|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
94-386 |
2.16e-166 |
|
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: 483.26 E-value: 2.16e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 94 ILGIFTLIEEGTRVVQPLFLGKIIEYFEkyDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFE--GNGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 174 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 253
Cdd:cd18593 79 IYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILF 333
Cdd:cd18593 159 FGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568987674 334 VTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLFFPSAIERGSEAIVSIRRI 386
Cdd:cd18593 239 LTFLAYILLGNILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-818 |
3.03e-160 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 506.97 E-value: 3.03e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 12 PLQDANLCSRVFFWWLNPLFKTGHKRRLEEDDMFSVLPEDRSKHLGEELQRYWDKELLRAKkdsrkPSLTKAIIKCYWKS 91
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPK-----PWLLRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 92 YLILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPddsvaLHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMC 171
Cdd:PLN03130 303 FWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEP-----AWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQ 251
Cdd:PLN03130 378 AAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 252 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMasfFIANKVI 331
Cdd:PLN03130 458 TFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNS---FILNSIP 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 332 LFVT---FTSYVLLGNEITASHVFVAMTLYGAVRLTvtLF-FPSAIERGSEAIVSIRRIKNFLLLDEL-----PQRKAHV 402
Cdd:PLN03130 535 VLVTvvsFGVFTLLGGDLTPARAFTSLSLFAVLRFP--LFmLPNLITQAVNANVSLKRLEELLLAEERvllpnPPLEPGL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 403 PSdgkaiVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPAS-GLVSVHGRIAYVSQQ 481
Cdd:PLN03130 613 PA-----ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQV 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 482 PWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:PLN03130 688 SWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 562 LSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLL----KKENEE 637
Cdd:PLN03130 768 LSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMenagKMEEYV 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 638 AEPSTAPGTPTLRKRTfsEASIWSQQSSRPSLKDGAPEGQDAENTQavqpeESRSEGRIGFKAYKNYFSA-GASWFFIIf 716
Cdd:PLN03130 848 EENGEEEDDQTSSKPV--ANGNANNLKKDSSSKKKSKEGKSVLIKQ-----EERETGVVSWKVLERYKNAlGGAWVVMI- 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 717 LVLLNMVGQVFYVLQDWWLSHWANkQGAlnntrnangniTETLDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQT 796
Cdd:PLN03130 920 LFLCYVLTEVFRVSSSTWLSEWTD-QGT-----------PKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKR 987
|
810 820
....*....|....*....|..
gi 568987674 797 LHNRMFESILKAPVLFFDRNPI 818
Cdd:PLN03130 988 LHDAMLGSILRAPMSFFHTNPL 1009
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-817 |
9.25e-156 |
|
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: 493.31 E-value: 9.25e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 6 TEVKPNPLQD--ANLCSRVFFWWLNPLFKTGHKRRLEEDDMFSVLPEDRSKHLGEELQRYWDKE----------LLRAKK 73
Cdd:TIGR00957 195 TNHDPNPCPEssASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKEckktrkqpvsAVYGKK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 74 DS--------------------------RKPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDD 127
Cdd:TIGR00957 275 DPskpkgssqldaneevealivksphkpRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPD 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 128 svalHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ 207
Cdd:TIGR00957 355 ----WQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 208 VTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIK 287
Cdd:TIGR00957 431 LATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 288 MYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTSYVLL--GNEITASHVFVAMTLYGAVRLTV 365
Cdd:TIGR00957 511 LYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVdeNNILDAEKAFVSLALFNILRFPL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 366 TLfFPSAIERGSEAIVSIRRIKNFLLLDEL-PQ---RKAHVPSDGKAI-VHVQDFTafWDKAlDSPTLQGLSFIARPGEL 440
Cdd:TIGR00957 591 NI-LPMVISSIVQASVSLKRLRIFLSHEELePDsieRRTIKPGEGNSItVHNATFT--WARD-LPPTLNGITFSIPEGAL 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 441 LAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLL 520
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEIL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 521 EDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQ--ALHEKITILVTHQLQYLK 598
Cdd:TIGR00957 747 PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTHGISYLP 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 599 AASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKK--------------------ENEEAEP--STAPGTPTLRK---RT 653
Cdd:TIGR00957 827 QVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTyapdeqqghledswtalvsgEGKEAKLieNGMLVTDVVGKqlqRQ 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 654 FSEASIWSQQSSR---PSLKDGAPEGQdaENTQAVQPEESRSEGRIGFKAYKNYfsAGASWFFIIFLVLLNMVGQ-VFYV 729
Cdd:TIGR00957 907 LSASSSDSGDQSRhhgSSAELQKAEAK--EETWKLMEADKAQTGQVELSVYWDY--MKAIGLFITFLSIFLFVCNhVSAL 982
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 730 LQDWWLSHWANKqgALNNTRNANGNITetldlswyLGIYAGLtavtvlfGIARSLLVF-YIL------VNASQTLHNRMF 802
Cdd:TIGR00957 983 ASNYWLSLWTDD--PMVNGTQNNTSLR--------LSVYGAL-------GILQGFAVFgYSMavsiggIQASRVLHQDLL 1045
|
890
....*....|....*
gi 568987674 803 ESILKAPVLFFDRNP 817
Cdd:TIGR00957 1046 HNKLRSPMSFFERTP 1060
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-817 |
4.79e-150 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 477.55 E-value: 4.79e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 12 PLQDANLCSRVFFWWLNPLFKTGHKRRLEEDDMFSVLPEDRSKHLGEELQRYWDKELLRAKkdsrkPSLTKAIIKCYWKS 91
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPK-----PWLLRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 92 YLILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPddsvaLHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMC 171
Cdd:PLN03232 303 FWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDP-----AWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQ 251
Cdd:PLN03232 378 AAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 252 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMasfFIANK-- 329
Cdd:PLN03232 458 TLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNS---FILNSip 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 330 -VILFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLFfPSAIERGSEAIVSIRRIKNFLLLDE--LPQRKAHVPsdG 406
Cdd:PLN03232 535 vVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNML-PNLLSQVVNANVSLQRIEELLLSEEriLAQNPPLQP--G 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 407 KAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA-SGLVSVHGRIAYVSQQPWVF 485
Cdd:PLN03232 612 APAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSWIF 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 486 SGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PLN03232 692 NATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 566 DAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENE-EAEPSTAP 644
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKmDATQEVNT 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 645 GTPTLRKRTFSEASIWSQQSSrpslkdgAPEGQDAENTQAVQPEESRSEGRIGFKAYKNYFSAGASWFFIIFLVLLNMVG 724
Cdd:PLN03232 852 NDENILKLGPTVTIDVSERNL-------GSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTT 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 725 QVFYVLQDWWLSHWANkQGALNNTRNAngnitetldlsWYLGIYA--GLTAVTVLFgiARSLLVFYILVNASQTLHNRMF 802
Cdd:PLN03232 925 EVLRVSSSTWLSIWTD-QSTPKSYSPG-----------FYIVVYAllGFGQVAVTF--TNSFWLISSSLHAAKRLHDAML 990
|
810
....*....|....*
gi 568987674 803 ESILKAPVLFFDRNP 817
Cdd:PLN03232 991 NSILRAPMLFFHTNP 1005
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-687 |
1.61e-146 |
|
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: 467.85 E-value: 1.61e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 11 NPLQDANLCSRVFFWWLNPLFKTGHKRRLEEDDMFSVLPEDRSKHLGEELQRYWDKELLRAKKdsrKPSLTKAIIKCYWK 90
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKK---NPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 91 SYLILGIFTLIEEGTRVVQPLFLGKIIEyfeKYDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAM 170
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRIIA---SYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 171 CHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPL 250
Cdd:TIGR01271 158 FSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 251 QSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKV 330
Cdd:TIGR01271 238 QACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 331 ILFVTFTSYVLLgNEITASHVFVAMTLYGAVRLTVTLFFPSAIERGSEAIVSIRRIKNFLLLDELPQRKAHVPSDGKAIV 410
Cdd:TIGR01271 318 VVFLSVVPYALI-KGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 411 HVqdfTAFWDKALD-------------------------------SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVL 459
Cdd:TIGR01271 397 NV---TASWDEGIGelfekikqnnkarkqpngddglffsnfslyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 460 GELPPASGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQ 539
Cdd:TIGR01271 474 GELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 540 KARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:TIGR01271 554 RARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSE 633
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 620 FLKSGVDFGSLL----KKENEEAEPSTAPGTPTLRKRTF-SEASIWS-QQSSRPSLKDGAPE-GQDAENTQAVQP 687
Cdd:TIGR01271 634 LQAKRPDFSSLLlgleAFDNFSAERRNSILTETLRRVSIdGDSTVFSgPETIKQSFKQPPPEfAEKRKQSIILNP 708
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
94-386 |
4.10e-131 |
|
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: 392.38 E-value: 4.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 94 ILGIFTLIEEGTRVVQPLFLGKIIEYFekyDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYF---VPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 174 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 253
Cdd:cd18594 78 IYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILF 333
Cdd:cd18594 158 LGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSF 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568987674 334 VTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLFFPSAIERGSEAIVSIRRI 386
Cdd:cd18594 238 ATFVPYVLTGNTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
94-386 |
1.75e-117 |
|
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: 357.18 E-value: 1.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 94 ILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDsvaLHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEP---LSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 174 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 253
Cdd:cd18579 78 IYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILF 333
Cdd:cd18579 158 LAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568987674 334 VTFTSYVLLGNEITASHVFVAMTLYGAVRlTVTLFFPSAIERGSEAIVSIRRI 386
Cdd:cd18579 238 ATFATYVLLGNPLTAAKVFTALSLFNLLR-FPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
410-610 |
