRRRARELLARLGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 488 SAVDAEVSRHLFELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGKMVqkgtyTEFLKSGIDFGSLLKK------D 559
Cdd:COG1129 169 ASLTEREVERLFRI-IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLV-----GTGPVAELTEDELVRLmvgrelE 242
|
250
....*....|....*.
gi 685504970 560 NEESEQPPVPGTPTLR 575
Cdd:COG1129 243 DLFPKRAAAPGEVVLE 258
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
340-547 |
1.47e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 340 FTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPS---HGLVSVHG----------RIAYVsQQ 406
Cdd:TIGR00955 28 RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemraISAYV-QQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 407 PWVFSGTL--RSNILF----------GKKYEKERYEKVIKACALKKDLQlledgdlTVIGDRGTT--LSGGQKARVNLAR 472
Cdd:TIGR00955 107 DDLFIPTLtvREHLMFqahlrmprrvTKKEKRERVDEVLQALGLRKCAN-------TRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 473 AVYQDADIYLLDDPLSAVDA----EVSRHLFELCicqiLHEKITILVTHQLQY--LKAASQILILKDGKMVQKGTYTEFL 546
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSfmaySVVQVLKGLA----QKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
.
gi 685504970 547 K 547
Cdd:TIGR00955 256 P 256
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
350-541 |
2.04e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.48 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWV-FSG-T 413
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklVGIVFQNPETqFVGrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 LRSNILFGKKyekeryekviKACALKKDLQLLEDGDLTVIG------DRGTTLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:PRK13644 95 VEEDLAFGPE----------NLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 488 SAVDAEVSRHLFELCicQILHEK--ITILVTHQLQYLKAASQILILKDGKMVQKGT 541
Cdd:PRK13644 165 SMLDPDSGIAVLERI--KKLHEKgkTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
352-549 |
2.18e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 68.24 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 352 TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------LVSVHGRIAYVSQQP---WVFSgTLR 415
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaitddnFEKLRKHIGIVFQNPdnqFVGS-IVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNILFGKKYEKERYEKVIKACAlkkdlQLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 494
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVS-----EALKQVDMLERADyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 495 SRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 549
Cdd:PRK13648 178 RQNLLDL-VRKVKSEHnITIIsITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-547 |
2.99e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.90 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 342 AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP---SHGLVSVHG-------------RIAYVSQ 405
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGitltaktvwdireKVGIVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 406 QP-WVFSG-TLRSNILFGKKYEKERYEKVIKACAlkkdlQLLED-GDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYL 482
Cdd:PRK13640 92 NPdNQFVGaTVGDDVAFGLENRAVPRPEMIKIVR-----DVLADvGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 483 LDDPLSAVDAEVSRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 547
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKL-IRKLKKKNnLTVIsITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
350-544 |
3.91e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.33 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQ----PWVfsgTL 414
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyalyPHM---SV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 RSNILFG---KKYEKERYEKVIKACAlkkdlQLLEDGDLTvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 490
Cdd:PRK11650 94 RENMAYGlkiRGMPKAEIEERVAEAA-----RILELEPLL---DRKpRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 491 DAEVSRHL-FELcicQILHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 544
Cdd:PRK11650 166 DAKLRVQMrLEI---QRLHRRLkttSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
353-550 |
4.06e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------------------IAYVSQQPwvf 410
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyalseaerrrllrteWGFVHQHP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 411 SGTLRSNILFGKKY-EK-----ERYEKVIKACALKKdLQLLEDgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLD 484
Cdd:PRK11701 99 RDGLRMQVSAGGNIgERlmavgARHYGDIRATAGDW-LERVEI-DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 485 DPLSAVDAEVSRHLFELcICQILHEK--ITILVTHQLQYLK-AASQILILKDGKMVQKG-----------TYTEFLKSGI 550
Cdd:PRK11701 177 EPTGGLDVSVQARLLDL-LRGLVRELglAVVIVTHDLAVARlLAHRLLVMKQGRVVESGltdqvlddpqhPYTQLLVSSV 255
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
352-535 |
5.01e-12 |
|
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: 66.66 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 352 TLQGLSFTVRPG-----ELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-RIAYVSQQPWV-FSGTLRSnILFGK-- 422
Cdd:cd03237 9 TLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKAdYEGTVRD-LLSSItk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 423 -KYEKERYEKVIKacalkKDLQLlEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------V 494
Cdd:cd03237 88 dFYTHPYFKTEIA-----KPLQI-EQ----ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmaskV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 685504970 495 SRHLfelcicqILHEKITILVT-HQLQYLKAASQILILKDGK 535
Cdd:cd03237 158 IRRF-------AENNEKTAFVVeHDIIMIDYLADRLIVFEGE 192
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
348-547 |
5.64e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVSVHGRI-------------AYVSQQpwvfsgtl 414
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelarhrAYLSQQ-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 rSNILF------------GKKYEKERYEKVIKACAlkkdlQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQ------ 476
Cdd:PRK03695 78 -QTPPFampvfqyltlhqPDKTRTEAVASALNEVA-----EALGLDDK--LGRSVNQLSGGEWQRVRLAAVVLQvwpdin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 477 -DADIYLLDDPLSAVD----AEVSRHLFELCicqilHEKITILVT-HQLQY-LKAASQILILKDGKMVQKGTYTEFLK 547
Cdd:PRK03695 150 pAGQLLLLDEPMNSLDvaqqAALDRLLSELC-----QQGIAVVMSsHDLNHtLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
353-544 |
6.05e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.90 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------------IAYVSQQpwvF----SG 412
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrkarrqIGMIFQH---FnllsSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGKKYEKERYEKvIKacalKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:PRK11153 98 TVFDNVALPLELAGTPKAE-IK----ARVTELLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 492 AEVSRHLFELcICQILHE-KITI-LVTHQLQYLKA-ASQILILKDGKMVQKGTYTE 544
Cdd:PRK11153 173 PATTRSILEL-LKDINRElGLTIvLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSE 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
328-502 |
6.55e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 328 PSDGKKMVHVQDFTAfwdkaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------- 399
Cdd:COG1129 250 AAPGEVVLEVEGLSV-------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirspr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 400 ------IAYVS----QQPWVFSGTLRSNI------------LFGKKYEKERYEKVIKACALKkdlqlLEDGDLTVigdrg 457
Cdd:COG1129 323 dairagIAYVPedrkGEGLVLDLSIRENItlasldrlsrggLLDRRRERALAEEYIKRLRIK-----TPSPEQPV----- 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 685504970 458 TTLSGG--QKarVNLARAVYQDADIYLLDDPLSAVD----AEVSRHLFELC 502
Cdd:COG1129 393 GNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGIDvgakAEIYRLIRELA 441
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-541 |
6.76e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.06 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRiayvsqqPwvFSGTLRSNIlfGkkY--EkER-- 428
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-------P--LDPEDRRRI--G--YlpE-ERgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 429 Y--EKVI-------------KACALKKDLQLLEDGDltvIGDRGT----TLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:COG4152 83 YpkMKVGeqlvylarlkglsKAEAKRRADEWLERLG---LGDRANkkveELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 490 VDAeVSRHLFElcicQILHE-----KITILVTHQLQYLKA-ASQILILKDGKMVQKGT 541
Cdd:COG4152 160 LDP-VNVELLK----DVIRElaakgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
345-548 |
8.60e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 67.75 E-value: 8.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 345 DKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP 407
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 408 WVFSG-TLRSNILFGKKYE----KERYEKVIKAcalkkdlqLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYL 482
Cdd:PRK10070 116 ALMPHmTVLDNTAFGMELAginaEERREKALDA--------LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 483 LDDPLSAVDAEVSRHLF-ELCICQILHEKITILVTHQL-QYLKAASQILILKDGKMVQKGTYTEFLKS 548
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
353-541 |
1.36e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.62 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL---APSHGlVSVHGRI-------------------AYVSQ--QPw 408
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRG-ARVTGDVtlngeplaaidaprlarlrAVLPQaaQP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 409 VFSGTLRSNILFGkkyekeRYEKVIKACALKKdlqllEDGDL-----------TVIGDRGTTLSGGQKARVNLARAVYQ- 476
Cdd:PRK13547 95 AFAFSAREIVLLG------RYPHARRAGALTH-----RDGEIawqalalagatALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 477 --------DADIYLLDDPLSAVDAEVSRHLFE----------LCICQILHEkITILVTHqlqylkaASQILILKDGKMVQ 538
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDtvrrlardwnLGVLAIVHD-PNLAARH-------ADRIAMLADGAIVA 235
|
...
gi 685504970 539 KGT 541
Cdd:PRK13547 236 HGA 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
356-546 |
1.84e-11 |
|
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: 67.27 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTvrPGELLAVVGPVGAGKSSLL-------SAVLGELAPSHGLvsvhgRIAYVSQQPWV-FSGTLRSNILFG------ 421
Cdd:TIGR03719 26 LSFF--PGAKIGVLGLNGAGKSTLLrimagvdKDFNGEARPQPGI-----KVGYLPQEPQLdPTKTVRENVEEGvaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 422 --KKY-------------------EKERYEKVIKAC-ALKKDLQL--------LEDGDLTVigdrgTTLSGGQKARVNLA 471
Cdd:TIGR03719 99 alDRFneisakyaepdadfdklaaEQAELQEIIDAAdAWDLDSQLeiamdalrCPPWDADV-----TKLSGGERRRVALC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 472 RAVYQDADIYLLDDPLSAVDAE----VSRHLFElcicqilHEKITILVTHQLQYL-KAASQILILKDGKMVQ-KGTYTEF 545
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAEsvawLERHLQE-------YPGTVVAVTHDRYFLdNVAGWILELDRGRGIPwEGNYSSW 246
|
.
