|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-833 |
1.71e-168 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 530.47 E-value: 1.71e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 12 PLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAendaqKPSLTRAIIKCYWKS 91
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKP-----KPWLLRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 92 YLVLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDSvalntAYAYATVLtFCTLILAIL-HHLYFYHVQCAGMRLRVAM 170
Cdd:PLN03130 303 FWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEPAWI-----GYIYAFSI-FVGVVLGVLcEAQYFQNVMRVGFRLRSTL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 171 CHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPL 250
Cdd:PLN03130 377 VAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPI 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 251 QSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNlaSFFSASkI 330
Cdd:PLN03130 457 QTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFN--SFILNS-I 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 331 IVFVT---FTTYVLLGSVITASRVFVAVTLYGAVRLTvtLF-FPSAIERVSEAIVSIRRIQTFLLLDE-ISQRNRQLPSd 405
Cdd:PLN03130 534 PVLVTvvsFGVFTLLGGDLTPARAFTSLSLFAVLRFP--LFmLPNLITQAVNANVSLKRLEELLLAEErVLLPNPPLEP- 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 406 GKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP-SHGLVSVHGRIAYVSQQPWV 484
Cdd:PLN03130 611 GLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPQVSWI 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 FSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PLN03130 691 FNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 565 VDAEVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKKDNEESEQPPVP 644
Cdd:PLN03130 771 LDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVEEN 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 645 GTPTLRNrtfsESSVWSQQSSRPSL-KDGALESQDTENVPVTLSEENRSEGKVGFQAYKNYFRA-GAHWIVFIfLILLNT 722
Cdd:PLN03130 851 GEEEDDQ----TSSKPVANGNANNLkKDSSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNAlGGAWVVMI-LFLCYV 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 723 AAQVAYVLQDWWLSYWANKQSmlnvtvngggnvTEKLDLNWYLGIYSGLTVATVLFGIARSllvfYVLVNSS----QTLH 798
Cdd:PLN03130 926 LTEVFRVSSSTWLSEWTDQGT------------PKTHGPLFYNLIYALLSFGQVLVTLLNS----YWLIMSSlyaaKRLH 989
|
810 820 830
....*....|....*....|....*....|....*
gi 157502203 799 NKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLD 833
Cdd:PLN03130 990 DAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDID 1024
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-844 |
6.97e-165 |
|
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: 518.73 E-value: 6.97e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 3 PVYQE--VKPNPLQD--ANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKE----------- 67
Cdd:TIGR00957 190 PLFSEtnHDPNPCPEssASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKEckktrkqpvsa 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 68 -------------------------VLRAENDAQKPSLTRAIIKCYWKSYLVLGIFTLIEESAKVIQPIFLGKIINYFEN 122
Cdd:TIGR00957 270 vygkkdpskpkgssqldaneevealIVKSPHKPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVND 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 123 YDPMDSvalnTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDV 202
Cdd:TIGR00957 350 PMAPDW----QGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDA 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 203 NKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITG 282
Cdd:TIGR00957 426 QRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 283 IRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLL--GSVITASRVFVAVTLYGA 360
Cdd:TIGR00957 506 IKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVdeNNILDAEKAFVSLALFNI 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 361 VRLTVTLFfPSAIERVSEAIVSIRRIQTFLLLDEI---SQRNRQLPSDGKKMVHVQDFTAFWDKaSETPTLQGLSFTVRP 437
Cdd:TIGR00957 586 LRFPLNIL-PMVISSIVQASVSLKRLRIFLSHEELepdSIERRTIKPGEGNSITVHNATFTWAR-DLPPTLNGITFSIPE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 438 GELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDL 517
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDL 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 518 QLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQ--ILHEKITILVTHQLQ 595
Cdd:TIGR00957 744 EILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTHGIS 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 596 YLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKK--------DNEES----------EQPPVPGTPTLRN------ 651
Cdd:TIGR00957 824 YLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTyapdeqqgHLEDSwtalvsgegkEAKLIENGMLVTDvvgkql 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 652 -RTFSESSVWSQQSSRPSLKDGALESQDTENVPVTLSEENRSE-GKVGFQAYKNYFRAGAHWIVF--IFLILLNTAAQVA 727
Cdd:TIGR00957 904 qRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQtGQVELSVYWDYMKAIGLFITFlsIFLFVCNHVSALA 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 728 yvlQDWWLSYWANkQSMLNVTVNgggNVTEKLDLNWYLGIYSGLTVatvlFGIARSLLVFYVLvnSSQTLHNKMFESILK 807
Cdd:TIGR00957 984 ---SNYWLSLWTD-DPMVNGTQN---NTSLRLSVYGALGILQGFAV----FGYSMAVSIGGIQ--ASRVLHQDLLHNKLR 1050
|
890 900 910
....*....|....*....|....*....|....*..
gi 157502203 808 APVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFI 844
Cdd:TIGR00957 1051 SPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM 1087
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
94-386 |
6.33e-164 |
|
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: 478.25 E-value: 6.33e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 94 VLGIFTLIEESAKVIQPIFLGKIINYFENydPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEG--NGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 174 IYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSC 253
Cdd:cd18593 79 IYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 254 FGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVF 333
Cdd:cd18593 159 FGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 334 VTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRI 386
Cdd:cd18593 239 LTFLAYILLGNILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-833 |
4.33e-160 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 505.67 E-value: 4.33e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 12 PLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAendaqKPSLTRAIIKCYWKS 91
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRP-----KPWLLRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 92 YLVLGIFTLIEESAKVIQPIFLGKIINYFENYDPMdsvalNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMC 171
Cdd:PLN03232 303 FWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDPA-----WVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 172 HMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQ 251
Cdd:PLN03232 378 AAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 252 SCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKII 331
Cdd:PLN03232 458 TLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVV 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 332 VFVTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFfPSAIERVSEAIVSIRRIQTFLLLDE-ISQRNRQLpSDGKKMV 410
Cdd:PLN03232 538 TLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNML-PNLLSQVVNANVSLQRIEELLLSEErILAQNPPL-QPGAPAI 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 411 HVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH-GLVSVHGRIAYVSQQPWVFSGTL 489
Cdd:PLN03232 616 SIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATV 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 RSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 570 SRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKKDNEESEQPPV-PGTPT 648
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVnTNDEN 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 649 LRNRTFSESSVWSQQSSrpslkdgALESQDTENVPVTLSEENRSEGKVGFQAYKNYFRA-GAHWIVFIfLILLNTAAQVA 727
Cdd:PLN03232 856 ILKLGPTVTIDVSERNL-------GSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAvGGLWVVMI-LLVCYLTTEVL 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 728 YVLQDWWLSYWANKQSMlnvtvngggnvtEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILK 807
Cdd:PLN03232 928 RVSSSTWLSIWTDQSTP------------KSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILR 995
|
810 820
....*....|....*....|....*.
gi 157502203 808 APVLFFDRNPIGRILNRFSKDIGHLD 833
Cdd:PLN03232 996 APMLFFHTNPTGRVINRFSKDIGDID 1021
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-845 |
1.21e-157 |
|
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: 499.05 E-value: 1.21e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 11 NPLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAEndaQKPSLTRAIIKCYWK 90
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAK---KNPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 91 SYLVLGIFTLIEESAKVIQPIFLGKIINyfeNYDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAM 170
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRIIA---SYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 171 CHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPL 250
Cdd:TIGR01271 158 FSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 251 QSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKI 330
Cdd:TIGR01271 238 QACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 331 IVFVTFTTYVLLGSVITaSRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRIQTFLLLDEISQRNRQLPSDGKKMV 410
Cdd:TIGR01271 318 VVFLSVVPYALIKGIIL-RRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 411 HVqdfTAFWD--------KASE-----------------------TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL 459
Cdd:TIGR01271 397 NV---TASWDegigelfeKIKQnnkarkqpngddglffsnfslyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 460 GELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQ 539
Cdd:TIGR01271 474 GELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 540 KARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTE 619
Cdd:TIGR01271 554 RARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSE 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 620 FLKSGIDFGSLL----KKDNEESE---------------------------------QPP-------------------- 642
Cdd:TIGR01271 634 LQAKRPDFSSLLlgleAFDNFSAErrnsiltetlrrvsidgdstvfsgpetikqsfkQPPpefaekrkqsiilnpiasar 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 643 -------------------------------VP----GTPTL------------------------------------RN 651
Cdd:TIGR01271 714 kfsfvqmgpqkaqattiedavrepserkfslVPedeqGEESLprgnqyhhglqhqaqrrqsvlqlmthsnrgenrreqLQ 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 652 RTFSESSVWSQQS---------SRPSLKDGALE--------------SQDTENVPVTLSeenrsegkvgFQAYKNYFRAG 708
Cdd:TIGR01271 794 TSFRKKSSITQQNelaseldiySRRLSKDSVYEiseeineedlkecfADERENVFETTT----------WNTYLRYITTN 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 709 AHWIVFIFLILLNTAAQVAYVLQDWWL----SYWANKQSMLNVTVNGGGNVTEKLDLN----WYLGIYSGLTVATVLFGI 780
Cdd:TIGR01271 864 RNLVFVLIFCLVIFLAEVAASLLGLWLitdnPSAPNYVDQQHANASSPDVQKPVIITPtsayYIFYIYVGTADSVLALGF 943
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 781 ARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:TIGR01271 944 FRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQ 1008
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
94-387 |
1.80e-129 |
|
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: 389.30 E-value: 1.80e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 94 VLGIFTLIEESAKVIQPIFLGKIINYFenyDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYF---VPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 174 IYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSC 253
Cdd:cd18594 78 IYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 254 FGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVF 333
Cdd:cd18594 158 LGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSF 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 157502203 334 VTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRIQ 387
Cdd:cd18594 238 ATFVPYVLTGNTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
410-610 |
1.38e-115 |
|
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: 349.85 E-value: 1.38e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTAFWDKASET--PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSG 487
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 157502203 568 EVSRHLFELCICQIL-HEKITILVTHQLQYLKAASQILILKDGK 610
Cdd:cd03250 161 HVGRHIFENCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
94-386 |
1.49e-114 |
|
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: 350.63 E-value: 1.49e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 94 VLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDsvaLNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEP---LSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 174 IYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSC 253
Cdd:cd18579 78 IYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 254 FGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVF 333
Cdd:cd18579 158 LAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 334 VTFTTYVLLGSVITASRVFVAVTLYGAVRlTVTLFFPSAIERVSEAIVSIRRI 386
Cdd:cd18579 238 ATFATYVLLGNPLTAAKVFTALSLFNLLR-FPLLMLPQAISSLIEALVSLKRI 289
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
79-845 |
7.75e-112 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 374.89 E-value: 7.75e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 79 SLTRAIIKCYWKSYLVLGIFTLIEESAKVIQPIFLGKIINYFEnydpmdsvALNTAYAYATVLTFcTLILA------ILH 152
Cdd:PTZ00243 233 SLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLD--------ADNATWGRGLGLVL-TLFLTqliqsvCLH 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 153 HLYFYHVQCaGMRLRVAMCHMIYRKALRLSNMAMGK--TTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLW 230
Cdd:PTZ00243 304 RFYYISIRC-GLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 231 MEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISki 310
Cdd:PTZ00243 383 RLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELR-- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 311 lrssCLRGMNLA----SFFS--ASKIIVFVTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFfPSAIERVSEAIVSIR 384
Cdd:PTZ00243 461 ----YLRDVQLArvatSFVNnaTPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMI-PWVFTTVLQFLVSIK 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 385 RIQTFLLLDEIS-------------QRNR---------------------QLPSDGKKM--------------------- 409
Cdd:PTZ00243 536 RISTFLECDNATcstvqdmeeywreQREHstacqlaavlenvdvtafvpvKLPRAPKVKtsllsralrmlcceqcrptkr 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 -----VHVQDF----------------TAFWDKASETPT---------------------LQGLSFTVRPGELLAVVGPV 447
Cdd:PTZ00243 616 hpspsVVVEDTdygspssasrhiveggTGGGHEATPTSErsaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGAT 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 448 GAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTV 527
Cdd:PTZ00243 696 GSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 528 IGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILK 607
Cdd:PTZ00243 776 IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALG 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 608 DGKMVQKGTYTEFLKSGI--DFGSLLK---------KDNEESEQPPVPGTPTLRNRTFsessvwSQQSSRPSLKDGAleS 676
Cdd:PTZ00243 856 DGRVEFSGSSADFMRTSLyaTLAAELKenkdskegdADAEVAEVDAAPGGAVDHEPPV------AKQEGNAEGGDGA--A 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 677 QDTENVPVTLSEENRSeGKVGFQAYKNYFRA--GAHWIVFIFLI-----LLNTAAQVayvlqdwWLSYWANKQsmlnvtv 749
Cdd:PTZ00243 928 LDAAAGRLMTREEKAS-GSVPWSTYVAYLRFcgGLHAAGFVLATfavteLVTVSSGV-------WLSMWSTRS------- 992
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 750 ngggnvtEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDI 829
Cdd:PTZ00243 993 -------FKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDI 1065
|
890
....*....|....*.
gi 157502203 830 GHLDDLLPLTFLDFIQ 845
Cdd:PTZ00243 1066 DILDNTLPMSYLYLLQ 1081
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
96-386 |
5.73e-80 |
|
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: 259.71 E-value: 5.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 96 GIFTLIEESAKVIQPIFLGKIINYFENydpmDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHMIY 175
Cdd:cd18595 3 ALLKLLSDILLFASPQLLKLLINFVED----PDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 176 RKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFG 255
Cdd:cd18595 79 RKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 256 KLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVT 335
Cdd:cd18595 159 RKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLAT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 336 FTTYVLLGS--VITASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 386
Cdd:cd18595 239 FATYVLSDPdnVLDAEKAFVSLSLFNILRFPLS-MLPMVISNLVQASVSLKRL 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
82-624 |
1.73e-77 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 262.41 E-value: 1.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 82 RAIIKCYWKSYLVLGIFTLIEESAKVIQPIFLGKIINyfenyDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQC 161
Cdd:COG1132 13 LRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIID-----ALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 162 AGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQ-VTVFLHFLWAGPLQAIAVTALLWM---EIGISC 237
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVidwRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 238 LAGMAVLIILLPLqscFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKS----FSNLITNLRKKEISKILRS 313
Cdd:COG1132 168 LLVLPLLLLVLRL---FGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 314 SCLrgMNLASFFSASKIIVFVTFTTYVLLGSVITASrVFVAVTLYgavrlTVTLFFP-----SAIERVSEAIVSIRRIQT 388
Cdd:COG1132 245 ALF--FPLMELLGNLGLALVLLVGGLLVLSGSLTVG-DLVAFILY-----LLRLFGPlrqlaNVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 389 FLLL-DEISQRNRQLP-SDGKKMVHVQDFTAFWDKasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH 466
Cdd:COG1132 317 LLDEpPEIPDPPGAVPlPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 467 G-------------LVSVHGRIAYVSQQPWVFSGTLRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVIGDRG 532
Cdd:COG1132 395 GrilidgvdirdltLESLRRQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 533 TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFElCICQILHEKITILVTHQLQYLKAASQILILKDGKMV 612
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570
....*....|..
gi 157502203 613 QKGTYTEFLKSG 624
Cdd:COG1132 554 EQGTHEELLARG 565
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
96-386 |
3.31e-75 |
|
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: 246.98 E-value: 3.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 96 GIFTLIEESAKVIQPIFLGKIINYFEN-YDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHMI 174
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEDaYLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 175 YRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCF 254
Cdd:cd18597 83 YRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 255 GKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFV 334
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 157502203 335 TFTTYVLLGSVITASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 386
Cdd:cd18597 243 SFITYYATGHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
710-845 |
1.88e-69 |
|
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: 232.21 E-value: 1.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 710 HWIVFIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNV------TVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARS 783
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDttdrvqGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 784 LLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQ 142
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
425-631 |
2.39e-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: 220.11 E-value: 2.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERY 504
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 505 EKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHE 584
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMAN 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 157502203 585 KITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLL 631
Cdd:cd03291 210 KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
94-386 |
9.20e-63 |
|
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: 213.90 E-value: 9.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 94 VLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDSValnTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDPGEDATV---RPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 174 IYRKALRLSNMA-------------------MGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIG 234
Cdd:cd18596 78 IFEKALRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 235 ISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSS 314
Cdd:cd18596 158 WSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRF 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157502203 315 CLRGMNLASFFSASKIIVFVTFTTYVLL-GSVITASRVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 386
Cdd:cd18596 238 LLDLLLSLLWFLIPILVTVVTFATYTLVmGQELTASVAFTSLALFNMLRGPLN-VLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
110-386 |
1.20e-62 |
|
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: 212.81 E-value: 1.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 110 PIFLGKIINYFENYDPmdsvALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNMamGKT 189
Cdd:cd18592 18 TILIRKLLEYLEDSDS----SVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRSL--GDK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 190 TTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFT 269
Cdd:cd18592 92 SVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVIT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 270 DARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGSVITAS 349
Cdd:cd18592 172 DKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLTAA 251
|
250 260 270
....*....|....*....|....*....|....*..
gi 157502203 350 RVFVAVTLYGAVRLTVTlFFPSAIERVSEAIVSIRRI 386
Cdd:cd18592 252 QAFTVIAVFNSMRFSLR-MLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
94-386 |
5.59e-59 |
|
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: 202.78 E-value: 5.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 94 VLGIFTLIEESAKVIQPIFLGKIINYFENydpmDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18598 1 PLGLLKLLADVLGFAGPLLLNKLVEFLED----SSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 174 IYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSC 253
Cdd:cd18598 77 VYRKALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 254 FGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEIS-----KILRSSClrgmnlaSFFSAS 328
Cdd:cd18598 157 IAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKalkgrKYLDALC-------VYFWAT 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 329 K--IIVFVTFTTYVLLGSVITASRVFVAVTLYGavRLTVTL-FFPSAIERVSEAIVSIRRI 386
Cdd:cd18598 230 TpvLISILTFATYVLMGNTLTAAKVFTSLALFN--MLIGPLnAFPWVLNGLVEAWVSLKRL 288
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
165-622 |
6.64e-58 |
|
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: 208.08 E-value: 6.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 165 RLRVAmchmIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDqvTVFLHFL------WAGPLQAIAVTALLWMEIGISCL 238
Cdd:COG4987 89 DLRVR----LYRRLEPLAPAGLARLRSGDLLNRLVADVDALD--NLYLRVLlpllvaLLVILAAVAFLAFFSPALALVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 239 AGMAVLIILLPLqscfgkLFSSL-----RSKTATFTDARIRTMnEVITGIRIIKMY----AWEKSFSNLITNLRKKEisk 309
Cdd:COG4987 163 LGLLLAGLLLPL------LAARLgrragRRLAAARAALRARLT-DLLQGAAELAAYgaldRALARLDAAEARLAAAQ--- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 310 ilrssclRGMNLASFFSASKIIVFVTFTTYVLLGSVITASR------VFVAVtlygAVRLTVTLF-----FPSAIERVSE 378
Cdd:COG4987 233 -------RRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAagalsgPLLAL----LVLAALALFealapLPAAAQHLGR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 379 AIVSIRRIqtFLLLDE---ISQRNRQLPSDGKKMVHVQDFTAFWDKASEtPTLQGLSFTVRPGELLAVVGPVGAGKSSLL 455
Cdd:COG4987 302 VRAAARRL--NELLDAppaVTEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 456 SAVLGELAPSHGLV-------------SVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKEryEKVIKACA---LKKDLQL 519
Cdd:COG4987 379 ALLLRFLDPQSGSItlggvdlrdldedDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD--EELWAALErvgLGDWLAA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 520 LEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKA 599
Cdd:COG4987 457 LPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLER 535
|
490 500
....*....|....*....|...
gi 157502203 600 ASQILILKDGKMVQKGTYTEFLK 622
Cdd:COG4987 536 MDRILVLEDGRIVEQGTHEELLA 558
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
90-624 |
1.40e-57 |
|
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: 207.30 E-value: 1.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 90 KSYLVLGI-FTLIEESAKVIQPIFLGKIIN-YFenydpMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLR 167
Cdd:COG4988 16 RRWLALAVlLGLLSGLLIIAQAWLLASLLAgLI-----IGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 168 VAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVnkfDQVTVFL-HFLwagPLQAIAVTALLWMEIGISCLAGMAVLII 246
Cdd:COG4988 91 RRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV---EALDGYFaRYL---PQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 247 LL--PLQSCFGKLFsslRSKTATFTDARIRTMN-------EVITGIRIIKMY----AWEKSFSNLITNLRKKEIsKILR- 312
Cdd:COG4988 165 LVtaPLIPLFMILV---GKGAAKASRRQWRALArlsghflDRLRGLTTLKLFgrakAEAERIAEASEDFRKRTM-KVLRv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 313 ---SSCLrgMNLASFFSASKIIVFVTFTtyvLLGSVITASRVFVAVTL----YGAVRLTVTLFFPSAiervsEAIVSIRR 385
Cdd:COG4988 241 aflSSAV--LEFFASLSIALVAVYIGFR---LLGGSLTLFAALFVLLLapefFLPLRDLGSFYHARA-----NGIAAAEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 386 IQTFLLLDE--ISQRNRQLPSDGKKMVHVQDFTAFWDkaSETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELA 463
Cdd:COG4988 311 IFALLDAPEpaAPAGTAPLPAAGPPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 464 PSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIG 529
Cdd:COG4988 389 PYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLG 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 530 DRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDG 609
Cdd:COG4988 469 EGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDG 547
|
570
....*....|....*
gi 157502203 610 KMVQKGTYTEFLKSG 624
Cdd:COG4988 548 RIVEQGTHEELLAKN 562
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
58-632 |
2.99e-57 |
|
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: 209.30 E-value: 2.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 58 EELQGFWDKEVLRAE-------NDAQKPSLTR--AIIKCYWKSY-------LVLGIFTLIeesakviQPIFLGKIInyfe 121
Cdd:COG2274 115 EEFAESWTGVALLLEptpefdkRGEKPFGLRWflRLLRRYRRLLlqvllasLLINLLALA-------TPLFTQVVI---- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 122 nydpmDSVALNTAYAYATVLT-------FCTLILAILHHLYFYHvqcAGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQI 194
Cdd:COG2274 184 -----DRVLPNQDLSTLWVLAiglllalLFEGLLRLLRSYLLLR---LGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 195 VNLLsNDVNKF-DQVTVFLHFLWAGPLQAIAVTALLWMeIGIScLAgmAVLIILLPLQSCFGKLFSSLRSKTA--TFTDA 271
Cdd:COG2274 256 ASRF-RDVESIrEFLTGSLLTALLDLLFVLIFLIVLFF-YSPP-LA--LVVLLLIPLYVLLGLLFQPRLRRLSreESEAS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 272 RIR--TMNEVITGIRIIKMYA--------WEKSFSNLI-TNLRKKEISKILrssclrgMNLASFFSASKIIVFVTFTTYV 340
Cdd:COG2274 331 AKRqsLLVETLRGIETIKALGaesrfrrrWENLLAKYLnARFKLRRLSNLL-------STLSGLLQQLATVALLWLGAYL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 341 LLGSVITASrVFVAVTLYgAVRLT---VTLFfpSAIERVSEAIVSIRRIQTFLLL--DEISQRNRQLPSDGKKMVHVQDF 415
Cdd:COG2274 404 VIDGQLTLG-QLIAFNIL-SGRFLapvAQLI--GLLQRFQDAKIALERLDDILDLppEREEGRSKLSLPRLKGDIELENV 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 416 TaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQP 482
Cdd:COG2274 480 S-FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDV 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 483 WVFSGTLRSNILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:COG2274 559 FLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 562 LSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLK 632
Cdd:COG2274 639 TSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
96-386 |
4.56e-54 |
|
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: 190.14 E-value: 4.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 96 GIFTLIEESAKVIQPIFLGKIINYFENYDPMDSVALNTA--------------YAYATVLTFCTLILAILHHLYFYHVQC 161
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLsvsyvtveeffsngYVLAVILFLALLLQATFSQASYHIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 162 AGMRLRVAMCHMIYRKALRLS--NMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLA 239
Cdd:cd18591 83 EGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 240 GMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEIsKILRSSCLRGM 319
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKEL-KLLLKDAVYWS 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 320 NLASFFSASKIIV-FVTFTTYVLL-GSVITASRVFVAVTLYGavRLTVTLF-FPSAIERVSEAIVSIRRI 386
Cdd:cd18591 242 LMTFLTQASPILVtLVTFGLYPYLeGEPLTAAKAFSSLALFN--QLTVPLFiFPVVIPILINAVVSTRRL 309
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
412-609 |
2.26e-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: 2.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 412 VQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-----------------SVHGR 474
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 475 IAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDAD 554
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 555 IYLLDDPLSAVDAEVSRHLFELCICQILHE--KITILVTHQLQYLKAASQILILKDG 609
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
423-610 |
1.03e-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: 152.92 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTL 489
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 RSNIlfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:cd03228 93 RENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157502203 570 SRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGK 610
Cdd:cd03228 132 EALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
423-624 |
2.00e-42 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 154.31 E-value: 2.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------LVSVHGRIAYVSQQPWVFSGTL 489
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirdisRKSLRSMIGVVLQDTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 RSNILFGKKYEKEryEKVIKACALKKDLQL---LEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:cd03254 94 MENIRLGRPNATD--EEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 567 AEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:cd03254 172 TE-TEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
421-615 |
1.96e-40 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 148.51 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 421 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG 487
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:cd03245 93 TLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157502203 567 AEVSRHLFElCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKG 615
Cdd:cd03245 173 MNSEERLKE-RLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
386-637 |
4.38e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 156.93 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 386 IQTFLLLDEISQRN--RQLPSDGKKMVHVQDFTAFwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELa 463
Cdd:PRK11174 324 LVTFLETPLAHPQQgeKELASNDPVTIEAEDLEIL--SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 464 PSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVIG 529
Cdd:PRK11174 401 PYQGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 530 DRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDG 609
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH-SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
250 260
....*....|....*....|....*...