3.19e-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: 347.92 E-value: 3.19e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDKA--LDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSG 487
Cdd:cd03250 1 ISVEDASFTWDSGeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 TVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568987674 568 EVGKHLFQLCICQAL-HEKITILVTHQLQYLKAASHILILKDGE 610
Cdd:cd03250 161 HVGRHIFENCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
76-818 |
7.67e-100 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 339.83 E-value: 7.67e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 76 RKPSLTKAIIKCYWKSYLILGIFTLIEEGTRVVQPLflgkIIEYFEKYDPDDSVALHTAYGYAAVLSMCTLILAILHHLY 155
Cdd:PTZ00243 230 KRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPV----LLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRF 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 156 FYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGK--TTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEI 233
Cdd:PTZ00243 306 YYISIRCGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLV 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 234 GISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFadlIANLRKKEISKIlgs 313
Cdd:PTZ00243 386 GWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCF---VANIEDKRAREL--- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 314 SYLRGM---NMASFFIAN---KVILFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLFfPSAIERGSEAIVSIRRIK 387
Cdd:PTZ00243 460 RYLRDVqlaRVATSFVNNatpTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMI-PWVFTTVLQFLVSIKRIS 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 388 NFLLLDEL-------------PQRKAHVPSDGKAIVHVQDFTAFW-----------------------------DKALDS 425
Cdd:PTZ00243 539 TFLECDNAtcstvqdmeeywrEQREHSTACQLAAVLENVDVTAFVpvklprapkvktsllsralrmlcceqcrpTKRHPS 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PT-------------------------------------------------------LQGLSFIARPGELLAVVGPVGAG 450
Cdd:PTZ00243 619 PSvvvedtdygspssasrhiveggtgggheatptsersaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSG 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 451 KSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGD 530
Cdd:PTZ00243 699 KSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGE 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 531 RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGE 610
Cdd:PTZ00243 779 KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGR 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 611 MVQKGTYTEFLKSGV--DFGSLLK---------KENEEAEPSTAPGTPTLRKRtfseasiwsqqssRPSLKDGAPEGQDA 679
Cdd:PTZ00243 859 VEFSGSSADFMRTSLyaTLAAELKenkdskegdADAEVAEVDAAPGGAVDHEP-------------PVAKQEGNAEGGDG 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 680 ENTQAVQP----EESRSEGRIGFKAYKNYFSA--GASWffIIFLVLLNMVGQVFYVLQDWWLSHWANKQGALNNTRNang 753
Cdd:PTZ00243 926 AALDAAAGrlmtREEKASGSVPWSTYVAYLRFcgGLHA--AGFVLATFAVTELVTVSSGVWLSMWSTRSFKLSAATY--- 1000
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 754 nitetldLSWYLGIyagltavtVLFGIA----RSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:PTZ00243 1001 -------LYVYLGI--------VLLGTFsvplRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPL 1054
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
94-386 |
1.67e-81 |
|
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: 263.18 E-value: 1.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 94 ILGIFTLIEEGTRVVQPLFLGKIIEYFEkydpDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVE----DPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 174 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 253
Cdd:cd18595 77 IYRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILF 333
Cdd:cd18595 157 LARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 334 VTFTSYVLLG--NEITASHVFVAMTLYGAVRLTVTlFFPSAIERGSEAIVSIRRI 386
Cdd:cd18595 237 ATFATYVLSDpdNVLDAEKAFVSLSLFNILRFPLS-MLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
96-386 |
7.99e-80 |
|
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: 258.54 E-value: 7.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 96 GIFTLIEEGTRVVQPLFLGKIIEYFE-KYDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMI 174
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEdAYLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 175 YRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCI 254
Cdd:cd18597 83 YRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 255 GKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILFV 334
Cdd:cd18597 163 MKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASML 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568987674 335 TFTSYVLLGNEITASHVFVAMTLYGAVRLTVTlFFPSAIERGSEAIVSIRRI 386
Cdd:cd18597 243 SFITYYATGHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
83-624 |
3.96e-78 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 263.56 E-value: 3.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 83 AIIKCYWKSYLILGIFTLIEEGTRVVQPLFLGKII-EYFEKYDpddsvaLHTAYGYAAVLSMCTLILAILHHLYFYHVQC 161
Cdd:COG1132 14 RYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGD------LSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 162 AGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIAVTVLLWV---EIGISC 237
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVidwRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 238 LAGLAVLVILL-PLQSCIGKLFSSLRSKTAAFTdariRTMNEVITGMRIIKMYAWEKS----FADLIANLRKKEISKILG 312
Cdd:COG1132 168 LLVLPLLLLVLrLFGRRLRKLFRRVQEALAELN----GRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 313 SSYLRGMNMASFFIAnkVILFVTFTSYVLLGNEITAShVFVAMTLYgavrlTVTLFFP-----SAIERGSEAIVSIRRIk 387
Cdd:COG1132 244 SALFFPLMELLGNLG--LALVLLVGGLLVLSGSLTVG-DLVAFILY-----LLRLFGPlrqlaNVLNQLQRALASAERI- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 388 nFLLLDELPQRK----AHVPSDGKAIVHVQDFTAFWDKalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELP 463
Cdd:COG1132 315 -FELLDEPPEIPdppgAVPLPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 464 PASG-------------LVSVHGRIAYVSQQPWVFSGTVRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVIG 529
Cdd:COG1132 392 PTSGrilidgvdirdltLESLRRQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 530 DRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlCICQALHEKITILVTHQLQYLKAASHILILKDG 609
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE-ALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
570
....*....|....*
gi 568987674 610 EMVQKGTYTEFLKSG 624
Cdd:COG1132 551 RIVEQGTHEELLARG 565
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
92-386 |
1.12e-65 |
|
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: 220.51 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 92 YLILGIFTLIeegtrvVQPLFLGKIIEYFEKYDPDdsvaLHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMC 171
Cdd:cd18592 6 LLISLIFGFI------GPTILIRKLLEYLEDSDSS----VWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 172 HMIYRKALRLSNSamGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQ 251
Cdd:cd18592 76 GLLYKKILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 252 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVI 331
Cdd:cd18592 154 AFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 332 LFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTlFFPSAIERGSEAIVSIRRI 386
Cdd:cd18592 234 SVVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLR-MLPYAVKALAEAKVALQRI 287
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
425-651 |
3.24e-64 |
|
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: 216.65 E-value: 3.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 425 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKERY 504
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 505 EKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHE 584
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMAN 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 585 KITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLL----KKENEEAEPSTAPGTPTLRK 651
Cdd:cd03291 210 KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLmgydTFDQFSAERRNSILTETLRR 280
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
94-386 |
5.70e-64 |
|
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: 216.59 E-value: 5.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 94 ILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDdsvALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDPGED---ATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 174 IYRKALRLSNSA-------------------MGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIG 234
Cdd:cd18596 78 IFEKALRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 235 ISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSS 314
Cdd:cd18596 158 WSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRF 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 315 YLRGMNMASFFIANKVILFVTFTSYVLL-GNEITASHVFVAMTLYGAVRLTVTlFFPSAIERGSEAIVSIRRI 386
Cdd:cd18596 238 LLDLLLSLLWFLIPILVTVVTFATYTLVmGQELTASVAFTSLALFNMLRGPLN-VLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
94-386 |
1.31e-63 |
|
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: 215.11 E-value: 1.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 94 ILGIFTLIEEGTRVVQPLFLGKIIEYFEkydpDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHM 173
Cdd:cd18598 1 PLGLLKLLADVLGFAGPLLLNKLVEFLE----DSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 174 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSC 253
Cdd:cd18598 77 VYRKALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMnMASFFIANKVIL- 332
Cdd:cd18598 157 IAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL-CVYFWATTPVLIs 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 333 FVTFTSYVLLGNEITASHVFVAMTLYGavRLTVTL-FFPSAIERGSEAIVSIRRI 386
Cdd:cd18598 236 ILTFATYVLMGNTLTAAKVFTSLALFN--MLIGPLnAFPWVLNGLVEAWVSLKRL 288
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
165-622 |
4.15e-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: 208.47 E-value: 4.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 165 RLRVAmchmIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVtiFLHFL---WAGPLQAIAVTVLLWV---EIGISCL 238
Cdd:COG4987 89 DLRVR----LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL--YLRVLlplLVALLVILAAVAFLAFfspALALVLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 239 AGLAVLVILLPLqscigkLFSSL-----RSKTAAFTDARIRTMnEVITGMRIIKMY----AWEKSFADLIANLRKKE--I 307
Cdd:COG4987 163 LGLLLAGLLLPL------LAARLgrragRRLAAARAALRARLT-DLLQGAAELAAYgaldRALARLDAAEARLAAAQrrL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 308 SKILGSSylRGMNMASFFIAnkVILFVTFTSYVLLGNEITASH----VFVAMTLYGAVrltVTLffPSAIERGSEAIVSI 383
Cdd:COG4987 236 ARLSALA--QALLQLAAGLA--VVAVLWLAAPLVAAGALSGPLlallVLAALALFEAL---APL--PAAAQHLGRVRAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 384 RRIKNflLLDELPQR---KAHVPSDGKAIVHVQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLG 460
Cdd:COG4987 307 RRLNE--LLDAPPAVtepAEPAPAPGGPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 461 ELPPASGLV-------------SVHGRIAYVSQQPWVFSGTVRSNILFGKKYEKEryEKVIKACA---LKKDLQLLEDGD 524
Cdd:COG4987 384 FLDPQSGSItlggvdlrdldedDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD--EELWAALErvgLGDWLAALPDGL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 525 LTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITILVTHQLQYLKAASHIL 604
Cdd:COG4987 462 DTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRIL 540
|
490
....*....|....*...