gi 685504970 546 L 546
Cdd:TIGR03719 247 L 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-551 |
2.86e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 335 VHVQDFTAFWDKASetpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAvLGELAPSHGLVSVHGRIAYVSQ--------- 405
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQniyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 406 ------------QPWVFSGTLRSNILFGKK----YEKERYEKVIKACALKKDLQlleDGDLTVIGDRGTTLSGGQKARVN 469
Cdd:PRK14258 84 nrlrrqvsmvhpKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDADLW---DEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 470 LARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITI-LVTHQLQYLKAASQILIL------KDGKMVQKGTY 542
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMvIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEFGLT 240
|
....*....
gi 685504970 543 TEFLKSGID 551
Cdd:PRK14258 241 KKIFNSPHD 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-541 |
4.04e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 66.25 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVSVHGR-IAYVSQ---QPW------VFS---GTL--RSN 417
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdLDGLSRralRPLrrrmqvVFQdpfGSLspRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 I----------LFGKKYEKERYEKVIkacalkkdlQLLEDGDLtvigDRGTT------LSGGQKARVNLARAVYQDADIY 481
Cdd:COG4172 381 VgqiiaeglrvHGPGLSAAERRARVA---------EALEEVGL----DPAARhrypheFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 482 LLDDPLSAVDAEVSRhlfelcicQIL--------HEKIT-ILVTHQLQYLKA-ASQILILKDGKMVQKGT 541
Cdd:COG4172 448 VLDEPTSALDVSVQA--------QILdllrdlqrEHGLAyLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
348-493 |
5.75e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.94 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------IAYVSQQPwvfsgtlrsn 417
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLP---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ilfGKKYEKERYEKVIKACALK-KDLQLLEDGDLTVIGDRG------TTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 490
Cdd:PRK13543 92 ---GLKADLSTLENLHFLCGLHgRRAKQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
...
gi 685504970 491 DAE 493
Cdd:PRK13543 169 DLE 171
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
347-541 |
5.88e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 347 ASETP----TLQGLSFTVRPGELLAVVGPVGAGKSSLLS------------AVLGELAPSHGLVSV------HGRIAYVS 404
Cdd:PRK13645 17 AKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIkevkrlRKEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 405 QQP--WVFSGTLRSNILFGKKYEKERYEKVIKACA-LKKDLQLLEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIY 481
Cdd:PRK13645 97 QFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPeLLKLVQLPED----YVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 482 LLDDPLSAVDAEVSRHLFELCI-CQILHEKITILVTHQL-QYLKAASQILILKDGKMVQKGT 541
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFErLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
353-537 |
7.34e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSaVLGEL-APSHGLVSVHGR-----------------IAYVSQQPWVFSG-T 413
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQdvatldadalaqlrrehFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 LRSNILFGKKYE-KERYEKVIKACALKKDLQLLEDgdltvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:PRK10535 103 AAQNVEVPAVYAgLERKQRLLRAQELLQRLGLEDR-----VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 685504970 493 EVSRHLfeLCICQILHEK--ITILVTHQLQYLKAASQILILKDGKMV 537
Cdd:PRK10535 178 HSGEEV--MAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
353-546 |
8.18e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG----------LVSVHGR----IAYVSQQPWVFSgtlRSNI 418
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedisLLPLHARarrgIGYLPQEASIFR---RLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 lfgkkyekerYEKVIKACALKKDL----------QLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:PRK10895 96 ----------YDNLMAVLQIRDDLsaeqredranELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 488 SAVDAeVSRHLFELCICQILHEKITILVT-HQL-QYLKAASQILILKDGKMVQKGTYTEFL 546
Cdd:PRK10895 166 AGVDP-ISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
353-548 |
8.34e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV-------FSG 412
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqRIRMIFQDPSTslnprqrISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFGKKYEKERYEKVIKAcALKKdLQLLEDGdltvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIE-TLRQ-VGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 493 EVSRHLFELCI-CQILHEKITILVTHQLQYLKAAS-QILILKDGKMVQKGTYTEFLKS 548
Cdd:PRK15112 183 SMRSQLINLMLeLQEKQGISYIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVLAS 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
353-537 |
8.49e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 417
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 IL------FGKKYEKERYEKVIKACALKKDLQLledgDL-TVIGDrgttLSGGQKARVNLARAVYQDADIYLLDDPlSAV 490
Cdd:COG3845 101 IVlgleptKGGRLDRKAARARIRELSERYGLDV----DPdAKVED----LSVGEQQRVEILKALYRGARILILDEP-TAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 491 --DAEVsRHLFElcicqILHE-----KITILVTHQLQYLKAAS-QILILKDGKMV 537
Cdd:COG3845 172 ltPQEA-DELFE-----ILRRlaaegKSIIFITHKLREVMAIAdRVTVLRRGKVV 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-540 |
8.67e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 8.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAV-----LGELAPSHGLVSVHGRIAY---------------VSQQPWVFSG 412
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpievrrevgmVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 -TLRSNILFGKKYEK---------ERYEKVIKACALKKDLQlledgdlTVIGDRGTTLSGGQKARVNLARAVYQDADIYL 482
Cdd:PRK14267 100 lTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 483 LDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQ-LQYLKAASQILILKDGKMVQKG 540
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEEL-LFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
353-538 |
9.16e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQ-PWVFSGTLRSN 417
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAIIYQElHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGKKYEKeryEKVIKACALKKD--LQLLEDG-DLtvigDRGT---TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:PRK11288 100 LYLGQLPHK---GGIVNRRLLNYEarEQLEHLGvDI----DPDTplkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 685504970 492 AEVSRHLFELcICQILHE-KITILVTHQLQYLKAAS-QILILKDGKMVQ 538
Cdd:PRK11288 173 AREIEQLFRV-IRELRAEgRVILYVSHRMEEIFALCdAITVFKDGRYVA 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
353-537 |
9.45e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.58 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVSQQPWVFsgtLRSNI--LFGKKY---EK 426
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITRLKNREVPF---LRRQIgmIFQDHHllmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 427 ERYEKV----IKACALKKDLQLLEDGDLTVIG--DRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:PRK10908 95 TVYDNVaiplIIAGASGDDIRRRVSAALDKVGllDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 685504970 497 ---HLFElcicQILHEKITILV-THQLQYLKAAS-QILILKDGKMV 537
Cdd:PRK10908 175 gilRLFE----EFNRVGVTVLMaTHDIGLISRRSyRMLTLSDGHLH 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-548 |
1.17e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.76 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 331 GKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAY-------- 402
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 403 -----------VSQQPWVFSG-TLRSNILFGKKY----EKERYEKVIKACalkkdlqLLEDGDLTVIGDR----GTTLSG 462
Cdd:PRK14246 84 daiklrkevgmVFQQPNPFPHlSIYDNIAYPLKShgikEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 463 GQKARVNLARAVYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQYL-KAASQILILKDGKMVQKGT 541
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGS 235
|
....*..
gi 685504970 542 YTEFLKS 548
Cdd:PRK14246 236 SNEIFTS 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
353-580 |
1.24e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.82 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG--ELAPSHGLVSVH----------GRIAYVSQQPWVFSGTL------ 414
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyvERPSKVGEPCPVCGGTLepeevd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 --------------RSNILFGKK---YEKER-YEKVIKAC---------ALKKDLQLLEdgdLTVIGDRGT----TLSGG 463
Cdd:TIGR03269 96 fwnlsdklrrrirkRIAIMLQRTfalYGDDTvLDNVLEALeeigyegkeAVGRAVDLIE---MVQLSHRIThiarDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 464 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVT-HQLQYL-KAASQILILKDGKMVQKGT 541
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIeDLSDKAIWLENGEIKEEGT 252
|
250 260 270
....*....|....*....|....*....|....*....