gi 157502203 610 KMVQKGTYTEFLKSGIDFGSLLKKDNEE 637
Cdd:PRK11174 560 QIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
424-624 |
6.67e-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: 147.38 E-value: 6.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLR 490
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNILFGKKYE-KERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEv 569
Cdd:cd03251 94 ENIAYGRPGAtREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTE- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 570 SRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:cd03251 173 SERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
424-624 |
2.42e-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: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 490
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlrwlrsQIGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNILFGKKYEK-ERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEv 569
Cdd:cd03249 95 ENIRYGKPDATdEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 570 SRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:cd03249 174 SEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
424-606 |
4.01e-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: 152.83 E-value: 4.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 490
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNILFGKKYEKE-RYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:TIGR02857 414 ENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|....*....
gi 157502203 570 SRHLFE--LCICQilhEKITILVTHQLQYLKAASQILIL 606
Cdd:TIGR02857 494 EAEVLEalRALAQ---GRTVLLVTHRLALAALADRIVVL 529
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
127-624 |
7.20e-39 |
|
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: 152.93 E-value: 7.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 127 DSVALNTAYAYATVLTfctLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFD 206
Cdd:TIGR02204 53 SSGLLNRYFAFLLVVA---LVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 207 QV--TVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLqSCFGKlfsSLRSKTATFTDaRIRTMN----EVI 280
Cdd:TIGR02204 130 SVigSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPI-LLFGR---RVRKLSRESQD-RIADAGsyagETL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 281 TGIRIIKMYAWEKSFSNLITnlrkKEISKILRSSCLRGMNLASFFSASKIIVF--VTFTTYVLLGSVITASrvFVAVTLY 358
Cdd:TIGR02204 205 GAIRTVQAFGHEDAERSRFG----GAVEKAYEAARQRIRTRALLTAIVIVLVFgaIVGVLWVGAHDVIAGK--MSAGTLG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 359 GAVRLTVtlFFPSAIERVSEAIVSIRRI-----QTFLLLDEISQ-----RNRQLPSDGKKMVHVQDFTAFWDKASETPTL 428
Cdd:TIGR02204 279 QFVFYAV--MVAGSIGTLSEVWGELQRAagaaeRLIELLQAEPDikapaHPKTLPVPLRGEIEFEQVNFAYPARPDQPAL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 429 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILF 495
Cdd:TIGR02204 357 DGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVMENIRY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 496 GKKYEKEryEKVIKACALKKD---LQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvSRH 572
Cdd:TIGR02204 437 GRPDATD--EEVEAAARAAHAhefISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAE-SEQ 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 157502203 573 LFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:TIGR02204 514 LVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG 565
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
408-609 |
4.89e-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: 4.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 408 KMVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------RIAYVS 479
Cdd:COG1121 5 PAIELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 480 QQ---PWVF---------SGTLRSNILFgKKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDR--GtTLSGGQKARVNL 545
Cdd:COG1121 82 QRaevDWDFpitvrdvvlMGRYGRRGLF-RRPSRADREAVDEA---------LERVGLEDLADRpiG-ELSGGQQQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 546 ARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITIL-VTHQLQYL-KAASQILILKDG 609
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYEL-LRELRREGKTILvVTHDLGAVrEYFDRVLLLNRG 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
165-594 |
3.39e-37 |
|
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: 147.12 E-value: 3.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 165 RLRVAMchmiYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPL----QAIAVTALLWMEIGISCLAG 240
Cdd:TIGR02868 87 ALRVRV----YERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALvvgaAAVAAIAVLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 241 MAVLIILLPLqscfgklFSSLRSKTATFTDARIRtmNEVITGIRIIKMYAWEKSFSNLITNLRKK------EISKILRSS 314
Cdd:TIGR02868 163 LLLAGFVAPL-------VSLRAARAAEQALARLR--GELAAQLTDALDGAAELVASGALPAALAQveeadrELTRAERRA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 315 ClRGMNLASffSASKIIVFVTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLF-----FPSAIERVSEAIVSIRRIqTF 389
Cdd:TIGR02868 234 A-AATALGA--ALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFeafaaLPAAAQQLTRVRAAAERI-VE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 390 LLLDEISQRNRQLPSDG-----KKMVHVQDFTAFWDKASetPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP 464
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGavglgKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 465 SHGLVSVHG-------------RIAYVSQQPWVFSGTLRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVIGD 530
Cdd:TIGR02868 388 LQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 531 RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQL 594
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
403-611 |
2.71e-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: 2.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 403 PSDGKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV----------- 471
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpisqyehk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 472 --HGRIAYVSQQPWVFSGTLRSNILFG---KKYEKeryekvIKACALKKD----LQLLEDGDLTVIGDRGTTLSGGQKAR 542
Cdd:cd03248 85 ylHSKVSLVGQEPVLFARSLQDNIAYGlqsCSFEC------VKEAAQKAHahsfISELASGYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 543 VNLARAVYQDADIYLLDDPLSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKM 611
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 ... |
426-624 |
5.41e-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: 136.21 E-value: 5.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLRSN 492
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrraIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:cd03253 95 IRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 572 HLFElCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:cd03253 175 EIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
423-623 |
6.91e-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: 143.74 E-value: 6.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTL 489
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 RSNI-LFGKkyekERYEKVIKACALK--KDLQL-LEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:COG4618 423 AENIaRFGD----ADPEKVVAAAKLAgvHEMILrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 566 DAEVSRHLFELcicqILHEK----ITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKS 623
Cdd:COG4618 499 DDEGEAALAAA----IRALKargaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
373-617 |
1.02e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 143.31 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 373 IERVSEAIVSIRRiqtflLLDE---ISQRNRQLPsDGKKMVHVqDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGA 449
Cdd:PRK10789 280 VERGSAAYSRIRA-----MLAEapvVKDGSEPVP-EGRGELDV-NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 450 GKSSLLSAVLGELAPSHGLVSVH-------------GRIAYVSQQPWVFSGTLRSNILFGK-KYEKERYEKVIKACALKK 515
Cdd:PRK10789 353 GKSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHD 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 516 DLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRhlfelcicQILH-------EKITI 588
Cdd:PRK10789 433 DILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH--------QILHnlrqwgeGRTVI 504
|
250 260
....*....|....*....|....*....
gi 157502203 589 LVTHQLQYLKAASQILILKDGKMVQKGTY 617
Cdd:PRK10789 505 ISAHRLSALTEASEILVMQHGHIAQRGNH 533
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
89-631 |
1.05e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 144.86 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 89 WKSYLVLGIFTLIEESAKVIQPIFLGKIINyfenydpmDSVALNTAYAYATVLTFctliLAILHHLYFYHVQCAGMRLRV 168
Cdd:TIGR00958 160 WPWLISAFVFLTLSSLGEMFIPFYTGRVID--------TLGGDKGPPALASAIFF----MCLLSIASSVSAGLRGGSFNY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 169 AMCHM-------IYRKALRLSNMAMGKTTTGQIVNLLSNDVNKF-----DQVTVFLHFLwagplqaIAVTALLWMEIGIS 236
Cdd:TIGR00958 228 TMARInlriredLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsrslsLNVNVLLRNL-------VMLLGLLGFMLWLS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 237 CLAGMaVLIILLPL----QSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKS----FSNLITNL----RK 304
Cdd:TIGR00958 301 PRLTM-VTLINLPLvflaEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETlqlnKR 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 305 KEISKIL----RSSCLRGMNLASFFSASKIIV--------FVTFTTYVLLgsviTASRVFVAVTLYGAVRLTVtlffpSA 372
Cdd:TIGR00958 380 KALAYAGylwtTSVLGMLIQVLVLYYGGQLVLtgkvssgnLVSFLLYQEQ----LGEAVRVLSYVYSGMMQAV-----GA 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 373 IERVseaivsirriqtFLLLDeisqRNRQLPSDGKKM-------VHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVG 445
Cdd:TIGR00958 451 SEKV------------FEYLD----RKPNIPLTGTLAplnleglIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVG 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 446 PVGAGKSSLLSAVLGELAPSHGLV-------------SVHGRIAYVSQQPWVFSGTLRSNILFG-KKYEKERYEKVIKAC 511
Cdd:TIGR00958 515 PSGSGKSTVAALLQNLYQPTGGQVlldgvplvqydhhYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAA 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 512 ALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcicQILHEKITILVT 591
Cdd:TIGR00958 595 NAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIA 671
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 157502203 592 HQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLL 631
Cdd:TIGR00958 672 HRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
714-845 |
1.73e-35 |
|
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: 136.48 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 714 FIFLILLNTAAQVAYVLQDWWLSYWANKQSMlnvtvngggnvTEKLDLNWYLGIYSGLTV-ATVLFGIARSLLVFYVLVN 792
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSS-----------SPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLR 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 793 SSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd18580 70 ASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQ 122
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
423-607 |
6.06e-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: 132.27 E-value: 6.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------RIAYVSQQ---PWVFSGT--- 488
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRrsiDRDFPISvrd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 -----LRSNILFGKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:cd03235 90 vvlmgLYGHKGLFRRLSKADKAKV---------DEALERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 157502203 563 SAVDAEVSRHLFELcICQILHEKITIL-VTHQL-QYLKAASQILILK 607
Cdd:cd03235 161 AGVDPKTQEDIYEL-LRELRREGMTILvVTHDLgLVLEYFDRVLLLN 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
428-636 |
1.14e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.49 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSNIL 494
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 495 F-------GKKYEKERYEKVIKACALKKdlqlledgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTD-----------AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157502203 568 EVSRHLFELcICQILHEKITILV-THQLQYL-KAASQILILKDGKMVQKGTYTEFLKSGID--FGSLLKKDNE 636
Cdd:COG1131 165 EARRELWEL-LRELAAEGKTVLLsTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLLEdvFLELTGEEAR 236
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
135-386 |
1.49e-34 |
|
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: 133.88 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 135 YAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHF 214
Cdd:cd18559 38 QVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 215 LWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKS 294
Cdd:cd18559 118 MWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 295 FSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGS--VITASRVFVAVTLYGAVRLTVTLfFPSA 372
Cdd:cd18559 198 FIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSlaGLVALKVFYSLALTTYLNWPLNM-SPEV 276
|
250
....*....|....
gi 157502203 373 IERVSEAIVSIRRI 386
Cdd:cd18559 277 ITNIVAAEVSLERS 290
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
423-615 |
6.90e-33 |
|
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: 125.12 E-value: 6.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSGTLR 490
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNIlfgkkyekeryekvikacalkkdlqlledgdltvigdrGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 570
Cdd:cd03247 93 NNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157502203 571 RHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKG 615
Cdd:cd03247 135 RQLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
711-845 |
8.62e-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: 128.74 E-value: 8.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 711 WIVFIFLILLntaAQVAYVLQDWWLSYWANKQSMLNVTVNGGGNVtekldlNWYLGIYSGLTVATVLFGIARSLLVFYVL 790
Cdd:cd18604 1 WALLLLLFVL---SQLLSVGQSWWLGIWASAYETSSALPPSEVSV------LYYLGIYALISLLSVLLGTLRYLLFFFGS 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 791 VNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd18604 72 LRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLE 126
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
410-615 |
1.04e-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: 123.01 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYV 478
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 479 SQQPWVFSG-TLRSNILFG----KKYEKERYEKVIKAcalkkdLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQDA 553
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlklrGVPKAEIRARVREL------LELVGLEGL--LNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 554 DIYLLDDPLSAVDAEVSRHLFELcICQILHE--KITILVTH-QLQYLKAASQILILKDGKMVQKG 615
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREE-LKELQRElgITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
404-609 |
1.90e-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: 123.66 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 404 SDGKKMVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------R 474
Cdd:COG1116 2 SAAAPALELRGVSkRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 475 IAYVSQQ----PWVfsgTLRSNILFG----KKYEKERYEKVikacalkkdLQLLEDGDLTvigDRGT----TLSGGQKAR 542
Cdd:COG1116 82 RGVVFQEpallPWL---TVLDNVALGlelrGVPKAERRERA---------RELLELVGLA---GFEDayphQLSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 543 VNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KITIL-VTHQLQ---YLkaASQILILKDG 609
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDE-LLRLWQEtGKTVLfVTHDVDeavFL--ADRVVVLSAR 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
409-616 |
2.65e-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: 123.23 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFTAfwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RI 475
Cdd:COG1120 1 MLEAENLSV---GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 476 AYVSQQPWV-FSGTLRSNILFG--------KKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVNL 545
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphlglfGRPSAEDREAVEEA---------LERTGLEHLADRPvDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 546 ARAVYQDADIYLLDDPLSAVD----AEVSRHLFELCICQilhEKITILVTHQL----QYlkaASQILILKDGKMVQKGT 616
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARER---GRTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGP 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
410-616 |
2.68e-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: 122.22 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTAFWDKASEtPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIA 476
Cdd:cd03244 3 IEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 477 YVSQQPWVFSGTLRSNI-LFGKKYEKERYEkVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADI 555
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 556 YLLDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGT 616
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 ... |
424-611 |
3.03e-31 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 120.40 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLR 490
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnelgdHVGYLPQDDELFSGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNIlfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 570
Cdd:cd03246 94 ENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157502203 571 RHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKM 611
Cdd:cd03246 133 RALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
428-615 |
6.16e-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: 119.85 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQqpwvfsgtlrsnil 494
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 495 fgkkyekeryekvikacalkkdlqLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 573
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157502203 574 FELcICQILHE--KITILVTHQL-QYLKAASQILILKDGKMVQKG 615
Cdd:cd03214 137 LEL-LRRLARErgKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
417-606 |
7.80e-31 |
|
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: 120.65 E-value: 7.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 417 AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------IAYVSQQ----PWV 484
Cdd:cd03293 9 TYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQdallPWL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 fsgTLRSNILFG----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:cd03293 89 ---TVLDNVALGlelqGVPKAEARERA---------EELLELVGLSGFENAyPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157502203 560 DPLSAVDAEVSRHLFELcICQILHE--KITILVTHQLQ---YLkaASQILIL 606
Cdd:cd03293 157 EPFSALDALTREQLQEE-LLDIWREtgKTVLLVTHDIDeavFL--ADRVVVL 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
428-563 |
9.61e-31 |
|
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: 118.13 E-value: 9.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG-TLRSNI 493
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 494 LFGKkyEKERYEKVIKACALKKDLQLLEDGDL--TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
426-622 |
1.55e-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: 120.73 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSN 492
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 I-LFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeVSR 571
Cdd:COG4555 95 IrYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-----GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MAR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 572 HLFELCICQILHEKITILV-THQLQYLKA-ASQILILKDGKMVQKGTYTEFLK 622
Cdd:COG4555 169 RLLREILRALKKEGKTVLFsSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
710-845 |
1.58e-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: 122.67 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 710 HWIVFIFLILLNTAAQVAYVLQDWWLSYW-----ANKQSMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSL 784
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 785 LVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQ 141
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
714-844 |
2.29e-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: 121.82 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 714 FIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNVTVNGggnvteklDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNS 793
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTE--------QRDYRLGVYGALGLGQAIFVFLGSLALALGCVRA 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 157502203 794 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFI 844
Cdd:cd18603 73 SRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFL 123
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
714-844 |
5.26e-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: 120.71 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 714 FIFLILLNTAAQVAYVLQDWWLSYWANKQsmlnvtvNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNS 793
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHS-------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRA 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 157502203 794 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFI 844
Cdd:cd18605 74 ARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILL 124
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
426-647 |
7.06e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 125.84 E-value: 7.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSN 492
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGKK--YEKERYEKVIKACALkkDLQLL-EDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK13657 429 IRVGRPdaTDEEMRAAAERAQAH--DFIERkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 570 SRHLfELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLK-----KDNEESEQPPVP 644
Cdd:PRK13657 507 EAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRaqgmlQEDERRKQPAAE 585
|
...
gi 157502203 645 GTP 647
Cdd:PRK13657 586 GAN 588
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
418-624 |
8.52e-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: 8.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 418 FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV 484
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 FSGTLRSNILFGKkyEKERYEKVIKACALKKD---LQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:cd03252 88 FNRSIRDNIALAD--PGMSMERVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157502203 562 LSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:cd03252 166 TSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
428-616 |
1.26e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.02 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQP------WVFSG-------TLRSNIL 494
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvgFVFQHyalfphmTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 495 FG----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA-- 567
Cdd:COG1118 98 FGlrvrPPSKAEIRARV---------EELLELVQLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkv 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 568 --EVSRHLFElcicqiLHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGT 616
Cdd:COG1118 169 rkELRRWLRR------LHDELggtTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
423-621 |
1.74e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 124.55 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTL 489
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 RSNILFGK-KYEKERYEKVIKACALKKdlqLLEDGD-L-TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK11160 431 RDNLLLAApNASDEALIEVLQQVGLEK---LLEDDKgLnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 567 AEVSRHLFELcICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL 621
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 ... |
412-610 |
1.75e-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: 116.41 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 412 VQDFTAFWDKaSETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYV 478
Cdd:cd03225 2 LKNLSFSYPD-GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 479 SQQP--WVFSGTLRSNILFGKKYEKERYEKVIkacalKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADI 555
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIE-----ERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 556 YLLDDPLSAVDAEVSRHLFELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGK 610
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLEL-LKKLKAEGKTIIiVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
711-845 |
3.23e-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: 118.35 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 711 WIVFIFLILLntaAQVAYVLQDWWLSYWANKqsmlnvtvngggnvTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVL 790
Cdd:cd18606 1 LPLLLLLLIL---SQFAQVFTNLWLSFWTED--------------FFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLG 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 791 VNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd18606 64 IRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLY 118
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
421-611 |
8.29e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.53 E-value: 8.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 421 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG 487
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGKKYEKERYEKViKACALKKDLQLledgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:COG4619 89 TVRDNLPFPFQLRERKFDRE-RALELLERLGL----PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 157502203 568 EVSRHLFELcICQILHEK-ITIL-VTH-QLQYLKAASQILILKDGKM 611
Cdd:COG4619 164 ENTRRVEEL-LREYLAEEgRAVLwVSHdPEQIERVADRVLTLEAGRL 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
424-619 |
1.99e-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: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVF-SGTLRS 491
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQSYALYpHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 NILFG----KKYEKERYEKVIKACALkkdLQLLEdgdltvIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG3839 95 NIAFPlklrKVPKAEIDRRVREAAEL---LGLED------LLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 567 AEvSRHLFELCICQiLHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 619
Cdd:COG3839 166 AK-LRVEMRAEIKR-LHRRLgttTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
426-606 |
4.47e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.94 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQ---PWVFSGTLRSNI---LFGK 497
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 498 KYEKERY----EKVIKACALKKDLQLLEDGDLTvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 573
Cdd:NF040873 86 RGLWRRLtrddRAAVDDALERVGLADLAGRQLG-------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190
....*....|....*....|....*....|....
gi 157502203 574 FELcICQILHEKITIL-VTHQLQYLKAASQILIL 606
Cdd:NF040873 159 IAL-LAEEHARGATVVvVTHDLELVRRADPCVLL 191
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
424-622 |
5.30e-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: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPW--VFSGT 488
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 LRSNILFGKKY----EKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:COG1122 93 VEEDVAFGPENlglpREEIRERVEEA---------LELVGLEHLADRPPhELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 564 AVDAEVSRHLFELcICQILHEKIT-ILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLK 622
Cdd:COG1122 164 GLDPRGRRELLEL-LKRLNKEGKTvIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
423-620 |
4.01e-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: 110.74 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPW--- 483
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMIFQQFNlie 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 484 -------VFSG------TLRSniLFGKKYEKERYekviKACALKKDLQLLEDgdltvIGDRGTTLSGGQKARVNLARAVY 550
Cdd:cd03256 92 rlsvlenVLSGrlgrrsTWRS--LFGLFPKEEKQ----RALAALERVGLLDK-----AYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 551 QDADIYLLDDPLSAVDAEVSRHLFELC--ICQilHEKITILVT-HQLQYLKA-ASQILILKDGKMVQKGTYTEF 620
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLkrINR--EEGITVIVSlHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
409-619 |
4.75e-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: 110.36 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 473
Cdd:cd03258 1 MIELKNVSkVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 --RIAYVSQQPWVFSG-TLRSNILF----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNL 545
Cdd:cd03258 81 rrRIGMIFQHFNLLSSrTVFENVALpleiAGVPKAEIEERV---------LELLELVGLEDKADAyPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 546 ARAVYQDADIYLLDDPLSAVDAEVSRHLFELcicqiLHE-----KITI-LVTHQLQYLKA-ASQILILKDGKMVQKGTYT 618
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILAL-----LRDinrelGLTIvLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
.
gi 157502203 619 E 619
Cdd:cd03258 227 E 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
93-365 |
1.09e-26 |
|
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: 110.43 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 93 LVLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDSVALNtayAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCH 172
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALN---VYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 173 MIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGIS-CLAGMAVLIILLPLQ 251
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 252 SCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKII 331
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 157502203 332 VFVT--FTTYVLLGSVITASRVFVAVTLYGAVRLTV 365
Cdd:pfam00664 239 YALAlwFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
424-616 |
1.59e-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: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQqpwvfSGTL--- 489
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQ-----DYALfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 ---RSNILFG----KKYEKERYEKVIKACALkkdLQLledGDLtviGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:COG3842 92 ltvAENVAFGlrmrGVPKAEIRARVAELLEL---VGL---EGL---ADRYpHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 562 LSAVDAEVSRHL-FELciCQILHE-KIT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 616
Cdd:COG3842 163 LSALDAKLREEMrEEL--RRLQRElGITfIYVTHdQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
714-859 |
2.40e-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: 110.39 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 714 FIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNVTVNGGGNVTEKLDLNW-YLGIYSGLTVATVLFGIARSLLVFYVLVN 792
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSyYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 793 SSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQRWdLAVLSWLVSNS 859
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFL-LLCLSAIIVNA 146
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
410-621 |
4.86e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 113.96 E-value: 4.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL-------GE-LAPSHG-----LVSVHGRIA 476
Cdd:PRK11176 342 IEFRNVT-FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTrfydideGEiLLDGHDlrdytLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 477 YVSQQPWVFSGTLRSNILF--GKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDAD 554
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 555 IYLLDDPLSAVDAEvSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL 621
Cdd:PRK11176 501 ILILDEATSALDTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
426-630 |
5.20e-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: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLRSN 492
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGKKyEKERYEKVIKACAL---KKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:TIGR01193 568 LLLGAK-ENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 570 SRHLFELCIcqILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSL 630
Cdd:TIGR01193 647 EKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
426-619 |
1.21e-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: 106.27 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNI 493
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 LFGKKyEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 572
Cdd:cd03296 96 AFGLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157502203 573 LFELciCQILHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 619
Cdd:cd03296 175 LRRW--LRRLHDELhvtTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
425-623 |
1.64e-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: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG-TLR 490
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNI-LFGK--KYEKERYEKVIKacalkkdlQLLEDGDLTVIGDRG---TTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:cd03295 94 ENIaLVPKllKWPKEKIRERAD--------ELLALVGLDPAEFADrypHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 565 VDAEVSRHLFE--LCICQILHEKItILVTHQLQ-YLKAASQILILKDGKMVQKGTYTEFLKS 623
Cdd:cd03295 166 LDPITRDQLQEefKRLQQELGKTI-VFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
409-610 |
1.74e-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: 104.87 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIA 476
Cdd:COG4133 2 MLEAENLSCRRG---ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 477 YVSQQPWVFSG-TLRSNILFgkkyekeryekvikACALKKD-------LQLLEDGDLTVIGDR-GTTLSGGQKARVNLAR 547
Cdd:COG4133 79 YLGHADGLKPElTVRENLRF--------------WAALYGLradreaiDEALEAVGLAGLADLpVRQLSAGQKRRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 548 AVYQDADIYLLDDPLSAVDAEvSRHLFElcicQILHE-----KITILVTHQLQYLKAAsQILILKDGK 610
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAA-GVALLA----ELIAAhlargGAVLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
409-606 |
1.97e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.87 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP---SHGLVSVHG-----------R 474
Cdd:COG4136 1 MLSLENLTITLGG---RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltalpaeqrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 475 IAYVSQQPWVFSG-TLRSNILFG-----KKyeKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVNLAR 547
Cdd:COG4136 78 IGILFQDDLLFPHlSVGENLAFAlpptiGR--AQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 548 AVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKI-TILVTHQLQYLKAASQILIL 606
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
424-623 |
2.16e-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: 105.66 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWVFSG 487
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 -TLRSNILFGKKYEKERYEKVIKACALKKdlqlledgdLTVIGDRGTT------LSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:cd03261 92 lTVFENVAFPLREHTRLSEEEIREIVLEK---------LEAVGLRGAEdlypaeLSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 561 PLSAVDAEVSRHLFELcicqI--LHEKI---TILVTHQLQ-YLKAASQILILKDGKMVQKGTYTEFLKS 623
Cdd:cd03261 163 PTAGLDPIASGVIDDL----IrsLKKELgltSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
424-610 |
3.17e-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: 104.49 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------------IAYVSQQPWVFS 486
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 487 G-TLRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLtviGDRGT----TLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:cd03255 96 DlTALENVELPL-----LLAGVPKKERRERAEELLERVGL---GDRLNhypsELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157502203 562 LSAVDAEVSRHLFELcICQILHEKIT--ILVTHQLQYLKAASQILILKDGK 610
Cdd:cd03255 168 TGNLDSETGKEVMEL-LRELNKEAGTtiVVVTHDPELAEYADRIIELRDGK 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
428-611 |
4.03e-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: 102.86 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSNIl 494
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEEPSLYENlTVRENL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 495 fgkkyekeryekvikacalkkdlqlledgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 574
Cdd:cd03230 95 ---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 157502203 575 ELcICQILHEKITILV-THQLQYLKA-ASQILILKDGKM 611
Cdd:cd03230 136 EL-LRELKKEGKTILLsSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
424-610 |
5.85e-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: 101.94 E-value: 5.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQqpwvfsgtlr 490
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiaklpleelrrRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 snilfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvS 570
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-S 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157502203 571 RHLFELCICQILHEKITIL-VTHQLQYL-KAASQILILKDGK 610
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 ... |
427-612 |
7.17e-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: 103.11 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 427 TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------IAYVSQQP--WVFSGTLRSNIL 494
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrksIGYVMQDVdyQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 495 FGKKYEKERYEKVikACALKK-DLQLLEDgdltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 573
Cdd:cd03226 95 LGLKELDAGNEQA--ETVLKDlDLYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 157502203 574 FELcicqILH----EKITILVTHQLQYL-KAASQILILKDGKMV 612
Cdd:cd03226 166 GEL----IRElaaqGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
409-650 |
1.33e-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: 108.84 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPS---HGLVSVHG------------ 473
Cdd:COG1123 4 LLEVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelsealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 -RIAYVSQQPWV--FSGTLRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAV 549
Cdd:COG1123 83 rRIGMVFQDPMTqlNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYPhQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 550 YQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKIT--ILVTHQLQY-LKAASQILILKDGKMVQKGTYTEFLKSGID 626
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDL-LRELQRERGTtvLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
250 260
....*....|....*....|....*.