gi 568987674 605 ILKDGEMVQKGTYTEFLK 622
Cdd:COG4987 541 VLEDGRIVEQGTHEELLA 558
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
61-624 |
4.18e-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: 205.38 E-value: 4.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 61 QRYWDKELLRAKKDSRKPsltkaiikcywksYLILGIFTLIEEGTRVVQPLFLGKII-EYFEKYDPDDSVALHTayGYAA 139
Cdd:COG4988 1 QKPLDKRLKRLARGARRW-------------LALAVLLGLLSGLLIIAQAWLLASLLaGLIIGGAPLSALLPLL--GLLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 140 VLSMCTLILAILHHLYFYHvqcAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVnkfDQVTIFL-HFLwag 218
Cdd:COG4988 66 AVLLLRALLAWLRERAAFR---AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV---EALDGYFaRYL--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 219 P--LQAIAVTVLLWVEI-GISCLAGLAVLV--ILLPL-QSCIGKlfsslrsKTAAFTDARIRTMN-------EVITGMRI 285
Cdd:COG4988 137 PqlFLAALVPLLILVAVfPLDWLSGLILLVtaPLIPLfMILVGK-------GAAKASRRQWRALArlsghflDRLRGLTT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 286 IKMYAWEKSFADLIA----NLRKK--EISKI--LGSSYLRGMnmASFFIAnKVILFVTFTsyvLLGNEITASHVFVAMTL 357
Cdd:COG4988 210 LKLFGRAKAEAERIAeaseDFRKRtmKVLRVafLSSAVLEFF--ASLSIA-LVAVYIGFR---LLGGSLTLFAALFVLLL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 358 ----YGAVRLTVTLFFPSAiergsEAIVSIRRIKNFLLLDELPQRKAHV--PSDGKAIVHVQDFTAFWDKalDSPTLQGL 431
Cdd:COG4988 284 apefFLPLRDLGSFYHARA-----NGIAAAEKIFALLDAPEPAAPAGTAplPAAGPPSIELEDVSFSYPG--GRPALDGL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 432 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGK- 497
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRp 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 498 KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLc 577
Cdd:COG4988 437 DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA- 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 568987674 578 ICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:COG4988 516 LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
58-635 |
5.71e-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: 208.15 E-value: 5.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 58 EELQRYWDKELL------RAKKDSRKPSLTKAI---IKCYWKSYLILGIFTLIEEGTRVVQPLFLGKIIeyfekydpdDS 128
Cdd:COG2274 115 EEFAESWTGVALlleptpEFDKRGEKPFGLRWFlrlLRRYRRLLLQVLLASLLINLLALATPLFTQVVI---------DR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 129 V----ALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLsNDVNK 204
Cdd:COG2274 186 VlpnqDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVES 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 205 FDQV--TIFLHFLWAGPLQAIAVTVLL-------WVEIGISCLAGLAVLVILLPLQSCIGKLFSsLRSKTAAFtdarirt 275
Cdd:COG2274 265 IREFltGSLLTALLDLLFVLIFLIVLFfyspplaLVVLLLIPLYVLLGLLFQPRLRRLSREESE-ASAKRQSL------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 276 MNEVITGMRIIKMYA--------WEKSFADLI-ANLRKKEISKILGssylrgmNMASFFIANKVILFVTFTSYVLLGNEI 346
Cdd:COG2274 337 LVETLRGIETIKALGaesrfrrrWENLLAKYLnARFKLRRLSNLLS-------TLSGLLQQLATVALLWLGAYLVIDGQL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 347 TASHVFVAMTLYGAVRLTVTLFFpSAIERGSEAIVSIRRIKNFLLL--DELPQRKAHVPSDGKAIVHVQDFTaFWDKALD 424
Cdd:COG2274 410 TLGQLIAFNILSGRFLAPVAQLI-GLLQRFQDAKIALERLDDILDLppEREEGRSKLSLPRLKGDIELENVS-FRYPGDS 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 425 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRS 491
Cdd:COG2274 488 PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:COG2274 568 NITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE 647
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 571 KHLFQLcICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKEN 635
Cdd:COG2274 648 AIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
96-386 |
3.97e-55 |
|
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: 192.45 E-value: 3.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 96 GIFTLIEEGTRVVQPLFLGKIIEYFEK--YDPDDSVALHTAY----------GY--AAVLSMCTLILAILHHLYFYHVQC 161
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEEntYSSSNSTDKLSVSyvtveeffsnGYvlAVILFLALLLQATFSQASYHIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 162 AGMRLRVAMCHMIYRKALRLS--NSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGISCLA 239
Cdd:cd18591 83 EGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 240 GLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGM 319
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 320 NMASFFIANKVILFVTFTSYVLLGNE-ITASHVFVAMTLYGavRLTVTLF-FPSAIERGSEAIVSIRRI 386
Cdd:cd18591 243 MTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFN--QLTVPLFiFPVVIPILINAVVSTRRL 309
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
412-609 |
1.03e-50 |
|
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: 177.14 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 412 VQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV-----------------SVHGR 474
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 475 IAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDAD 554
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 555 IYLLDDPLSAVDAEVGKHLFQLCICQALHE--KITILVTHQLQYLKAASHILILKDG 609
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
710-818 |
5.05e-43 |
|
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: 158.64 E-value: 5.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 710 SWFFIIFLVLLNMVGQVFYVLQDWWLSHWANKQGALNNTRNANGNIT------ETLDLSWYLGIYAGLTAVTVLFGIARS 783
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGENstnvdiEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 568987674 784 LLVFYILVNASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPI 115
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
426-624 |
4.15e-42 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 153.15 E-value: 4.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASG-------------LVSVHGRIAYVSQQPWVFSGTVRSN 492
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirdisRKSLRSMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGKKYEKEryEKVIKACALKKDLQL---LEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:cd03254 97 IRLGRPNATD--EEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 570 GKhLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:cd03254 175 EK-LIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
165-594 |
6.31e-42 |
|
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: 160.99 E-value: 6.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 165 RLRVAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVL----LWVEIGISCLAG 240
Cdd:TIGR02868 87 ALRVRV----YERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAaiavLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 241 LAVLVILLPLqscigklFSSLRSKTAAFTDARIRtmnevitGMRIIKMYAWEKSFADLIANLRKKEI---SKILGSSYLR 317
Cdd:TIGR02868 163 LLLAGFVAPL-------VSLRAARAAEQALARLR-------GELAAQLTDALDGAAELVASGALPAAlaqVEEADRELTR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 318 GMNMASFFIA-----NKVILFVTFTSYVLLGNEITASHVFVAMTLYGAVRLTVTLF-----FPSAIERGSEAIVSIRRIk 387
Cdd:TIGR02868 229 AERRAAAATAlgaalTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFeafaaLPAAAQQLTRVRAAAERI- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 388 NFLLLDELPQRKAHVPSDG-----KAIVHVQDFTAFWDKalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGEL 462
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGavglgKPTLELRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 463 PPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVI 528
Cdd:TIGR02868 386 DPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 529 GDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITILVTHQL 594
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
426-610 |
1.09e-40 |
|
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: 147.14 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV-------------SVHGRIAYVSQQPWVFSGTVRSN 492
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdldleSLRKNIAYVPQDPFLFSGTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 IlfgkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 572
Cdd:cd03228 96 I-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 568987674 573 LFQLcICQALHEKITILVTHQLQYLKAASHILILKDGE 610
Cdd:cd03228 135 ILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
425-606 |
2.17e-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: 153.60 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 425 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRS 491
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILFGKKYEKE-RYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:TIGR02857 415 NIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 568987674 571 KHLFQ--LCICQAlheKITILVTHQLQYLKAASHILIL 606
Cdd:TIGR02857 495 AEVLEalRALAQG---RTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
386-637 |
2.58e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.23 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 386 IKNFLLLDELPQRKAHVPSDGKAIVHV--QDFTAFwdkALDSPTLQG-LSFIARPGELLAVVGPVGAGKSSLLSAVLGEL 462
Cdd:PRK11174 324 LVTFLETPLAHPQQGEKELASNDPVTIeaEDLEIL---SPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 463 PpASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGKK-YEKERYEKVIKACALKKDLQLLEDGDLTVI 528
Cdd:PRK11174 401 P-YQGSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPI 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 529 GDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlCICQALHEKITILVTHQLQYLKAASHILILKD 608
Cdd:PRK11174 480 GDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ-ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQD 558
|
250 260
....*....|....*....|....*....
gi 568987674 609 GEMVQKGTYTEFLKSGVDFGSLLKKENEE 637
Cdd:PRK11174 559 GQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
424-624 |
1.64e-38 |
|
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: 143.45 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVR 490
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlrwlrsQIGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILFGKKYEK-ERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:cd03249 95 ENIRYGKPDATdEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 570 GKhLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:cd03249 175 EK-LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
89-631 |
4.45e-38 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 152.18 E-value: 4.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 89 WKsYLILGIFTL-IEEGTRVVQPLFLGKIIEY-FEKYDPDdsvALHTAygyaaVLSMCTLILAilhhlYFYHVQCAGMRL 166
Cdd:TIGR00958 160 WP-WLISAFVFLtLSSLGEMFIPFYTGRVIDTlGGDKGPP---ALASA-----IFFMCLLSIA-----SSVSAGLRGGSF 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 167 RVAMCHM-------IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKF-DQVTIFLH-FLWAGPLQAIAVTVLLWVEIGISC 237
Cdd:TIGR00958 226 NYTMARInlriredLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsRSLSLNVNvLLRNLVMLLGLLGFMLWLSPRLTM 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 238 LAGLAV-LVILLPlqSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKS----FADLIANL----RKKEIS 308
Cdd:TIGR00958 306 VTLINLpLVFLAE--KVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETlqlnKRKALA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 309 KILGSSYLRGMNMASFF----------IANKVI--LFVTFtsyvLLGNEITASHVFVAMTLYGAVRltvtlffpsaierg 376
Cdd:TIGR00958 384 YAGYLWTTSVLGMLIQVlvlyyggqlvLTGKVSsgNLVSF----LLYQEQLGEAVRVLSYVYSGMM-------------- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 377 sEAIVSIRRIknFLLLD---ELPQRKAHVPSDGKAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSS 453
Cdd:TIGR00958 446 -QAVGASEKV--FEYLDrkpNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 454 LLSAVLGELPPASGLV-------------SVHGRIAYVSQQPWVFSGTVRSNILFG-KKYEKERYEKVIKACALKKDLQL 519
Cdd:TIGR00958 523 VAALLQNLYQPTGGQVlldgvplvqydhhYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIME 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 520 LEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVgKHLFQLCICQAlhEKITILVTHQLQYLKA 599
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-EQLLQESRSRA--SRTVLLIAHRLSTVER 679
|
570 580 590
....*....|....*....|....*....|..
gi 568987674 600 ASHILILKDGEMVQKGTYTEFLKSGVDFGSLL 631
Cdd:TIGR00958 680 ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
424-624 |
4.63e-38 |
|
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: 141.98 E-value: 4.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVR 490
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILFGKKYE-KERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEv 569
Cdd:cd03251 94 ENIAYGRPGAtREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTE- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 570 GKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:cd03251 173 SERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
424-624 |
2.38e-37 |
|
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: 148.31 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVR 490
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVM 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILFGKKYEKEryEKVIKACALKKD---LQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:TIGR02204 432 ENIRYGRPDATD--EEVEAAARAAHAhefISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 568 EvGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG 565
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
135-386 |
3.61e-37 |
|
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: 141.20 E-value: 3.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 135 YGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHF 214
Cdd:cd18559 38 QVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 215 LWAGPLQAIAVTVLLWVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKS 294
Cdd:cd18559 118 MWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 295 FADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTSYVLLG--NEITASHVFVAMTLYGAVRLTVTLfFPSA 372
Cdd:cd18559 198 FIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHslAGLVALKVFYSLALTTYLNWPLNM-SPEV 276
|
250
....*....|....
gi 568987674 373 IERGSEAIVSIRRI 386
Cdd:cd18559 277 ITNIVAAEVSLERS 290
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
146-617 |
2.74e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 144.86 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 146 LILAILHHL--YFYHVQC--AGMRLRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVnkfDQVtIFlhflwagplq 221
Cdd:PRK10789 43 VLIAVVVYLlrYVWRVLLfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDV---DRV-VF---------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 222 AIAVTVLLWVEigiSCLAGLAVLVIL---------------LPLQSCIGK-----LFSSLRSKTAAFTDARIRTmNEVIT 281
Cdd:PRK10789 109 AAGEGVLTLVD---SLVMGCAVLIVMstqiswqltllallpMPVMAIMIKrygdqLHERFKLAQAAFSSLNDRT-QESLT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 282 GMRIIKMYAWEK----SFADLIANLRKKE--ISKI-----------LGSSYLRGMNMASFFIANKVILFVTFTSYVL-LG 343
Cdd:PRK10789 185 SIRMIKAFGLEDrqsaLFAADAEDTGKKNmrVARIdarfdptiyiaIGMANLLAIGGGSWMVVNGSLTLGQLTSFVMyLG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 344 NEITAshvfvaMtlygavrLTVTLFFpSAIERGSEAIVSIRRiknflLLDELPqrkahVPSDGKAIVHVQ------DFTA 417
Cdd:PRK10789 265 LMIWP------M-------LALAWMF-NIVERGSAAYSRIRA-----MLAEAP-----VVKDGSEPVPEGrgeldvNIRQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 418 FWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH-------------GRIAYVSQQPWV 484
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 485 FSGTVRSNILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:PRK10789 401 FSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 568987674 564 AVDAEVGKHLFQlCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTY 617
Cdd:PRK10789 481 AVDGRTEHQILH-NLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNH 533
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
426-615 |
3.06e-36 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 136.18 E-value: 3.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSN 492
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:cd03245 98 ITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568987674 572 HLFQlCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKG 615
Cdd:cd03245 178 RLKE-RLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
403-611 |
3.15e-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: 136.45 E-value: 3.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 403 PSDGKAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV----------- 471
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpisqyehk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 472 --HGRIAYVSQQPWVFSGTVRSNILFG---KKYEKeryekvIKACALKKD----LQLLEDGDLTVIGDRGATLSGGQKAR 542
Cdd:cd03248 85 ylHSKVSLVGQEPVLFARSLQDNIAYGlqsCSFEC------VKEAAQKAHahsfISELASGYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 543 VNLARAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQAL---HEKITILV-THQLQYLKAASHILILKDGEM 611
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAES-----EQQVQQALydwPERRTVLViAHRLSTVERADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
377-623 |
8.33e-36 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 143.35 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 377 SEAIVSIRRIKNflLLDELPQRKAHVPS-DGKAIVHVQDFTAFwDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLL 455
Cdd:COG4618 299 VSARQAYRRLNE--LLAAVPAEPERMPLpRPKGRLSVENLTVV-PPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 456 SAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVRSNI-LFGKkyekERYEKVIKACALK--KDLQL 519
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTIAENIaRFGD----ADPEKVVAAAKLAgvHEMIL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 520 -LEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlCIcQALHE--KITILVTHQLQY 596
Cdd:COG4618 452 rLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA-AI-RALKArgATVVVITHRPSL 529
|
250 260
....*....|....*....|....*..