gi 685504970 542 YTEFLKSGIDFGSLLKKDNEESEQPPVPGTPTLRNRTFS 580
Cdd:TIGR03269 253 PDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYIS 291
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
353-535 |
1.43e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG--------LVSVHGRIAYVSQQ----PWvfsgtlrsnilf 420
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtapLAEAREDTRLMFQDarllPW------------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 421 gkkyekeryEKVIKACAL-------KKDLQLLEDGDLTvigDRGT----TLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:PRK11247 96 ---------KKVIDNVGLglkgqwrDAALQALAAVGLA---DRANewpaALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 685504970 490 VDAeVSR----HLFELCICQilHEKITILVTHQLQYLKA-ASQILILKDGK 535
Cdd:PRK11247 164 LDA-LTRiemqDLIESLWQQ--HGFTVLLVTHDVSEAVAmADRVLLIEEGK 211
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
230-537 |
1.60e-10 |
|
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: 64.43 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 230 KEISKILRSSCLRGMNlasFFSASKIIVFVTFttYVLLGSVITASRVFVAVTLYGAVRLTVTLFF---P-----SAIERV 301
Cdd:COG4615 215 QPTAERYRDLRIRADT---IFALANNWGNLLF--FALIGLILFLLPALGWADPAVLSGFVLVLLFlrgPlsqlvGALPTL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 302 SEAIVSIRRIQTF-LLLDEISQRNRQLPSDgkkmVHVQDFT---------AFWDKASETP-TLQGLSFTVRPGELLAVVG 370
Cdd:COG4615 290 SRANVALRKIEELeLALAAAEPAAADAAAP----PAPADFQtlelrgvtyRYPGEDGDEGfTLGPIDLTIRRGELVFIVG 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 371 PVGAGKSSLLSAVLGELAPSHGLVSVHGRIayVSQQPWvfsGTLRSNI--------LFGKKYEKERYEKVIKACALKKDL 442
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQP--VTADNR---EAYRQLFsavfsdfhLFDRLLGLDGEADPARARELLERL 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 443 QLleDGDLTVIGDRGTT--LSGGQKARVNLARAVYQDADIYLLD------DPlsavdaeVSRHLFelcICQILHE----- 509
Cdd:COG4615 441 EL--DHKVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFRRVF---YTELLPElkarg 508
|
330 340
....*....|....*....|....*...
gi 685504970 510 KITILVTHQLQYLKAASQILILKDGKMV 537
Cdd:COG4615 509 KTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
353-540 |
1.68e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL------GEL----APSHG-----LVSVHGRIAYVSQQPwvfSGTL--R 415
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLrlinsqGEIwfdgQPLHNlnrrqLLPVRHRIQVVFQDP---NSSLnpR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNIL----------FGKKYEKERYEKVIKAcalkkdlqLLEDG-DLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLD 484
Cdd:PRK15134 379 LNVLqiieeglrvhQPTLSAAQREQQVIAV--------MEEVGlDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 485 DPLSAVDAEVSRHLFELC-ICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 540
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLkSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
346-537 |
1.85e-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: 61.12 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 346 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELapsHGLVSV------------------HGRIAYVSQQP 407
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVegdihyngipykefaekyPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 408 WVFSG-TLRSNILFgkkyekeryekvikACALKkdlqlledGDLTVigdRGttLSGGQKARVNLARAVYQDADIYLLDDP 486
Cdd:cd03233 93 VHFPTlTVRETLDF--------------ALRCK--------GNEFV---RG--ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 487 LSAVDAEVSRHLFElCICQILHE-KITILVThqlqyLKAAS--------QILILKDGKMV 537
Cdd:cd03233 146 TRGLDSSTALEILK-CIRTMADVlKTTTFVS-----LYQASdeiydlfdKVLVLYEGRQI 199
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
353-555 |
2.11e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.11 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQ-PWVFSGTLRSNI 418
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 LFGK-----------KYEKERYEKVIKACALKKDLQLLEDgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:PRK10575 107 AIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 488 SAVDaeVSRHLFELCICQILHEKITILVTHQLQYLKAASQ----ILILKDGKMVQKGTYTEFLKS-------GIDFGSL 555
Cdd:PRK10575 176 SALD--IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARycdyLVALRGGEMIAQGTPAELMRGetleqiyGIPMGIL 252
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
353-540 |
2.72e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 417
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGK--------------KYEKERYEKVIKACALKKDLQlledgdlTVIGDrgttLSGGQKARVNLARAVYQDADIYLL 483
Cdd:PRK09700 101 LYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDLD-------EKVAN----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 484 DDPLSAVDAEVSRHLFeLCICQILHE-KITILVTHQLQYLKA-ASQILILKDGKMVQKG 540
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF-LIMNQLRKEgTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
350-544 |
3.10e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.79 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 350 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR---------------IAYVSQQP--WVFSG 412
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklresVGMVFQDPdnQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TLRSNILFG----KKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:PRK13636 99 SVYQDVSFGavnlKLPEDEVRKRVDNA---------LKRTGIEHLKDKPThCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 488 SAVDAEVSRHLFELCICQILHEKITILV-THQLQYLKA-ASQILILKDGKMVQKGTYTE 544
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKELGLTIIIaTHDIDIVPLyCDNVFVMKEGRVILQGNPKE 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
359-541 |
3.12e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 359 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------------IAYVSQQP--WVFSGTLRSNIL 419
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkknkklkplrkkVGIVFQFPehQLFEETVEKDIC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 420 FG-------KKYEKERYEKVIKACALKKDLQlledgdltvigDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:PRK13634 109 FGpmnfgvsEEDAKQKAREMIELVGLPEELL-----------ARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 492 AEVSRHLFELcICQILHEK--ITILVTHQL----QYlkaASQILILKDGKMVQKGT 541
Cdd:PRK13634 178 PKGRKEMMEM-FYKLHKEKglTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGT 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-552 |
3.26e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 359 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQqpWV---FSGT----LRSNilfGKKYEKERYE- 430
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTvedlLRSI---TDDLGSSYYKs 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 431 KVIKACALKKdlqLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VSRHLFElci 503
Cdd:PRK13409 436 EIIKPLQLER---LLDK--------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlavakAIRRIAE--- 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 504 cqiLHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYT----------EFLKS-GIDF 552
Cdd:PRK13409 502 ---EREATALVVDHDIYMIDYISDRLMVFEGEPGKHGHASgpmdmregmnRFLKElGITF 558
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
632-770 |
3.45e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 63.26 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 632 AGAHWIVFIFLILLNTAAQVAYVLQDWWLSYWANkqsmlnvTVNGGGNVTEkldLNWYLGIYSGLTVATVLFGIARSLLV 711
Cdd:COG1132 16 LRPYRGLLILALLLLLLSALLELLLPLLLGRIID-------ALLAGGDLSA---LLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 712 FYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVR 144
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
363-540 |
3.80e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 363 GELLAVVGPVGAGKSSLLSAVLG-ELAPSHGLVSVHGRIAYVsqQP------WVFSG-------TLRSNILFGKKYEK-- 426
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGlEDITSGDLFIGEKRMNDV--PPaergvgMVFQSyalyphlSVAENMSFGLKLAGak 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 427 --ERYEKVIKACALKKDLQLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA--------EVSR 496
Cdd:PRK11000 107 keEINQRVNQVAEVLQLAHLLDR--------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmriEISR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 685504970 497 hlfelcicqiLHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKG 540
Cdd:PRK11000 179 ----------LHKRLgrtMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
359-522 |
3.98e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 61.23 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 359 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGL------------------------------VSVHGRIAYVSQQPW 408
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkllegdVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 409 VFSGTLRSniLFGKKYEKERYEKVIKACALKKDLqlledgdltvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:cd03236 102 AVKGKVGE--LLKKKDERGKLDELVDQLELRHVL------------DRNiDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 685504970 488 SAVD-------AEVSRHLFElcicqilHEKITILVTHQLQYL 522
Cdd:cd03236 168 SYLDikqrlnaARLIRELAE-------DDNYVLVVEHDLAVL 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
351-510 |
4.18e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.34 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTL-QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV--SVHGRIAYVSQQPwVFSGTLRSNILFgkkYEKE 427
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMAVFSQHH-VDGLDLSSNPLL---YMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 428 RYEKVIKAcALKKDLqlledGDLTVIGDRGT----TLSGGQKARVNLARAVYQDADIYLLDDP-----LSAVDAEVS-RH 497
Cdd:PLN03073 598 CFPGVPEQ-KLRAHL-----GSFGVTGNLALqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPsnhldLDAVEALIQgLV 671
|
170
....*....|...