gi 157502203 627 FGSL--LKKDNEESEQPPVPGTPTLR 650
Cdd:COG1123 237 LAAVprLGAARGRAAPAAAAAEPLLE 262
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
409-623 |
2.57e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 102.96 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFTA-FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------R 474
Cdd:COG1124 1 MLEVRNLSVsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 475 IAYVSQQP-----------WVFSGTLRsniLFGKKYEKERYEKVIKACALKKDLQlledgdltvigDR-GTTLSGGQKAR 542
Cdd:COG1124 81 VQMVFQDPyaslhprhtvdRILAEPLR---IHGLPDREERIAELLEQVGLPPSFL-----------DRyPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 543 VNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KIT-ILVTHQLQYLKA-ASQILILKDGKMVQKGTYTE 619
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNL-LKDLREErGLTyLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
....
gi 157502203 620 FLKS 623
Cdd:COG1124 226 LLAG 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
428-623 |
2.81e-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: 102.41 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------RIAYVSQQPWVFSG-TLRSNILF 495
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 496 GKKyeKERYEKVIKAcalKKDLQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 574
Cdd:cd03299 95 GLK--KRKVDKKEIE---RKVLEIAEMLGIDHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 157502203 575 ELcICQILHE-KITIL-VTHQLQYLKA-ASQILILKDGKMVQKGTYTEFLKS 623
Cdd:cd03299 170 EE-LKKIRKEfGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
407-612 |
3.01e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.04 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 407 KKMVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------- 474
Cdd:COG1136 2 SPLLELRNLTkSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 475 ------IAYVSQQPWVFSG-TLRSNI----LFGKKYEKERYEKVikacalkkdLQLLED-GdltvIGDRG----TTLSGG 538
Cdd:COG1136 82 rlrrrhIGFVFQFFNLLPElTALENValplLLAGVSRKERRERA---------RELLERvG----LGDRLdhrpSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 539 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKMV 612
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELgTTIVmVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
410-615 |
7.32e-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: 7.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYV 478
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 479 SQQPWVFSG-TLRSNILFGKKYEKERY----EKVIKACALKKDLQLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDA 553
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGLKLRKVPKdeidERVREVAELLQIEHLLDR--------KPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 554 DIYLLDDPLSAVDAEVSRHL-FELCICQILHEKITILVTH-QLQYLKAASQILILKDGKMVQKG 615
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMrAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
428-620 |
1.09e-23 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 100.33 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAV-----LGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG 487
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGKKYEKERYEKVIKAcalkKDLQLLEDGDLT-VIGDR--GTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:cd03260 96 SIYDNVAYGLRLHGIKLKEELDE----RVEEALRKAALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 565 VDAeVSRHLFELCICQiLHEKITIL-VTHQL-QYLKAASQILILKDGKMVQKGTYTEF 620
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 ... |
421-621 |
1.20e-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: 101.57 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 421 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQPW 483
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 484 VFSG-TLRSNILFG-------KKYEKERYEKVIKACALKKDLQLLEDgdltvigdrgtTLSGGQKARVNLARAVYQDADI 555
Cdd:cd03294 113 LLPHrTVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 556 YLLDDPLSAVD----AEVSRHLFELcicQILHEKITILVTHQL-QYLKAASQILILKDGKMVQKGTYTEFL 621
Cdd:cd03294 182 LLMDEAFSALDplirREMQDELLRL---QAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
428-623 |
1.68e-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: 100.05 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWVFSG-TLR 490
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGMLFQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNILF-----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGTT-LSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:COG1127 101 ENVAFplrehTDLSEAEIRELV---------LEKLELVGLPGAADKMPSeLSGGMRKRVALARALALDPEILLYDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 565 VDAEVSRHLFELcICQILHE-KIT-ILVTHQLQYLKA-ASQILILKDGKMVQKGTYTEFLKS 623
Cdd:COG1127 172 LDPITSAVIDEL-IRELRDElGLTsVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
78-621 |
3.30e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 105.19 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 78 PSLTRAIIkcY---WKSYLVLGIFTL-IEESAKVIQPIflgkIINYF-ENYDPMDSVALNTAYAYATVLTFCTLILAILH 152
Cdd:PRK10790 9 PTLKRLLA--YgspWRKPLGLAVLMLwVAAAAEVSGPL----LISYFiDNMVAKGNLPLGLVAGLAAAYVGLQLLAAGLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 153 H---LYFYH-----VQcagmRLRVAmchmIYRKALRLSNMAMGKTTTGQIVNLLSND--VNKFDQVTVFLHFLWAGPLQA 222
Cdd:PRK10790 83 YaqsLLFNRaavgvVQ----QLRTD----VMDAALRQPLSAFDTQPVGQLISRVTNDteVIRDLYVTVVATVLRSAALIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 223 IAVTALLWMEIGISCLAGM---AVLIILLPLQSCFGKLFSSLRSKTATFTDArirtMNEVITGIRIIKMYAWEKSFSnli 299
Cdd:PRK10790 155 AMLVAMFSLDWRMALVAIMifpAVLVVMVIYQRYSTPIVRRVRAYLADINDG----FNEVINGMSVIQQFRQQARFG--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 300 tnlrkKEISKILRSSCLRGMN-----------LASFFSAskiivfvtfttYVLLGSVITASrvFVAVtlyGAVRLTVTLF 368
Cdd:PRK10790 228 -----ERMGEASRSHYMARMQtlrldgfllrpLLSLFSA-----------LILCGLLMLFG--FSAS---GTIEVGVLYA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 369 FPSAIERVSE--------------AIVSIRRIqtFLLLDEISQR----NRQLPSdGKkmVHVQDFTAFWDKasETPTLQG 430
Cdd:PRK10790 287 FISYLGRLNEplielttqqsmlqqAVVAGERV--FELMDGPRQQygndDRPLQS-GR--IDIDNVSFAYRD--DNLVLQN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQPWVFSGTLRSNILFGK 497
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvlrqgVAMVQQDPVVLADTFLANVTLGR 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 498 KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA----EVSRHL 573
Cdd:PRK10790 440 DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSgteqAIQQAL 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 157502203 574 felcicQILHEKITILV-THQLQYLKAASQILILKDGKMVQKGTYTEFL 621
Cdd:PRK10790 520 ------AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
409-615 |
3.43e-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: 99.12 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 473
Cdd:cd03257 1 LLEVKNLSvSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 --RIAYVSQQP-----------WVFSGTLRSNilfGKKYEKERYEKVIkaCALKKDLQLLEDgdltVIGDRGTTLSGGQK 540
Cdd:cd03257 81 rkEIQMVFQDPmsslnprmtigEQIAEPLRIH---GKLSKKEARKEAV--LLLLVGVGLPEE----VLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 541 ARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFEL--CICQILheKITIL-VTHQLQYLKA-ASQILILKDGKMVQKG 615
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkKLQEEL--GLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
432-621 |
4.79e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.67 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 432 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNILFGK-- 497
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQENNLFPHlTVAQNIGLGLrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 498 --KYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 574
Cdd:COG3840 99 glKLTAEQRAQVEQA---------LERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157502203 575 ELcICQILHE-KITIL-VTHQLQ-YLKAASQILILKDGKMVQKGTYTEFL 621
Cdd:COG3840 170 DL-VDELCRErGLTVLmVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
428-610 |
8.38e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 96.10 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG-TLRS 491
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 NILFGkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157502203 572 HLFELciCQILHEK--IT-ILVTHQLQYL-KAASQILILKDGK 610
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 ... |
431-615 |
2.48e-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: 96.21 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTVrPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQPWVFSG-TLRSN 492
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYALFPHlNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGKKYeKERYEKVIKACALkkdLQLLedgDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:cd03297 96 LAFGLKR-KRNREDRISVDEL---LDLL---GLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157502203 572 hlfelcICQILHEKI-------TILVTH---QLQYLkaASQILILKDGKMVQKG 615
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 ... |
409-615 |
6.51e-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: 95.13 E-value: 6.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGriAYVSQQPW---- 483
Cdd:cd03266 1 MITADALTkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAearr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 484 ---VFSG--------TLRSNIL-FGKKYEKERYEkvIKAcALKKDLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQ 551
Cdd:cd03266 79 rlgFVSDstglydrlTARENLEyFAGLYGLKGDE--LTA-RLEELADRLGMEEL--LDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 552 DADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILV-THQLQYLKA-ASQILILKDGKMVQKG 615
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREF-IRQLRALGKCILFsTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
428-616 |
9.95e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.57 E-value: 9.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRiAYVSQQPWV---------------FSGTLRSN 492
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLAAWSPWElarrravlpqhsslaFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGK---KYEKERYEKVIKACalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVNLARA---VYQDAD----IYLLDDP 561
Cdd:COG4559 96 VALGRaphGSSAAQDRQIVREA--------LALVGLAHLAGRSyQTLSGGEQQRVQLARVlaqLWEPVDggprWLFLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 562 LSAVDAevsRHlfELCICQIL----HEKITIL-VTHQL----QYlkaASQILILKDGKMVQKGT 616
Cdd:COG4559 168 TSALDL---AH--QHAVLRLArqlaRRGGGVVaVLHDLnlaaQY---ADRILLLHQGRLVAQGT 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
426-624 |
1.31e-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: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-------------SVHGRIAYVSQQPWVFSGTLRSN 492
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvtqaSLRAAIGIVPQDTVLFNDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----- 566
Cdd:COG5265 452 IAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDsrter 531
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 567 ------AEVSRHlfelcicqilheKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:COG5265 532 aiqaalREVARG------------RTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQG 583
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
424-621 |
1.42e-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: 94.04 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-T 488
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 LRSNILFG-----KKYEKERYEKVikacalkkdLQL---LEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:cd03224 92 VEENLLLGayarrRAKRKARLERV---------YELfprLKE----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 561 P---LSAVdaeVSRHLFElCICQILHEKITILVTHqlQYLKAASQI----LILKDGKMVQKGTYTEFL 621
Cdd:cd03224 159 PsegLAPK---IVEEIFE-AIRELRDEGVTILLVE--QNARFALEIadraYVLERGRVVLEGTAAELL 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
54-621 |
1.86e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.82 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 54 QHLGEELQGFWDKEVLRAENDAQKPSLTRAIIKCYWKSY------LVLGIFTLIEESAKVIQPIFLGKIINY--FENYDP 125
Cdd:PLN03232 870 RNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVgglwvvMILLVCYLTTEVLRVSSSTWLSIWTDQstPKSYSP 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 126 MDSVALNTAYAYATV-LTFCT---LILAILHhlyfyhvqcAGMRLRVAMCHMIyrkaLRLSNMAMGKTTTGQIVNLLSND 201
Cdd:PLN03232 950 GFYIVVYALLGFGQVaVTFTNsfwLISSSLH---------AAKRLHDAMLNSI----LRAPMLFFHTNPTGRVINRFSKD 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 202 VNKFDQ-----VTVFLHFLWagplQAIAVTALLWMEIGISCLAGMAVLIIL----LPLQSC---FGKLFSSLRSKT-ATF 268
Cdd:PLN03232 1017 IGDIDRnvanlMNMFMNQLW----QLLSTFALIGTVSTISLWAIMPLLILFyaayLYYQSTsreVRRLDSVTRSPIyAQF 1092
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 269 TDArirtMNEvITGIRIIKMYAWE-----KSFSNlitNLRKKEISK------ILRSSCLRGMnlasffsaskiIVFVTfT 337
Cdd:PLN03232 1093 GEA----LNG-LSSIRAYKAYDRMakingKSMDN---NIRFTLANTssnrwlTIRLETLGGV-----------MIWLT-A 1152
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 338 TYVLLGSVITASRVFVAVT--LYGAVRLTVTLFFPSAIERVSEA---IVSIRRIQTFLLL----DEISQRNRQL---PSD 405
Cdd:PLN03232 1153 TFAVLRNGNAENQAGFASTmgLLLSYTLNITTLLSGVLRQASKAensLNSVERVGNYIDLpseaTAIIENNRPVsgwPSR 1232
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 406 GkkMVHVQDFTAFWdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL-------GEL------APSHGLVSVH 472
Cdd:PLN03232 1233 G--SIKFEDVHLRY-RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFrivelekGRImiddcdVAKFGLTDLR 1309
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 473 GRIAYVSQQPWVFSGTLRSNI---------LFGKKYEKERYEKVIKACALKKDLQLLEDGDltvigdrgtTLSGGQKARV 543
Cdd:PLN03232 1310 RVLSIIPQSPVLFSGTVRFNIdpfsehndaDLWEALERAHIKDVIDRNPFGLDAEVSEGGE---------NFSVGQRQLL 1380
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 544 NLARAVYQDADIYLLDDPLSAVDAEVSRhLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL 621
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDS-LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
428-610 |
4.29e-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: 92.59 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG-TLRS 491
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 NILFGKKYEKeryeKVIKACALKKDLQLLED-GDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 570
Cdd:cd03262 96 NITLAPIKVK----GMSKAEAEERALELLEKvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157502203 571 RHLFELcICQILHEKIT-ILVTHQLQY-LKAASQILILKDGK 610
Cdd:cd03262 172 GEVLDV-MKDLAEEGMTmVVVTHEMGFaREVADRVIFMDDGR 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
428-615 |
6.61e-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: 6.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAyvsqqpWV------FSGTL--RSNILFG--- 496
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLlglgggFNPELtgRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 497 ----KKYEKERYEKVIKACALKKDLqlledgDLTVigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE---- 568
Cdd:cd03220 112 lglsRKEIDEKIDEIIEFSELGDFI------DLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqek 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157502203 569 VSRHLFELcicqILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 615
Cdd:cd03220 181 CQRRLREL----LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
428-619 |
8.30e-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: 92.11 E-value: 8.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 492
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFG--------------KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYL 557
Cdd:cd03219 96 VMVAaqartgsglllaraRREEREARERA---------EELLERVGLADLADRpAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 558 LDDPLSAVDAEVSRHLFELcICQILHEKITILVT-HQLQYLKA-ASQILILKDGKMVQKGTYTE 619
Cdd:cd03219 167 LDEPAAGLNPEETEELAEL-IRELRERGITVLLVeHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
425-616 |
8.65e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 8.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------RIAYVSQQPWVFSG-TLRSN 492
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGKKYeKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:PRK10851 95 IAFGLTV-LPRRERPNAAAIKAKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157502203 572 HLFELciCQILHE--KIT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 616
Cdd:PRK10851 174 ELRRW--LRQLHEelKFTsVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
376-616 |
9.94e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 96.90 E-value: 9.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 376 VSEAIVSIRRIQTFLLLDEISQRNRQLPSDGKKMVHVQDFTA--FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSS 453
Cdd:COG1123 227 PEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKST 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 454 LLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPwvFSG-----TLRSNI-----LFGKKYEKERYEKV 507
Cdd:COG1123 307 LARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDP--YSSlnprmTVGDIIaeplrLHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 508 ikacalkkdLQLLEDGDL--TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcicqiLHE- 584
Cdd:COG1123 385 ---------AELLERVGLppDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL-----LRDl 450
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 157502203 585 ----KITIL-VTHQL---QYLkaASQILILKDGKMVQKGT 616
Cdd:COG1123 451 qrelGLTYLfISHDLavvRYI--ADRVAVMYDGRIVEDGP 488
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
165-613 |
1.07e-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: 98.44 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 165 RLRVAMCHMIyrkaLRLSNMAMGKTTTGQIVNLLSNDVNKFDQ---VTVF-LHFLWAGPLQAIAVTALLWMEIgisCLAG 240
Cdd:TIGR01271 959 RLHEQMLHSV----LQAPMAVLNTMKAGRILNRFTKDMAIIDDmlpLTLFdFIQLTLIVLGAIFVVSVLQPYI---FIAA 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 241 MAVLIILLPLQSCFGKLFSSLRSKTAtftDARIRTMNEVITGIR---IIKMYAWEKSFSNLITN-LRKKEISKILRSSCL 316
Cdd:TIGR01271 1032 IPVAVIFIMLRAYFLRTSQQLKQLES---EARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKaLNLHTANWFLYLSTL 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 317 RgmnlasFFSASKIIVFVTFTTYVLLGSVIT----ASRVFVAVTLYGAVRLTVTLFFPSAIErVSEAIVSIRRIQTFL-- 390
Cdd:TIGR01271 1109 R------WFQMRIDIIFVFFFIAVTFIAIGTnqdgEGEVGIILTLAMNILSTLQWAVNSSID-VDGLMRSVSRVFKFIdl 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 391 -------------------LLDEISQRNRQLPSDGKKMVhvQDFTAFWDKASETpTLQGLSFTVRPGELLAVVGPVGAGK 451
Cdd:TIGR01271 1182 pqeeprpsggggkyqlstvLVIENPHAQKCWPSGGQMDV--QGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGK 1258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 452 SSLLSAVLgELAPSHGLVSVHG-----------RIAY--VSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQ 518
Cdd:TIGR01271 1259 STLLSALL-RLLSTEGEIQIDGvswnsvtlqtwRKAFgvIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIE 1337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 519 LLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQYLK 598
Cdd:TIGR01271 1338 QFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALL 1416
|
490
....*....|....*
gi 157502203 599 AASQILILKDGKMVQ 613
Cdd:TIGR01271 1417 ECQQFLVIEGSSVKQ 1431
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
428-621 |
1.51e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.14 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV-FSGTLRSNI 493
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 LFGkkyekeRYekvIKACALKKDLQL----LEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDAD------IYLLDDPL 562
Cdd:PRK13548 98 AMG------RA---PHGLSRAEDDALvaaaLAQVDLAHLAGRDyPQLSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 563 SAVD----AEVSRHLFELCICQILHekiTILVTHQL----QYlkaASQILILKDGKMVQKGTYTEFL 621
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 ... |
403-616 |
2.70e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 90.16 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 403 PSDGKkmVHVQDFTAFWdkASETP-TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------- 473
Cdd:cd03369 2 PEHGE--IEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 -----RIAYVSQQPWVFSGTLRSNI-LFGKKYEKERYEkvikacALKkdlqlledgdltvIGDRGTTLSGGQKARVNLAR 547
Cdd:cd03369 78 edlrsSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIYG------ALR-------------VSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157502203 548 AVYQDADIYLLDDPLSAVDAEvSRHLfelcICQILHE---KITIL-VTHQLQYLKAASQILILKDGKMVQKGT 616
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYA-TDAL----IQKTIREeftNSTILtIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
409-567 |
2.88e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.46 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFTAFWD-KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI--------AYVS 479
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 480 QQ----PWVfsgTLRSNILFGKKY----EKERYEKvikACALkkdLQL--LEDgdltVIGDRGTTLSGGQKARVNLARAV 549
Cdd:COG4525 83 QKdallPWL---NVLDNVAFGLRLrgvpKAERRAR---AEEL---LALvgLAD----FARRRIWQLSGGMRQRVGIARAL 149
|
170
....*....|....*...
gi 157502203 550 YQDADIYLLDDPLSAVDA 567
Cdd:COG4525 150 AADPRFLLMDEPFGALDA 167
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
421-622 |
4.90e-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: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 421 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG- 487
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILF-------GKKYEKERYEKVIKACALKKdlqlledgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:cd03263 91 TVREHLRFyarlkglPKSEIKEEVELLLRVLGLTD-----------KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157502203 561 PLSAVDAEVSRHLFELcICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKGTYTEfLK 622
Cdd:cd03263 160 PTSGLDPASRRAIWDL-ILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQE-LK 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
428-623 |
5.75e-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: 5.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV----------SVHGR----IAYVSQQPWVFSG-TLRSN 492
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklPMHKRarlgIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD- 566
Cdd:cd03218 96 ILavleIRGLSKKEREEKLE---------ELLEEFHITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157502203 567 ---AEVSRhlfelcICQILHEK-ITILVT-HQL-QYLKAASQILILKDGKMVQKGTYTEFLKS 623
Cdd:cd03218 167 iavQDIQK------IIKILKDRgIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
424-624 |
8.87e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV-FSGTL 489
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 RSNILFGKKYEKERYEKVIKACALKKDlQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDae 568
Cdd:PRK09536 95 RQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 569 VSRHLFELCICQILHE--KITILVTHQLQyLKA--ASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:PRK09536 172 INHQVRTLELVRRLVDdgKTAVAAIHDLD-LAAryCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
428-616 |
1.92e-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: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAyvsqqpWVF---SG-----TLRSNILFG--- 496
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLelgAGfhpelTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 497 ----KKYEKERYEKVIkacalkkdlqlledgDLTVIGD------RgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG1134 116 lglsRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 567 AE----VSRHLFELcicqILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKGT 616
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 ... |
428-616 |
2.09e-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: 88.06 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI-----AYVSQQPWVFSG-------TLRSNILF 495
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRPVNTVFQNyalfphlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 496 G----KKYEKERYEKVIKACALkkdLQLLEDGDltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:cd03300 96 GlrlkKLPKAEIKERVAEALDL---VQLEGYAN-----RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157502203 572 HL-FELcicQILHEK--IT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 616
Cdd:cd03300 168 DMqLEL---KRLQKElgITfVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
342-593 |
2.67e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.56 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 342 LGSVITASRVFVAVTlyGAVRltvtlFFPSAIERVSEAIVSIRRIQTFL----LLDEISQRNRQLPSDGKKMVHVQDFTA 417
Cdd:COG4178 298 LGGLMQAASAFGQVQ--GALS-----WFVDNYQSLAEWRATVDRLAGFEealeAADALPEAASRIETSEDGALALEDLTL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 418 FwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPS-HGLVSV--HGRIAYVSQQPWVFSGTLRSNIL 494
Cdd:COG4178 371 R--TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARpaGARVLFLPQRPYLPLGTLREALL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 495 F---GKKYEKERYEKVIKACALKKDLQLLEDGDltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:COG4178 448 YpatAEAFSDAELREALEAVGLGHLAERLDEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
250 260
....*....|....*....|..