gi 568987674 597 LKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:COG4618 530 LAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
426-607 |
2.69e-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: 133.43 E-value: 2.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------RIAYVSQQ---PWVFSGTVR---- 490
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRrsiDRDFPISVRdvvl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 ----SNILFGKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:cd03235 93 mglyGHKGLFRRLSKADKAKV---------DEALERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568987674 566 DAEVGKHLFQLciCQALHEK-ITIL-VTHQL-QYLKAASHILILK 607
Cdd:cd03235 164 DPKTQEDIYEL--LRELRREgMTILvVTHDLgLVLEYFDRVLLLN 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
408-623 |
3.08e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.06 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 408 AIVHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------RIAYVS 479
Cdd:COG1121 5 PAIELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 480 QQ---PWVFSGTVR--------SNILFGKKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLAR 547
Cdd:COG1121 82 QRaevDWDFPITVRdvvlmgryGRRGLFRRPSRADREAVDEA---------LERVGLEDLADRPiGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 548 AVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITIL-VTHQLQYL-KAASHILILkDGEMVQKGTYTEFLKS 623
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYEL-LRELRREGKTILvVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEVLTP 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
426-634 |
8.42e-33 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 126.96 E-value: 8.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVRSN 492
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrraIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:cd03253 95 IRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 572 HLFQlCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKE 634
Cdd:cd03253 175 EIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
428-616 |
2.47e-32 |
|
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: 125.93 E-value: 2.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWV-FSGTVRSNI 493
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPApFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFG--------KKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:COG1120 97 ALGryphlglfGRPSAEDREAVEEA---------LERTGLEHLADRPvDELSGGERQRVLIARALAQEPPLLLLDEPTSH 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 565 VD----AEVGKHLFQLCicqALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGT 616
Cdd:COG1120 168 LDlahqLEVLELLRRLA---RERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
410-616 |
4.56e-32 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 124.14 E-value: 4.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDKALDsPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIA 476
Cdd:cd03244 3 IEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 477 YVSQQPWVFSGTVRSNI-LFGKKYEKERYEkVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADI 555
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 556 YLLDDPLSAVDAEVGKHLFQLcICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGT 616
Cdd:cd03244 161 LVLDEATASVDPETDALIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
428-636 |
5.79e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.41 E-value: 5.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVRSNIL 494
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 F-------GKKYEKERYEKVIKACALKKdlqlledgdltVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTD-----------AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 568 EVGKHLFQLcICQALHEKITILV-THQLQYL-KAASHILILKDGEMVQKGTYTEFLKSGVD--FGSLLKKENE 636
Cdd:COG1131 165 EARRELWEL-LRELAAEGKTVLLsTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLLEdvFLELTGEEAR 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
428-563 |
1.53e-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: 120.45 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG-TVRSNI 493
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 494 LFGKkyEKERYEKVIKACALKKDLQLLEDGDL--TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
93-365 |
2.53e-31 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 123.91 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDSVALhtaYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMCH 172
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAL---NVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 173 MIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVEIGIS-CLAGLAVLVILLPLQ 251
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 252 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRG-MNMASFFIANKV 330
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGlSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 568987674 331 ILFVTFTSYVL-LGNEITASHVFVAMTLYGAVRLTV 365
Cdd:pfam00664 239 YALALWFGAYLvISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
428-615 |
3.73e-30 |
|
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: 117.54 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQqpwvfsgtvrsnil 494
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 fgkkyekeryekvikacalkkdlqLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEV 569
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568987674 570 GKHLFQLCicqALHEKITILVTHQL-QYLKAASHILILKDGEMVQKG 615
Cdd:cd03214 137 LELLRRLA---RERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
424-638 |
3.99e-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: 119.58 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVR 490
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNI-LFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeV 569
Cdd:COG4555 93 ENIrYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-----GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-M 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 570 GKHLFQLCICQALHEKITILV-THQLQYLKA-ASHILILKDGEMVQKGTYTEFLKSGVD------FGSLLKKENEEA 638
Cdd:COG4555 167 ARRLLREILRALKKEGKTVLFsSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEenledaFVALIGSEEGEA 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
389-647 |
4.43e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 126.23 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 389 FLLLDELPQRkaHVPSDGKAIVHVQDFTAFWDKALD----SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPP 464
Cdd:PRK13657 310 FEVEDAVPDV--RDPPGAIDLGRVKGAVEFDDVSFSydnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 465 ASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGKK--YEKERYEKVIKACALkkDLQLL-EDGDLTVI 528
Cdd:PRK13657 388 QSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEMRAAAERAQAH--DFIERkPDGYDTVV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 529 GDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLfQLCICQALHEKITILVTHQLQYLKAASHILILKD 608
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568987674 609 GEMVQKGTYTEFLKSGVDFGSLLK-----KENEEAEPSTAPGTP 647
Cdd:PRK13657 545 GRVVESGSFDELVARGGRFAALLRaqgmlQEDERRKQPAAEGAN 588
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
426-606 |
1.28e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 116.18 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--RIAYVSQQ---PWVFSGTVRSNI---LFGK 497
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 498 KYEKERY----EKVIKACALKKDLQLLEDGDLtvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 573
Cdd:NF040873 86 RGLWRRLtrddRAAVDDALERVGLADLAGRQL-------GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180 190
....*....|....*....|....*....|....
gi 568987674 574 FQLcICQALHEKITIL-VTHQLQYLKAASHILIL 606
Cdd:NF040873 159 IAL-LAEEHARGATVVvVTHDLELVRRADPCVLL 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
410-615 |
2.57e-29 |
|
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: 116.08 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDKAldsPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYV 478
Cdd:cd03259 1 LELKGLSKTYGSV---RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 479 SQQPWVFSG-TVRSNILFG----KKYEKERYEKVIKAcalkkdLQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQDA 553
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlklrGVPKAEIRARVREL------LELVGLEGL--LNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987674 554 DIYLLDDPLSAVDAEVGKHLF-QLCICQALHEKITILVTH-QLQYLKAASHILILKDGEMVQKG 615
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELReELKELQRELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
424-624 |
4.74e-29 |
|
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: 116.05 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSP-TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTV 489
Cdd:cd03252 13 DGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 490 RSNILFGKkyEKERYEKVIKACALKKD---LQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:cd03252 93 RDNIALAD--PGMSMERVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 567 AEvGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:cd03252 171 YE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
428-616 |
1.07e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.33 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQP------WVFSG-------TVRSNIL 494
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvgFVFQHyalfphmTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 FG----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:COG1118 98 FGlrvrPPSKAEIRARV---------EELLELVQLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568987674 570 GKHLFQLCIcqALHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:COG1118 169 RKELRRWLR--RLHDELggtTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
428-606 |
1.39e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 114.11 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------IAYVSQQ----PWVfsgTVRSNILF 495
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQdallPWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 496 G----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA--- 567
Cdd:cd03293 97 GlelqGVPKAEARERA---------EELLELVGLSGFENAyPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltr 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568987674 568 -EVGKHLFQLCicqALHEKITILVTHQLQ---YLkaASHILIL 606
Cdd:cd03293 168 eQLQEELLDIW---RETGKTVLLVTHDIDeavFL--ADRVVVL 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
404-609 |
3.36e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.42 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 404 SDGKAIVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------R 474
Cdd:COG1116 2 SAAAPALELRGVSkRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 475 IAYVSQQ----PWVfsgTVRSNILFG----KKYEKERYEKVikacalkkdLQLLEDGDLTviGDRGA---TLSGGQKARV 543
Cdd:COG1116 82 RGVVFQEpallPWL---TVLDNVALGlelrGVPKAERRERA---------RELLELVGLA--GFEDAyphQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 544 NLARAVYQDADIYLLDDPLSAVDA----EVGKHLFQLCicqALHEKITILVTHQLQ---YLkaASHILILKDG 609
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDAltreRLQDELLRLW---QETGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
426-611 |
3.56e-28 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.54 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSN 492
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnelgdHVGYLPQDDELFSGSIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILfgkkyekeryekvikacalkkdlqlledgdltvigdrgatlSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 572
Cdd:cd03246 96 IL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 568987674 573 LFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEM 611
Cdd:cd03246 135 LNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
428-611 |
1.10e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.45 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSNIL 494
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 FGKKYEKERYEKViKACALKKDLQLledgDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE----VG 570
Cdd:COG4619 96 FPFQLRERKFDRE-RALELLERLGL----PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEntrrVE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568987674 571 KHLFQLCicqaLHEKITIL-VTH-QLQYLKAASHILILKDGEM 611
Cdd:COG4619 171 ELLREYL----AEEGRAVLwVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
424-615 |
4.27e-27 |
|
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: 108.55 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSGTVRS 491
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NIlfgkkyekeryekvikacalkkdlqlledgdltvigdrGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:cd03247 94 NL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568987674 572 HLFQLcICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKG 615
Cdd:cd03247 136 QLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
412-610 |
7.97e-27 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 108.71 E-value: 7.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 412 VQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYV 478
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 479 SQQP--WVFSGTVRSNILFGKKYEKERYEKVIkacalKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADI 555
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIE-----ERVEEALELVGLEGLRDRSpFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 556 YLLDDPLSAVDAEVGKHLFQLcICQALHEKITIL-VTHQLQYLKA-ASHILILKDGE 610
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLEL-LKKLKAEGKTIIiVTHDLDLLLElADRVIVLEDGK 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
426-619 |
1.23e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.09 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVF-SGTVRSNI 493
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQSYALYpHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFG----KKYEKERYEKVIKACALkkdLQLLEdgdltvIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:COG3839 97 AFPlklrKVPKAEIDRRVREAAEL---LGLED------LLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 569 VgKHLFQLCIcQALHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:COG3839 168 L-RVEMRAEI-KRLHRRLgttTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
424-619 |
2.82e-26 |
|
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: 108.20 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRS 491