gi 685504970 498 LFELCICQILHEK 510
Cdd:PLN03073 672 LFQGGVLMVSHDE 684
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-552 |
6.08e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 359 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAY----VSQQpwvFSGT----LRSNI---LFGKKYEKE 427
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyISPD---YDGTveefLRSANtddFGSSYYKTE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 428 ryekVIKACALKKdlqLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VSRHLFE 500
Cdd:COG1245 439 ----IIKPLGLEK---LLDK--------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlavakAIRRFAE 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685504970 501 lcicqiLHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYT----------EFLKS-GIDF 552
Cdd:COG1245 504 ------NRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASgpmdmregmnRFLKElGITF 560
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
349-552 |
6.97e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH--GLVSVHG---------RIAYVSQQPWVFSG-TLRS 416
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrkptkqilkRTGFVTQDDILYPHlTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 NILF------GKKYEKEryEKVIKACALKKDLQLLEDGDlTVIGD---RGttLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQ--EKILVAESVISELGLTKCEN-TIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 488 SAVDAEVSRHLFeLCICQILHEKITILVT-HQ--LQYLKAASQILILKDGK--MVQKGTYTEFLKSGIDF 552
Cdd:PLN03211 235 SGLDATAAYRLV-LTLGSLAQKGKTIVTSmHQpsSRVYQMFDSVLVLSEGRclFFGKGSDAMAYFESVGF 303
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
353-537 |
6.97e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSL---LSAVL------GE-------LAPSH-------GLVSVHGRIAYVSQQpwv 409
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYphgtyeGEiifegeeLQASNirdteraGIAIIHQELALVKEL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 fsgTLRSNILFGKKYEKE---RYEKVIKAC-ALKKDLQLLEDGDLTViGDrgttLSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:PRK13549 98 ---SVLENIFLGNEITPGgimDYDAMYLRAqKLLAQLKLDINPATPV-GN----LGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 685504970 486 PLSAVDAEVSRHLFELcICQILHEKIT-ILVTHQLQYLKAAS-QILILKDGKMV 537
Cdd:PRK13549 170 PTASLTESETAVLLDI-IRDLKAHGIAcIYISHKLNEVKAISdTICVIRDGRHI 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
353-544 |
6.98e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQP--WVFSGTLRSN 417
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:PRK13652 100 IAFGpinlgldEETVAHRVSSALHMLGLEE------------LRDRVPhHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 490 VDAEVSRHLFELCICQILHEKIT-ILVTHQLQYL-KAASQILILKDGKMVQKGTYTE 544
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTvIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEE 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
353-541 |
8.43e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.89 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 417
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimreaVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGKKY-EKERYEKVIKACAlkkDL--QLLEDGdltviGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 494
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWVY---ELfpRLHERR-----IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 685504970 495 SRHLFELcICQILHEKITILVTHQ--LQYLKAASQILILKDGKMVQKGT 541
Cdd:PRK11614 173 IQQIFDT-IEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDT 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
310-521 |
1.03e-09 |
|
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: 61.87 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 310 RIQTF--LLLDEISQRNRQL-------PSDGKKMVHVQDFT-AFWDKasetPTLQGLSFTVRPGELLAVVGPVGAGKSSL 379
Cdd:TIGR03719 289 RLARYeeLLSQEFQKRNETAeiyippgPRLGDKVIEAENLTkAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 380 LSAVLGELAPSHGLVSVhG---RIAYVSQQpwvfsgtlRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGD 455
Cdd:TIGR03719 365 FRMITGQEQPDSGTIEI-GetvKLAYVDQS--------RDAL----DPNKTVWEEI-------------SGGlDIIKLGK 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 456 R--------------GT-------TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL------FELCICQILH 508
Cdd:TIGR03719 419 ReipsrayvgrfnfkGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALeeallnFAGCAVVISH 498
|
250
....*....|....*
gi 685504970 509 EK--ITILVTHQLQY 521
Cdd:TIGR03719 499 DRwfLDRIATHILAF 513
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
353-546 |
2.51e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------------IAYVSQQP--------- 407
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklnraqrkafrrdIQMVFQDSisavnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 408 --WVFSGTLRSNILFGKKYEKERYEKVIKACALkkdlqlledgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:PRK10419 108 vrEIIREPLRHLLSLDKAERLARASEMLRAVDL----------DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 486 PLSAVDaevsRHLfELCICQIL----HEKIT--ILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFL 546
Cdd:PRK10419 178 AVSNLD----LVL-QAGVIRLLkklqQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKL 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
353-501 |
2.80e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.06 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPShglvsvhgriayvsqqpwvfSGTLRsniLFGKKYEKERYEKV 432
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA--------------------SGEIT---LDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 433 IKA-CALkkdlqLLED-------GDLTV-----IGDRgttLSGG--QKarVNLARAVYQDADIYLLDDPLSAVD----AE 493
Cdd:cd03215 73 IRAgIAY-----VPEDrkreglvLDLSVaeniaLSSL---LSGGnqQK--VVLARWLARDPRVLILDEPTRGVDvgakAE 142
|
....*...
gi 685504970 494 VSRHLFEL 501
Cdd:cd03215 143 IYRLIREL 150
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
351-580 |
3.12e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------------IAYVSQQPWVFSG-TLRSN 417
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGKKYEKERYEKVikacALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 497
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEA----QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 498 LFELcICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKGTyTEFLKSGIDFGSLL----KKDNEESEQPPVPGTP 572
Cdd:TIGR01257 1100 IWDL-LLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT-PLFLKNCFGTGFYLtlvrKMKNIQSQRGGCEGTC 1177
|
....*...
gi 685504970 573 TLRNRTFS 580
Cdd:TIGR01257 1178 SCTSKGFS 1185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
353-540 |
4.40e-09 |
|
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: 57.15 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGElapsHGLVSVHGRIAYVSQqpwvfsgtlrsNILFGKKYEKER---- 428
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----PKYEVTEGEILFKGE-----------DITDLPPEERARlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 429 ----YEKVIKACALKKDLQLLEDGdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcIC 504
Cdd:cd03217 81 lafqYPPEIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV-IN 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 685504970 505 QILHEKIT-ILVTHQ---LQYLKaASQILILKDGKMVQKG 540
Cdd:cd03217 149 KLREEGKSvLIITHYqrlLDYIK-PDRVHVLYDGRIVKSG 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
353-537 |
4.43e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.45 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG----------------ELAPSH-------GLVSVHGRIAYVSQQpwv 409
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASNirdteraGIVIIHQELTLVPEL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 fsgTLRSNILFGK----KYEKERYEKVIKAC-ALKKDLQLLEDGDLTVIGDRGttlsGGQKARVNLARAVYQDADIYLLD 484
Cdd:TIGR02633 94 ---SVAENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 685504970 485 DPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAAS-QILILKDGKMV 537
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCdTICVIRDGQHV 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
343-544 |
5.23e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.56 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 343 FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVSQQPW---------VFSG 412
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWravrsdiqmIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TL-----RSNI---------LFGKKYEKERYEKVIKACALKkdLQLLEDgdltVIGDRGTTLSGGQKARVNLARAVYQDA 478
Cdd:PRK15079 107 PLaslnpRMTIgeiiaeplrTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 479 DIYLLDDPLSAVDAEVSRHLFELciCQILHEKI---TILVTHQLQYLKAAS-QILILKDGKMVQKGTYTE 544
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNL--LQQLQREMglsLIFIAHDLAVVKHISdRVLVMYLGHAVELGTYDE 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
318-548 |
6.20e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.03 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 318 DEISQRNRQLPSDGKK--MVHVQDFTAFWDKASeTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG--- 392
Cdd:TIGR01257 1919 DDVAEERQRIISGGNKtdILRLNELTKVYSGTS-SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdat 1997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 393 ---------LVSVHGRIAYVSQqpwvFSGTlrSNILFGKK--YEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTL 460
Cdd:TIGR01257 1998 vagksiltnISDVHQNMGYCPQ----FDAI--DDLLTGREhlYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRlAGTY 2071
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 461 SGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQK 539
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCL 2151
|
....*....
gi 685504970 540 GTyTEFLKS 548
Cdd:TIGR01257 2152 GT-IQHLKS 2159
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
349-491 |
1.19e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------RIAYvsQQPWVFSG---------T 413
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTY--QKQLCFVGhrsginpylT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 414 LRSNILFGKKYEKERYEkVIKACALKKdLQLLEDGDLTVigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-ITELCRLFS-LEHLIDYPCGL-------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
356-552 |
1.25e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV-----------------HGRIAYVSQQP--WVFSGTLRS 416
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeikpvRKKVGVVFQFPesQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 NILFGKK---YEKERYEKV----IKACALKKdlQLLEDGDLTvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:PRK13643 105 DVAFGPQnfgIPKEKAEKIaaekLEMVGLAD--EFWEKSPFE--------LSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 490 VDAEVSRHLFELciCQILHE--KITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLKSgIDF 552
Cdd:PRK13643 175 LDPKARIEMMQL--FESIHQsgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE-VDF 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-544 |
1.39e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.46 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPS---HGLVSVHG-------------RIAYVSQQP-WV 409
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifkmdvielrrRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 FSGTLRSNILFGKKY------EKERYEKVIKacALKKdLQLLEDgdltvIGDR----GTTLSGGQKARVNLARAVYQDAD 479
Cdd:PRK14247 95 PNLSIFENVALGLKLnrlvksKKELQERVRW--ALEK-AQLWDE-----VKDRldapAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 480 IYLLDDPLSAVDAEVSRHLFELCIcQILHEKITILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 544
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFL-ELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
362-537 |
1.58e-08 |
|
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: 54.30 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 362 PGELLAVVGPVGAGKSSLLSAVLGELAPSHGlvsvhgriayvsqqpwvfsgtlrsnilfgkkyekeryeKVIKACALKKD 441
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--------------------------------------GVIYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 442 LQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQIL-----HEKITILVT 516
Cdd:smart00382 43 EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILT 122
|
170 180
....*....|....*....|.