gi 157502203 572 HLFELcICQILHEKITILVTHQ 593
Cdd:COG4178 523 ALYQL-LREELPGTTVISVGHR 543
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
409-647 |
3.65e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.15 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RI 475
Cdd:PRK11231 2 TLRTENLTVGYGT---KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 476 AYVSQQPWVFSG-TLRS---------NILFGKKYEKERyEKVIKAcalkkdlqlLEDGDLTVIGDRG-TTLSGGQKARVN 544
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRElvaygrspwLSLWGRLSAEDN-ARVNQA---------MEQTRINHLADRRlTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 545 LARAVYQDADIYLLDDPLSAVDAEvsrHLFELC-ICQILHE--KITILVTHQL-QYLKAASQILILKDGKMVQKGTYTEF 620
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDIN---HQVELMrLMRELNTqgKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEV 225
|
250 260 270
....*....|....*....|....*....|
gi 157502203 621 LKSGidfgsLLKKD---NEESEQPPVPGTP 647
Cdd:PRK11231 226 MTPG-----LLRTVfdvEAEIHPEPVSGTP 250
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
425-612 |
4.29e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.03 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWVFSGt 488
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRLLPD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 lRS---NILF-----GKKyEKERYEKVIKacALKKdLQLLEDGDLTVIgdrgtTLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:COG2884 94 -RTvyeNVALplrvtGKS-RKEIRRRVRE--VLDL-VGLSDKAKALPH-----ELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157502203 561 PLSAVDAEVSRHLFELcICQILHEKITILV-THQLQYL-KAASQILILKDGKMV 612
Cdd:COG2884 164 PTGNLDPETSWEIMEL-LEEINRRGTTVLIaTHDLELVdRMPKRVLELEDGRLV 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
428-623 |
4.79e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQPWVFSG-TLRSNILFG-------- 496
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLDGdaelrale 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 497 KKYEK------------ERYEKVI-------------KACALKKDLQL-LEDGDLTVigdrgTTLSGGQKARVNLARAVY 550
Cdd:COG0488 94 AELEEleaklaepdedlERLAELQeefealggweaeaRAEEILSGLGFpEEDLDRPV-----SELSGGWRRRVALARALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 551 QDADIYLLDDP---LsavDAEvSRHLFElcicQILHE-KIT-ILVTHQLQYL-KAASQILILKDGKMVQ-KGTYTEFLKS 623
Cdd:COG0488 169 SEPDLLLLDEPtnhL---DLE-SIEWLE----EFLKNyPGTvLVVSHDRYFLdRVATRILELDRGKLTLyPGNYSAYLEQ 240
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
701-845 |
5.30e-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: 89.09 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 701 YKNYFRAGAHWIVFIFLILLNTAAQVAYVLQDWWL---SYWANKQSMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVL 777
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLlrsQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVADSLLA 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 778 FGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd18600 86 MGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQ 153
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
428-615 |
6.88e-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: 86.09 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGeLLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPwvfsgTLRSNIlf 495
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEF-----GVYPNF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 496 gKKYEKERYEKVIKACALKKD----LQLLEDGDLT-VIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvS 570
Cdd:cd03264 88 -TVREFLDYIAWLKGIPSKEVkarvDEVLELVNLGdRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE-E 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157502203 571 RHLFELCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 615
Cdd:cd03264 166 RIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
431-615 |
7.74e-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: 7.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNILFGK- 497
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGLs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 498 ---KYEKERYEKVIKACAlKKDLQLLEDgdltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 574
Cdd:cd03298 97 pglKLTAEDRQAIEVALA-RVGLAGLEK-------RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 157502203 575 ELC--ICQilHEKITIL-VTHQLQYLKAASQILI-LKDGKMVQKG 615
Cdd:cd03298 169 DLVldLHA--ETKMTVLmVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
426-595 |
1.12e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI--------AYVSQQ----PWVfsgTLRSNI 493
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNegllPWR---NVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 LFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 572
Cdd:PRK11248 92 AFGL-----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*
gi 157502203 573 LFELcICQILHE--KITILVTHQLQ 595
Cdd:PRK11248 167 MQTL-LLKLWQEtgKQVLLITHDIE 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
428-612 |
1.32e-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: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQqpwvfsgtlrsni 493
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevsfasprdarragIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 lfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 573
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157502203 574 FELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGKMV 612
Cdd:cd03216 122 FKV-IRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
405-624 |
2.02e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.22 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 405 DGKKMVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------- 473
Cdd:PRK13635 1 MKEEIIRVEHIS-FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 --RIAYVSQQP-WVFSG-TLRSNILFGKKYE----KERYEKVIKACALKKDLQLLEdgdltvigDRGTTLSGGQKARVNL 545
Cdd:PRK13635 80 rrQVGMVFQNPdNQFVGaTVQDDVAFGLENIgvprEEMVERVDQALRQVGMEDFLN--------REPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 546 ARAVYQDADIYLLDDPLSAVD----AEVsrhlfeLCICQILHEK--ITIL-VTHQLQYLKAASQILILKDGKMVQKGTYT 618
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDprgrREV------LETVRQLKEQkgITVLsITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....*.
gi 157502203 619 EFLKSG 624
Cdd:PRK13635 226 EIFKSG 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
432-621 |
2.16e-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: 87.85 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 432 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQPWVFSG-TLRSNI 493
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFPHlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 LFGKKYE-----KERYEKVIkacalkkdlQLLEDGDLTvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:COG4148 99 LYGRKRApraerRISFDEVV---------ELLGIGHLL---DRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 568 EvSRHlfelcicQIL------HEKITI---LVTHQL---QYLkaASQILILKDGKMVQKGTYTEFL 621
Cdd:COG4148 167 A-RKA-------EILpylerlRDELDIpilYVSHSLdevARL--ADHVVLLEQGRVVASGPLAEVL 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
424-623 |
4.11e-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: 84.75 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGL-VSVHG-------------RIAYVS---QQPWVFS 486
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGerrggedvwelrkRIGLVSpalQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 487 GTLRSNIL---FG-----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYL 557
Cdd:COG1119 95 ETVLDVVLsgfFDsiglyREPTDEQRERA---------RELLELLGLAHLADRPfGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 558 LDDPLSAVDAEvSRHLFELCICQILHEKIT--ILVTHQLQYLKAA-SQILILKDGKMVQKGTYTEFLKS 623
Cdd:COG1119 166 LDEPTAGLDLG-ARELLLALLDKLAAEGAPtlVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
432-631 |
4.52e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.25 E-value: 4.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 432 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---RIAYVSQQPW--------VFSG-TLRSNILFG--- 496
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRPVsmlfqennLFSHlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 497 ----KKYEKERYEKVIKACALKKDLQLLEdgdltvigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 572
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 573 LFELcICQILHEK-ITIL-VTHQLQ-YLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLL 631
Cdd:PRK10771 168 MLTL-VSQVCQERqLTLLmVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
714-845 |
6.17e-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: 85.00 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 714 FIFLILLNTAAQVAYVLQDWWLSYWANkqsmlnvtVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNS 793
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD--------VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERL 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 157502203 794 SQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:pfam00664 73 SRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQ 124
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
410-610 |
7.24e-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: 80.96 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTAFWDKaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQqpwvfsg 487
Cdd:cd03221 1 IELENLSKTYGG---KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 tlrsnilfgkkyekeryekvikacalkkdlqlledgdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157502203 568 EvSRHLFElcicQIL--HEKITILVTHQLQYLKA-ASQILILKDGK 610
Cdd:cd03221 104 E-SIEALE----EALkeYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
36-628 |
8.48e-18 |
|
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: 88.85 E-value: 8.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 36 KRRLEEDDMYSvlpEDRSQHLG--EELQGFWDKEVLRAENDAQKPSLTRAIIKCYWKSYLVLGIFTLIeesakVIQPIFL 113
Cdd:TIGR00957 904 QRQLSASSSDS---GDQSRHHGssAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITF-----LSIFLFV 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 114 GKIINYF-ENY-------DPM-DSVALNTAYAYAtVLTFCTLILAILHHLYFYHVQCAGM----RLRVAMCHMIYRkalr 180
Cdd:TIGR00957 976 CNHVSALaSNYwlslwtdDPMvNGTQNNTSLRLS-VYGALGILQGFAVFGYSMAVSIGGIqasrVLHQDLLHNKLR---- 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 181 lSNMAMGKTT-TGQIVNLLSNDVNKFDQVTVFLHFLWAGPL-QAIAVTALLWMEIGISclagmAVLIILLPLQSCFGKLF 258
Cdd:TIGR00957 1051 -SPMSFFERTpSGNLVNRFSKELDTVDSMIPPVIKMFMGSLfNVIGALIVILLATPIA-----AVIIPPLGLLYFFVQRF 1124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 259 SSLRSKTATFTDARIRT-----MNEVITGIRIIKMYAWEKSFSnLITNLRKKEISKILRSSCL--RGMNLASFFSASKII 331
Cdd:TIGR00957 1125 YVASSRQLKRLESVSRSpvyshFNETLLGVSVIRAFEEQERFI-HQSDLKVDENQKAYYPSIVanRWLAVRLECVGNCIV 1203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 332 VFVTFTTyVLLGSVITASRVFVAVTLygavRLTVTLFFPSAIERVSEA---IVSIRRIQTFLLLD-------EISQRNRQ 401
Cdd:TIGR00957 1204 LFAALFA-VISRHSLSAGLVGLSVSY----SLQVTFYLNWLVRMSSEMetnIVAVERLKEYSETEkeapwqiQETAPPSG 1278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 402 LPSDGKkmVHVQDFTAFWDKASETpTLQGLSFTVRPGELLAVVGPVGAGKSSL-------LSAVLGEL------APSHGL 468
Cdd:TIGR00957 1279 WPPRGR--VEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLtlglfriNESAEGEIiidglnIAKIGL 1355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 469 VSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARA 548
Cdd:TIGR00957 1356 HDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARA 1435
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 549 VYQDADIYLLDDPLSAVDAEVS-------RHLFELCicqilhekiTIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEF 620
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDnliqstiRTQFEDC---------TVLtIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
....*....
gi 157502203 621 LKS-GIDFG 628
Cdd:TIGR00957 1507 LQQrGIFYS 1515
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
390-622 |
1.09e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 390 LLLDEISQRNR----QLPSD---GKKMVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL 462
Cdd:COG0488 289 LEREEPPRRDKtveiRFPPPerlGKKVLELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGEL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 463 APSHGLVsVHG---RIAYVSQQPWVFSG--TLRSNIlfgKKYEKERYEKVIKacalkkdlQLLED----GD--LTVIGDr 531
Cdd:COG0488 366 EPDSGTV-KLGetvKIGYFDQHQEELDPdkTVLDEL---RDGAPGGTEQEVR--------GYLGRflfsGDdaFKPVGV- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 532 gttLSGGQKARVNLARAVYQDADIYLLDDP---LsavDAEvSRHL-------FELCIcqilhekitILVTHQLQYLKA-A 600
Cdd:COG0488 433 ---LSGGEKARLALAKLLLSPPNVLLLDEPtnhL---DIE-TLEAleealddFPGTV---------LLVSHDRYFLDRvA 496
|
250 260
....*....|....*....|...
gi 157502203 601 SQILILKDGKMVQK-GTYTEFLK 622
Cdd:COG0488 497 TRILEFEDGGVREYpGGYDDYLE 519
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
261-669 |
1.39e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.16 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 261 LRSKTAT-FTDARIRTMNEVITGIRIIKMYAWEKSFSNLItNLRKKEISK-ILRSS--------CLRGMNLAS----FFS 326
Cdd:PTZ00265 223 INKKTSLlYNNNTMSIIEEALVGIRTVVSYCGEKTILKKF-NLSEKLYSKyILKANfmeslhigMINGFILASyafgFWY 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 327 ASKIIVFVTFTTY----VLLGSVITasrVFVAVtLYGAVRLTVTLffPSAIERVS--EAIVSIRRIQTFLLLDEISQRNR 400
Cdd:PTZ00265 302 GTRIIISDLSNQQpnndFHGGSVIS---ILLGV-LISMFMLTIIL--PNITEYMKslEATNSLYEIINRKPLVENNDDGK 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 401 QLPsDGKKmVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVH-------- 472
Cdd:PTZ00265 376 KLK-DIKK-IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdi 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 473 ------GRIAYVSQQPWVFSGTLRSNI---LFGKK---YEKERYEK--------------VIKACA-------------- 512
Cdd:PTZ00265 454 nlkwwrSKIGVVSQDPLLFSNSIKNNIkysLYSLKdleALSNYYNEdgndsqenknkrnsCRAKCAgdlndmsnttdsne 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 513 ---LKKDLQLLEDGDL---------------------TVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:PTZ00265 534 lieMRKNYQTIKDSEVvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 569 vSRHLFELCICQIL--HEKITILVTHQLQYLKAASQILILKDGkmvQKGTYTEFLKSGIDFGSLLKKDNEESEQPPVPGT 646
Cdd:PTZ00265 614 -SEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNR---ERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNN 689
|
490 500
....*....|....*....|....
gi 157502203 647 PTLRNRTFS-ESSVWSQQSSRPSL 669
Cdd:PTZ00265 690 NNNNNNKINnAGSYIIEQGTHDAL 713
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
428-615 |
2.13e-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: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------RIAYVSQQPWVFSG-TLRSNILF 495
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkniealrRIGALIEAPGFYPNlTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 496 GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLF 574
Cdd:cd03268 96 LARLLGIRKKRI---------DEVLDVVGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157502203 575 ELcICQILHEKITILV-THQLQYL-KAASQILILKDGKMVQKG 615
Cdd:cd03268 167 EL-ILSLRDQGITVLIsSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
428-622 |
2.32e-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: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQQPWVFSG-TLRSNI- 493
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 LFGKKY------EKERYEKVIKAcalkkdLQLLEDGDLTVigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03265 96 IHARLYgvpgaeRRERIDELLDF------VGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 568 EVSRHLFELcICQILHEK-ITILVThqLQYLKAASQ----ILILKDGKMVQKGTYTEfLK 622
Cdd:cd03265 165 QTRAHVWEY-IEKLKEEFgMTILLT--THYMEEAEQlcdrVAIIDHGRIIAEGTPEE-LK 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
428-608 |
2.38e-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: 80.28 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLsAVLGELAPSH-GLVSVHGR--IAYVSQQPWVFSGTLRSNILfgkkYEKERy 504
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLWPWGsGRIGMPEGedLLFLPQRPYLPLGTLREQLI----YPWDD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 505 ekvikacalkkdlqlledgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCicqiLHE 584
Cdd:cd03223 91 -----------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KEL 137
|
170 180
....*....|....*....|....*
gi 157502203 585 KITIL-VTHQLQYLKAASQILILKD 608
Cdd:cd03223 138 GITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
410-615 |
4.33e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.48 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTAFWDKAseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPW------ 483
Cdd:PRK13647 5 IEVEDLHFRYKDG--TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskvg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 484 ---------VFSGTLRSNILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGTT-LSGGQKARVNLA 546
Cdd:PRK13647 83 lvfqdpddqVFSSTVWDDVAFGpvnmgldKDEVERRVEEALKAVRMWD------------FRDKPPYhLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 547 RAVYQDADIYLLDDPLSAVDAEVSRHLFElcICQILHE--KITILVTHQLQY-LKAASQILILKDGKMVQKG 615
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
420-616 |
5.74e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 420 DKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVSVHGRI-------------AYVSQQpwvfs 486
Cdd:COG4138 4 NDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPlsdwsaaelarhrAYLSQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 487 gTLRSNILFGKKY------EKERYEKVIKACAlkkdlQLLEDGDLTVIGDRG-TTLSGGQKARVNLARAVYQ-------D 552
Cdd:COG4138 78 -QSPPFAMPVFQYlalhqpAGASSEAVEQLLA-----QLAEALGLEDKLSRPlTQLSGGEWQRVRLAAVLLQvwptinpE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 553 ADIYLLDDPLSAVD----AEVSRHLFELCICQilhekITILV-THQLQY-LKAASQILILKDGKMVQKGT 616
Cdd:COG4138 152 GQLLLLDEPMNSLDvaqqAALDRLLRELCQQG-----ITVVMsSHDLNHtLRHADRVWLLKQGKLVASGE 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
412-656 |
9.33e-17 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 81.44 E-value: 9.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 412 VQDFTAFWDKASETpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLgELAPSHGLVSVHG-----------RIAY--V 478
Cdd:cd03289 5 VKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFgvI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 479 SQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLL 558
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 559 DDPLSAVDA-------EVSRHLFELCicqilhekITILVTHQLQYLKAASQILILKDGKMVQKGTY------TEFLKSGI 625
Cdd:cd03289 163 DEPSAHLDPityqvirKTLKQAFADC--------TVILSEHRIEAMLECQRFLVIEENKVRQYDSIqkllneKSHFKQAI 234
|
250 260 270
....*....|....*....|....*....|....*
gi 157502203 626 DFGSLLK----KDNEESEQPPVPGTPTLRNRTFSE 656
Cdd:cd03289 235 SPSDRLKlfprRNSSKSKRKPRPQIQALQEETEEE 269
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
419-615 |
1.10e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.13 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 419 WDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHglvsvhgriayvsqqpwvFSGTLRSNilfGKK 498
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG------------------VSGEVLIN---GRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 499 YEKERYEKVIkaCALKKDLQLLedGDLTV-------IGDRGttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:cd03213 75 LDKRSFRKII--GYVPQDDILH--PTLTVretlmfaAKLRG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 157502203 572 HLFELcICQILHEKITILVT-HQLQYL--KAASQILILKDGKMVQKG 615
Cdd:cd03213 149 QVMSL-LRRLADTGRTIICSiHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
428-593 |
1.19e-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: 80.01 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVS----VHG----------RIAYVSQ-----------QP 482
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTTSgqilFNGqprkpdqfqkCVAYVRQddillpgltvrET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 483 WVFSGTLRSNILFGKKYEKERYEkvikacalkkDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVE----------DVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|..
gi 157502203 563 SAVDAEVSRHLFELcICQILHEKITILVT-HQ 593
Cdd:cd03234 172 SGLDSFTALNLVST-LSQLARRNRIVILTiHQ 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
431-620 |
1.30e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.06 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTVRPGELLAVVGPVGAGKSSLLSaVLGEL-APSHGLVSVHGRIAYVSQQPWVFSG-TLRSNIlfGKKYEK------- 501
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLeMPRSGTLNIAGNHFDFSKTPSDKAIrELRRNV--GMVFQQynlwphl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 502 -------ERYEKVI---KACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 570
Cdd:PRK11124 98 tvqqnliEAPCRVLglsKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEIT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 571 RHlfelcICQILHE----KIT-ILVTHQLQYL-KAASQILILKDGKMVQKGTYTEF 620
Cdd:PRK11124 178 AQ-----IVSIIRElaetGITqVIVTHEVEVArKTASRVVYMENGHIVEQGDASCF 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
421-606 |
2.23e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 421 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG 487
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGKKYEKERYEKVikacALKKDLQLLEDgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPDPA----IFLDDLERFAL-PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157502203 568 EVSRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILIL 606
Cdd:PRK10247 171 SNKHNVNEI-IHRYVREQnIAVLwVTHDKDEINHADKVITL 210
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
428-577 |
2.60e-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: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSaVLGELAPSHG---LVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEkERY 504
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSE-DMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 505 EKVIKACALKKDLQLL-------EDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELC 577
Cdd:TIGR00954 546 RRGLSDKDLEQILDNVqlthileREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
428-590 |
5.41e-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: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 492
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFG-------------------KKYEKERYEKVikacalkkdLQLLEDGDLT-VIGDRGTTLSGGQKARVNLARAVYQD 552
Cdd:COG0411 100 VLVAaharlgrgllaallrlpraRREEREARERA---------EELLERVGLAdRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 157502203 553 ADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KITILV 590
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAEL-IRRLRDErGITILL 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
409-616 |
6.15e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 80.12 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 473
Cdd:COG1135 1 MIELENLSkTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalserelraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 --RIAYVSQQpwvF----SGTLRSNILF-----GKKyEKERYEKVikacalkkdLQLLEdgdLTVIGDRGTT----LSGG 538
Cdd:COG1135 81 rrKIGMIFQH---FnllsSRTVAENVALpleiaGVP-KAEIRKRV---------AELLE---LVGLSDKADAypsqLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 539 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRhlfelcicQIL------HEK--ITI-LVTHQLQYLKA-ASQILILKD 608
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTR--------SILdllkdiNRElgLTIvLITHEMDVVRRiCDRVAVLEN 216
|
....*...
gi 157502203 609 GKMVQKGT 616
Cdd:COG1135 217 GRIVEQGP 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
426-591 |
6.66e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQqpwvFSG-----T 488
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQ----FDNldlefT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 LRSNIL-FGKKY--EKERYEKVIKAcalkkdlqLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13536 131 VRENLLvFGRYFgmSTREIEAVIPS--------LLEFARLESKADaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180
....*....|....*....|....*..
gi 157502203 565 VDAEvSRHLFELCICQILHEKITILVT 591
Cdd:PRK13536 203 LDPH-ARHLIWERLRSLLARGKTILLT 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
407-603 |
8.29e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.89 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 407 KKMVHVQDFTAFWDKASetpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPShglVSVHGRIAY------- 477
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPE---VTITGSIVYnghniys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 478 --------------VSQQPWVFSGTLRSNILFGKKYEKERYEKVIKAcALKKDLQ--LLEDGDLTVIGDRGTTLSGGQKA 541
Cdd:PRK14239 77 prtdtvdlrkeigmVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKgaSIWDEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 542 RVNLARAVYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQylkAASQI 603
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQ---QASRI 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
424-622 |
1.20e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.17 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQP--WVFS 486
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 487 GTLRSNILFGKK----YEKERYEKVIKACALKKDlqlledgDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:PRK13637 99 ETIEKDIAFGPInlglSEEEIENRVKRAMNIVGL-------DYEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 562 LSAVDAEVSRHLFELciCQILHEK---ITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLK 622
Cdd:PRK13637 172 TAGLDPKGRDEILNK--IKELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
428-573 |
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 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------RIAYVSQQ----PwvfSGTLRSNI 493
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRnamkP---ALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 LFGKKYeKERYEKVIKACALKKDLQLLEDgdltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE----- 568
Cdd:PRK13539 95 EFWAAF-LGGEELDIAAALEAVGLAPLAH-------LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAavalf 166
|
....*...
gi 157502203 569 ---VSRHL 573
Cdd:PRK13539 167 aelIRAHL 174
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
428-566 |
1.38e-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: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 492
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 493 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG1137 99 ILavleLRKLSKKEREERLE---------ELLEEFGITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
425-616 |
1.44e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.22 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIayVSQQP-------WVFSG-------TLR 490
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--ITHVPaenrhvnTVFQSyalfphmTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNILFGKKYEK----ERYEKVIKACALkkdLQLLEDGDltvigDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK09452 105 ENVAFGLRMQKtpaaEITPRVMEALRM---VQLEEFAQ-----RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 567 AEVSRHL-FELcicQILHEK--IT-ILVTH-QLQYLKAASQILILKDGKMVQKGT 616
Cdd:PRK09452 177 YKLRKQMqNEL---KALQRKlgITfVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
410-615 |
1.54e-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: 76.17 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFT-AFWDKASetptLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------RIAYVS 479
Cdd:cd03269 1 LEVENVTkRFGRVTA----LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 480 QQPWVfsgtlrsnilfgkkYEKERYEKVI----------KACALKKDLQLLEDGDLTVIGD-RGTTLSGGQKARVNLARA 548
Cdd:cd03269 77 EERGL--------------YPKMKVIDQLvylaqlkglkKEEARRRIDEWLERLELSEYANkRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 549 VYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKIT-ILVTHQLQYLKA-ASQILILKDGKMVQKG 615
Cdd:cd03269 143 VIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTvILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
425-619 |
1.67e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.81 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAY--------------VSQQP--WVFSG 487
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYdkksllevrktvgiVFQNPddQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGK---KYEKERYEKVIKAcALKKdlqlledgdltvIGDRGTT------LSGGQKARVNLARAVYQDADIYLL 558
Cdd:PRK13639 95 TVEEDVAFGPlnlGLSKEEVEKRVKE-ALKA------------VGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 559 DDPLSAVD----AEVSRHLFELCicqilHEKITILV-THQLQYL-KAASQILILKDGKMVQKGTYTE 619
Cdd:PRK13639 162 DEPTSGLDpmgaSQIMKLLYDLN-----KEGITIIIsTHDVDLVpVYADKVYVMSDGKIIKEGTPKE 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
424-593 |
1.87e-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: 75.86 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------------IAYVSQQPWVfSGTLRS 491
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGL-KPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 nilfgkkYEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 570
Cdd:TIGR01189 91 -------LENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|...
gi 157502203 571 RHLFELCICQILHEKITILVTHQ 593
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHQ 186
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
410-594 |
2.42e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTAFWDKASETptLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------IAYVS 479
Cdd:PRK15056 7 IVVNDVTVTWRNGHTA--LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 480 QQP---WVFSGTLRSNILFGK-------KYEKERYEKVIKACALKKDLQLLEDGDltvIGDrgttLSGGQKARVNLARAV 549
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157502203 550 YQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEKITILV-THQL 594
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISL-LRELRDEGKTMLVsTHNL 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
403-595 |
2.60e-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: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 403 PSDGKKMVHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPS---HGLVSVHG---- 473
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLDGediy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 -----------RIAYVSQQPWVFSGTLRSNILFG--------KKYEKERYEKVIKACAL----KKDLQlledgdltvigD 530
Cdd:COG1117 82 dpdvdvvelrrRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSELDEIVEESLRKAALwdevKDRLK-----------K 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 531 RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQiLHEKITI-LVTHQLQ 595
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEEL-ILE-LKKDYTIvIVTHNMQ 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
428-620 |
2.82e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLL----SAVLGELAP-SH-----GLVSVHGRIA-----------YVSQQ-PWVF 485
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAgSHiellgRTVQREGRLArdirksrantgYIFQQfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 486 SGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDgdLTVIG------DRGTTLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157502203 560 DPLSAVDAEVSRHLFELCICQILHEKITILVT-HQLQY-LKAASQILILKDGKMVQKGTYTEF 620
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
423-625 |
3.19e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 76.28 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSG-T 488
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQENHINSRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 LRSNILFGK------KYEKERYEKVIKAcalkkdLQLLedgDLTVIGDRG-TTLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:COG4604 92 VRELVAFGRfpyskgRLTAEDREIIDEA------IAYL---DLEDLADRYlDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 562 LSAVD----AEVSRHLFELCicqilHE--KITILVTHQLQYLKA-ASQILILKDGKMVQKGTYTEFLKSGI 625
Cdd:COG4604 163 LNNLDmkhsVQMMKLLRRLA-----DElgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPEV 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
408-634 |
4.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.67 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 408 KMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------R 474
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrrK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 475 IAYVSQQP--WVFSGTLRSNILFGKKYEKERYEKVIKacalKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQD 552
Cdd:PRK13642 83 IGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 553 ADIYLLDDPLSAVDAEVSRHlfelcICQILHE-----KITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKS--- 623
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQE-----IMRVIHEikekyQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATsed 233
|
250
....*....|....*..