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILFGKKyEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:cd03296 94 NVAFGLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568987674 571 KHLFQLciCQALHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:cd03296 173 KELRRW--LRRLHDELhvtTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
428-620 |
4.87e-26 |
|
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: 107.65 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQPW-------- 483
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMIFQQFNlierlsvl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 484 --VFSG------TVRSniLFGKKYEKERYekviKACALKKDLQLLEDgdltvIGDRGATLSGGQKARVNLARAVYQDADI 555
Cdd:cd03256 97 enVLSGrlgrrsTWRS--LFGLFPKEEKQ----RALAALERVGLLDK-----AYQRADQLSGGQQQRVAIARALMQQPKL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 556 YLLDDPLSAVD---AEVGKHLFqLCICQalHEKITILVT-HQLQYLKA-ASHILILKDGEMVQKGTYTEF 620
Cdd:cd03256 166 ILADEPVASLDpasSRQVMDLL-KRINR--EEGITVIVSlHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
428-623 |
5.06e-26 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 107.20 E-value: 5.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQPWVFSG-TVR 490
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILFGKKYEKERYEKVIKACALKKdLQ---LLEDGDLtvigdRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03261 96 ENVAFPLREHTRLSEEEIREIVLEK-LEavgLRGAEDL-----YPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 568 eVGKHLFQLCI--CQALHEKITILVTHQLQ-YLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:cd03261 170 -IASGVIDDLIrsLKKELGLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
425-623 |
7.28e-26 |
|
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: 107.00 E-value: 7.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 425 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG-TVR 490
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNI-LFGK--KYEKERYEKVIKacalkkdlQLLEDGDLTVIGDRG---ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:cd03295 94 ENIaLVPKllKWPKEKIRERAD--------ELLALVGLDPAEFADrypHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 565 VDAEVGKHLFQ--LCICQALHEKItILVTHQLQ-YLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:cd03295 166 LDPITRDQLQEefKRLQQELGKTI-VFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
428-605 |
3.38e-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: 104.10 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVRSNIL 494
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 FgkkyekeryekvikACALKKD-------LQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG4133 98 F--------------WAALYGLradreaiDEALEAVGLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568987674 567 AEvGKHLFQLCICQALHE-KITILVTHQLQYLKAASHILI 605
Cdd:COG4133 164 AA-GVALLAELIAAHLARgGAVLLTTHQPLELAAARVLDL 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
426-621 |
5.60e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 110.30 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVRSN 492
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGK-KYEKERYEKVIKACALKKdlqLLEDGD-L-TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK11160 434 LLLAApNASDEALIEVLQQVGLEK---LLEDDKgLnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568987674 570 GKHLFQLCICQALHeKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK11160 511 ERQILELLAEHAQN-KTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
424-606 |
6.49e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 103.33 E-value: 6.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPP---ASGLVSVHG-----------RIAYVSQQPWVFSG-T 488
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltalpaeqrRIGILFQDDLLFPHlS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 489 VRSNILFG-----KKyeKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:COG4136 93 VGENLAFAlpptiGR--AQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568987674 563 SAVDAEVGKHLFQLCICQALHEKI-TILVTHQLQYLKAASHILIL 606
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIpALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
428-610 |
6.78e-25 |
|
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: 102.27 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------------RIAYVSQQPWVFSG-TVRS 491
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILFGkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----A 567
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDpitrR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568987674 568 EVGKHLFQLcicQALHEKITILVTHQLQYL-KAASHILILKDGE 610
Cdd:cd03229 138 EVRALLKSL---QAQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
424-622 |
8.18e-25 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 103.57 E-value: 8.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPW--VFSGT 488
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 489 VRSNILFGKKY----EKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:COG1122 93 VEEDVAFGPENlglpREEIRERVEEA---------LELVGLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 564 AVDAEVGKHLFQlcICQALHEK-IT-ILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLK 622
Cdd:COG1122 164 GLDPRGRRELLE--LLKRLNKEgKTvIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
407-650 |
1.22e-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: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 407 KAIVHVQDFTaFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVSVHG---------- 473
Cdd:COG1123 2 TPLLEVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 ---RIAYVSQQPWV--FSGTVRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLAR 547
Cdd:COG1123 81 rgrRIGMVFQDPMTqlNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYpHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 548 AVYQDADIYLLDDPLSAVDAEVGKHLFQL-CICQALHEKITILVTHQLQY-LKAASHILILKDGEMVQKGTYTEFLKSGV 625
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLlRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260
....*....|....*....|....*..
gi 568987674 626 DFGSL--LKKENEEAEPSTAPGTPTLR 650
Cdd:COG1123 236 ALAAVprLGAARGRAAPAAAAAEPLLE 262
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
409-619 |
2.80e-24 |
|
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: 102.27 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 409 IVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------- 473
Cdd:cd03258 1 MIELKNVSkVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 --RIAYVSQQPWVFSG-TVRSNILF----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GATLSGGQKARVNL 545
Cdd:cd03258 81 rrRIGMIFQHFNLLSSrTVFENVALpleiAGVPKAEIEERV---------LELLELVGLEDKADAyPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 546 ARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcicqaLHE-----KITI-LVTHQLQYLKA-ASHILILKDGEMVQKGTYT 618
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILAL-----LRDinrelGLTIvLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
.
gi 568987674 619 E 619
Cdd:cd03258 227 E 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
424-616 |
3.14e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 105.18 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQqpwvfSG----- 487
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQ-----DYalfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 -TVRSNILFG----KKYEKERYEKVIKACALkkdLQLledGDLtviGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:COG3842 92 lTVAENVAFGlrmrGVPKAEIRARVAELLEL---VGL---EGL---ADRYpHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 562 LSAVDAEVGKHLfQLCICQALHE-KIT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:COG3842 163 LSALDAKLREEM-REELRRLQRElGITfIYVTHdQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
424-610 |
3.46e-24 |
|
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: 99.63 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQqpwvfsgtvr 490
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiaklpleelrrRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 snilfgkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568987674 571 KHLFQLCICQALHEKITILVTHQLQYL-KAASHILILKDGE 610
Cdd:cd00267 117 ERLLELLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
389-625 |
4.08e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.80 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 389 FLLLDeLPQRK---AHVPSDGKAIVHVQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA 465
Cdd:PRK11176 319 FAILD-LEQEKdegKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 466 SG-------------LVSVHGRIAYVSQQPWVFSGTVRSNILF--GKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGD 530
Cdd:PRK11176 397 EGeilldghdlrdytLASLRNQVALVSQNVHLFNDTIANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 531 RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQALHE----KITILVTHQLQYLKAASHILIL 606
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES-----ERAIQAALDElqknRTSLVIAHRLSTIEKADEILVV 551
|
250 260
....*....|....*....|
gi 568987674 607 KDGEMVQKGTYTEFL-KSGV 625
Cdd:PRK11176 552 EDGEIVERGTHAELLaQNGV 571
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
423-630 |
6.64e-24 |
|
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: 107.52 E-value: 6.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 423 LDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTV 489
Cdd:TIGR01193 485 YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 490 RSNILFGKKyEKERYEKVIKACAL---KKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987674 567 AEVGKHLFQLCIcqALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSL 630
Cdd:TIGR01193 644 TITEKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
428-623 |
9.95e-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: 100.49 E-value: 9.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------RIAYVSQQPWVFSG-TVRSNILF 495
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 496 GKKyeKERYEKVIKAcalKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 574
Cdd:cd03299 95 GLK--KRKVDKKEIE---RKVLEIAEMLGIDHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568987674 575 QLcICQALHE-KITIL-VTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKS 623
Cdd:cd03299 170 EE-LKKIRKEfGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
427-612 |
1.13e-23 |
|
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: 99.64 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 427 TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------IAYVSQQP--WVFSGTVRSNIL 494
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrksIGYVMQDVdyQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 FGKKYEKERYEKVikACALKK-DLQLLEDgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE----V 569
Cdd:cd03226 95 LGLKELDAGNEQA--ETVLKDlDLYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568987674 570 GKHLFQLcicqALHEKITILVTHQLQYL-KAASHILILKDGEMV 612
Cdd:cd03226 166 GELIREL----AAQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
89-621 |
1.56e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 105.96 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 89 WKSYLILGIFTL-IEEGTRVVQPLflgkIIEYFekydPDDSVALHT-----AYGYAAVLSMCTLILAILHH---LYFYH- 158
Cdd:PRK10790 21 WRKPLGLAVLMLwVAAAAEVSGPL----LISYF----IDNMVAKGNlplglVAGLAAAYVGLQLLAAGLHYaqsLLFNRa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 159 ----VQcagmRLRVAmchmIYRKALRLSNSAMGKTTTGQIVNLLSND--VNKFDQVTIFLHFLWAGPL---QAIAVTVLL 229
Cdd:PRK10790 93 avgvVQ----QLRTD----VMDAALRQPLSAFDTQPVGQLISRVTNDteVIRDLYVTVVATVLRSAALigaMLVAMFSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 230 WVEIGISCLAGLAVLVILLPLQSCIGKLFSSLRSKTAAFTDArirtMNEVITGMRIIKMYAWEKSFADlianlRKKEISK 309
Cdd:PRK10790 165 WRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDG----FNEVINGMSVIQQFRQQARFGE-----RMGEASR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 310 ilgSSYLRGMN---MASFFIANkviLFVTFTSYVLLGneitashvfvAMTLYG-----AVRLTVTLFFPSAIERGSE--- 378
Cdd:PRK10790 236 ---SHYMARMQtlrLDGFLLRP---LLSLFSALILCG----------LLMLFGfsasgTIEVGVLYAFISYLGRLNEpli 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 379 -----------AIVSIRRIknFLLLDELPQRKAhvpSDGKAI----VHVQDFTAFWDKalDSPTLQGLSFIARPGELLAV 443
Cdd:PRK10790 300 elttqqsmlqqAVVAGERV--FELMDGPRQQYG---NDDRPLqsgrIDIDNVSFAYRD--DNLVLQNINLSVPSRGFVAL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 444 VGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKA 510
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvlrqgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 511 CALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQAL---HEKIT 587
Cdd:PRK10790 453 VQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-----EQAIQQALaavREHTT 527
|
570 580 590
....*....|....*....|....*....|....*
gi 568987674 588 ILV-THQLQYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK10790 528 LVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
432-621 |
2.73e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.44 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 432 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNILFGK-- 497
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQENNLFPHlTVAQNIGLGLrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 498 --KYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEVG 570
Cdd:COG3840 99 glKLTAEQRAQVEQA---------LERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568987674 571 KHLFQLCicqaLHEKITIL-VTHQLQ-YLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:COG3840 170 DLVDELC----RERGLTVLmVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
432-621 |
3.13e-23 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 100.03 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 432 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQPWVFSG-TVRSNI 493
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFG-------KKYEKERYEKVIKACALKKDLQLLEDgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:cd03294 124 AFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 567 ----AEVGKHLFQLcicQALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:cd03294 193 plirREMQDELLRL---QAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
426-610 |
1.25e-22 |
|
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: 96.79 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------------IAYVSQQPWVFSG- 487