gi 685504970 517 HQLQYLKAASQILILKDGKMV 537
Cdd:smart00382 123 TNDEKDLGPALLRRRFDRRIV 143
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
367-548 |
1.88e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 367 AVVGPVGAGKSSLL-----------------SAVLG--ELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKE 427
Cdd:PRK14271 51 SLMGPTGSGKTTFLrtlnrmndkvsgyrysgDVLLGgrSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 428 RYEKVIKACALKKdlqLLEDGDLTVIGDRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELci 503
Cdd:PRK14271 131 VPRKEFRGVAQAR---LTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF-- 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 685504970 504 CQILHEKIT-ILVTHQL-QYLKAASQILILKDGKMVQKGTYTEFLKS 548
Cdd:PRK14271 206 IRSLADRLTvIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
349-496 |
2.53e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL--APSHGLVSVhgriayvsqqPWVFSGTLRSNI-LFGKKYE 425
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV----------PDNQFGREASLIdAIGRKGD 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 426 KERYEKVIKACALkkdlqlledGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 496
Cdd:COG2401 112 FKDAVELLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
353-538 |
3.16e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSL---LSAVL------------GELA--------PSHGLVSVHGRIAYVSQQpwv 409
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLmkvLSGVYphgsyegeilfdGEVCrfkdirdsEALGIVIIHQELALIPYL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 fsgTLRSNILFGKkyEKERY------EKVIKACALKKDLQLLEDGDlTVIGDRGTtlsgGQKARVNLARAVYQDADIYLL 483
Cdd:NF040905 94 ---SIAENIFLGN--ERAKRgvidwnETNRRARELLAKVGLDESPD-TLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 484 DDPLSAVDAEVSRHLFELcICQILHEKIT-ILVTHQL-QYLKAASQILILKDGKMVQ 538
Cdd:NF040905 164 DEPTAALNEEDSAALLDL-LLELKAQGITsIIISHKLnEIRRVADSITVLRDGRTIE 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
349-541 |
5.74e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.75 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP--WV 409
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdikqirkKVGLVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 FSGTLRSNILFGKK---YEKERYEKVikacALKKdlqlledgdLTVIG------DRGT-TLSGGQKARVNLARAVYQDAD 479
Cdd:PRK13649 99 FEETVLKDVAFGPQnfgVSQEEAEAL----AREK---------LALVGiseslfEKNPfELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 480 IYLLDDPLSAVDAEVSRHLFELciCQILHEK-ITI-LVTHQLQYL-KAASQILILKDGKMVQKGT 541
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTL--FKKLHQSgMTIvLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
362-543 |
6.21e-08 |
|
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: 52.75 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 362 PGELLAVVGPVGAGKSSLLSAVLgelapshglvsvhgriayvsqqpWVFSGtlRSNILFGKKYEKERYekvIKACAlkkD 441
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG-----------------------LALGG--AQSATRRRSGVKAGC---IVAAV---S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 442 LQLLedgdLTVIGdrgttLSGGQKARVNLARAV----YQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTH 517
Cdd:cd03227 69 AELI----FTRLQ-----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
170 180
....*....|....*....|....*.
gi 685504970 518 QLQYLKAASQILILkdgKMVQKGTYT 543
Cdd:cd03227 140 LPELAELADKLIHI---KKVITGVYK 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-519 |
9.60e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 359 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------------------------LVSVHgRIAYVSQQP 407
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtelqnyfkklyngeIKVVH-KPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 408 WVFSGTLRSniLFGKKYEKERYEKVIKACALKKDLqlledgdltvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDP 486
Cdd:PRK13409 174 KVFKGKVRE--LLKKVDERGKLDEVVERLGLENIL------------DRDiSELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 685504970 487 LSAVD-------AEVSRHLFElcicqilhEKITILVTHQL 519
Cdd:PRK13409 240 TSYLDirqrlnvARLIRELAE--------GKYVLVVEHDL 271
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-547 |
9.99e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------RIAYVSQQPWVFsG-------------T 413
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrRKEFARRIGVVF-GqrsqlwwdlpaidS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 LRsniLFGKKYE--KERYEKVIKACAlkkdlQLLEDGDLTVIGDRgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:COG4586 117 FR---LLKAIYRipDAEYKKRLDELV-----ELLDLGELLDTPVR--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 492 AEVSRHLFELcICQILHE-KITILVT-HQLQYLKA-ASQILILKDGKMVQKGTYTEFLK 547
Cdd:COG4586 187 VVSKEAIREF-LKEYNRErGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
351-540 |
1.05e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.94 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPshGLVSVHGRIAY--VSQQPWVFSGTLRSNIL------FG- 421
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLdgKPVAPCALRGRKIATIMqnprsaFNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 422 ----KKYEKERYEKVIKACALKKDLQLLEDGDLtviGDRGTTL-------SGGQKARVNLARAVYQDADIYLLDDPLSAV 490
Cdd:PRK10418 95 lhtmHTHARETCLALGKPADDATLTAALEAVGL---ENAARVLklypfemSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 685504970 491 DAEVSRHLFELcICQILHEKI--TILVTHQLQYL-KAASQILILKDGKMVQKG 540
Cdd:PRK10418 172 DVVAQARILDL-LESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
353-536 |
1.62e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.86 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------RIAYVSQ------QPWVFSGTLRS 416
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeeaRAKLRAKhvgfvfQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 -------NILFGkkyEKERYEKViKACALKKDLQLledgdltviGDR----GTTLSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:PRK10584 106 lenvelpALLRG---ESSRQSRN-GAKALLEQLGL---------GKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 685504970 486 PLSAVDAEVSRHLFELcICQILHEKIT--ILVTHQLQYLKAASQILILKDGKM 536
Cdd:PRK10584 173 PTGNLDRQTGDKIADL-LFSLNREHGTtlILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-501 |
2.20e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 359 TVRPGELLAVVGPVGAGKSSLLSAVLGELAP------------------------------SHGLVSVHGRIAYVSQQPW 408
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPnlgdydeepswdevlkrfrgtelqdyfkklANGEIKVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 409 VFSGTLRSnILfgKKY-EKERYEKVIKACALKKDLqlleDGDLtvigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPL 487
Cdd:COG1245 175 VFKGTVRE-LL--EKVdERGKLDELAEKLGLENIL----DRDI-------SELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170
....*....|....*...
gi 685504970 488 SAVD----AEVSRHLFEL 501
Cdd:COG1245 241 SYLDiyqrLNVARLIREL 258
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
341-491 |
2.81e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 341 TAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH---------------GLVSVHGRIAYVSQ 405
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKgavlwqgkpldyskrGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 406 QP--WVFSGTLRSNILFGKK----YEKERYEKVIKACALkKDLQLLEDGDLTVigdrgttLSGGQKARVNLARAVYQDAD 479
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRnlgvPEAEITRRVDEALTL-VDAQHFRHQPIQC-------LSHGQKKRVAIAGALVLQAR 156
|
170
....*....|..
gi 685504970 480 IYLLDDPLSAVD 491
Cdd:PRK13638 157 YLLLDEPTAGLD 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
351-520 |
3.00e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGE--LAPSHGLVsVHGR--------------IAYVSQQ---PWVFS 411
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpQGYSNDLT-LFGRrrgsgetiwdikkhIGYVSSSlhlDYRVS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 412 GTLRSNILFGKKYEKERYEKVIKAcalkkdLQLLEDGDLTVIGDRGTT-------LSGGQKARVNLARAVYQDADIYLLD 484
Cdd:PRK10938 353 TSVRNVILSGFFDSIGIYQAVSDR------QQKLAQQWLDILGIDKRTadapfhsLSWGQQRLALIVRALVKHPTLLILD 426
|
170 180 190
....*....|....*....|....*....|....*...
gi 685504970 485 DPLSAVDAeVSRHLFELCICQILHEKITIL--VTHQLQ 520
Cdd:PRK10938 427 EPLQGLDP-LNRQLVRRFVDVLISEGETQLlfVSHHAE 463
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
331-498 |
4.04e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 331 GKKMVHVQDFT-AFWDKasetpTL-QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVhG---RIAYVSQ 405
Cdd:PRK11819 321 GDKVIEAENLSkSFGDR-----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GetvKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 406 QpwvfsgtlRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGDR--------------GT-------TLSGG 463
Cdd:PRK11819 395 S--------RDAL----DPNKTVWEEI-------------SGGlDIIKVGNReipsrayvgrfnfkGGdqqkkvgVLSGG 449
|
170 180 190
....*....|....*....|....*....|....*
gi 685504970 464 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 498
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRAL 484
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
362-536 |
4.24e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 362 PGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQPWVFsgtLRSNilfgkkyekERYEKVIKACALK 439
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQHQLEF---LRAD---------ESPLQHLARLAPQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 440 KDLQLLED--GDLTVIGDRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICqilHEKITI 513
Cdd:PRK10636 405 ELEQKLRDylGGFGFQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID---FEGALV 481
|
170 180
....*....|....*....|....