gi 157502203 624 ----GID--FGSLLKKD 634
Cdd:PRK13642 234 mveiGLDvpFSSNLMKD 250
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
409-613 |
4.69e-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: 75.55 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 409 MVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------- 473
Cdd:COG4181 8 IIELRGLTkTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 RIAYVSqqpWVF-------SGTLRSNI-----LFGKKYEKERYEKVIKACALkkdlqlledgdltviGDRGT----TLSG 537
Cdd:COG4181 88 RARHVG---FVFqsfqllpTLTALENVmlpleLAGRRDARARARALLERVGL---------------GHRLDhypaQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 538 GQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH----LFELCicqilHEKIT--ILVTHQLQYLKAASQILILKDGKM 611
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidlLFELN-----RERGTtlVLVTHDPALAARCDRVLRLRAGRL 224
|
..
gi 157502203 612 VQ 613
Cdd:COG4181 225 VE 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
428-621 |
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 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------------RIAYVSQQPWVFSG-TLRS 491
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltdskkdinklrrKVGMVFQQFNLFPHlTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 NILFGKKYEKeryeKVIKACALKKDLQLLEdgdlTV-IGDRG----TTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG1126 97 NVTLAPIKVK----KMSKAEAEERAMELLE----RVgLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 567 ----AEVsrhlfeL-CICQILHEKIT-ILVTHQLQY-LKAASQILILKDGKMVQKGTYTEFL 621
Cdd:COG1126 169 pelvGEV------LdVMRDLAKEGMTmVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
431-638 |
4.98e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVS--QQP--WVFSG-------TLRSNILFGKK 498
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPpyQRPinMMFQSyalfphmTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 499 yeKERYEKVIKACALKKDLQLLEDGDLTviGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVsRHLFELCI 578
Cdd:PRK11607 118 --QDKLPKAEIASRVNEMLGLVHMQEFA--KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL-RDRMQLEV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 579 CQILhEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGT------------YTEFLKSGIDFGSLLKKDNEES 638
Cdd:PRK11607 193 VDIL-ERVgvtCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEpeeiyehpttrySAEFIGSVNVFEGVLKERQEDG 267
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
431-623 |
5.27e-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: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPwvfSGTL--RSNI-- 493
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrckHIRMIFQDP---NTSLnpRLNIgq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 -------LFGKKYEKERYEKVIKAcaLKKdLQLLEDGDLTVIgdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG4167 109 ileeplrLNTDLTAEEREERIFAT--LRL-VGLLPEHANFYP----HMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 567 AEVSRHLFELCIcqILHEKIT---ILVTHQLQYLKAAS-QILILKDGKMVQKGTYTEFLKS 623
Cdd:COG4167 182 MSVRSQIINLML--ELQEKLGisyIYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
402-620 |
8.22e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 402 LPSDGKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------- 474
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 475 -------IAYVSQQPWVFSG-TLRSNILFGKKYEKERYEKVIK-----ACALKKDLQ--LLEdgdltvIGDRGTtlsggq 539
Cdd:PRK15439 81 akahqlgIYLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQllaalGCQLDLDSSagSLE------VADRQI------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 540 karVNLARAVYQDADIYLLDDPLSAVD-AEVSRhLFELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGKMVQKGT 616
Cdd:PRK15439 149 ---VEILRGLMRDSRILILDEPTASLTpAETER-LFSR-IRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGK 223
|
....
gi 157502203 617 YTEF 620
Cdd:PRK15439 224 TADL 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
424-625 |
1.03e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.00 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------RIAYVSQqpwvFSG---- 487
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQ----FDNldpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 -TLRSNIL-FGkkyekeRYEKVIKACALKKDLQLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13537 95 fTVRENLLvFG------RYFGLSAAAARALVPPLLEFAKLENKADaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 565 VDAEvSRHLFELCICQILHEKITILVThqLQYLKAASQ----ILILKDGKMVQKGTYTEFLKSGI 625
Cdd:PRK13537 169 LDPQ-ARHLMWERLRSLLARGKTILLT--THFMEEAERlcdrLCVIEEGRKIAEGAPHALIESEI 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
478-621 |
1.72e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 478 VSQQPWVFSGTLRSNILFGKkyEKERYEKVIKAC---ALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDAD 554
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 555 IYLLDDPLSAVDAEvSRHLFELCICQILH--EKITILVTHQLQYLKAASQILIL----KDGKMVQ-KGTYTEFL 621
Cdd:PTZ00265 1379 ILLLDEATSSLDSN-SEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELL 1451
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
428-593 |
2.38e-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: 72.53 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------------IAYVSQQPWVfSGTL--RSNI 493
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGI-KTTLsvLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 LFGKKYekeryekvikaCALKKDLQLLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 572
Cdd:cd03231 95 RFWHAD-----------HSDEQVEEALARVGLNGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|.
gi 157502203 573 LFELCICQILHEKITILVTHQ 593
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
424-615 |
2.43e-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: 73.52 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIayvsqqPWVFSGTLRSNI--LFGKK--- 498
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV------PWKRRKKFLRRIgvVFGQKtql 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 499 ----------------Y--EKERYEKVIKACAlkkdlQLLEDGDLTVIGDRgtTLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:cd03267 107 wwdlpvidsfyllaaiYdlPPARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 561 PLSAVDAEVSRHLFE-LCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 615
Cdd:cd03267 180 PTIGLDVVAQENIRNfLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
428-615 |
2.85e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.63 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV--------------HGRIAYVSQQ-PWVFSG----- 487
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQLRQHvGFVFQNfnlfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 --TLRSNILFGKKYEKeryeKVIKACALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK11264 99 hrTVLENIIEGPVIVK----GEPKEEATARARELLAKVGLAGKETSyPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 565 VDAEVSRHLFElCICQILHEKIT-ILVTHQLQYLK-AASQILILKDGKMVQKG 615
Cdd:PRK11264 175 LDPELVGEVLN-TIRQLAQEKRTmVIVTHEMSFARdVADRAIFMDQGRIVEQG 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
412-633 |
3.05e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.35 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 412 VQDFTAFWDK--ASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV-------------------- 469
Cdd:PRK13651 5 VKNIVKIFNKklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 470 -----------------SVHGRIAYVSQ--QPWVFSGTLRSNILFG-------KKYEKERYEKVIKACALkkDLQLLEDG 523
Cdd:PRK13651 85 eklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 524 DLTvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFElcICQILHE--KITILVTHQLQY-LKAA 600
Cdd:PRK13651 163 PFE--------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKqgKTIILVTHDLDNvLEWT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 157502203 601 SQILILKDGKMVQKG-TY-----TEFLKSG-------IDFGSLLKK 633
Cdd:PRK13651 233 KRTIFFKDGKIIKDGdTYdilsdNKFLIENnmeppklLNFVNKLEK 278
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
93-386 |
6.83e-14 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 72.97 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 93 LVLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDSVALntayaYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCH 172
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLW-----IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 173 MIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQ-VTVFLHFLWAGPLQAIAVTA-LLWMEIGIScLAGMAVLIILLPL 250
Cdd:cd07346 77 DLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALViLFYLNWKLT-LVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 251 QSCFGK----LFSSLRSKTATFTdariRTMNEVITGIRIIKMYAWEKS----FSNLITNLRKKEISKILRSSCLRGMnLA 322
Cdd:cd07346 156 LRYFRRrirkASREVRESLAELS----AFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPL-IG 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 323 SFFSASKIIVFVtFTTYVLLGSVITASrVFVAVTLYgavrlTVTLFFPsaIERVSE-------AIVSIRRI 386
Cdd:cd07346 231 LLTALGTALVLL-YGGYLVLQGSLTIG-ELVAFLAY-----LGMLFGP--IQRLANlynqlqqALASLERI 292
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
407-630 |
8.85e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.46 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 407 KKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------- 473
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 RIAYVSQQP-WVFSG-TLRSNILFGKKYE----KERYEKVIKAcalkkdLQLLedgDLTVIGDRGTT-LSGGQKARVNLA 546
Cdd:PRK13650 82 KIGMVFQNPdNQFVGaTVEDDVAFGLENKgiphEEMKERVNEA------LELV---GMQDFKEREPArLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 547 RAVYQDADIYLLDDPLSAVDAEVSRHLFELcICQILHE-KITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKT-IKGIRDDyQMTVIsITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
....*.
gi 157502203 625 IDFGSL 630
Cdd:PRK13650 232 NDLLQL 237
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
429-593 |
9.39e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 429 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIayVSQQPWVFsgtlRSNILF-----GKKYEKER 503
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDEY----HQDLLYlghqpGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 504 YEKVIKACALKkdlQLLEDGD----LTVIGDRGT------TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEV 569
Cdd:PRK13538 92 LENLRFYQRLH---GPGDDEAlweaLAQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvARL 168
|
170 180
....*....|....*....|....*.
gi 157502203 570 SRHLFELCicqilhEK--ITILVTHQ 593
Cdd:PRK13538 169 EALLAQHA------EQggMVILTTHQ 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
428-637 |
1.14e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPS---HGLVSVHG---------------RIAYVSQQPWVFSG 487
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGknlyapdvdpvevrrRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGKK---YE---KERYEKVIKACAL----KKDLQlledgdltvigDRGTTLSGGQKARVNLARAVYQDADIYL 557
Cdd:PRK14243 106 SIYDNIAYGARingYKgdmDELVERSLRQAALwdevKDKLK-----------QSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 558 LDDPLSAVDAEVSRHLFELciCQILHEKITI-LVTHQLQYLKAASQILILKDGKMVQKGTYT----EFLKSGIDFGSLLK 632
Cdd:PRK14243 175 MDEPCSALDPISTLRIEEL--MHELKEQYTIiIVTHNMQQAARVSDMTAFFNVELTEGGGRYgylvEFDRTEKIFNSPQQ 252
|
....*
gi 157502203 633 KDNEE 637
Cdd:PRK14243 253 QATRD 257
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
431-616 |
1.32e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.22 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQPWVFSG-TLRSNILFGKK 498
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHmSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 499 YEK----ERYEKVIKACALKkdlqlledgDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 573
Cdd:PRK11432 105 MLGvpkeERKQRVKEALELV---------DLAGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157502203 574 FElcicQI--LHEK--ITIL-VTH-QLQYLKAASQILILKDGKMVQKGT 616
Cdd:PRK11432 176 RE----KIreLQQQfnITSLyVTHdQSEAFAVSDTVIVMNKGKIMQIGS 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
426-621 |
1.34e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWVFSGTLRSN 492
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 I-LFGKKYEKERYEK--------VIKACALKKDLQLLEDGDltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:PLN03130 1333 LdPFNEHNDADLWESlerahlkdVIRRNSLGLDAEVSEAGE---------NFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 564 AVDAEVS-------RHLFELCicqilhekiTILV-THQLQYLKAASQILILKDGKMVQKGTYTEFL 621
Cdd:PLN03130 1404 AVDVRTDaliqktiREEFKSC---------TMLIiAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
383-623 |
1.35e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.16 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 383 IRRIQtfllLDEISQRNRQLPS----DGKKM----VHVQDFTAFWDkasETPTLQGLSFTVRPGELLAVVGPVGAGKSSL 454
Cdd:PRK15064 289 IDKIK----LEEVKPSSRQNPFirfeQDKKLhrnaLEVENLTKGFD---NGPLFKNLNLLLEAGERLAIIGENGVGKTTL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 455 LSAVLGELAPSHGLV--SVHGRIAYVSQQPwvfsgtlrsnilfgkkyekeryekvikACALKKDLQLLE---------DG 523
Cdd:PRK15064 362 LRTLVGELEPDSGTVkwSENANIGYYAQDH---------------------------AYDFENDLTLFDwmsqwrqegDD 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 524 DLTVigdRGT----------------TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLfelcicQILHEKIT 587
Cdd:PRK15064 415 EQAV---RGTlgrllfsqddikksvkVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL------NMALEKYE 485
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 157502203 588 ---ILVTHQLQYLKA-ASQILILKDGKMVQ-KGTYTEFLKS 623
Cdd:PRK15064 486 gtlIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYLRS 526
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
410-634 |
1.44e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 71.48 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTAFWDkASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIA 476
Cdd:cd03288 20 IKIHDLCVRYE-NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 477 YVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIY 556
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 557 LLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFL--KSGIdFGSLLKKD 634
Cdd:cd03288 179 IMDEATASIDM-ATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaqEDGV-FASLVRTD 256
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
403-616 |
2.37e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.81 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 403 PSDGKKMVHVQDFTAFWDKASETP--TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------- 473
Cdd:PRK13631 15 PLSDDIILRVKNLYCVFDEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 ----------------------RIAYVSQQP--WVFSGTLRSNILFG------KKYE-KERYEKVIKACALKKDLqlLED 522
Cdd:PRK13631 95 nnhelitnpyskkiknfkelrrRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLDDSY--LER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 523 GDLTvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQL-QYLKAAS 601
Cdd:PRK13631 173 SPFG--------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeHVLEVAD 244
|
250
....*....|....*
gi 157502203 602 QILILKDGKMVQKGT 616
Cdd:PRK13631 245 EVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
424-613 |
2.41e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP--WV 484
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFPeaQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 FSGTLRSNILFGKK----YEKERYEKVIKacALKKdLQLLEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK13641 99 FENTVLKDVEFGPKnfgfSEDEAKEKALK--WLKK-VGLSED----LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157502203 561 PLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYL-KAASQILILKDGKMVQ 613
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
425-611 |
3.25e-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: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG---------RIAYVSQQPWVfsgTLRSNILF 495
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKIGV---VFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 496 gkkYEKERYEKVikACAL-----------KKDLQLLEDGDLT-VIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:cd03292 91 ---PDRNVYENV--AFALevtgvppreirKRVPAALELVGLShKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157502203 564 AVDAEVSRHLFELcICQILHEKITILV-THQLQYLKAAS-QILILKDGKM 611
Cdd:cd03292 166 NLDPDTTWEIMNL-LKKINKAGTTVVVaTHAKELVDTTRhRVIALERGKL 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
426-568 |
3.95e-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: 69.77 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVH---------------------GRIAYVSQ---- 480
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 481 -----------QPWVFSGTlrsnilfgkkyekERYEKVIKACALKKDLQLLEdgdltvigdR-----GTTLSGGQKARVN 544
Cdd:COG4778 105 iprvsaldvvaEPLLERGV-------------DREEARARARELLARLNLPE---------RlwdlpPATFSGGEQQRVN 162
|
170 180
....*....|....*....|....
gi 157502203 545 LARAVYQDADIYLLDDPLSAVDAE 568
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAA 186
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
424-624 |
4.75e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP--WV 484
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 FSGTLRSNILFGKKYEKERYEKViKACALKKDLQLLEDGDltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13646 99 FEDTVEREIIFGPKNFKMNLDEV-KNYAHRLLMDLGFSRD--VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 565 VDAEVSRHLFELCI-CQILHEKITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:PRK13646 176 LDPQSKRQVMRLLKsLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
425-618 |
4.84e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.46 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRiaYVSQQPWVFSGTLRSN------------ 492
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQklgfiyqfhhll 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ------------ILFGKKYEKERYEK---VIKACALKKDLQlledgdltvigDRGTTLSGGQKARVNLARAVYQDADIYL 557
Cdd:PRK11629 100 pdftalenvampLLIGKKKPAEINSRaleMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 558 LDDPLSAVDAEVSRHLFELC-ICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYT 618
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLM 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
442-619 |
5.69e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 442 AVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------------IAYVSQQPWVFSG-TLRSNILFG-KKYEKE 502
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLFPHyKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 503 RYEKVIKACALKKdlqLLedgdltvigDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLfeLCICQI 581
Cdd:PRK11144 108 QFDKIVALLGIEP---LL---------DRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL--LPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157502203 582 LHE--KITIL-VTHQLQ-YLKAASQILILKDGKMVQKGTYTE 619
Cdd:PRK11144 174 LAReiNIPILyVSHSLDeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
407-623 |
5.97e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.02 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 407 KKMVHVQDFTaFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------------- 473
Cdd:PRK13632 5 SVMIKVENVS-FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 474 RIAYVSQQP-WVFSG-TLRSNILFG---KKYEKERYEKVIKACALKKDLQLLEDGDltvigdrGTTLSGGQKARVNLARA 548
Cdd:PRK13632 84 KIGIIFQNPdNQFIGaTVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDYLDKE-------PQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 549 VYQDADIYLLDDPLSAVDAEVSRHlfelcICQILHE------KITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 622
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKRE-----IKKIMVDlrktrkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
.
gi 157502203 623 S 623
Cdd:PRK13632 232 N 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
424-621 |
9.02e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.97 E-value: 9.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPSHGLV---SVHGRIA----------YVSQQPWVFSG- 487
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDLIVdglKVNDPKVderlirqeagMVFQQFYLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGKKyekeRYEKVIKACALKKDLQLLEDGDLtviGDRG----TTLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:PRK09493 93 TALENVMFGPL----RVRGASKEEAEKQARELLAKVGL---AERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 564 AVDAEVsRHlfE-LCICQILHEK--ITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFL 621
Cdd:PRK09493 166 ALDPEL-RH--EvLKVMQDLAEEgmTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
428-650 |
9.83e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 492
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFG----------KKYEKERYEKVIKACALKKDLQlledgdlTVIGDrgttLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:COG1129 100 IFLGreprrgglidWRAMRRRARELLARLGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 563 SAVDAEVSRHLFELcICQILHEKITIL-VTHQLQYLKA-ASQILILKDGKMVqkgtyTEFLKSGIDFGSLLKK------D 634
Cdd:COG1129 169 ASLTEREVERLFRI-IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLV-----GTGPVAELTEDELVRLmvgrelE 242
|
250
....*....|....*.
gi 157502203 635 NEESEQPPVPGTPTLR 650
Cdd:COG1129 243 DLFPKRAAAPGEVVLE 258
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
424-612 |
9.88e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV----------SVHGRIAYVSQqpwVF-------- 485
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklPEYKRAKYIGR---VFqdpmmgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 486 -SGTLRSNILF----GKKY---------EKERY-EKVikacalkKDLQL-LEDGDLTVIGdrgtTLSGGQKARVNLARAV 549
Cdd:COG1101 95 pSMTIEENLALayrrGKRRglrrgltkkRRELFrELL-------ATLGLgLENRLDTKVG----LLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 550 YQDADIYLLDDPLSAVDAEVSRHLFELcICQILHEK--ITILVTHQLQY-LKAASQILILKDGKMV 612
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLEL-TEKIVEENnlTTLMVTHNMEQaLDYGNRLIMMHEGRII 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
424-615 |
1.03e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.23 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------------------------RIAY 477
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 478 VSQQ--PWVFSgTLRSNIL--------FGKKYEKERYEKVIKACALKKDLQlledgdltviGDRGTTLSGGQKARVNLAR 547
Cdd:PRK10619 97 VFQHfnLWSHM-TVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 548 AVYQDADIYLLDDPLSAVDAEVSRHLfeLCICQILHE--KITILVTHQLQYLK-AASQILILKDGKMVQKG 615
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEV--LRIMQQLAEegKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEG 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
428-599 |
1.04e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQ-------PWVFS-------GTLRS 491
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQKlyldttlPLTVNrflrlrpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 NILfgkkyekERYEKVIKACALKKDLQlledgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:PRK09544 100 DIL-------PALKRVQAGHLIDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|
gi 157502203 572 HLFELcICQILHEK--ITILVTHQLQYLKA 599
Cdd:PRK09544 158 ALYDL-IDQLRRELdcAVLMVSHDLHLVMA 186
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
429-621 |
1.10e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.24 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 429 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQ----------QPWVF 485
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLAQnattpgditvQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 486 SGTLRSNILFgKKYEKERYEKVIKAcalkkdlqLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PRK10253 104 RGRYPHQPLF-TRWRKEDEEAVTKA--------MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 566 DAEVSRHLFELcICQILHEKITIL--VTHQL-QYLKAASQILILKDGKMVQKGTYTEFL 621
Cdd:PRK10253 175 DISHQIDLLEL-LSELNREKGYTLaaVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
417-622 |
1.90e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 417 AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP---SHGLVSVHG-------------RIAYVSQ 480
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGitltaktvwdireKVGIVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 481 QP-WVFSG-TLRSNILFGKKYEKERYEKVIKACAlkkdlQLLED-GDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYL 557
Cdd:PRK13640 92 NPdNQFVGaTVGDDVAFGLENRAVPRPEMIKIVR-----DVLADvGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 558 LDDPLSAVDAEVSRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 622
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKL-IRKLKKKNnLTVIsITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
415-622 |
1.93e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 415 FTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPS---HGLVSVHG----------RIAYVsQQ 481
Cdd:TIGR00955 28 RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemraISAYV-QQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 482 PWVFSGTL--RSNILF----------GKKYEKERYEKVIKACALKKDLQlledgdlTVIGDRGTT--LSGGQKARVNLAR 547
Cdd:TIGR00955 107 DDLFIPTLtvREHLMFqahlrmprrvTKKEKRERVDEVLQALGLRKCAN-------TRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 548 AVYQDADIYLLDDPLSAVDA----EVSRHLFELCicqiLHEKITILVTHQLQY--LKAASQILILKDGKMVQKGTYTEFL 621
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSfmaySVVQVLKGLA----QKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
.
gi 157502203 622 K 622
Cdd:TIGR00955 256 P 256
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
427-624 |
2.06e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 68.24 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 427 TLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------LVSVHGRIAYVSQQP---WVFSgTLR 490
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaitddnFEKLRKHIGIVFQNPdnqFVGS-IVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNILFGKKYEKERYEKVIKACAlkkdlQLLEDGDLTVIGD-RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVS-----EALKQVDMLERADyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 570 SRHLFELcICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSG 624
Cdd:PRK13648 178 RQNLLDL-VRKVKSEHnITIIsITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
425-616 |
2.29e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.48 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWV-FSG-T 488
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklVGIVFQNPETqFVGrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 LRSNILFGKKyekeryekviKACALKKDLQLLEDGDLTVIG------DRGTTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK13644 95 VEEDLAFGPE----------NLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 563 SAVDAEVSRHLFELCicQILHEK--ITILVTHQLQYLKAASQILILKDGKMVQKGT 616
Cdd:PRK13644 165 SMLDPDSGIAVLERI--KKLHEKgkTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
428-625 |
3.32e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.64 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------------------IAYVSQQPwvf 485
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyalseaerrrllrteWGFVHQHP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 486 SGTLRSNILFGKKY-EK-----ERYEKVIKACALKKdLQLLEDgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK11701 99 RDGLRMQVSAGGNIgERlmavgARHYGDIRATAGDW-LERVEI-DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 560 DPLSAVDAEVSRHLFELcICQILHEK--ITILVTHQLQYLKA-ASQILILKDGKMVQKG-----------TYTEFLKSGI 625
Cdd:PRK11701 177 EPTGGLDVSVQARLLDL-LRGLVRELglAVVIVTHDLAVARLlAHRLLVMKQGRVVESGltdqvlddpqhPYTQLLVSSV 255
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
425-619 |
4.44e-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: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------IAYVSQQ----PWVfsgTL 489
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyalyPHM---SV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 RSNILFG---KKYEKERYEKVIKACAlkkdlQLLEDGDLTvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PRK11650 94 RENMAYGlkiRGMPKAEIEERVAEAA-----RILELEPLL---DRKpRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 566 DAEVSRHL-FELcicQILHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 619
Cdd:PRK11650 166 DAKLRVQMrLEI---QRLHRRLkttSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
423-622 |
4.91e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVSVHGRI-------------AYVSQQpwvfsgtl 489
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelarhrAYLSQQ-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 rSNILF------------GKKYEKERYEKVIKACAlkkdlQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQ------ 551
Cdd:PRK03695 78 -QTPPFampvfqyltlhqPDKTRTEAVASALNEVA-----EALGLDDK--LGRSVNQLSGGEWQRVRLAAVVLQvwpdin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 552 -DADIYLLDDPLSAVD----AEVSRHLFELCicqilHEKITILVT-HQLQY-LKAASQILILKDGKMVQKGTYTEFLK 622
Cdd:PRK03695 150 pAGQLLLLDEPMNSLDvaqqAALDRLLSELC-----QQGIAVVMSsHDLNHtLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
428-616 |
5.04e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.44 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRiayvsqqPwvFSGTLRSNIlfGkkY--EkER-- 503
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-------P--LDPEDRRRI--G--YlpE-ERgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 504 Y--EKVI-------------KACALKKDLQLLEDGDltvIGDRGT----TLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:COG4152 83 YpkMKVGeqlvylarlkglsKAEAKRRADEWLERLG---LGDRANkkveELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 565 VDAeVSRHLFElcicQILHE-----KITILVTHQLQYLKA-ASQILILKDGKMVQKGT 616
Cdd:COG4152 160 LDP-VNVELLK----DVIRElaakgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
428-619 |
5.27e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.29 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------------IAYVSQQpwvF----SG 487
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrkarrqIGMIFQH---FnllsSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGKKYEKERYEKvIKacalKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK11153 98 TVFDNVALPLELAGTPKAE-IK----ARVTELLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 567 AEVSRHLFELcICQILHE-KITI-LVTHQLQYLKA-ASQILILKDGKMVQKGTYTE 619
Cdd:PRK11153 173 PATTRSILEL-LKDINRElGLTIvLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSE 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
427-610 |
5.62e-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: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 427 TLQGLSFTVRPG-----ELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-RIAYVSQQPWV-FSGTLRSnILFGK-- 497
Cdd:cd03237 9 TLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKAdYEGTVRD-LLSSItk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 498 -KYEKERYEKVIKacalkKDLQLlEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------V 569
Cdd:cd03237 88 dFYTHPYFKTEIA-----KPLQI-EQ----ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmaskV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157502203 570 SRHLfelcicqILHEKITILVT-HQLQYLKAASQILILKDGK 610
Cdd:cd03237 158 IRRF-------AENNEKTAFVVeHDIIMIDYLADRLIVFEGE 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
403-612 |
5.92e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 403 PSDGKKMVHVQDFTAfwdkaseTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------- 474
Cdd:COG1129 250 AAPGEVVLEVEGLSV-------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirspr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 475 ------IAYVS----QQPWVFSGTLRSNI------------LFGKKYEKERYEKVIKACALKkdlqlLEDGDLTVigdrg 532
Cdd:COG1129 323 dairagIAYVPedrkGEGLVLDLSIRENItlasldrlsrggLLDRRRERALAEEYIKRLRIK-----TPSPEQPV----- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 533 TTLSGG--QKarVNLARAVYQDADIYLLDDPLSAVD----AEVSRHLFELCicqilHEKITILVT----HQLqyLKAASQ 602
Cdd:COG1129 393 GNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGIDvgakAEIYRLIRELA-----AEGKAVIVIsselPEL--LGLSDR 463
|
250
....*....|
gi 157502203 603 ILILKDGKMV 612
Cdd:COG1129 464 ILVMREGRIV 473
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
420-623 |
7.30e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.14 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 420 DKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP 482
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 483 WVFSG-TLRSNILFGKKYE----KERYEKVIKAcalkkdlqLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYL 557
Cdd:PRK10070 116 ALMPHmTVLDNTAFGMELAginaEERREKALDA--------LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 558 LDDPLSAVDAEVSRHLF-ELCICQILHEKITILVTHQL-QYLKAASQILILKDGKMVQKGTYTEFLKS 623
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
428-616 |
1.53e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.62 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL---APSHGlVSVHGRI-------------------AYVSQ--QPw 483
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRG-ARVTGDVtlngeplaaidaprlarlrAVLPQaaQP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 484 VFSGTLRSNILFGkkyekeRYEKVIKACALKKdlqllEDGDL-----------TVIGDRGTTLSGGQKARVNLARAVYQ- 551
Cdd:PRK13547 95 AFAFSAREIVLLG------RYPHARRAGALTH-----RDGEIawqalalagatALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 552 --------DADIYLLDDPLSAVDAEVSRHLFE----------LCICQILHEkITILVTHqlqylkaASQILILKDGKMVQ 613
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDtvrrlardwnLGVLAIVHD-PNLAARH-------ADRIAMLADGAIVA 235
|
...