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLPDl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 TVRSNILFGKkyekeRYEKVIKACALKKDLQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:cd03255 98 TALENVELPL-----LLAGVPKKERRERAEELLERVGLGdRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568987674 567 AEVGKHLFQLciCQALHEK--ITIL-VTHQLQYLKAASHILILKDGE 610
Cdd:cd03255 173 SETGKEVMEL--LRELNKEagTTIVvVTHDPELAEYADRIIELRDGK 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
428-616 |
1.89e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.49 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRiAYVSQQPWV---------------FSGTVRSN 492
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLAAWSPWElarrravlpqhsslaFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGK---KYEKERYEKVIKACALKKDLQLLEDGDLTvigdrgaTLSGGQKARVNLARA---VYQDAD----IYLLDDPL 562
Cdd:COG4559 96 VALGRaphGSSAAQDRQIVREALALVGLAHLAGRSYQ-------TLSGGEQQRVQLARVlaqLWEPVDggprWLFLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 563 SAVDAevgKHlfQLCICQAL----HEKITIL-VTHQL----QYlkaASHILILKDGEMVQKGT 616
Cdd:COG4559 169 SALDL---AH--QHAVLRLArqlaRRGGGVVaVLHDLnlaaQY---ADRILLLHQGRLVAQGT 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
121-621 |
2.48e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.52 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 121 EKYDPDDSVALHTAYGYAAVLSMCT----LILAILHhlyfyhvqcAGMRLRVAMCHMIYRKALRLSNSamgkTTTGQIVN 196
Cdd:PLN03232 945 KSYSPGFYIVVYALLGFGQVAVTFTnsfwLISSSLH---------AAKRLHDAMLNSILRAPMLFFHT----NPTGRVIN 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 197 LLSNDVNKFDQ-----VTIFLHFLWagplQAIAVTVLLWVEIGISCLAGLAVLVIL----LPLQSC---IGKLFSSLRSK 264
Cdd:PLN03232 1012 RFSKDIGDIDRnvanlMNMFMNQLW----QLLSTFALIGTVSTISLWAIMPLLILFyaayLYYQSTsreVRRLDSVTRSP 1087
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 265 TAAftdarirTMNEVITGMRIIKMYAWEKSFADLIANLRKKEISKILGSSYLRGMNMASFFIANKVILFVTfTSYVLLGN 344
Cdd:PLN03232 1088 IYA-------QFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLT-ATFAVLRN 1159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 345 EITASHVFVA--MTLYGAVRLTVTLFFPSAIERGSEA---IVSIRRIKNFLlldELPQRKAHV----------PSDGkaI 409
Cdd:PLN03232 1160 GNAENQAGFAstMGLLLSYTLNITTLLSGVLRQASKAensLNSVERVGNYI---DLPSEATAIiennrpvsgwPSRG--S 1234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDKALdSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVL-------GELP------PASGLVSVHGRIA 476
Cdd:PLN03232 1235 IKFEDVHLRYRPGL-PPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFrivelekGRIMiddcdvAKFGLTDLRRVLS 1313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 477 YVSQQPWVFSGTVRSNI---------LFGKKYEKERYEKVIKACALKKDLQLLEDGDltvigdrgaTLSGGQKARVNLAR 547
Cdd:PLN03232 1314 IIPQSPVLFSGTVRFNIdpfsehndaDLWEALERAHIKDVIDRNPFGLDAEVSEGGE---------NFSVGQRQLLSLAR 1384
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987674 548 AVYQDADIYLLDDPLSAVDAEVGKhLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRTDS-LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
421-615 |
3.39e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 95.44 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDSPTLQgLSFIArPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQPW 483
Cdd:cd03297 8 KRLPDFTLK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 484 VFSG-TVRSNILFGKKYeKERYEKVIKACALkkdLQLLedgDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:cd03297 86 LFPHlNVRENLAFGLKR-KRNREDRISVDEL---LDLL---GLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 562 LSAVDAEVGKHLFQLciCQALHEKI---TILVTH---QLQYLkaASHILILKDGEMVQKG 615
Cdd:cd03297 159 FSALDRALRLQLLPE--LKQIKKNLnipVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
427-615 |
4.89e-22 |
|
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: 95.01 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 427 TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNIL 494
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMVFQNYALYPHmTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 FGKKYEKERY----EKVIKACALKKDLQLLEDgdltvigdRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA--- 567
Cdd:cd03301 95 FGLKLRKVPKdeidERVREVAELLQIEHLLDR--------KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAklr 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568987674 568 -EVGKHLFQLcicQALHEKITILVTH-QLQYLKAASHILILKDGEMVQKG 615
Cdd:cd03301 167 vQMRAELKRL---QQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
407-612 |
5.70e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 95.11 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 407 KAIVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------ 473
Cdd:COG1136 2 SPLLELRNLTkSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 -----RIAYVSQQPWVFSG-TVRSNI----LFGKKYEKERYEKVikacalkkdLQLLED-GdltvIGDRG----ATLSGG 538
Cdd:COG1136 82 rlrrrHIGFVFQFFNLLPElTALENValplLLAGVSRKERRERA---------RELLERvG----LGDRLdhrpSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 539 QKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQALHEK--ITIL-VTHQLQYLKAASHILILKDGEMV 612
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL--LRELNRElgTTIVmVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
428-611 |
7.17e-22 |
|
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: 93.23 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVRSNIl 494
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEEPSLYENlTVRENL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 fgkkyekeryekvikacalkkdlqlledgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 574
Cdd:cd03230 95 ---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 568987674 575 QLcICQALHEKITILV-THQLQYLKA-ASHILILKDGEM 611
Cdd:cd03230 136 EL-LRELKKEGKTILLsSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
428-620 |
7.84e-22 |
|
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: 94.94 E-value: 7.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAV-----LGELPPASGLVSVHG---------------RIAYVSQQPWVFSG 487
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 TVRSNILFGKKYEKERYEKVIKAcalkKDLQLLEDGDLT-VIGDR--GATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:cd03260 96 SIYDNVAYGLRLHGIKLKEELDE----RVEEALRKAALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 565 VDAeVGKHLFQLCIcQALHEKITIL-VTHQL-QYLKAASHILILKDGEMVQKGTYTEF 620
Cdd:cd03260 172 LDP-ISTAKIEELI-AELKKEYTIViVTHNMqQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
711-818 |
1.40e-21 |
|
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: 96.00 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 711 WFFIIFLVLLnmvGQVFYVLQDWWLSHWANKQGALNNTRNANGNitetldLSWYLGIYAGLTAVTVLFGIARSLLVFYIL 790
Cdd:cd18604 1 WALLLLLFVL---SQLLSVGQSWWLGIWASAYETSSALPPSEVS------VLYYLGIYALISLLSVLLGTLRYLLFFFGS 71
|
90 100
....*....|....*....|....*...
gi 568987674 791 VNASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:cd18604 72 LRASRKLHERLLHSVLRAPLRWLDTTPV 99
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
412-621 |
1.53e-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: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 412 VQDFTAFWDKaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAY 477
Cdd:cd03224 3 VENLNAGYGK---SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 478 VSQQPWVFSG-TVRSNILFG-----KKYEKERYEKVikacalkkdLQL---LEDgdltVIGDRGATLSGGQKARVNLARA 548
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGayarrRAKRKARLERV---------YELfprLKE----RRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 549 VYQDADIYLLDDP---LS-AVDAEVGKHLFQLCicqalHEKITILVTHqlQYLKAASHI----LILKDGEMVQKGTYTEF 620
Cdd:cd03224 147 LMSRPKLLLLDEPsegLApKIVEEIFEAIRELR-----DEGVTILLVE--QNARFALEIadraYVLERGRVVLEGTAAEL 219
|
.
gi 568987674 621 L 621
Cdd:cd03224 220 L 220
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
711-818 |
1.90e-21 |
|
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: 96.09 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 711 WFFIIFLVLLNMVGQVFyvlQDWWLSHWAnKQGALNNTRNAN------GNITETLDLSWYLGIYAGLTAVTVLFGIARSL 784
Cdd:cd18599 5 FLFVLLLFILSVGSTVF---SDWWLSYWL-KQGSGNTTNNVDnstvdsGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110
....*....|....*....|....*....|....
gi 568987674 785 LVFYILVNASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPT 114
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
438-616 |
2.04e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------RIAYVSQQPWVFSG-TVRSNILFGKKYeKERYE 505
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQHYALFRHmTVFDNIAFGLTV-LPRRE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 506 KVIKACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQALHE 584
Cdd:PRK10851 107 RPNAAAIKAKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW--LRQLHE 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 568987674 585 --KIT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK10851 185 elKFTsVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
409-615 |
2.13e-21 |
|
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: 93.72 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 409 IVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------- 473
Cdd:cd03257 1 LLEVKNLSvSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 --RIAYVSQQPwvFSG-----TVRSNI-----LFGKKYEKERYEKVIkacalkkdLQLLEDGDL--TVIGDRGATLSGGQ 539
Cdd:cd03257 81 rkEIQMVFQDP--MSSlnprmTIGEQIaeplrIHGKLSKKEARKEAV--------LLLLVGVGLpeEVLNRYPHELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 540 KARVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQALHE-----KITIL-VTHQLQYLKA-ASHILILKDGEMV 612
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKlqeelGLTLLfITHDLGVVAKiADRVAVMYAGKIV 225
|
...
gi 568987674 613 QKG 615
Cdd:cd03257 226 EEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
417-623 |
2.22e-21 |
|
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: 94.10 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 417 AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQP- 482
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrRVQMVFQDPy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 483 ------WvfsgTVRSNI-----LFGKKYEKERYEKVIKACALKKDLQlledgdltvigDR-GATLSGGQKARVNLARAVY 550
Cdd:COG1124 90 aslhprH----TVDRILaeplrIHGLPDREERIAELLEQVGLPPSFL-----------DRyPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 551 QDADIYLLDDPLSAVDAEVGKHLFQLciCQALHE--KIT-ILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKS 623
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNL--LKDLREerGLTyLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
428-623 |
2.48e-21 |
|
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: 93.89 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQPWVFSG-TVR 490
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGMLFQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILF-----GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:COG1127 101 ENVAFplrehTDLSEAEIRELV---------LEKLELVGLPGAADKMpSELSGGMRKRVALARALALDPEILLYDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 565 VDAEVGKHLFQLcIcQALHEKI---TILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKS 623
Cdd:COG1127 172 LDPITSAVIDEL-I-RELRDELgltSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
428-621 |
2.85e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWV-FSGTVRSNI 493
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFGkkyekeRYekvIKACALKKDLQL----LEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDAD------IYLLDDPL 562
Cdd:PRK13548 98 AMG------RA---PHGLSRAEDDALvaaaLAQVDLAHLAGRDyPQLSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987674 563 SAVDAEVGKHLFQLCICQALHEKITIL-VTHQL----QYlkaASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLAHERGLAVIvVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
428-610 |
3.39e-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: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------------RIAYVSQQPWVFSG-TVRS 491
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILFGKKYEKeryeKVIKACALKKDLQLLED-GDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:cd03262 96 NITLAPIKVK----GMSKAEAEERALELLEKvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568987674 571 KHLFQLcICQALHEKIT-ILVTHQLQY-LKAASHILILKDGE 610
Cdd:cd03262 172 GEVLDV-MKDLAEEGMTmVVVTHEMGFaREVADRVIFMDDGR 212
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
424-624 |
1.59e-20 |
|
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: 96.43 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV-------------SVHGRIAYVSQQPWVFSGTVR 490
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvtqaSLRAAIGIVPQDTVLFNDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILFGK-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:COG5265 450 YNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 570 GKHlfqlcICQALHE----KITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:COG5265 530 ERA-----IQAALREvargRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQG 583
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
428-615 |
2.60e-20 |
|
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: 90.28 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAyvsqqpWVF---SG-----TVRSNILFG--- 496
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLLglgGGfnpelTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 497 ----KKYEKERYEKVIKACALKKDLqlledgDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvgkh 572
Cdd:cd03220 112 lglsRKEIDEKIDEIIEFSELGDFI------DLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA---- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568987674 573 lFQL-CIcQALHE-----KITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03220 177 -FQEkCQ-RRLREllkqgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
392-616 |
3.28e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 94.97 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 392 LDELPQRKAHVPSDGKAIVHVQDFTA-FWDKALDSPT-LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV 469
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKrYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 470 SVHG----------------RIAYVSQQPwvFSG-----TVRSNI-----LFGKKYEKERYEKVikacalkkdLQLLEDG 523
Cdd:COG1123 323 LFDGkdltklsrrslrelrrRVQMVFQDP--YSSlnprmTVGDIIaeplrLHGLLSRAERRERV---------AELLERV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 524 DL--TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQALHEK--ITIL-VTHQL---Q 595
Cdd:COG1123 392 GLppDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL--LRDLQRElgLTYLfISHDLavvR 469
|
250 260
....*....|....*....|.