gi 685504970 514 LVTHQLQYLKAASQILIL-KDGKM 536
Cdd:PRK10636 482 VVSHDRHLLRSTTDDLYLvHDGKV 505
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
360-547 |
4.82e-07 |
|
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: 50.65 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 360 VRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-RIAYVSQQpwvfsgtlrsnilfgkkyekeryekvikacal 438
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 439 kkdlqlledgdltvigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VSRHLFElcicqiLHEKI 511
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnaarAIRRLSE------EGKKT 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 685504970 512 TILVTHQLQYLKAASQILILKDGkmvQKGTYTEFLK 547
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEG---EPGVYGIASQ 157
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
356-546 |
5.85e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTvrPGELLAVVGPVGAGKSSLLS--AVL-----GELAPSHGLvsvhgRIAYVSQQPWV-FSGTLRSNILFG---KKY 424
Cdd:PRK11819 28 LSFF--PGAKIGVLGLNGAGKSTLLRimAGVdkefeGEARPAPGI-----KVGYLPQEPQLdPEKTVRENVEEGvaeVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 425 EKERYEKV------------------------IKAC-ALKKDLQL--------LEDGDLTVigdrgTTLSGGQKARVNLA 471
Cdd:PRK11819 101 ALDRFNEIyaayaepdadfdalaaeqgelqeiIDAAdAWDLDSQLeiamdalrCPPWDAKV-----TKLSGGERRRVALC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 472 RAVYQDADIYLLDDPLSAVDAE-VS---RHL--FELCIcqilhekitILVTHQLQYL-KAASQILILKDGKMVQ-KGTYT 543
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAEsVAwleQFLhdYPGTV---------VAVTHDRYFLdNVAGWILELDRGRGIPwEGNYS 246
|
...
gi 685504970 544 EFL 546
Cdd:PRK11819 247 SWL 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
353-494 |
6.71e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWvfsGTL-- 414
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllkadpeaqkllrqKIQIVFQNPY---GSLnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 415 RSNIlfGKKYE-----------KERYEKVikacalkkdLQLLEdgdltVIGDRGT-------TLSGGQKARVNLARAVYQ 476
Cdd:PRK11308 108 RKKV--GQILEepllintslsaAERREKA---------LAMMA-----KVGLRPEhydryphMFSGGQRQRIAIARALML 171
|
170
....*....|....*...
gi 685504970 477 DADIYLLDDPLSAVDAEV 494
Cdd:PRK11308 172 DPDVVVADEPVSALDVSV 189
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
345-547 |
7.79e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.63 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 345 DKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------------RIAYVSQQP--W 408
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdirnKAGMVFQNPdnQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 409 VFSGTLRSNILFG-------KKYEKERYEKVIKACAL---KKDLQLLedgdltvigdrgttLSGGQKARVNLARAVYQDA 478
Cdd:PRK13633 98 IVATIVEEDVAFGpenlgipPEEIRERVDESLKKVGMyeyRRHAPHL--------------LSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 479 DIYLLDDPLSAVDA----EVSRHLFELCicqiLHEKIT-ILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 547
Cdd:PRK13633 164 ECIIFDEPTAMLDPsgrrEVVNTIKELN----KKYGITiILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
104-311 |
8.89e-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: 51.40 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 104 LRLSNMAMGKTTTGQIVNLLSNDVNKFDQ-VTVFLHFLWAGPLQAIAVTA-LLWMEIGIScLAGMAVLIILLPLQSCFGK 181
Cdd:cd07346 83 QRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALViLFYLNWKLT-LVALLLLPLYVLILRYFRR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 182 ----LFSSLRSKTATFTdariRTMNEVITGIRIIKMYAWEKS----FSNLITNLRKKEISKILRSSCLRGMnLASFFSAS 253
Cdd:cd07346 162 rirkASREVRESLAELS----AFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPL-IGLLTALG 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 254 KIIVFVtFTTYVLLGSVITASrVFVAVTLYgavrlTVTLFFPsaIERVSE-------AIVSIRRI 311
Cdd:cd07346 237 TALVLL-YGGYLVLQGSLTIG-ELVAFLAY-----LGMLFGP--IQRLANlynqlqqALASLERI 292
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-546 |
1.82e-06 |
|
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: 51.34 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 355 GLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV----------------HGR----IAYVSQQPWVFS-GT 413
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRakryIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 414 LRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 493
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 494 VSRHLFElcicQILH-----EKITILVTHQLQY-LKAASQILILKDGKMVQKGTYTEFL 546
Cdd:TIGR03269 462 TKVDVTH----SILKareemEQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
322-486 |
1.84e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.18 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 322 QRNRQLPSDGKKMVHVQDFTAfwDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-- 399
Cdd:COG3845 245 RVEKAPAEPGEVVLEVENLSV--RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdi 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 400 ------------IAYVSQQPW----VFSGTLRSNILFGkKYEKERYEK--VIKACALKKD-LQLLEDGDL--TVIGDRGT 458
Cdd:COG3845 323 tglsprerrrlgVAYIPEDRLgrglVPDMSVAENLILG-RYRRPPFSRggFLDRKAIRAFaEELIEEFDVrtPGPDTPAR 401
|
170 180 190
....*....|....*....|....*....|
gi 685504970 459 TLSGG--QKarVNLARAVYQDADIYLLDDP 486
Cdd:COG3845 402 SLSGGnqQK--VILARELSRDPKLLIAAQP 429
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
637-770 |
2.93e-06 |
|
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: 49.86 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 637 IVFIFLILLNTAAQVAYvlqdwwlsYWANKQSMLNVTVNGGGNVtekldLNWYLGIYSGLTVATVLFGIARSLLVFYVLV 716
Cdd:cd07346 2 LLALLLLLLATALGLAL--------PLLTKLLIDDVIPAGDLSL-----LLWIALLLLLLALLRALLSYLRRYLAARLGQ 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 685504970 717 NSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd07346 69 RVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLS 122
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
353-541 |
4.35e-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: 49.15 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL-----------GELAPSHGLVSVH---GRIAYVSQQPwvFSGTLRSN- 417
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkKEQPGNHDRIEGLehiDKVIVIDQSP--IGRTPRSNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 -----------ILF-----GKKYEKE----RYE-KVI----------------KACALKKDLQLLEDGDLTVI--GDRGT 458
Cdd:cd03271 89 atytgvfdeirELFcevckGKRYNREtlevRYKgKSIadvldmtveealeffeNIPKIARKLQTLCDVGLGYIklGQPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 459 TLSGGQKARVNLARAVYQDAD---IYLLDDPLSAVDAEVSRHLFElcicqILHEKI----TILVT-HQLQYLKAASQILI 530
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLE-----VLQRLVdkgnTVVVIeHNLDVIKCADWIID 243
|
250
....*....|....*..
gi 685504970 531 L------KDGKMVQKGT 541
Cdd:cd03271 244 LgpeggdGGGQVVASGT 260
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
353-518 |
6.35e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP---SHGLVSVHGR---------IAYVSQQ-----------PWV 409
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRpldssfqrsIGYVQQQdlhlptstvreSLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 410 FSGTLR-SNILfgKKYEKERY-EKVIKacalkkdlqLLEDGDL--TVIGDRGTTLSGGQKARVNLA-RAVYQDADIYLLD 484
Cdd:TIGR00956 859 FSAYLRqPKSV--SKSEKMEYvEEVIK---------LLEMESYadAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLD 927
|
170 180 190
....*....|....*....|....*....|....*....