gi 157502203 614 KGT 616
Cdd:PRK13547 236 HGA 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
431-621 |
2.10e-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: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTvrPGELLAVVGPVGAGKSSLL-------SAVLGELAPSHGLvsvhgRIAYVSQQPWV-FSGTLRSNILFG------ 496
Cdd:TIGR03719 26 LSFF--PGAKIGVLGLNGAGKSTLLrimagvdKDFNGEARPQPGI-----KVGYLPQEPQLdPTKTVRENVEEGvaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 497 --KKY-------------------EKERYEKVIKAC-ALKKDLQL--------LEDGDLTVigdrgTTLSGGQKARVNLA 546
Cdd:TIGR03719 99 alDRFneisakyaepdadfdklaaEQAELQEIIDAAdAWDLDSQLeiamdalrCPPWDADV-----TKLSGGERRRVALC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 547 RAVYQDADIYLLDDPLSAVDAE----VSRHLFElcicqilHEKITILVTHQLQYL-KAASQILILKDGKMVQ-KGTYTEF 620
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAEsvawLERHLQE-------YPGTVVAVTHDRYFLdNVAGWILELDRGRGIPwEGNYSSW 246
|
.
gi 157502203 621 L 621
Cdd:TIGR03719 247 L 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
410-626 |
3.21e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 410 VHVQDFTAFWDKASetpTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAvLGELAPSHGLVSVHGRIAYVSQ--------- 480
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQniyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 481 ------------QPWVFSGTLRSNILFGKK----YEKERYEKVIKACALKKDLQlleDGDLTVIGDRGTTLSGGQKARVN 544
Cdd:PRK14258 84 nrlrrqvsmvhpKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDADLW---DEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 545 LARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITI-LVTHQLQYLKAASQILIL------KDGKMVQKGTY 617
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMvIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEFGLT 240
|
....*....
gi 157502203 618 TEFLKSGID 626
Cdd:PRK14258 241 KKIFNSPHD 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
428-616 |
4.09e-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: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGeLAPSHGLVSVHGR-IAYVSQ---QPW------VFS---GTL--RSN 492
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdLDGLSRralRPLrrrmqvVFQdpfGSLspRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 I----------LFGKKYEKERYEKVIkacalkkdlQLLEDGDLtvigDRGTT------LSGGQKARVNLARAVYQDADIY 556
Cdd:COG4172 381 VgqiiaeglrvHGPGLSAAERRARVA---------EALEEVGL----DPAARhrypheFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 557 LLDDPLSAVDAEVSRhlfelcicQIL--------HEKIT-ILVTHQLQYLKA-ASQILILKDGKMVQKGT 616
Cdd:COG4172 448 VLDEPTSALDVSVQA--------QILdllrdlqrEHGLAyLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
423-568 |
6.42e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.94 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------IAYVSQQPwvfsgtlrsn 492
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLP---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ilfGKKYEKERYEKVIKACALK-KDLQLLEDGDLTVIGDRG------TTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PRK13543 92 ---GLKADLSTLENLHFLCGLHgRRAKQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
...
gi 157502203 566 DAE 568
Cdd:PRK13543 169 DLE 171
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
428-612 |
6.54e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSaVLGEL-APSHGLVSVHGR-----------------IAYVSQQPWVFSG-T 488
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQdvatldadalaqlrrehFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 LRSNILFGKKYE-KERYEKVIKACALKKDLQLLEDgdltvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PRK10535 103 AAQNVEVPAVYAgLERKQRLLRAQELLQRLGLEDR-----VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 157502203 568 EVSRHLfeLCICQILHEK--ITILVTHQLQYLKAASQILILKDGKMV 612
Cdd:PRK10535 178 HSGEEV--MAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
422-616 |
6.62e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 422 ASETP----TLQGLSFTVRPGELLAVVGPVGAGKSSLLS------------AVLGELAPSHGLVSV------HGRIAYVS 479
Cdd:PRK13645 17 AKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIkevkrlRKEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 480 QQP--WVFSGTLRSNILFGKKYEKERYEKVIKACA-LKKDLQLLEDgdltVIGDRGTTLSGGQKARVNLARAVYQDADIY 556
Cdd:PRK13645 97 QFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPeLLKLVQLPED----YVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 557 LLDDPLSAVDAEVSRHLFELCI-CQILHEKITILVTHQL-QYLKAASQILILKDGKMVQKGT 616
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFErLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
428-612 |
7.66e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 492
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 IL------FGKKYEKERYEKVIKACALKKDLQLledgDL-TVIGDrgttLSGGQKARVNLARAVYQDADIYLLDDPlSAV 565
Cdd:COG3845 101 IVlgleptKGGRLDRKAARARIRELSERYGLDV----DPdAKVED----LSVGEQQRVEILKALYRGARILILDEP-TAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 566 --DAEVsRHLFElcicqILHE-----KITILVTHQLQYLKAAS-QILILKDGKMV 612
Cdd:COG3845 172 ltPQEA-DELFE-----ILRRlaaegKSIIFITHKLREVMAIAdRVTVLRRGKVV 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
428-615 |
8.86e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.32 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAV-----LGELAPSHGLVSVHGRIAY---------------VSQQPWVFSG 487
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpievrrevgmVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 -TLRSNILFGKKYEK---------ERYEKVIKACALKKDLQlledgdlTVIGDRGTTLSGGQKARVNLARAVYQDADIYL 557
Cdd:PRK14267 100 lTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 558 LDDPLSAVDAEVSRHLFELcICQILHEKITILVTHQ-LQYLKAASQILILKDGKMVQKG 615
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEEL-LFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
428-621 |
9.16e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG----------LVSVHGR----IAYVSQQPWVFSgtlRSNI 493
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedisLLPLHARarrgIGYLPQEASIFR---RLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 lfgkkyekerYEKVIKACALKKDL----------QLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK10895 96 ----------YDNLMAVLQIRDDLsaeqredranELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 563 SAVDAeVSRHLFELCICQILHEKITILVT-HQL-QYLKAASQILILKDGKMVQKGTYTEFL 621
Cdd:PRK10895 166 AGVDP-ISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
428-623 |
9.36e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-------------RIAYVSQQPWV-------FSG 487
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqRIRMIFQDPSTslnprqrISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFGKKYEKERYEKVIKAcALKKdLQLLEDGdltvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIE-TLRQ-VGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 568 EVSRHLFELCI-CQILHEKITILVTHQLQYLKAAS-QILILKDGKMVQKGTYTEFLKS 623
Cdd:PRK15112 183 SMRSQLINLMLeLQEKQGISYIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVLAS 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
428-613 |
1.01e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQ-PWVFSGTLRSN 492
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAIIYQElHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGKKYEKeryEKVIKACALKKD--LQLLEDG-DLtvigDRGT---TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK11288 100 LYLGQLPHK---GGIVNRRLLNYEarEQLEHLGvDI----DPDTplkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157502203 567 AEVSRHLFELcICQILHE-KITILVTHQLQYLKAAS-QILILKDGKMVQ 613
Cdd:PRK11288 173 AREIEQLFRV-IRELRAEgRVILYVSHRMEEIFALCdAITVFKDGRYVA 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
428-612 |
1.05e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.58 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVSQQPWVFsgtLRSNI--LFGKKY---EK 501
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITRLKNREVPF---LRRQIgmIFQDHHllmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 502 ERYEKV----IKACALKKDLQLLEDGDLTVIG--DRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:PRK10908 95 TVYDNVaiplIIAGASGDDIRRRVSAALDKVGllDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157502203 572 ---HLFElcicQILHEKITILV-THQLQYLKAAS-QILILKDGKMV 612
Cdd:PRK10908 175 gilRLFE----EFNRVGVTVLMaTHDIGLISRRSyRMLTLSDGHLH 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
406-623 |
1.10e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 406 GKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAY-------- 477
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 478 -----------VSQQPWVFSG-TLRSNILFGKKY----EKERYEKVIKACalkkdlqLLEDGDLTVIGDR----GTTLSG 537
Cdd:PRK14246 84 daiklrkevgmVFQQPNPFPHlSIYDNIAYPLKShgikEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 538 GQKARVNLARAVYQDADIYLLDDPLSAVDAeVSRHLFELCICQILHEKITILVTHQLQYL-KAASQILILKDGKMVQKGT 616
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGS 235
|
....*..
gi 157502203 617 YTEFLKS 623
Cdd:PRK14246 236 SNEIFTS 242
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
428-615 |
1.38e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL------GEL----APSHG-----LVSVHGRIAYVSQQPwvfSGTL--R 490
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLrlinsqGEIwfdgQPLHNlnrrqLLPVRHRIQVVFQDP---NSSLnpR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNIL----------FGKKYEKERYEKVIKAcalkkdlqLLEDG-DLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK15134 379 LNVLqiieeglrvhQPTLSAAQREQQVIAV--------MEEVGlDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 560 DPLSAVDAEVSRHLFELC-ICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKG 615
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLkSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
428-655 |
1.41e-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: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG--ELAPSHGLVSVH----------GRIAYVSQQPWVFSGTL------ 489
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyvERPSKVGEPCPVCGGTLepeevd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 --------------RSNILFGKK---YEKER-YEKVIKAC---------ALKKDLQLLEdgdLTVIGDRGT----TLSGG 538
Cdd:TIGR03269 96 fwnlsdklrrrirkRIAIMLQRTfalYGDDTvLDNVLEALeeigyegkeAVGRAVDLIE---MVQLSHRIThiarDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 539 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVT-HQLQYL-KAASQILILKDGKMVQKGT 616
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIeDLSDKAIWLENGEIKEEGT 252
|
250 260 270
....*....|....*....|....*....|....*....
gi 157502203 617 YTEFLKSGIDFGSLLKKDNEESEQPPVPGTPTLRNRTFS 655
Cdd:TIGR03269 253 PDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYIS 291
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
428-610 |
1.60e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG--------LVSVHGRIAYVSQQ----PWvfsgtlrsnilf 495
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtapLAEAREDTRLMFQDarllPW------------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 496 gkkyekeryEKVIKACAL-------KKDLQLLEDGDLTvigDRGT----TLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK11247 96 ---------KKVIDNVGLglkgqwrDAALQALAAVGLA---DRANewpaALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157502203 565 VDAeVSR----HLFELCICQilHEKITILVTHQLQYLKA-ASQILILKDGK 610
Cdd:PRK11247 164 LDA-LTRiemqDLIESLWQQ--HGFTVLLVTHDVSEAVAmADRVLLIEEGK 211
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
305-612 |
1.82e-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: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 305 KEISKILRSSCLRGMNlasFFSASKIIVFVTFttYVLLGSVITASRVFVAVTLYGAVRLTVTLFF---P-----SAIERV 376
Cdd:COG4615 215 QPTAERYRDLRIRADT---IFALANNWGNLLF--FALIGLILFLLPALGWADPAVLSGFVLVLLFlrgPlsqlvGALPTL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 377 SEAIVSIRRIQTF-LLLDEISQRNRQLPSDgkkmVHVQDFT---------AFWDKASETP-TLQGLSFTVRPGELLAVVG 445
Cdd:COG4615 290 SRANVALRKIEELeLALAAAEPAAADAAAP----PAPADFQtlelrgvtyRYPGEDGDEGfTLGPIDLTIRRGELVFIVG 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 446 PVGAGKSSLLSAVLGELAPSHGLVSVHGRIayVSQQPWvfsGTLRSNI--------LFGKKYEKERYEKVIKACALKKDL 517
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQP--VTADNR---EAYRQLFsavfsdfhLFDRLLGLDGEADPARARELLERL 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 518 QLleDGDLTVIGDRGTT--LSGGQKARVNLARAVYQDADIYLLD------DPlsavdaeVSRHLFelcICQILHE----- 584
Cdd:COG4615 441 EL--DHKVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFRRVF---YTELLPElkarg 508
|
330 340
....*....|....*....|....*...
gi 157502203 585 KITILVTHQLQYLKAASQILILKDGKMV 612
Cdd:COG4615 509 KTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
421-612 |
2.11e-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: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 421 KASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELapsHGLVSV------------------HGRIAYVSQQP 482
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVegdihyngipykefaekyPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 483 WVFSG-TLRSNILFgkkyekeryekvikACALKkdlqlledGDLTVigdRGttLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:cd03233 93 VHFPTlTVRETLDF--------------ALRCK--------GNEFV---RG--ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 562 LSAVDAEVSRHLFElCICQILHE-KITILVThqlqyLKAAS--------QILILKDGKMV 612
Cdd:cd03233 146 TRGLDSSTALEILK-CIRTMADVlKTTTFVS-----LYQASdeiydlfdKVLVLYEGRQI 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
428-615 |
2.29e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 492
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGK--------------KYEKERYEKVIKACALKKDLQlledgdlTVIGDrgttLSGGQKARVNLARAVYQDADIYLL 558
Cdd:PRK09700 101 LYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDLD-------EKVAN----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 559 DDPLSAVDAEVSRHLFeLCICQILHE-KITILVTHQLQYLKA-ASQILILKDGKMVQKG 615
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF-LIMNQLRKEgTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
428-630 |
2.37e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.11 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQ-PWVFSGTLRSNI 493
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 LFGK-----------KYEKERYEKVIKACALKKDLQLLEDgdltvigdrgtTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK10575 107 AIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 563 SAVDaeVSRHLFELCICQILHEKITILVTHQLQYLKAASQ----ILILKDGKMVQKGTYTEFLKS-------GIDFGSL 630
Cdd:PRK10575 176 SALD--IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARycdyLVALRGGEMIAQGTPAELMRGetleqiyGIPMGIL 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
425-619 |
3.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.17 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 425 TPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR---------------IAYVSQQP--WVFSG 487
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklresVGMVFQDPdnQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TLRSNILFG----KKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK13636 99 SVYQDVSFGavnlKLPEDEVRKRVDNA---------LKRTGIEHLKDKPThCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 563 SAVDAEVSRHLFELCICQILHEKITILV-THQLQYLKA-ASQILILKDGKMVQKGTYTE 619
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKELGLTIIIaTHDIDIVPLyCDNVFVMKEGRVILQGNPKE 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
434-616 |
3.51e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 434 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-----------------IAYVSQQP--WVFSGTLRSNIL 494
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkknkklkplrkkVGIVFQFPehQLFEETVEKDIC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 495 FG-------KKYEKERYEKVIKACALKKDLQlledgdltvigDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13634 109 FGpmnfgvsEEDAKQKAREMIELVGLPEELL-----------ARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 567 AEVSRHLFELcICQILHEK--ITILVTHQL----QYlkaASQILILKDGKMVQKGT 616
Cdd:PRK13634 178 PKGRKEMMEM-FYKLHKEKglTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGT 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
434-627 |
3.72e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 434 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQqpWV---FSGT----LRSNilfGKKYEKERYE- 505
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTvedlLRSI---TDDLGSSYYKs 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 506 KVIKACALKKdlqLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VSRHLFElci 578
Cdd:PRK13409 436 EIIKPLQLER---LLDK--------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlavakAIRRIAE--- 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 579 cqiLHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYT----------EFLKS-GIDF 627
Cdd:PRK13409 502 ---EREATALVVDHDIYMIDYISDRLMVFEGEPGKHGHASgpmdmregmnRFLKElGITF 558
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
707-845 |
3.90e-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: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 707 AGAHWIVFIFLILLNTAAQVAYVLQDWWLSYWANkqsmlnvTVNGGGNVTEkldLNWYLGIYSGLTVATVLFGIARSLLV 786
Cdd:COG1132 16 LRPYRGLLILALLLLLLSALLELLLPLLLGRIID-------ALLAGGDLSA---LLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 787 FYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVR 144
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
438-615 |
4.30e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 438 GELLAVVGPVGAGKSSLLSAVLG-ELAPSHGLVSVHGRIAYVsqQP------WVFSG-------TLRSNILFGKKYEK-- 501
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGlEDITSGDLFIGEKRMNDV--PPaergvgMVFQSyalyphlSVAENMSFGLKLAGak 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 502 --ERYEKVIKACALKKDLQLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA--------EVSR 571
Cdd:PRK11000 107 keEINQRVNQVAEVLQLAHLLDR--------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmriEISR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157502203 572 hlfelcicqiLHEKI---TILVTH-QLQYLKAASQILILKDGKMVQKG 615
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) ... |
434-597 |
4.46e-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: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 434 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGL------------------------------VSVHGRIAYVSQQPW 483
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkllegdVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 484 VFSGTLRSniLFGKKYEKERYEKVIKACALKKDLqlledgdltvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:cd03236 102 AVKGKVGE--LLKKKDERGKLDELVDQLELRHVL------------DRNiDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157502203 563 SAVD-------AEVSRHLFElcicqilHEKITILVTHQLQYL 597
Cdd:cd03236 168 SYLDikqrlnaARLIRELAE-------DDNYVLVVEHDLAVL 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
426-585 |
4.57e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.34 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTL-QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLV--SVHGRIAYVSQQPwVFSGTLRSNILFgkkYEKE 502
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMAVFSQHH-VDGLDLSSNPLL---YMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 503 RYEKVIKAcALKKDLqlledGDLTVIGDRGT----TLSGGQKARVNLARAVYQDADIYLLDDP-----LSAVDAEVS-RH 572
Cdd:PLN03073 598 CFPGVPEQ-KLRAHL-----GSFGVTGNLALqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPsnhldLDAVEALIQgLV 671
|
170
....*....|...
gi 157502203 573 LFELCICQILHEK 585
Cdd:PLN03073 672 LFQGGVLMVSHDE 684
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
434-627 |
6.93e-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: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 434 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAY----VSQQpwvFSGT----LRSNI---LFGKKYEKE 502
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyISPD---YDGTveefLRSANtddFGSSYYKTE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 503 ryekVIKACALKKdlqLLEDgdltvigdRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VSRHLFE 575
Cdd:COG1245 439 ----IIKPLGLEK---LLDK--------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlavakAIRRFAE 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157502203 576 lcicqiLHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYT----------EFLKS-GIDF 627
Cdd:COG1245 504 ------NRGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASgpmdmregmnRFLKElGITF 560
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
428-619 |
6.96e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-------------IAYVSQQP--WVFSGTLRSN 492
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGT-TLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13652 100 IAFGpinlgldEETVAHRVSSALHMLGLEE------------LRDRVPhHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 565 VDAEVSRHLFELCICQILHEKIT-ILVTHQLQYL-KAASQILILKDGKMVQKGTYTE 619
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTvIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEE 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
424-627 |
7.10e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH--GLVSVHG---------RIAYVSQQPWVFSG-TLRS 491
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrkptkqilkRTGFVTQDDILYPHlTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 NILF------GKKYEKEryEKVIKACALKKDLQLLEDGDlTVIGD---RGttLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQ--EKILVAESVISELGLTKCEN-TIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 563 SAVDAEVSRHLFeLCICQILHEKITILVT-HQ--LQYLKAASQILILKDGK--MVQKGTYTEFLKSGIDF 627
Cdd:PLN03211 235 SGLDATAAYRLV-LTLGSLAQKGKTIVTSmHQpsSRVYQMFDSVLVLSEGRclFFGKGSDAMAYFESVGF 303
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
428-616 |
7.68e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQPWVFSG-TLRSN 492
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimreaVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGKKY-EKERYEKVIKACAlkkDL--QLLEDGdltviGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWVY---ELfpRLHERR-----IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 157502203 570 SRHLFELcICQILHEKITILVTHQ--LQYLKAASQILILKDGKMVQKGT 616
Cdd:PRK11614 173 IQQIFDT-IEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
428-612 |
7.93e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSL---LSAVL------GE-------LAPSH-------GLVSVHGRIAYVSQQpwv 484
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYphgtyeGEiifegeeLQASNirdteraGIAIIHQELALVKEL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 fsgTLRSNILFGKKYEKE---RYEKVIKAC-ALKKDLQLLEDGDLTViGDrgttLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK13549 98 ---SVLENIFLGNEITPGgimDYDAMYLRAqKLLAQLKLDINPATPV-GN----LGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157502203 561 PLSAVDAEVSRHLFELcICQILHEKIT-ILVTHQLQYLKAAS-QILILKDGKMV 612
Cdd:PRK13549 170 PTASLTESETAVLLDI-IRDLKAHGIAcIYISHKLNEVKAISdTICVIRDGRHI 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
385-596 |
1.17e-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: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 385 RIQTF--LLLDEISQRNRQL-------PSDGKKMVHVQDFT-AFWDKasetPTLQGLSFTVRPGELLAVVGPVGAGKSSL 454
Cdd:TIGR03719 289 RLARYeeLLSQEFQKRNETAeiyippgPRLGDKVIEAENLTkAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 455 LSAVLGELAPSHGLVSVhG---RIAYVSQQpwvfsgtlRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGD 530
Cdd:TIGR03719 365 FRMITGQEQPDSGTIEI-GetvKLAYVDQS--------RDAL----DPNKTVWEEI-------------SGGlDIIKLGK 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 531 R--------------GT-------TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL------FELCICQILH 583
Cdd:TIGR03719 419 ReipsrayvgrfnfkGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALeeallnFAGCAVVISH 498
|
250
....*....|....*
gi 157502203 584 EK--ITILVTHQLQY 596
Cdd:TIGR03719 499 DRwfLDRIATHILAF 513
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
428-576 |
1.86e-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: 57.83 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPShglvsvhgriayvsqqpwvfSGTLRsniLFGKKYEKERYEKV 507
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA--------------------SGEIT---LDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 508 IKA-CALkkdlqLLED-------GDLTV-----IGDRgttLSGG--QKarVNLARAVYQDADIYLLDDPLSAVD----AE 568
Cdd:cd03215 73 IRAgIAY-----VPEDrkreglvLDLSVaeniaLSSL---LSGGnqQK--VVLARWLARDPRVLILDEPTRGVDvgakAE 142
|
....*...
gi 157502203 569 VSRHLFEL 576
Cdd:cd03215 143 IYRLIREL 150
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
428-621 |
2.06e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.32 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR----------------IAYVSQQP--------- 482
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklnraqrkafrrdIQMVFQDSisavnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 483 --WVFSGTLRSNILFGKKYEKERYEKVIKACALkkdlqlledgDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK10419 108 vrEIIREPLRHLLSLDKAERLARASEMLRAVDL----------DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 561 PLSAVDaevsRHLfELCICQIL----HEKIT--ILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFL 621
Cdd:PRK10419 178 AVSNLD----LVL-QAGVIRLLkklqQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKL 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
426-655 |
3.56e-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: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR------------IAYVSQQPWVFSG-TLRSN 492
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGKKYEKERYEKVikacALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRH 572
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEA----QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 573 LFELcICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQKGTyTEFLKSGIDFGSLL----KKDNEESEQPPVPGTP 647
Cdd:TIGR01257 1100 IWDL-LLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT-PLFLKNCFGTGFYLtlvrKMKNIQSQRGGCEGTC 1177
|
....*...