gi 568987674 596 YLkaASHILILKDGEMVQKGT 616
Cdd:COG1123 470 YI--ADRVAVMYDGRIVEDGP 488
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
714-818 |
4.56e-20 |
|
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: 91.41 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 714 IIFLVLLNMVGQVFYVLQDWWLSHWANkqgalNNTRNANgnitetLDLSWYLGIYAGLTAV-TVLFGIARSLLVFYILVN 792
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSS-----DWSSSPN------SSSGYYLGVYAALLVLaSVLLVLLRWLLFVLAGLR 69
|
90 100
....*....|....*....|....*.
gi 568987674 793 ASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:cd18580 70 ASRRLHDKLLRSVLRAPMSFFDTTPS 95
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
432-631 |
7.30e-20 |
|
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: 92.09 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 432 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQPWVFSG-TVRSNI 493
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFPHlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFGKKYE-----KERYEKVIkacalkkdlQLLEDGDLTvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD- 566
Cdd:COG4148 99 LYGRKRApraerRISFDEVV---------ELLGIGHLL---DRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDl 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987674 567 ---AEVGKHLfqlcicQALHEKITI---LVTHQL---QYLkaASHILILKDGEMVQKGTYTEFLkSGVDFGSLL 631
Cdd:COG4148 167 arkAEILPYL------ERLRDELDIpilYVSHSLdevARL--ADHVVLLEQGRVVASGPLAEVL-SRPDLLPLA 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
50-632 |
1.08e-19 |
|
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: 95.01 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 50 EDRSKHLG--EELQRYWDKELLRAKKDSRKPSLTKAIIKCYWKSYLILGIFTlieegTRVVQPLFLGKII-----EYFEK 122
Cdd:TIGR00957 915 GDQSRHHGssAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFI-----TFLSIFLFVCNHVsalasNYWLS 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 123 YDPDDSVALHTAYGYAAVLSM---CTLILAILHHLYFYHVQCAGM----RLRVAMCHMIyrkaLRLSNSAMGKTTTGQIV 195
Cdd:TIGR00957 990 LWTDDPMVNGTQNNTSLRLSVygaLGILQGFAVFGYSMAVSIGGIqasrVLHQDLLHNK----LRSPMSFFERTPSGNLV 1065
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 196 NLLSNDVNKFDQVTIFLHFLWAGPL-QAIAVTVLLWVEIGISclaglAVLVILLPLQSCIGKLFSSLRSKTAAFTDARIR 274
Cdd:TIGR00957 1066 NRFSKELDTVDSMIPPVIKMFMGSLfNVIGALIVILLATPIA-----AVIIPPLGLLYFFVQRFYVASSRQLKRLESVSR 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 275 T-----MNEVITGMRIIKMYAWEKSFaDLIANLRKKEISKILGSSYL--RGMNMASFFIANKVILFVTFTSyVLLGNEIT 347
Cdd:TIGR00957 1141 SpvyshFNETLLGVSVIRAFEEQERF-IHQSDLKVDENQKAYYPSIVanRWLAVRLECVGNCIVLFAALFA-VISRHSLS 1218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 348 ASHVFVAMTLygavRLTVTLFFPSAIERGSEA---IVSIRRIKNFLLLD-ELP-QRKAHVPSDG---KAIVHVQDFTAFW 419
Cdd:TIGR00957 1219 AGLVGLSVSY----SLQVTFYLNWLVRMSSEMetnIVAVERLKEYSETEkEAPwQIQETAPPSGwppRGRVEFRNYCLRY 1294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 420 DKALDSpTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFS 486
Cdd:TIGR00957 1295 REDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIPQDPVLFS 1373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 487 GTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:TIGR00957 1374 GSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 567 AEVgKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLK 632
Cdd:TIGR00957 1454 LET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
405-624 |
1.69e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.30 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 405 DGKAIVHVQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------- 473
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 --RIAYVSQQP-WVFSG-TVRSNILFGKKYE----KERYEKVIKACALKKDLQLLEdgdltvigDRGATLSGGQKARVNL 545
Cdd:PRK13635 80 rrQVGMVFQNPdNQFVGaTVQDDVAFGLENIgvprEEMVERVDQALRQVGMEDFLN--------REPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 546 ARAVYQDADIYLLDDPLSAVD----AEVgkhlfqLCICQALHEK--ITIL-VTHQLQYLKAASHILILKDGEMVQKGTYT 618
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDprgrREV------LETVRQLKEQkgITVLsITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....*.
gi 568987674 619 EFLKSG 624
Cdd:PRK13635 226 EIFKSG 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
424-616 |
2.41e-19 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 87.68 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRI-----AYVSQQPWVFSG-------TVRS 491
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRPVNTVFQNyalfphlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILFG----KKYEKERYEKVIKACALkkdLQLLEDGDltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03300 92 NIAFGlrlkKLPKAEIKERVAEALDL---VQLEGYAN-----RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568987674 568 EVGKHLfQLCIcQALHEK--IT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:cd03300 164 KLRKDM-QLEL-KRLQKElgITfVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
403-616 |
2.62e-19 |
|
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: 87.08 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 403 PSDGKaiVHVQDFTAFWDKALdSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------- 473
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDL-PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistiple 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 ----RIAYVSQQPWVFSGTVRSNI-LFGKKYEKERYEkvikacALKkdlqlledgdltvIGDRGATLSGGQKARVNLARA 548
Cdd:cd03369 79 dlrsSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIYG------ALR-------------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 549 VYQDADIYLLDDPLSAVDAEVgKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGT 616
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYAT-DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
438-615 |
2.66e-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: 87.16 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNILFGK----KYEK 501
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGLspglKLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 502 ERYEKVIKACAlKKDLQLLEDgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQA 581
Cdd:cd03298 104 EDRQAIEVALA-RVGLAGLEK-------RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 568987674 582 LHEKITIL-VTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03298 176 AETKMTVLmVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
428-623 |
5.45e-19 |
|
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: 86.83 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV----------SVHGR----IAYVSQQPWVFSG-TVRSN 492
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklPMHKRarlgIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD- 566
Cdd:cd03218 96 ILavleIRGLSKKEREEKLE---------ELLEEFHITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 567 ---AEVGKhlfqlcICQALHEK-ITILVT-HQL-QYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:cd03218 167 iavQDIQK------IIKILKDRgIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
424-616 |
8.40e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG-TV 489
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 490 RS---------NILFGKKYEKERyEKVIKAcalkkdlqlLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK11231 94 RElvaygrspwLSLWGRLSAEDN-ARVNQA---------MEQTRINHLADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 560 DPLSAVD----AEVGKHLFQLcicqALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGT 616
Cdd:PRK11231 164 EPTTYLDinhqVELMRLMREL----NTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
428-619 |
9.41e-19 |
|
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: 86.34 E-value: 9.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFG--------------KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYL 557
Cdd:cd03219 96 VMVAaqartgsglllaraRREEREARERA---------EELLERVGLADLADRPAgELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987674 558 LDDPLSAVDAEVGKHLFQLcICQALHEKITILVT-HQLQYLKA-ASHILILKDGEMVQKGTYTE 619
Cdd:cd03219 167 LDEPAAGLNPEETEELAEL-IRELRERGITVLLVeHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
424-566 |
1.07e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWV-FSGTV 489
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 490 RSNILFGKKYEKERYEKVIKACALKKDlQLLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK09536 95 RQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
428-616 |
1.19e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAyvsqqpWVF---SG-----TVRSNILFG--- 496
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLelgAGfhpelTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 497 ----KKYEKERYEKVIkacalkkdlqlledgDLTVIGD------RgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG1134 116 lglsRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 567 AEvgkhlFQL-CIcQALHE-----KITILVTHQLQYLKA-ASHILILKDGEMVQKGT 616
Cdd:COG1134 179 AA-----FQKkCL-ARIRElresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
432-631 |
1.36e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.79 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 432 SFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---RIAYVSQQPW--------VFSG-TVRSNILFG--- 496
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRPVsmlfqennLFSHlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 497 ----KKYEKERYEKVIKACALKKDLQLLEdgdltvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 572
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 573 LFQLC--ICQalHEKITIL-VTHQLQ-YLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLL 631
Cdd:PRK10771 168 MLTLVsqVCQ--ERQLTLLmVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
426-567 |
1.41e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.45 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRI--------AYVSQQ----PWVfsgTVRSNI 493
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPWL---NVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFGKKY----EKERYEKvikACALkkdLQL--LEDgdltVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:COG4525 98 AFGLRLrgvpKAERRAR---AEEL---LALvgLAD----FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
368-609 |
2.20e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 368 FFPSAIERGSEAIVSIRRIKNFL----LLDELPQRKAHVPSDGKAIVHVQDFTafwdkaLDSPT----LQGLSFIARPGE 439
Cdd:COG4178 317 WFVDNYQSLAEWRATVDRLAGFEealeAADALPEAASRIETSEDGALALEDLT------LRTPDgrplLEDLSLSLKPGE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 440 LLAVVGPVGAGKSSLLSAVLGELPPASGLVSV--HGRIAYVSQQPWVFSGTVRSNILF---GKKYEKERYEKVIKACALK 514
Cdd:COG4178 391 RLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 515 KDLQLLEDGDltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITILVTHQL 594
Cdd:COG4178 471 HLAERLDEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPGTTVISVGHRS 544
|
250
....*....|....*
gi 568987674 595 QYLKAASHILILKDG 609
Cdd:COG4178 545 TLAAFHDRVLELTGD 559
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
428-623 |
3.92e-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: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGL-VSVHG-------------RIAYVS---QQPWVFSGTVR 490
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGerrggedvwelrkRIGLVSpalQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNIL---FG-----KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:COG1119 99 DVVLsgfFDsiglyREPTDEQRERA---------RELLELLGLAHLADRPfGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 562 LSAVDAEvGKHLF-----QLCicqALHEKITILVTHQLQYLKAA-SHILILKDGEMVQKGTYTEFLKS 623
Cdd:COG1119 170 TAGLDLG-ARELLlalldKLA---AEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
714-818 |
4.64e-18 |
|
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: 85.61 E-value: 4.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 714 IIFLVLLNMVGQVFYVLQDWWLSHWANkqgalNNTRNANGNITETldlSWYLGIYAGLTAVTVLFGIARSLLVFYILVNA 793
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSD-----DPALNGTQDTEQR---DYRLGVYGALGLGQAIFVFLGSLALALGCVRA 72
|
90 100
....*....|....*....|....*
gi 568987674 794 SQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:cd18603 73 SRNLHNKLLHNILRAPMSFFDTTPL 97
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
428-593 |
5.58e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------RIAYVSQQ----PwvfSGTVRSNI 493
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRnamkP---ALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFGKKYeKERYEKVIKACALKKDLQLLEDgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvGKHL 573
Cdd:PRK13539 95 EFWAAF-LGGEELDIAAALEAVGLAPLAH-------LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVAL 165
|
170 180
....*....|....*....|...