gi 685504970 485 DPLSAVDAEVSrhlfeLCICQILHEKI----TILVT-HQ 518
Cdd:TIGR00956 928 EPTSGLDSQTA-----WSICKLMRKLAdhgqAILCTiHQ 961
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
640-761 |
6.56e-06 |
|
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: 48.54 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 640 IFLILLNTAAQVA--YVLqdwwlsywanKQSMLNVTVNGGGNVTEkldLNWYLGIYSGLTVATVLFGIARSLLVFYVLVN 717
Cdd:cd18544 5 LLLLLLATALELLgpLLI----------KRAIDDYIVPGQGDLQG---LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQR 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 685504970 718 SSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLL 761
Cdd:cd18544 72 IIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELF 115
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
637-754 |
7.12e-06 |
|
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: 48.55 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 637 IVFIFLILLNTAAQVA--YVLQDWWLSYWANKQSMLNVTVNGggnvtekldLNWYLGIYSGLTVATVLFGIARSLLVFYV 714
Cdd:cd18547 2 ILVIILAIISTLLSVLgpYLLGKAIDLIIEGLGGGGGVDFSG---------LLRILLLLLGLYLLSALFSYLQNRLMARV 72
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 685504970 715 LVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDI 754
Cdd:cd18547 73 SQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDV 112
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
330-577 |
7.96e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 330 DGKKMVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVS------------- 395
Cdd:PRK10261 8 DARDVLAVENLNiAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 396 -------------VHGR-IAYVSQQPWVfsgTLRSNILFGKKY-EKER-YEKVIKACALKKDLQLLEDGDL----TVIGD 455
Cdd:PRK10261 88 ielseqsaaqmrhVRGAdMAMIFQEPMT---SLNPVFTVGEQIaESIRlHQGASREEAMVEAKRMLDQVRIpeaqTILSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 456 RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELciCQILHEKIT---ILVTHQLQYL-KAASQILIL 531
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQL--IKVLQKEMSmgvIFITHDMGVVaEIADRVLVM 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 532 KDGKMVQKGT-----------YTEFL---------KSGIDFG---SLLKKDNEESEQPP------VPGTPTLRNR 577
Cdd:PRK10261 243 YQGEAVETGSveqifhapqhpYTRALlaavpqlgaMKGLDYPrrfPLISLEHPAKQEPPieqdtvVDGEPILQVR 317
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
353-529 |
8.25e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVlgeLAPSHGLVSVHGRIAYvSQQPWVFSGTLRSNILFGKKYekeryekv 432
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFLPKF-SRNKLIFIDQLQFLIDVGLGY-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 433 ikacalkkdlqlledgdLTvIGDRGTTLSGGQKARVNLARAVYQDAD--IYLLDDPLSAVDAEVSRHLFElCICQILHEK 510
Cdd:cd03238 79 -----------------LT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE-VIKGLIDLG 139
|
170 180
....*....|....*....|
gi 685504970 511 IT-ILVTHQLQYLKAASQIL 529
Cdd:cd03238 140 NTvILIEHNLDVLSSADWII 159
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-541 |
9.38e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 355 GLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVSQQPWVFSGTLR------------------ 415
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhIEGLPGHQIARMGVVRtfqhvrlfremtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 --------SNILFG-------KKYEKEryekvikacALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDAD 479
Cdd:PRK11300 103 vaqhqqlkTGLFSGllktpafRRAESE---------ALDRAATWLERVGLLEHANRqAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 480 IYLLDDPLSAVDAEVSRHLFELcICQILHE-KITI-LVTHQLQYLKAAS-QILILKDGKMVQKGT 541
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDEL-IAELRNEhNVTVlLIEHDMKLVMGISdRIYVVNQGTPLANGT 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
353-537 |
1.23e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQ-PWVFSGTLRSN 417
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 418 ILFGkkyekeRYEK----VIKACALKKDLQLLEDGDLTV-IGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:PRK10982 94 MWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIDIdPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 685504970 493 EVSRHLFElcICQILHEK--ITILVTHQL-QYLKAASQILILKDGKMV 537
Cdd:PRK10982 168 KEVNHLFT--IIRKLKERgcGIVYISHKMeEIFQLCDEITILRDGQWI 213
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
640-769 |
1.38e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 47.85 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 640 IFLILLNTAAQVA--YVLqdwwlsywanKQSMLNVTVNGggNVTeklDLNWYLGIYSGLTVATVLFGIARSLLVFYVlvn 717
Cdd:cd18545 6 LLLMLLSTAASLAgpYLI----------KIAIDEYIPNG--DLS---GLLIIALLFLALNLVNWVASRLRIYLMAKV--- 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 685504970 718 SSQTLHN---KMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFI 769
Cdd:cd18545 68 GQRILYDlrqDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLI 122
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
357-501 |
1.62e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 357 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-RIAYVSQQPWVFSG-----------------TLRSNI 418
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkaegiipvhSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 -------------LFGKKYEKERYEKVIKACALKKdlqllEDGDlTVIGdrgtTLSGGQKARVNLARAVYQDADIYLLDD 485
Cdd:PRK11288 353 nisarrhhlragcLINNRWEAENADRFIRSLNIKT-----PSRE-QLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180
....*....|....*....|
gi 685504970 486 PLSAVD----AEVSRHLFEL 501
Cdd:PRK11288 423 PTRGIDvgakHEIYNVIYEL 442
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
353-537 |
1.68e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 46.47 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSaVL---GELAPSHGLVSVHGR---------IAYVSQQPwVFSG--TLRSNI 418
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLD-VLagrKTAGVITGEILINGRpldknfqrsTGYVEQQD-VHSPnlTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 419 LFgkkyekeryekvikACALkkdlqlledgdltvigdRGttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSrhl 498
Cdd:cd03232 101 RF--------------SALL-----------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA--- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 685504970 499 feLCICQILhEKI-----TILVT-HQ--LQYLKAASQILILK-DGKMV 537
Cdd:cd03232 145 --YNIVRFL-KKLadsgqAILCTiHQpsASIFEKFDRLLLLKrGGKTV 189
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
353-491 |
2.18e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSqqpwVFSG-----TLRSNI-----LFG- 421
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA----ISSGlngqlTGIENIelkglMMGl 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685504970 422 -KKYEKERYEKVIKACALKKdlqlledgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 491
Cdd:PRK13545 116 tKEKIKEIIPEIIEFADIGK-----------FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
351-536 |
2.25e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQ---QPWVFS-- 411
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinnhnaneainhgFALVTEerrSTGIYAyl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 412 ----GTLRSNIlfgKKYeKERYeKVIKACALKKDLQLLED-------GDLTVIGdrgtTLSGGQKARVNLARAVYQDADI 480
Cdd:PRK10982 342 digfNSLISNI---RNY-KNKV-GLLDNSRMKSDTQWVIDsmrvktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 685504970 481 YLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQL-QYLKAASQILILKDGKM 536
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLV 469
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
337-402 |
2.39e-05 |
|
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: 47.76 E-value: 2.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685504970 337 VQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKS-SLLSaVLGeLAPsHGLVSVHGRIAY 402
Cdd:COG4172 9 VEDLSvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILR-LLP-DPAAHPSGSILF 73
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
671-770 |
2.75e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 46.73 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 671 NVTVNGGGNVTEKLdLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRF 750
Cdd:cd18563 28 DVLIQLGPGGNTSL-LLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRV 106
|
90 100
....*....|....*....|
gi 685504970 751 SKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd18563 107 TSDTDRLQDFLSDGLPDFLT 126
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
354-538 |
4.73e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 354 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG--------------ELAPSHGLVSVHGRIAYVSQ---QPWVFSG-TLR 415
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkraggeirlngkDISPRSPLDAVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 416 SNILFGKKYEKERYEKVIKACALKKDLQLLED--GDLTV----IGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqrELLALkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 685504970 490 VDAEVSRHLFELcICQILHEKITIL-VTHQL-QYLKAASQILILKDGKMVQ 538
Cdd:PRK09700 440 IDVGAKAEIYKV-MRQLADDGKVILmVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
113-276 |
5.72e-05 |
|
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: 45.63 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 113 KTTTGQIVNLLSNDVNKF-DQVTVFLHFLWAGPLQAIAVTALLWMeigISC-LAGmaVLIILLPLQSCFGKLFSS-LRSK 189
Cdd:cd18557 89 KHKTGELTSRLSSDTSVLqSAVTDNLSQLLRNILQVIGGLIILFI---LSWkLTL--VLLLVIPLLLIASKIYGRyIRKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 190 TATFTDARIRTM---NEVITGIRIIkmyaweKSFSNLITNLRK--KEISKILRSSCLRGMNLASFFSASKIIVFV-TFTT 263
Cdd:cd18557 164 SKEVQDALAKAGqvaEESLSNIRTV------RSFSAEEKEIRRysEALDRSYRLARKKALANALFQGITSLLIYLsLLLV 237
|
170
....*....|...
gi 685504970 264 YVLLGSVITASRV 276
Cdd:cd18557 238 LWYGGYLVLSGQL 250
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
360-587 |
9.29e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 360 VRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSvhGRIAY-----------------------------VSQQPWVF 410
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVE--GVITYdgitpeeikkhyrgdvvynaetdvhfphlTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 411 SGTLRSNILFGKKYEKERYEKVIKACALKK-DLQLLEDgdlTVIGD---RGttLSGGQKARVNLARAVYQDADIYLLDDP 486
Cdd:TIGR00956 162 AARCKTPQNRPDGVSREEYAKHIADVYMATyGLSHTRN---TKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 487 LSAVDAEVSrhlfeLCICQILHEKITILVTHQLQYLKAASQ--------ILILKDGKMVQKGTYTE----FLKSGI---- 550
Cdd:TIGR00956 237 TRGLDSATA-----LEFIRALKTSANILDTTPLVAIYQCSQdayelfdkVIVLYEGYQIYFGPADKakqyFEKMGFkcpd 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 685504970 551 -----DFGSLLKKDNEESEQP----PVPGTPTLRNRTFSESSVWSQ 587
Cdd:TIGR00956 312 rqttaDFLTSLTSPAERQIKPgyekKVPRTPQEFETYWRNSPEYAQ 357
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
692-770 |
9.53e-05 |
|
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: 45.23 E-value: 9.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 692 IYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd18572 41 LLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLR 119
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
353-562 |
1.03e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVfSGTLR--SNILFgKKYEKERYE 430
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQLTgiENIEF-KMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 431 KVIKACaLKKDLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHlfelCICQILH-- 508
Cdd:PRK13546 118 KEIKAM-TPKIIEFSELGEF--IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK----CLDKIYEfk 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 509 --EKITILVTHQL-QYLKAASQILILKDGKMVQKG-------TYTEFLKsgiDFGSLLKKDNEE 562
Cdd:PRK13546 191 eqNKTIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGelddvlpKYEAFLN---DFKKKSKAEQKE 251
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
353-491 |
1.14e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------------RIAYVSQqpwvfsG------ 412
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrravcpRIAYMPQ------Glgknly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 -TL--RSNI-----LFGKKyEKERYEKVikacalkkdLQLLEDGDLTVIGDR--GtTLSGGQKARVNLARAVYQDADIYL 482
Cdd:NF033858 91 pTLsvFENLdffgrLFGQD-AAERRRRI---------DELLRATGLAPFADRpaG-KLSGGMKQKLGLCCALIHDPDLLI 159
|
....*....