gi 157502203 648 TLRNRTFS 655
Cdd:TIGR01257 1178 SCTSKGFS 1185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
428-615 |
4.38e-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: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGElapsHGLVSVHGRIAYVSQqpwvfsgtlrsNILFGKKYEKER---- 503
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----PKYEVTEGEILFKGE-----------DITDLPPEERARlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 504 ----YEKVIKACALKKDLQLLEDGdltvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELcIC 579
Cdd:cd03217 81 lafqYPPEIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV-IN 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157502203 580 QILHEKIT-ILVTHQ---LQYLKaASQILILKDGKMVQKG 615
Cdd:cd03217 149 KLREEGKSvLIITHYqrlLDYIK-PDRVHVLYDGRIVKSG 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
428-612 |
5.03e-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: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG----------------ELAPSH-------GLVSVHGRIAYVSQQpwv 484
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASNirdteraGIVIIHQELTLVPEL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 fsgTLRSNILFGK----KYEKERYEKVIKAC-ALKKDLQLLEDGDLTVIGDRGttlsGGQKARVNLARAVYQDADIYLLD 559
Cdd:TIGR02633 94 ---SVAENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 157502203 560 DPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAAS-QILILKDGKMV 612
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCdTICVIRDGQHV 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
418-619 |
5.89e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.56 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 418 FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVSQQPW---------VFSG 487
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWravrsdiqmIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TL-----RSNI---------LFGKKYEKERYEKVIKACALKkdLQLLEDgdltVIGDRGTTLSGGQKARVNLARAVYQDA 553
Cdd:PRK15079 107 PLaslnpRMTIgeiiaeplrTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 554 DIYLLDDPLSAVDAEVSRHLFELciCQILHEKI---TILVTHQLQYLKAAS-QILILKDGKMVQKGTYTE 619
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNL--LQQLQREMglsLIFIAHDLAVVKHISdRVLVMYLGHAVELGTYDE 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
393-623 |
7.07e-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: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 393 DEISQRNRQLPSDGKK--MVHVQDFTAFWDKASeTPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG--- 467
Cdd:TIGR01257 1919 DDVAEERQRIISGGNKtdILRLNELTKVYSGTS-SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdat 1997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 468 ---------LVSVHGRIAYVSQqpwvFSGTlrSNILFGKK--YEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GTTL 535
Cdd:TIGR01257 1998 vagksiltnISDVHQNMGYCPQ----FDAI--DDLLTGREhlYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRlAGTY 2071
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 536 SGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMVQK 614
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCL 2151
|
....*....
gi 157502203 615 GTyTEFLKS 623
Cdd:TIGR01257 2152 GT-IQHLKS 2159
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
424-566 |
1.32e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------RIAYvsQQPWVFSG---------T 488
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTY--QKQLCFVGhrsginpylT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 489 LRSNILFGKKYEKERYEkVIKACALKKdLQLLEDGDLTVigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-ITELCRLFS-LEHLIDYPCGL-------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
431-627 |
1.40e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.05 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV-----------------HGRIAYVSQQP--WVFSGTLRS 491
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeikpvRKKVGVVFQFPesQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 NILFGKK---YEKERYEKV----IKACALKKdlQLLEDGDLTvigdrgttLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13643 105 DVAFGPQnfgIPKEKAEKIaaekLEMVGLAD--EFWEKSPFE--------LSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 565 VDAEVSRHLFELciCQILHE--KITILVTHQLQYL-KAASQILILKDGKMVQKGTYTEFLKSgIDF 627
Cdd:PRK13643 175 LDPKARIEMMQL--FESIHQsgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE-VDF 237
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
424-619 |
1.55e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.46 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAV--LGELAPS---HGLVSVHG-------------RIAYVSQQP-WV 484
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifkmdvielrrRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 FSGTLRSNILFGKKY------EKERYEKVIKacALKKdLQLLEDgdltvIGDR----GTTLSGGQKARVNLARAVYQDAD 554
Cdd:PRK14247 95 PNLSIFENVALGLKLnrlvksKKELQERVRW--ALEK-AQLWDE-----VKDRldapAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 555 IYLLDDPLSAVDAEVSRHLFELCIcQILHEKITILVTH-QLQYLKAASQILILKDGKMVQKGTYTE 619
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFL-ELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
437-612 |
1.57e-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: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 437 PGELLAVVGPVGAGKSSLLSAVLGELAPSHGlvsvhgriayvsqqpwvfsgtlrsnilfgkkyekeryeKVIKACALKKD 516
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--------------------------------------GVIYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 517 LQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQIL-----HEKITILVT 591
Cdd:smart00382 43 EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILT 122
|
170 180
....*....|....*....|.
gi 157502203 592 HQLQYLKAASQILILKDGKMV 612
Cdd:smart00382 123 TNDEKDLGPALLRRRFDRRIV 143
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
442-623 |
2.11e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 442 AVVGPVGAGKSSLL-----------------SAVLG--ELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKE 502
Cdd:PRK14271 51 SLMGPTGSGKTTFLrtlnrmndkvsgyrysgDVLLGgrSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 503 RYEKVIKACALKKdlqLLEDGDLTVIGDRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELci 578
Cdd:PRK14271 131 VPRKEFRGVAQAR---LTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF-- 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 157502203 579 CQILHEKIT-ILVTHQL-QYLKAASQILILKDGKMVQKGTYTEFLKS 623
Cdd:PRK14271 206 IRSLADRLTvIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
424-571 |
2.24e-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: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGEL--APSHGLVSVhgriayvsqqPWVFSGTLRSNI-LFGKKYE 500
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV----------PDNQFGREASLIdAIGRKGD 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 501 KERYEKVIKACALkkdlqlledGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSR 571
Cdd:COG2401 112 FKDAVELLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
428-613 |
3.14e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.11 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSL---LSAVL------------GELA--------PSHGLVSVHGRIAYVSQQpwv 484
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLmkvLSGVYphgsyegeilfdGEVCrfkdirdsEALGIVIIHQELALIPYL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 fsgTLRSNILFGKkyEKERY------EKVIKACALKKDLQLLEDGDlTVIGDRGTtlsgGQKARVNLARAVYQDADIYLL 558
Cdd:NF040905 94 ---SIAENIFLGN--ERAKRgvidwnETNRRARELLAKVGLDESPD-TLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 559 DDPLSAVDAEVSRHLFELcICQILHEKIT-ILVTHQL-QYLKAASQILILKDGKMVQ 613
Cdd:NF040905 164 DEPTAALNEEDSAALLDL-LLELKAQGITsIIISHKLnEIRRVADSITVLRDGRTIE 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
424-616 |
4.44e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.52 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-----------------RIAYVSQQP--WV 484
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdikqirkKVGLVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 FSGTLRSNILFGKK---YEKERYEKVikacALKKdlqlledgdLTVIG------DRGT-TLSGGQKARVNLARAVYQDAD 554
Cdd:PRK13649 99 FEETVLKDVAFGPQnfgVSQEEAEAL----AREK---------LALVGiseslfEKNPfELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 555 IYLLDDPLSAVDAEVSRHLFELciCQILHEK-ITI-LVTHQLQYL-KAASQILILKDGKMVQKGT 616
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTL--FKKLHQSgMTIvLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
97-351 |
4.69e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 55.26 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 97 IFTLIEESAKVIQPIFLGKIINYFenYDPMDSVALNTAyayATVLTFCTLILAILHHLYFYHVQCAG----MRLRVAMch 172
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTI--IKGGDLDVLNEL---ALILLAIYLLQSVFTFVRYYLFNIAGerivARLRRDL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 173 miYRKALRLSNMAMGKTTTGQIVNLLSNDVNKF-DQVTVFLHFLWAGPLQAIAVTALLWMeigISC-LAGmaVLIILLPL 250
Cdd:cd18557 76 --FSSLLRQEIAFFDKHKTGELTSRLSSDTSVLqSAVTDNLSQLLRNILQVIGGLIILFI---LSWkLTL--VLLLVIPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 251 QSCFGKLFSS-LRSKTATFTDARIRTM---NEVITGIRIIkmyaweKSFSNLITNLRK--KEISKILRSSCLRGMNLASF 324
Cdd:cd18557 149 LLIASKIYGRyIRKLSKEVQDALAKAGqvaEESLSNIRTV------RSFSAEEKEIRRysEALDRSYRLARKKALANALF 222
|
250 260
....*....|....*....|....*...
gi 157502203 325 FSASKIIVFV-TFTTYVLLGSVITASRV 351
Cdd:cd18557 223 QGITSLLIYLsLLLVLWYGGYLVLSGQL 250
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
437-618 |
9.00e-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: 52.36 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 437 PGELLAVVGPVGAGKSSLLSAVLgelapshglvsvhgriayvsqqpWVFSGtlRSNILFGKKYEKERYekvIKACAlkkD 516
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG-----------------------LALGG--AQSATRRRSGVKAGC---IVAAV---S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 517 LQLLedgdLTVIGdrgttLSGGQKARVNLARAV----YQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTH 592
Cdd:cd03227 69 AELI----FTRLQ-----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
170 180
....*....|....*....|....*.
gi 157502203 593 QLQYLKAASQILILkdgKMVQKGTYT 618
Cdd:cd03227 140 LPELAELADKLIHI---KKVITGVYK 162
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
428-622 |
9.39e-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: 9.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG------RIAYVSQQPWVFsG-------------T 488
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrRKEFARRIGVVF-GqrsqlwwdlpaidS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 LRsniLFGKKYE--KERYEKVIKACAlkkdlQLLEDGDLTVIGDRgtTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG4586 117 FR---LLKAIYRipDAEYKKRLDELV-----ELLDLGELLDTPVR--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 567 AEVSRHLFELcICQILHE-KITILVT-HQLQYLKA-ASQILILKDGKMVQKGTYTEFLK 622
Cdd:COG4586 187 VVSKEAIREF-LKEYNRErGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
434-594 |
1.09e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 434 TVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------------------------------LVSVHgRIAYVSQQP 482
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtelqnyfkklyngeIKVVH-KPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 483 WVFSGTLRSniLFGKKYEKERYEKVIKACALKKDLqlledgdltvigDRG-TTLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:PRK13409 174 KVFKGKVRE--LLKKVDERGKLDEVVERLGLENIL------------DRDiSELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157502203 562 LSAVD-------AEVSRHLFElcicqilhEKITILVTHQL 594
Cdd:PRK13409 240 TSYLDirqrlnvARLIRELAE--------GKYVLVVEHDL 271
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
426-615 |
1.17e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.94 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPshGLVSVHGRIAY--VSQQPWVFSGTLRSNIL------FG- 496
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLdgKPVAPCALRGRKIATIMqnprsaFNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 497 ----KKYEKERYEKVIKACALKKDLQLLEDGDLtviGDRGTTL-------SGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PRK10418 95 lhtmHTHARETCLALGKPADDATLTAALEAVGL---ENAARVLklypfemSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 566 DAEVSRHLFELcICQILHEKI--TILVTHQLQYL-KAASQILILKDGKMVQKG 615
Cdd:PRK10418 172 DVVAQARILDL-LESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
428-611 |
1.31e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------RIAYVSQ------QPWVFSGTLRS 491
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeeaRAKLRAKhvgfvfQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 -------NILFGkkyEKERYEKViKACALKKDLQLledgdltviGDR----GTTLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK10584 106 lenvelpALLRG---ESSRQSRN-GAKALLEQLGL---------GKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 561 PLSAVDAEVSRHLFELcICQILHEKIT--ILVTHQLQYLKAASQILILKDGKM 611
Cdd:PRK10584 173 PTGNLDRQTGDKIADL-LFSLNREHGTtlILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
97-386 |
2.12e-07 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 53.56 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 97 IFTLIEESAKVIQPIFLGKIINYFenydpmdSVALNTAYAYAT-----VLTFCTLILAILHHLYFYHV-QCAGMRLRvam 170
Cdd:cd18548 6 LFKLLEVLLELLLPTLMADIIDEG-------IANGDLSYILRTgllmlLLALLGLIAGILAGYFAAKAsQGFGRDLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 171 cHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQ-VTVFLHFLWAGPLQAI-AVTALLWMEIGISC--LAGMAVLII 246
Cdd:cd18548 76 -KDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNfVMMLLRMLVRAPIMLIgAIIMAFRINPKLALilLVAIPILAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 247 LLPLQSCFG-KLFSSLRSKtatfTDARIRTMNEVITGIRIIKMYAWE----KSFSNLITNLRKKEIsKILRSSCLRG--- 318
Cdd:cd18548 155 VVFLIMKKAiPLFKKVQKK----LDRLNRVVRENLTGIRVIRAFNREdyeeERFDKANDDLTDTSL-KAGRLMALLNplm 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 319 ---MNLAS----FFSASKIIV-------FVTFTTYV--LLGSVITASRVFVAvtlygavrltvtlffpsaierVSEAIVS 382
Cdd:cd18548 230 mliMNLAIvailWFGGHLINAgslqvgdLVAFINYLmqILMSLMMLSMVFVM---------------------LPRASAS 288
|
....
gi 157502203 383 IRRI 386
Cdd:cd18548 289 AKRI 292
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
426-595 |
2.41e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGE--LAPSHGLVsVHGR--------------IAYVSQQ---PWVFS 486
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpQGYSNDLT-LFGRrrgsgetiwdikkhIGYVSSSlhlDYRVS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 487 GTLRSNILFGKKYEKERYEKVIKAcalkkdLQLLEDGDLTVIGDRGTT-------LSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK10938 353 TSVRNVILSGFFDSIGIYQAVSDR------QQKLAQQWLDILGIDKRTadapfhsLSWGQQRLALIVRALVKHPTLLILD 426
|
170 180 190
....*....|....*....|....*....|....*...
gi 157502203 560 DPLSAVDAeVSRHLFELCICQILHEKITIL--VTHQLQ 595
Cdd:PRK10938 427 EPLQGLDP-LNRQLVRRFVDVLISEGETQLlfVSHHAE 463
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
434-576 |
2.48e-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: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 434 TVRPGELLAVVGPVGAGKSSLLSAVLGELAP------------------------------SHGLVSVHGRIAYVSQQPW 483
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPnlgdydeepswdevlkrfrgtelqdyfkklANGEIKVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 484 VFSGTLRSnILfgKKY-EKERYEKVIKACALKKDLqlleDGDLtvigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:COG1245 175 VFKGTVRE-LL--EKVdERGKLDELAEKLGLENIL----DRDI-------SELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170
....*....|....*...
gi 157502203 563 SAVD----AEVSRHLFEL 576
Cdd:COG1245 241 SYLDiyqrLNVARLIREL 258
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
416-566 |
3.14e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 416 TAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH---------------GLVSVHGRIAYVSQ 480
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKgavlwqgkpldyskrGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 481 QP--WVFSGTLRSNILFGKK----YEKERYEKVIKACALkKDLQLLEDGDLTVigdrgttLSGGQKARVNLARAVYQDAD 554
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRnlgvPEAEITRRVDEALTL-VDAQHFRHQPIQC-------LSHGQKKRVAIAGALVLQAR 156
|
170
....*....|..
gi 157502203 555 IYLLDDPLSAVD 566
Cdd:PRK13638 157 YLLLDEPTAGLD 168
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
437-611 |
3.43e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 437 PGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--RIAYVSQQPWVFsgtLRSNilfgkkyekERYEKVIKACALK 514
Cdd:PRK10636 337 PGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQHQLEF---LRAD---------ESPLQHLARLAPQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 515 KDLQLLED--GDLTVIGDRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFElciCQILHEKITI 588
Cdd:PRK10636 405 ELEQKLRDylGGFGFQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE---ALIDFEGALV 481
|
170 180
....*....|....*....|....
gi 157502203 589 LVTHQLQYLKAASQILIL-KDGKM 611
Cdd:PRK10636 482 VVSHDRHLLRSTTDDLYLvHDGKV 505
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
406-573 |
4.37e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 406 GKKMVHVQDFT-AFWDKasetpTL-QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVhG---RIAYVSQ 480
Cdd:PRK11819 321 GDKVIEAENLSkSFGDR-----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GetvKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 481 QpwvfsgtlRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGDR--------------GT-------TLSGG 538
Cdd:PRK11819 395 S--------RDAL----DPNKTVWEEI-------------SGGlDIIKVGNReipsrayvgrfnfkGGdqqkkvgVLSGG 449
|
170 180 190
....*....|....*....|....*....|....*
gi 157502203 539 QKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHL 573
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRAL 484
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
435-622 |
5.35e-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: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 435 VRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-RIAYVSQQpwvfsgtlrsnilfgkkyekeryekvikacal 513
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 514 kkdlqlledgdltvigdrgTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VSRHLFElcicqiLHEKI 586
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnaarAIRRLSE------EGKKT 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 157502203 587 TILVTHQLQYLKAASQILILKDGkmvQKGTYTEFLK 622
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEG---EPGVYGIASQ 157
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
431-621 |
6.17e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTvrPGELLAVVGPVGAGKSSLLS--AVL-----GELAPSHGLvsvhgRIAYVSQQPWV-FSGTLRSNILFG---KKY 499
Cdd:PRK11819 28 LSFF--PGAKIGVLGLNGAGKSTLLRimAGVdkefeGEARPAPGI-----KVGYLPQEPQLdPEKTVRENVEEGvaeVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 500 EKERYEKV------------------------IKAC-ALKKDLQL--------LEDGDLTVigdrgTTLSGGQKARVNLA 546
Cdd:PRK11819 101 ALDRFNEIyaayaepdadfdalaaeqgelqeiIDAAdAWDLDSQLeiamdalrCPPWDAKV-----TKLSGGERRRVALC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 547 RAVYQDADIYLLDDPLSAVDAE-VS---RHL--FELCIcqilhekitILVTHQLQYL-KAASQILILKDGKMVQ-KGTYT 618
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAEsVAwleQFLhdYPGTV---------VAVTHDRYFLdNVAGWILELDRGRGIPwEGNYS 246
|
...
gi 157502203 619 EFL 621
Cdd:PRK11819 247 SWL 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
428-569 |
7.53e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG----------------RIAYVSQQPWvfsGTL-- 489
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllkadpeaqkllrqKIQIVFQNPY---GSLnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 490 RSNIlfGKKYE-----------KERYEKVikacalkkdLQLLEdgdltVIGDRGT-------TLSGGQKARVNLARAVYQ 551
Cdd:PRK11308 108 RKKV--GQILEepllintslsaAERREKA---------LAMMA-----KVGLRPEhydryphMFSGGQRQRIAIARALML 171
|
170
....*....|....*...
gi 157502203 552 DADIYLLDDPLSAVDAEV 569
Cdd:PRK11308 172 DPDVVVADEPVSALDVSV 189
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
420-622 |
8.73e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.63 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 420 DKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------------RIAYVSQQP--W 483
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdirnKAGMVFQNPdnQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 484 VFSGTLRSNILFG-------KKYEKERYEKVIKACAL---KKDLQLLedgdltvigdrgttLSGGQKARVNLARAVYQDA 553
Cdd:PRK13633 98 IVATIVEEDVAFGpenlgipPEEIRERVDESLKKVGMyeyRRHAPHL--------------LSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 554 DIYLLDDPLSAVDA----EVSRHLFELCicqiLHEKIT-ILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLK 622
Cdd:PRK13633 164 ECIIFDEPTAMLDPsgrrEVVNTIKELN----KKYGITiILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
397-555 |
1.81e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 397 QRNRQLPSDGKKMVHVQDFTAfwDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-- 474
Cdd:COG3845 245 RVEKAPAEPGEVVLEVENLSV--RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdi 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 475 ------------IAYVSQQPW----VFSGTLRSNILFGkKYEKERYEK--VIKACALKKD-LQLLEDGDL--TVIGDRGT 533
Cdd:COG3845 323 tglsprerrrlgVAYIPEDRLgrglVPDMSVAENLILG-RYRRPPFSRggFLDRKAIRAFaEELIEEFDVrtPGPDTPAR 401
|
170 180
....*....|....*....|....
gi 157502203 534 TLSGG--QKarVNLARAVYQDADI 555
Cdd:COG3845 402 SLSGGnqQK--VILARELSRDPKL 423
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
430-621 |
2.05e-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: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 430 GLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSV----------------HGR----IAYVSQQPWVFS-GT 488
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRakryIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 489 LRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPI 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 569 VSRHLFElcicQILH-----EKITILVTHQLQY-LKAASQILILKDGKMVQKGTYTEFL 621
Cdd:TIGR03269 462 TKVDVTH----SILKareemEQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
712-845 |
3.76e-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: 49.47 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 712 IVFIFLILLNTAAQVAYvlqdwwlsYWANKQSMLNVTVNGGGNVtekldLNWYLGIYSGLTVATVLFGIARSLLVFYVLV 791
Cdd:cd07346 2 LLALLLLLLATALGLAL--------PLLTKLLIDDVIPAGDLSL-----LLWIALLLLLLALLRALLSYLRRYLAARLGQ 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 157502203 792 NSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd07346 69 RVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLS 122
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
428-616 |
4.32e-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: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL-----------GELAPSHGLVSVH---GRIAYVSQQPwvFSGTLRSN- 492
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkKEQPGNHDRIEGLehiDKVIVIDQSP--IGRTPRSNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 -----------ILF-----GKKYEKE----RYE-KVI----------------KACALKKDLQLLEDGDLTVI--GDRGT 533
Cdd:cd03271 89 atytgvfdeirELFcevckGKRYNREtlevRYKgKSIadvldmtveealeffeNIPKIARKLQTLCDVGLGYIklGQPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 534 TLSGGQKARVNLARAVYQDAD---IYLLDDPLSAVDAEVSRHLFElcicqILHEKI----TILVT-HQLQYLKAASQILI 605
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLE-----VLQRLVdkgnTVVVIeHNLDVIKCADWIID 243
|
250
....*....|....*..
gi 157502203 606 L------KDGKMVQKGT 616
Cdd:cd03271 244 LgpeggdGGGQVVASGT 260
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
97-386 |
5.04e-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: 49.31 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 97 IFTLIEESAKVIQPIFLGKIINyfeNYDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMR----LRVAmch 172
Cdd:cd18544 6 LLLLLATALELLGPLLIKRAID---DYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRiiydLRRD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 173 mIYRKALRLSnmaMG---KTTTGQIVNLLSNDVNKFDQ--VTVFLHFLWAGPLQAIAVTALLWMEIGISCLAgMAVLIIL 247
Cdd:cd18544 80 -LFSHIQRLP---LSffdRTPVGRLVTRVTNDTEALNElfTSGLVTLIGDLLLLIGILIAMFLLNWRLALIS-LLVLPLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 248 LPLQSCFGKL----FSSLRSKTAtftdaRIRT-MNEVITGIRIIKMYAWEKSFSNlitnlRKKEISKILRSSCLRGMNLA 322
Cdd:cd18544 155 LLATYLFRKKsrkaYREVREKLS-----RLNAfLQESISGMSVIQLFNREKREFE-----EFDEINQEYRKANLKSIKLF 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 323 SFF-------SASKIIVFVTFTTYVLLGSVITASrVFVAVTLYgavrltVTLFF-PsaIERVSE-------AIVSIRRI 386
Cdd:cd18544 225 ALFrplvellSSLALALVLWYGGGQVLSGAVTLG-VLYAFIQY------IQRFFrP--IRDLAEkfnilqsAMASAERI 294
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
428-604 |
6.52e-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: 47.32 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVlgeLAPSHGLVSVHGRIAYvSQQPWVFSGTLRSNILFGKKYekeryekv 507
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFLPKF-SRNKLIFIDQLQFLIDVGLGY-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 508 ikacalkkdlqlledgdLTvIGDRGTTLSGGQKARVNLARAVYQDAD--IYLLDDPLSAVDAEVSRHLFElCICQILHEK 585
Cdd:cd03238 79 -----------------LT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE-VIKGLIDLG 139
|
170 180
....*....|....*....|
gi 157502203 586 IT-ILVTHQLQYLKAASQIL 604
Cdd:cd03238 140 NTvILIEHNLDVLSSADWII 159
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
405-652 |
8.02e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 405 DGKKMVHVQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVS------------- 470
Cdd:PRK10261 8 DARDVLAVENLNiAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 471 -------------VHGR-IAYVSQQPWVfsgTLRSNILFGKKY-EKER-YEKVIKACALKKDLQLLEDGDL----TVIGD 530
Cdd:PRK10261 88 ielseqsaaqmrhVRGAdMAMIFQEPMT---SLNPVFTVGEQIaESIRlHQGASREEAMVEAKRMLDQVRIpeaqTILSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 531 RGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELciCQILHEKIT---ILVTHQLQYL-KAASQILIL 606
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQL--IKVLQKEMSmgvIFITHDMGVVaEIADRVLVM 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 607 KDGKMVQKGT-----------YTEFL---------KSGIDFG---SLLKKDNEESEQPP------VPGTPTLRNR 652
Cdd:PRK10261 243 YQGEAVETGSveqifhapqhpYTRALlaavpqlgaMKGLDYPrrfPLISLEHPAKQEPPieqdtvVDGEPILQVR 317
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
428-593 |
8.63e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 8.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAP---SHGLVSVHGR---------IAYVSQQ-----------PWV 484
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRpldssfqrsIGYVQQQdlhlptstvreSLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 485 FSGTLR-SNILfgKKYEKERY-EKVIKacalkkdlqLLEDGDL--TVIGDRGTTLSGGQKARVNLA-RAVYQDADIYLLD 559
Cdd:TIGR00956 859 FSAYLRqPKSV--SKSEKMEYvEEVIK---------LLEMESYadAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLD 927
|
170 180 190
....*....|....*....|....*....|....*....