gi 685504970 483 LDDPLSAVD 491
Cdd:NF033858 160 LDEPTTGVD 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
357-521 |
1.19e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 357 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--IAYVSQ-----QPwvfSGTLRSNILFGKKyekery 429
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKleVAYFDQhraelDP---EKTVMDNLAEGKQ------ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 430 ekvikacalkkdlqlledgDLTVIG----------------DRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSA 489
Cdd:PRK11147 410 -------------------EVMVNGrprhvlgylqdflfhpKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 685504970 490 VDAEVsrhlFELcicqiLHEKIT------ILVTHQLQY 521
Cdd:PRK11147 471 LDVET----LEL-----LEELLDsyqgtvLLVSHDRQF 499
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
689-762 |
1.66e-04 |
|
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: 44.51 E-value: 1.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685504970 689 YLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLP 762
Cdd:cd18559 40 YLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAP 113
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
353-418 |
1.70e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI--AY-----------VSQQPWVFSGTLRSNI 418
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigAYglrelrrqfsmIPQDPVLFDGTVRQNV 1404
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
348-546 |
1.78e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 348 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-LVSVHGRIAYVS---QQPWVFSGTLRSN--IL-- 419
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGeRQSQFSHITRLSfeqLQKLVSDEWQRNNtdMLsp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 420 ----FGKKYEKERYEKVIKACALKKDLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 495
Cdd:PRK10938 94 geddTGRTTAEIIQDEVKDPARCEQLAQQFGITAL--LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 685504970 496 RHLFELcICQILHEKITI-LVTHQLQYLKA-ASQILILKDGKMVQKGTYTEFL 546
Cdd:PRK10938 172 QQLAEL-LASLHQSGITLvLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
356-536 |
2.01e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.58 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 356 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------LVSVHGRIAYVSQQPWVFSGTLrsniLF-------G 421
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGeilldgkPVTAEQPEDYRKLFSAVFTDFH----LFdqllgpeG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 422 KKYEKERYEKVIKACALKKDLQLlEDGDLTvigdrGTTLSGGQKARVNLARAVYQDADIYLLDDplSAVDAE-VSRHLFE 500
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKLEL-EDGRIS-----NLKLSKGQKKRLALLLALAEERDILLLDE--WAADQDpHFRREFY 489
|
170 180 190
....*....|....*....|....*....|....*...
gi 685504970 501 LCICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKM 536
Cdd:PRK10522 490 QVLLPLLQEMgKTIFaISHDDHYFIHADRLLEMRNGQL 527
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
343-548 |
2.16e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.35 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 343 FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGelapshgLVSVHGRiayVSQQPWVFSGTlrsNILfgK 422
Cdd:PRK11022 13 FGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG-------LIDYPGR---VMAEKLEFNGQ---DLQ--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 423 KYEKERYEKV--------------IKAC---------ALK------------KDLQLLEdgdLTVIGDRGT-------TL 460
Cdd:PRK11022 78 ISEKERRNLVgaevamifqdpmtsLNPCytvgfqimeAIKvhqggnkktrrqRAIDLLN---QVGIPDPASrldvyphQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 461 SGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKIT-ILVTHQLQYL-KAASQILILKDGKMVQ 538
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlVLITHDLALVaEAAHKIIVMYAGQVVE 234
|
250
....*....|
gi 685504970 539 KGTYTEFLKS 548
Cdd:PRK11022 235 TGKAHDIFRA 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
351-536 |
2.63e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 351 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQpwvfsgTLRS 416
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISED------RKRD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 417 NILFGKKYeKERyekvIKACAL----KKDLQLLEDGDLTVIGD-----------RGTT---LSGGQKARVNLARAVYQDA 478
Cdd:PRK10762 340 GLVLGMSV-KEN----MSLTALryfsRAGGSLKHADEQQAVSDfirlfniktpsMEQAiglLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 479 DIYLLDDPLSAVDAEVSRHLFELcICQILHEKITI-LVTHQL-QYLKAASQILILKDGKM 536
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQL-INQFKAEGLSIiLVSSEMpEVLGMSDRILVMHEGRI 473
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
361-397 |
2.93e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 42.49 E-value: 2.93e-04
10 20 30
....*....|....*....|....*....|....*..
gi 685504970 361 RPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVH 397
Cdd:COG3709 3 GPGRLIYVVGPSGAGKDSLLAAARARLAADPRLVFAR 39
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
349-543 |
4.89e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 349 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG--ELAPSHGLVSVHGR--------------IAYVSQQPWVFSG 412
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdllelspedragegIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 413 TlrSNILF-------GKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLD 484
Cdd:PRK09580 93 V--SNQFFlqtalnaVRSYrGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685504970 485 DPLSAVDAEVSRHLFELCICQILHEKITILVTHQ---LQYLKaASQILILKDGKMVQKGTYT 543
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDFT 231
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
367-534 |
1.52e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 367 AVVGPVGAGKSSLLSAVL----GELAPS----HGLVSVHG---RIAYVsqqpwvfsgTLRSNILFGKKYEKERYEKVIKA 435
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNskggAHDPKLIRegeVRAQV---------KLAFENANGKKYTITRSLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 436 CAlkkdlqLLEDGDLTVIGDRG-TTLSGGQKA------RVNLARAVYQDADIYLLDDPLSAVDAE-VSRHLFELcICQIL 507
Cdd:cd03240 97 VI------FCHQGESNWPLLDMrGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEI-IEERK 169
|
170 180 190
....*....|....*....|....*....|
gi 685504970 508 HEKI--TILVTHQLQYLKAASQIL-ILKDG 534
Cdd:cd03240 170 SQKNfqLIVITHDEELVDAADHIYrVEKDG 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
459-545 |
1.55e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 459 TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVsrhLFELCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMV 537
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSHAREFLNTvVTDILHLHGQKLV 420
|
....*....
gi 685504970 538 Q-KGTYTEF 545
Cdd:PLN03073 421 TyKGDYDTF 429
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
332-543 |
1.62e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.17 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 332 KKMVHVQDFTAfwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGElaPSHGLVSvhGRIAYVSQQPWVFS 411
Cdd:CHL00131 5 KPILEIKNLHA---SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAYKILE--GDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 412 GTLRSN--ILFGKKYEKE------------RYEKVIKACALKK--DLQLLE--DGDLTVIGDRGTTL--------SGGQK 465
Cdd:CHL00131 78 PEERAHlgIFLAFQYPIEipgvsnadflrlAYNSKRKFQGLPEldPLEFLEiiNEKLKLVGMDPSFLsrnvnegfSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 466 ARVNLARAVYQDADIYLLDDPLSAVDAEVSRhlfelCICQILH-----EKITILVTHQ---LQYLKaASQILILKDGKMV 537
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALK-----IIAEGINklmtsENSIILITHYqrlLDYIK-PDYVHVMQNGKII 231
|
....*.
gi 685504970 538 QKGTYT 543
Cdd:CHL00131 232 KTGDAE 237
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
685-754 |
2.30e-03 |
|
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: 40.86 E-value: 2.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 685 DLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDI 754
Cdd:cd18541 38 QLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
442-541 |
2.38e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 442 LQLLEDGDLTVI--GDRGTTLSGGQKARVNLARAVYQDAD---IYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVT 516
Cdd:TIGR00630 810 LQTLCDVGLGYIrlGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEV-LQRLVDKGNTVVVI 888
|
90 100 110
....*....|....*....|....*....|..
gi 685504970 517 -HQLQYLKAASQILIL------KDGKMVQKGT 541
Cdd:TIGR00630 889 eHNLDVIKTADYIIDLgpeggdGGGTVVASGT 920
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
695-770 |
4.79e-03 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 39.71 E-value: 4.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685504970 695 GLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 770
Cdd:cd18552 47 GLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVR 122
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
307-385 |
5.96e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.91 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 307 SIRRIQTFLLLDEISQRNRQLPSD-GKKMVHVQDFTAfWDKA-SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL 384
Cdd:PRK13549 231 TEDDIITMMVGRELTALYPREPHTiGEVILEVRNLTA-WDPVnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLF 309
|
.
gi 685504970 385 G 385
Cdd:PRK13549 310 G 310
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
688-769 |
6.18e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 39.47 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 688 WYLGIYSGLTVATVLFGIARSLLVFYVLVNssqtLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLD 767
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVAR----LRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
..
gi 685504970 768 FI 769
Cdd:cd18557 117 LL 118
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
353-492 |
6.45e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 353 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH--GLVSVHG---------RIAYVSQQPWVFSG--TLRSNIL 419
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYieGDIRISGfpkkqetfaRISGYCEQNDIHSPqvTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 420 FGK--KYEKE--RYEKVIkacALKKDLQLLEDGDL--TVIGDRGTT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 492
Cdd:PLN03140 976 YSAflRLPKEvsKEEKMM---FVDEVMELVELDNLkdAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
684-753 |
9.32e-03 |
|
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: 39.03 E-value: 9.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 684 LDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKD 753
Cdd:cd18573 38 LSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSD 107
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
686-769 |
9.51e-03 |
|
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: 39.43 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685504970 686 LNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSkDIGHLDDLLPLTF 765
Cdd:COG2274 195 LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSL 273
|
....
gi 685504970 766 LDFI 769
Cdd:COG2274 274 LTAL 277
|
|
| |