gi 157502203 560 DPLSAVDAEVSrhlfeLCICQILHEKI----TILVT-HQ 593
Cdd:TIGR00956 928 EPTSGLDSQTA-----WSICKLMRKLAdhgqAILCTiHQ 961
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
715-836 |
9.26e-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: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 715 IFLILLNTAAQVA--YVLqdwwlsywanKQSMLNVTVNGGGNVTEkldLNWYLGIYSGLTVATVLFGIARSLLVFYVLVN 792
Cdd:cd18544 5 LLLLLLATALELLgpLLI----------KRAIDDYIVPGQGDLQG---LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQR 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 157502203 793 SSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLL 836
Cdd:cd18544 72 IIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELF 115
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
712-829 |
9.36e-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: 9.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 712 IVFIFLILLNTAAQVA--YVLQDWWLSYWANKQSMLNVTVNGggnvtekldLNWYLGIYSGLTVATVLFGIARSLLVFYV 789
Cdd:cd18547 2 ILVIILAIISTLLSVLgpYLLGKAIDLIIEGLGGGGGVDFSG---------LLRILLLLLGLYLLSALFSYLQNRLMARV 72
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 157502203 790 LVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDI 829
Cdd:cd18547 73 SQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDV 112
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
430-616 |
1.05e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 430 GLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR-IAYVSQQPWVFSGTLR------------------ 490
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhIEGLPGHQIARMGVVRtfqhvrlfremtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 --------SNILFG-------KKYEKEryekvikacALKKDLQLLEDGDLTVIGDR-GTTLSGGQKARVNLARAVYQDAD 554
Cdd:PRK11300 103 vaqhqqlkTGLFSGllktpafRRAESE---------ALDRAATWLERVGLLEHANRqAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 555 IYLLDDPLSAVDAEVSRHLFELcICQILHE-KITI-LVTHQLQYLKAAS-QILILKDGKMVQKGT 616
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDEL-IAELRNEhNVTVlLIEHDMKLVMGISdRIYVVNQGTPLANGT 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
428-612 |
1.18e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQ-PWVFSGTLRSN 492
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 493 ILFGkkyekeRYEK----VIKACALKKDLQLLEDGDLTV-IGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PRK10982 94 MWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIDIdPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157502203 568 EVSRHLFElcICQILHEK--ITILVTHQL-QYLKAASQILILKDGKMV 612
Cdd:PRK10982 168 KEVNHLFT--IIRKLKERgcGIVYISHKMeEIFQLCDEITILRDGQWI 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
428-612 |
1.34e-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: 46.85 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSaVL---GELAPSHGLVSVHGR---------IAYVSQQPwVFSG--TLRSNI 493
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLD-VLagrKTAGVITGEILINGRpldknfqrsTGYVEQQD-VHSPnlTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 LFgkkyekeryekvikACALkkdlqlledgdltvigdRGttLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSrhl 573
Cdd:cd03232 101 RF--------------SALL-----------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA--- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 157502203 574 feLCICQILhEKI-----TILVT-HQ--LQYLKAASQILILK-DGKMV 612
Cdd:cd03232 145 --YNIVRFL-KKLadsgqAILCTiHQpsASIFEKFDRLLLLKrGGKTV 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
432-576 |
1.81e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 432 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG-RIAYVSQQPWVFSG-----------------TLRSNI 493
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkaegiipvhSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 494 -------------LFGKKYEKERYEKVIKACALKKdlqllEDGDlTVIGdrgtTLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK11288 353 nisarrhhlragcLINNRWEAENADRFIRSLNIKT-----PSRE-QLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180
....*....|....*....|
gi 157502203 561 PLSAVD----AEVSRHLFEL 576
Cdd:PRK11288 423 PTRGIDvgakHEIYNVIYEL 442
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
715-844 |
1.86e-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: 47.46 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 715 IFLILLNTAAQVA--YVLqdwwlsywanKQSMLNVTVNGggNVTeklDLNWYLGIYSGLTVATVLFGIARSLLVFYVlvn 792
Cdd:cd18545 6 LLLMLLSTAASLAgpYLI----------KIAIDEYIPNG--DLS---GLLIIALLFLALNLVNWVASRLRIYLMAKV--- 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 157502203 793 SSQTLHN---KMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFI 844
Cdd:cd18545 68 GQRILYDlrqDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLI 122
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
428-566 |
2.05e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSqqpwVFSG-----TLRSNI-----LFG- 496
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA----ISSGlngqlTGIENIelkglMMGl 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157502203 497 -KKYEKERYEKVIKACALKKdlqlledgdltVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13545 116 tKEKIKEIIPEIIEFADIGK-----------FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
426-611 |
2.15e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQ---QPWVFS-- 486
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinnhnaneainhgFALVTEerrSTGIYAyl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 487 ----GTLRSNIlfgKKYeKERYeKVIKACALKKDLQLLED-------GDLTVIGdrgtTLSGGQKARVNLARAVYQDADI 555
Cdd:PRK10982 342 digfNSLISNI---RNY-KNKV-GLLDNSRMKSDTQWVIDsmrvktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 556 YLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQL-QYLKAASQILILKDGKM 611
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLV 469
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
412-477 |
2.60e-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: 2.60e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157502203 412 VQDFT-AFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKS-SLLSaVLGeLAPsHGLVSVHGRIAY 477
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 ... |
746-845 |
3.10e-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: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 746 NVTVNGGGNVTEKLdLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRF 825
Cdd:cd18563 28 DVLIQLGPGGNTSL-LLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRV 106
|
90 100
....*....|....*....|
gi 157502203 826 SKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd18563 107 TSDTDRLQDFLSDGLPDFLT 126
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
429-613 |
4.14e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 429 QGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG--------------ELAPSHGLVSVHGRIAYVSQ---QPWVFSG-TLR 490
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkraggeirlngkDISPRSPLDAVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 491 SNILFGKKYEKERYEKVIKACALKKDLQLLED--GDLTV----IGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK09700 360 QNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqrELLALkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157502203 565 VDAEVSRHLFELcICQILHEKITIL-VTHQL-QYLKAASQILILKDGKMVQ 613
Cdd:PRK09700 440 IDVGAKAEIYKV-MRQLADDGKVILmVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
432-596 |
9.88e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 432 SFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--IAYVSQ-----QPwvfSGTLRSNILFGKKyekery 504
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKleVAYFDQhraelDP---EKTVMDNLAEGKQ------ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 505 ekvikacalkkdlqlledgDLTVIG----------------DRGTT----LSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK11147 410 -------------------EVMVNGrprhvlgylqdflfhpKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 157502203 565 VDAEVsrhlFELcicqiLHEKIT------ILVTHQLQY 596
Cdd:PRK11147 471 LDVET----LEL-----LEELLDsyqgtvLLVSHDRQF 499
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
428-637 |
1.02e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVfSGTLR--SNILFgKKYEKERYE 505
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQLTgiENIEF-KMLCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 506 KVIKACaLKKDLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHlfelCICQILH-- 583
Cdd:PRK13546 118 KEIKAM-TPKIIEFSELGEF--IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK----CLDKIYEfk 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 584 --EKITILVTHQL-QYLKAASQILILKDGKMVQKG-------TYTEFLKsgiDFGSLLKKDNEE 637
Cdd:PRK13546 191 eqNKTIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGelddvlpKYEAFLN---DFKKKSKAEQKE 251
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
767-845 |
1.20e-04 |
|
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: 44.84 E-value: 1.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 767 IYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd18572 41 LLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLR 119
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
435-662 |
1.21e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 435 VRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSvhGRIAY-----------------------------VSQQPWVF 485
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVE--GVITYdgitpeeikkhyrgdvvynaetdvhfphlTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 486 SGTLRSNILFGKKYEKERYEKVIKACALKK-DLQLLEDgdlTVIGD---RGttLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:TIGR00956 162 AARCKTPQNRPDGVSREEYAKHIADVYMATyGLSHTRN---TKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 562 LSAVDAEVSrhlfeLCICQILHEKITILVTHQLQYLKAASQ--------ILILKDGKMVQKGTYTE----FLKSGI---- 625
Cdd:TIGR00956 237 TRGLDSATA-----LEFIRALKTSANILDTTPLVAIYQCSQdayelfdkVIVLYEGYQIYFGPADKakqyFEKMGFkcpd 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 157502203 626 -----DFGSLLKKDNEESEQP----PVPGTPTLRNRTFSESSVWSQ 662
Cdd:TIGR00956 312 rqttaDFLTSLTSPAERQIKPgyekKVPRTPQEFETYWRNSPEYAQ 357
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
428-566 |
1.25e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHG--------------RIAYVSQqpwvfsG------ 487
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrravcpRIAYMPQ------Glgknly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 -TL--RSNI-----LFGKKyEKERYEKVikacalkkdLQLLEDGDLTVIGDR--GtTLSGGQKARVNLARAVYQDADIYL 557
Cdd:NF033858 91 pTLsvFENLdffgrLFGQD-AAERRRRI---------DELLRATGLAPFADRpaG-KLSGGMKQKLGLCCALIHDPDLLI 159
|
....*....
gi 157502203 558 LDDPLSAVD 566
Cdd:NF033858 160 LDEPTTGVD 168
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
90-393 |
1.48e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 44.75 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 90 KSYLVLG-IFTLIeesAKVIQPIF---LGKIINYFenYDPMDSVALNTAYAYA---TVLTFCTLILAILHHLYFYHvqcA 162
Cdd:cd18578 8 WPLLLLGlIGAII---AGAVFPVFailFSKLISVF--SLPDDDELRSEANFWAlmfLVLAIVAGIAYFLQGYLFGI---A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 163 GMRLRVAMCHMIYRKALRlsnMAMG-----KTTTGQIVNLLSNDVNkfdQVTVFLHFLWAGPLQAIA--VTALLWMeIGI 235
Cdd:cd18578 80 GERLTRRLRKLAFRAILR---QDIAwfddpENSTGALTSRLSTDAS---DVRGLVGDRLGLILQAIVtlVAGLIIA-FVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 236 S---CLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILR 312
Cdd:cd18578 153 GwklALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 313 SSCLRGMnlasFFSASKiivFVTFTTYVLL---GSVITAS---------RVFVAV--TLYGAVRLTVtlFFPSaierVSE 378
Cdd:cd18578 233 RALISGL----GFGLSQ---SLTFFAYALAfwyGGRLVANgeytfeqffIVFMALifGAQSAGQAFS--FAPD----IAK 299
|
330
....*....|....*
gi 157502203 379 AIVSIRRIqtFLLLD 393
Cdd:cd18578 300 AKAAAARI--FRLLD 312
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
423-621 |
1.58e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 423 SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-LVSVHGRIAYVS---QQPWVFSGTLRSN--IL-- 494
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGeRQSQFSHITRLSfeqLQKLVSDEWQRNNtdMLsp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 495 ----FGKKYEKERYEKVIKACALKKDLQLLEDGDLtvIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVS 570
Cdd:PRK10938 94 geddTGRTTAEIIQDEVKDPARCEQLAQQFGITAL--LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 157502203 571 RHLFELcICQILHEKITI-LVTHQLQYLKA-ASQILILKDGKMVQKGTYTEFL 621
Cdd:PRK10938 172 QQLAEL-LASLHQSGITLvLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
428-493 |
1.86e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRI--AY-----------VSQQPWVFSGTLRSNI 493
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigAYglrelrrqfsmIPQDPVLFDGTVRQNV 1404
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
764-837 |
1.95e-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: 44.13 E-value: 1.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157502203 764 YLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLP 837
Cdd:cd18559 40 YLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAP 113
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
431-611 |
2.21e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.96 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 431 LSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHG-------LVSVHGRIAYVSQQPWVFSGTLrsniLF-------G 496
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGeilldgkPVTAEQPEDYRKLFSAVFTDFH----LFdqllgpeG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 497 KKYEKERYEKVIKACALKKDLQLlEDGDLTvigdrGTTLSGGQKARVNLARAVYQDADIYLLDDplSAVDAE-VSRHLFE 575
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKLEL-EDGRIS-----NLKLSKGQKKRLALLLALAEERDILLLDE--WAADQDpHFRREFY 489
|
170 180 190
....*....|....*....|....*....|....*...
gi 157502203 576 LCICQILHEK-ITIL-VTHQLQYLKAASQILILKDGKM 611
Cdd:PRK10522 490 QVLLPLLQEMgKTIFaISHDDHYFIHADRLLEMRNGQL 527
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
418-623 |
2.42e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.35 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 418 FWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGelapshgLVSVHGRiayVSQQPWVFSGTlrsNILfgK 497
Cdd:PRK11022 13 FGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMG-------LIDYPGR---VMAEKLEFNGQ---DLQ--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 498 KYEKERYEKV--------------IKAC---------ALK------------KDLQLLEdgdLTVIGDRGT-------TL 535
Cdd:PRK11022 78 ISEKERRNLVgaevamifqdpmtsLNPCytvgfqimeAIKvhqggnkktrrqRAIDLLN---QVGIPDPASrldvyphQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 536 SGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKIT-ILVTHQLQYL-KAASQILILKDGKMVQ 613
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlVLITHDLALVaEAAHKIIVMYAGQVVE 234
|
250
....*....|
gi 157502203 614 KGTYTEFLKS 623
Cdd:PRK11022 235 TGKAHDIFRA 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
426-611 |
2.95e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 426 PTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGR--------------IAYVSQQpwvfsgTLRS 491
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISED------RKRD 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 492 NILFGKKYeKERyekvIKACAL----KKDLQLLEDGDLTVIGD-----------RGTT---LSGGQKARVNLARAVYQDA 553
Cdd:PRK10762 340 GLVLGMSV-KEN----MSLTALryfsRAGGSLKHADEQQAVSDfirlfniktpsMEQAiglLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 554 DIYLLDDPLSAVDAEVSRHLFELcICQILHEKITI-LVTHQL-QYLKAASQILILKDGKM 611
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQL-INQFKAEGLSIiLVSSEMpEVLGMSDRILVMHEGRI 473
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
436-472 |
3.25e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 42.49 E-value: 3.25e-04
10 20 30
....*....|....*....|....*....|....*..
gi 157502203 436 RPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVH 472
Cdd:COG3709 3 GPGRLIYVVGPSGAGKDSLLAAARARLAADPRLVFAR 39
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
424-618 |
4.39e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.86 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 424 ETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLG--ELAPSHGLVSVHGR--------------IAYVSQQPWVFSG 487
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdllelspedragegIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 488 TlrSNILF-------GKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK09580 93 V--SNQFFlqtalnaVRSYrGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 560 DPLSAVDAEVSRHLFELCICQILHEKITILVTHQ---LQYLKaASQILILKDGKMVQKGTYT 618
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDFT 231
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
164-386 |
7.70e-04 |
|
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: 42.41 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 164 MRLRVAMchmiYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQ-VTVFLHFLWAGPLQAIA-VTALLWMEIGISCLAGM 241
Cdd:cd18552 72 RDLRNDL----FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGlLGVLFYLDWKLTLIALV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 242 AVLIILLPLQScFGKLF--SSLRS--KTATFTdariRTMNEVITGIRIIKMYAWEKS----FSNLITNLRKKEISKILRS 313
Cdd:cd18552 148 VLPLAALPIRR-IGKRLrkISRRSqeSMGDLT----SVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARAR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 314 SclrgmnLAS----FFSASKIIVFVTFTTYVLLGSVITASRVFVAVTLYGAV-----RLTvtlffpSAIERVSEAIVSIR 384
Cdd:cd18552 223 A------LSSplmeLLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLyqpikRLS------NVNANLQRGLAAAE 290
|
..
gi 157502203 385 RI 386
Cdd:cd18552 291 RI 292
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
93-389 |
1.25e-03 |
|
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: 41.72 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 93 LVLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAgmrlrvamcH 172
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRAS---------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 173 MIYRKALR-LSNMAMG---KTTTGQIVNLLSNDVNKFDQV--TVFLHFLWAGpLQAIAVTALLWMEIGISCLAGMAVLII 246
Cdd:cd18580 73 RLHDKLLRsVLRAPMSffdTTPSGRILNRFSKDIGLIDEElpLALLDFLQSL-FSVLGSLIVIAIVSPYFLIVLPPLLVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 247 LLPLQSCFGKLFSSLR-----SKTATFTdarirTMNEVITGIRIIKMYAWEKSF-----SNLITNLRkkeiSKILRSSCL 316
Cdd:cd18580 152 YYLLQRYYLRTSRQLRrleseSRSPLYS-----HFSETLSGLSTIRAFGWQERFieenlRLLDASQR----AFYLLLAVQ 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157502203 317 RGMNL-ASFFSAskIIVFVTFTTYVLLGSVITASrvFVAVTLYGAVRLTVTLFFpsAIERVSE---AIVSIRRIQTF 389
Cdd:cd18580 223 RWLGLrLDLLGA--LLALVVALLAVLLRSSISAG--LVGLALTYALSLTGSLQW--LVRQWTEletSMVSVERILEY 293
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
407-618 |
1.58e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.17 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 407 KKMVHVQDFTAfwdKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGElaPSHGLVSvhGRIAYVSQQPWVFS 486
Cdd:CHL00131 5 KPILEIKNLHA---SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAYKILE--GDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 487 GTLRSN--ILFGKKYEKE------------RYEKVIKACALKK--DLQLLE--DGDLTVIGDRGTTL--------SGGQK 540
Cdd:CHL00131 78 PEERAHlgIFLAFQYPIEipgvsnadflrlAYNSKRKFQGLPEldPLEFLEiiNEKLKLVGMDPSFLsrnvnegfSGGEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 541 ARVNLARAVYQDADIYLLDDPLSAVDAEVSRhlfelCICQILH-----EKITILVTHQ---LQYLKaASQILILKDGKMV 612
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALK-----IIAEGINklmtsENSIILITHYqrlLDYIK-PDYVHVMQNGKII 231
|
....*.
gi 157502203 613 QKGTYT 618
Cdd:CHL00131 232 KTGDAE 237
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
442-609 |
1.59e-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: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 442 AVVGPVGAGKSSLLSAVL----GELAPS----HGLVSVHG---RIAYVsqqpwvfsgTLRSNILFGKKYEKERYEKVIKA 510
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNskggAHDPKLIRegeVRAQV---------KLAFENANGKKYTITRSLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 511 CAlkkdlqLLEDGDLTVIGDRG-TTLSGGQKA------RVNLARAVYQDADIYLLDDPLSAVDAE-VSRHLFELcICQIL 582
Cdd:cd03240 97 VI------FCHQGESNWPLLDMrGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEI-IEERK 169
|
170 180 190
....*....|....*....|....*....|
gi 157502203 583 HEKI--TILVTHQLQYLKAASQIL-ILKDG 609
Cdd:cd03240 170 SQKNfqLIVITHDEELVDAADHIYrVEKDG 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
534-620 |
1.68e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 534 TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVsrhLFELCICQILHEKITILVTHQLQYLKA-ASQILILKDGKMV 612
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSHAREFLNTvVTDILHLHGQKLV 420
|
....*....
gi 157502203 613 Q-KGTYTEF 620
Cdd:PLN03073 421 TyKGDYDTF 429
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
517-616 |
2.66e-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: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 517 LQLLEDGDLTVI--GDRGTTLSGGQKARVNLARAVYQDAD---IYLLDDPLSAVDAEVSRHLFELcICQILHEKITILVT 591
Cdd:TIGR00630 810 LQTLCDVGLGYIrlGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEV-LQRLVDKGNTVVVI 888
|
90 100 110
....*....|....*....|....*....|..
gi 157502203 592 -HQLQYLKAASQILIL------KDGKMVQKGT 616
Cdd:TIGR00630 889 eHNLDVIKTADYIIDLgpeggdGGGTVVASGT 920
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
93-308 |
2.76e-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: 40.47 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 93 LVLGIFTLI-EESAKVIQPIFLGKIINYFENydpmDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMC 171
Cdd:cd18541 1 YLLGILFLIlVDLLQLLIPRIIGRAIDALTA----GTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 172 HMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVT--VFLHFLWAGPLQAIAVTALLWMEIGISCLAgmavlIILLP 249
Cdd:cd18541 77 NDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALgpGILYLVDALFLGVLVLVMMFTISPKLTLIA-----LLPLP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157502203 250 LQSCFGKLFSSL---RSKTA--TFTDarirtMN----EVITGIRIIKMYAWE----KSFSNLITNLRKKEIS 308
Cdd:cd18541 152 LLALLVYRLGKKihkRFRKVqeAFSD-----LSdrvqESFSGIRVIKAFVQEeaeiERFDKLNEEYVEKNLR 218
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
760-829 |
2.91e-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: 40.47 E-value: 2.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 760 DLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDI 829
Cdd:cd18541 38 QLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
93-386 |
4.92e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 39.77 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 93 LVLG-IFTLIEESAKVIQPIFLGKIINYFENYDPMD---SVALNTAYAYA---TVLTFCTLILAILHHLYFYHV---QCA 162
Cdd:cd18577 1 LIIGlLAAIAAGAALPLMTIVFGDLFDAFTDFGSGEsspDEFLDDVNKYAlyfVYLGIGSFVLSYIQTACWTITgerQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 163 GMRLRVamchmiYRKALRLSNMAMGKTTTGQIVNLLSNDVNKF-----DQVTVFLHFLwagplqAIAVTAllwmeIGISC 237
Cdd:cd18577 81 RIRKRY------LKALLRQDIAWFDKNGAGELTSRLTSDTNLIqdgigEKLGLLIQSL------STFIAG-----FIIAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 238 -----LAGmaVLIILLPLQSCFGKLFSSLRSKTAtftdARIRTM--------NEVITGIRIIKMYAWE----KSFSNLIT 300
Cdd:cd18577 144 iyswkLTL--VLLATLPLIAIVGGIMGKLLSKYT----KKEQEAyakagsiaEEALSSIRTVKAFGGEekeiKRYSKALE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 301 NLRKKEIskilRSSCLRGMNLASFFsaskiivFVTFTTYVL---------------LGSVITasrVFVAVtLYGAvrLTV 365
Cdd:cd18577 218 KARKAGI----KKGLVSGLGLGLLF-------FIIFAMYALafwygsrlvrdgeisPGDVLT---VFFAV-LIGA--FSL 280
|
330 340
....*....|....*....|.
gi 157502203 366 TLFFPSaIERVSEAIVSIRRI 386
Cdd:cd18577 281 GQIAPN-LQAFAKARAAAAKI 300
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
770-845 |
5.83e-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: 5.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502203 770 GLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQ 845
Cdd:cd18552 47 GLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVR 122
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
92-293 |
6.05e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 39.72 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 92 YLVLGIFTLIEESAKVIQPIFLGKIInyfenydpmDSVALNTAYAYATVLTFCTLILAILH------HLYFYHV--QCAG 163
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII---------DSVIGGGLRELLWLLALLILGVALLRgvfrylQGYLAEKasQKVA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 164 MRLRVAMchmiYRKALRLSNMAMGKTTTGQIVNLLSNDVnkfDQV-----TVFLHFLWAGPLQAIAVTALLWMEIGIScL 238
Cdd:cd18542 72 YDLRNDL----YDHLQRLSFSFHDKARTGDLMSRCTSDV---DTIrrflaFGLVELVRAVLLFIGALIIMFSINWKLT-L 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157502203 239 AGMAVLIILLPLQSCFGK----LFSSLRSKTATFTdariRTMNEVITGIRIIKMYAWEK 293
Cdd:cd18542 144 ISLAIIPFIALFSYVFFKkvrpAFEEIREQEGELN----TVLQENLTGVRVVKAFARED 198
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
428-567 |
6.63e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.21 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 428 LQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSH--GLVSVHG---------RIAYVSQQPWVFSG--TLRSNIL 494
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYieGDIRISGfpkkqetfaRISGYCEQNDIHSPqvTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 495 FGK--KYEKE--RYEKVIkacALKKDLQLLEDGDL--TVIGDRGTT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PLN03140 976 YSAflRLPKEvsKEEKMM---FVDEVMELVELDNLkdAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
382-460 |
6.65e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.91 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 382 SIRRIQTFLLLDEISQRNRQLPSD-GKKMVHVQDFTAfWDKA-SETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVL 459
Cdd:PRK13549 231 TEDDIITMMVGRELTALYPREPHTiGEVILEVRNLTA-WDPVnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLF 309
|
.
gi 157502203 460 G 460
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 ... |
763-844 |
6.71e-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: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 763 WYLGIYSGLTVATVLFGIARSLLVFYVLVNssqtLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLD 842
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVAR----LRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
..
gi 157502203 843 FI 844
Cdd:cd18557 117 LL 118
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
155-342 |
8.03e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 39.06 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 155 YFYHVqcAGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQvtVFLHflwAGP------LQAIAVTAL 228
Cdd:cd18778 62 YLNHV--AEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVER--LIAD---GIPqgitnvLTLVGVAII 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157502203 229 LwmeIGISCLAGMAVLI---ILLplqscFGKLFSSLRSKTAtFTDARIRT--MNEV----ITGIRIIKMYAWEKSFSNli 299
Cdd:cd18778 135 L---FSINPKLALLTLIpipFLA-----LGAWLYSKKVRPR-YRKVREALgeLNALlqdnLSGIREIQAFGREEEEAK-- 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157502203 300 tnlRKKEISKILRSSCLRGMNLASFFSASkiIVFVTFTTYVLL 342
Cdd:cd18778 204 ---RFEALSRRYRKAQLRAMKLWAIFHPL--MEFLTSLGTVLV 241
|
|
| |