gi 568987674 574 FQLCIcqALHEK---ITILVTHQ 593
Cdd:PRK13539 166 FAELI--RAHLAqggIVIAATHI 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
410-610 |
5.67e-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: 81.34 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--RIAYVSQqpwvfsg 487
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 tvrsnilfgkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568987674 568 EVgkhlfqlciCQAL------HEKITILVTHQLQYLKA-ASHILILKDGE 610
Cdd:cd03221 104 ES---------IEALeealkeYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
417-639 |
6.90e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 6.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 417 AFWDKALdsptLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--RIAYVSQQPWVFSG-TVRSNI 493
Cdd:COG0488 7 SFGGRPL----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFG--------KKYEK------------ERYEKVI-------------KACALKKDLQL-LEDGDLTVigdrgATLSGGQ 539
Cdd:COG0488 83 LDGdaelraleAELEEleaklaepdedlERLAELQeefealggweaeaRAEEILSGLGFpEEDLDRPV-----SELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 540 KARVNLARAVYQDADIYLLDDP---LsavDAE-VG---KHLfqlcicqaLHEKIT-ILVTHQLQYL-KAASHILILKDGE 610
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPtnhL---DLEsIEwleEFL--------KNYPGTvLVVSHDRYFLdRVATRILELDRGK 226
|
250 260 270
....*....|....*....|....*....|
gi 568987674 611 MVQ-KGTYTEFLKSgvdfgsllKKENEEAE 639
Cdd:COG0488 227 LTLyPGNYSAYLEQ--------RAERLEQE 248
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
424-622 |
8.25e-18 |
|
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: 82.94 E-value: 8.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVR 490
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILF-------GKKYEKERYEKVIKACALKKDLqlledgdltvigDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:cd03263 94 EHLRFyarlkglPKSEIKEEVELLLRVLGLTDKA------------NKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 563 SAVDAeVGKHLfqlcICQALHEKIT----ILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEfLK 622
Cdd:cd03263 162 SGLDP-ASRRA----IWDLILEVRKgrsiILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQE-LK 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
409-615 |
2.21e-17 |
|
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: 81.65 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 409 IVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGriAYVSQQPW---- 483
Cdd:cd03266 1 MITADALTkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAearr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 484 ---VFSG--------TVRSNIL-FGKKYEKERYEkvIKAcALKKDLQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQ 551
Cdd:cd03266 79 rlgFVSDstglydrlTARENLEyFAGLYGLKGDE--LTA-RLEELADRLGMEEL--LDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 552 DADIYLLDDPLSAVDAEVGKHLFQlcICQALHE--KITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALRE--FIRQLRAlgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
426-593 |
4.85e-17 |
|
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: 80.10 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR------------IAYVSQQPWVFSG-TVRSN 492
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGKKyekeryekvIKACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvGK 571
Cdd:TIGR01189 94 LHFWAA---------IHGGAQRTIEDALAAVGLTGFEDLpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GV 163
|
170 180
....*....|....*....|...
gi 568987674 572 HLFQLCICQALHEK-ITILVTHQ 593
Cdd:TIGR01189 164 ALLAGLLRAHLARGgIVLLTTHQ 186
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
431-620 |
6.04e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 431 LSFIARPGELLAVVGPVGAGKSSLLSaVLGELP-PASGLVSVHGRIAYVSQQP-------------WVFSG-------TV 489
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIAGNHFDFSKTPsdkairelrrnvgMVFQQynlwphlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 490 RSNILfgkkyekERYEKVI---KACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PRK11124 100 QQNLI-------EAPCRVLglsKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 566 DAEVGKHLFQlcICQALHE-KIT-ILVTHQLQYL-KAASHILILKDGEMVQKGTYTEF 620
Cdd:PRK11124 173 DPEITAQIVS--IIRELAEtGITqVIVTHEVEVArKTASRVVYMENGHIVEQGDASCF 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
428-615 |
8.58e-17 |
|
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: 79.93 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGeLLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPwvfsgTVRSNIlf 495
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEF-----GVYPNF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 496 gKKYEKERYEKVIKACALKKD----LQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvG 570
Cdd:cd03264 88 -TVREFLDYIAWLKGIPSKEVkarvDEVLELVNLGdRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE-E 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568987674 571 KHLFQLCICQALHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03264 166 RIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
424-612 |
1.20e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.71 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQPWVFSG 487
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 -TVRSNILF-----GKKyEKERYEKVIKacALKKdlqlledgdltV-IGDRG----ATLSGGQKARVNLARAVYQDADIY 556
Cdd:COG2884 94 rTVYENVALplrvtGKS-RKEIRRRVRE--VLDL-----------VgLSDKAkalpHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 557 LLDDPLSAVDAEVGKHLFQLciCQALHEK-ITILV-THQLQYLKAASH-ILILKDGEMV 612
Cdd:COG2884 160 LADEPTGNLDPETSWEIMEL--LEEINRRgTTVLIaTHDLELVDRMPKrVLELEDGRLV 216
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
710-818 |
1.28e-16 |
|
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: 81.42 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 710 SWFFIIFLVLLnmvgQVFYVLQDWWLSHWANKQgalNNTRNANGNITETLdlswYLGIYAGLTAVTVLFGIARSLLVFYI 789
Cdd:cd18605 1 LILILLSLILM----QASRNLIDFWLSYWVSHS---NNSFFNFINDSFNF----FLTVYGFLAGLNSLFTLLRAFLFAYG 69
|
90 100
....*....|....*....|....*....
gi 568987674 790 LVNASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:cd18605 70 GLRAARRLHNKLLSSILFAKMSFFDKTPV 98
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
428-615 |
1.85e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 78.36 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA--SGLVSVHGR----------IAYVSQQPWVFSG-TVRSNIL 494
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRpldkrsfrkiIGYVPQDDILHPTlTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 FgkkyekeryekvikACALKKdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 574
Cdd:cd03213 105 F--------------AAKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568987674 575 QLCICQALHEKITILVTHQLQYL--KAASHILILKDGEMVQKG 615
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
391-613 |
2.27e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 84.19 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 391 LLDELPQRKAHVPSDGKaiVHVQDFTAFWDKALDSpTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLgELPPASGLVS 470
Cdd:TIGR01271 1201 LVIENPHAQKCWPSGGQ--MDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQ 1276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 471 VHG-----------RIAY--VSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSG 537
Cdd:TIGR01271 1277 IDGvswnsvtlqtwRKAFgvIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSN 1356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 538 GQKARVNLARAVYQDADIYLLDDPLSAVDAeVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQ 613
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
426-595 |
2.86e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.36 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRI--------AYVSQQ----PWVfsgTVRSNI 493
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNegllPWR---NVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFGKkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 572
Cdd:PRK11248 92 AFGL-----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*
gi 568987674 573 LfQLCICQALHE--KITILVTHQLQ 595
Cdd:PRK11248 167 M-QTLLLKLWQEtgKQVLLITHDIE 190
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
714-818 |
4.44e-16 |
|
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: 79.96 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 714 IIFLVLLNMVGQVFYVLQDWWLSHWANKQGALNN-TRNANGNITETLDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVN 792
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASvVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100
....*....|....*....|....*.
gi 568987674 793 ASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPI 106
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
428-622 |
6.19e-16 |
|
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: 77.80 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQQPWVFSG-TVRSNI- 493
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFGKKY------EKERYEKVIKAcalkkdLQLLEDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03265 96 IHARLYgvpgaeRRERIDELLDF------VGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 568 EVGKHLFQlcICQALHEK--ITILVThqLQYL----KAASHILILKDGEMVQKGTYTEfLK 622
Cdd:cd03265 165 QTRAHVWE--YIEKLKEEfgMTILLT--THYMeeaeQLCDRVAIIDHGRIIAEGTPEE-LK 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
428-615 |
8.28e-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: 77.31 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVSVHG----------RIAYVSQQP-WVFSGTVRSNI 493
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGqprkpdqfqkCVAYVRQDDiLLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LF------GKKYEKERYEKVIkacalkKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03234 103 TYtailrlPRKSSDAIRKKRV------EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 568 ----EVGKHLFQLCicqalHEKITILVT-HQ--LQYLKAASHILILKDGEMVQKG 615
Cdd:cd03234 177 ftalNLVSTLSQLA-----RRNRIVILTiHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
424-625 |
8.29e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.82 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG-TV 489
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQENHINSRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 490 RSNILFGK------KYEKERYEKVIKAcalkkdLQLLedgDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:COG4604 93 RELVAFGRfpyskgRLTAEDREIIDEA------IAYL---DLEDLADRYLdELSGGQRQRAFIAMVLAQDTDYVLLDEPL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 563 SAVD----AEVGKHLFQLCicqalHE--KITILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKSGV 625
Cdd:COG4604 164 NNLDmkhsVQMMKLLRRLA-----DElgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPEV 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
428-615 |
9.37e-16 |
|
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: 76.87 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------RIAYVSQQPWVFSG-TVRSNILF 495
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkniealrRIGALIEAPGFYPNlTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 496 GKKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 574
Cdd:cd03268 96 LARLLGIRKKRI---------DEVLDVVGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568987674 575 QLCICQAlHEKITILV-THQLQYL-KAASHILILKDGEMVQKG 615
Cdd:cd03268 167 ELILSLR-DQGITVLIsSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
385-622 |
1.11e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 385 RIKNF--LLLDELPQRKAHV----PSD---GKAIVHVQDFT-AFWDKALdsptLQGLSFIARPGELLAVVGPVGAGKSSL 454
Cdd:COG0488 282 RIKALekLEREEPPRRDKTVeirfPPPerlGKKVLELEGLSkSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 455 LSAVLGELPPASGLVsVHG---RIAYVSQQPWVFSG--TVRSNIlfgKKYEKERYEKVIKacalkkdlQLLED----GD- 524
Cdd:COG0488 358 LKLLAGELEPDSGTV-KLGetvKIGYFDQHQEELDPdkTVLDEL---RDGAPGGTEQEVR--------GYLGRflfsGDd 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 525 -LTVIGDrgatLSGGQKARVNLARAVYQDADIYLLDDP-----LSAVDAevgkhL------FQLCIcqalhekitILVTH 592
Cdd:COG0488 426 aFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA-----LeealddFPGTV---------LLVSH 487
|
250 260 270
....*....|....*....|....*....|..
gi 568987674 593 QLQYLKA-ASHILILKDGEMVQK-GTYTEFLK 622
Cdd:COG0488 488 DRYFLDRvATRILEFEDGGVREYpGGYDDYLE 519
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
428-593 |
1.19e-15 |
|
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: 76.38 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR------------IAYVSQQPWVFSG-TVRSNIL 494
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIKTTlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 FGKKYekeryekvikaCALKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 573
Cdd:cd03231 96 FWHAD-----------HSDEQVEEALARVGLNGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 568987674 574 FQLCICQALHEKITILVTHQ 593
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQ 184
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
428-566 |
1.20e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.38 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 493 IL----FGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG1137 99 ILavleLRKLSKKEREERLE---------ELLEEFGITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
428-621 |
1.39e-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: 76.96 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------------RIAYVSQQPWVFSG-TVRS 491
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltdskkdinklrrKVGMVFQQFNLFPHlTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILFGKKYEKeryeKVIKACALKKDLQLLEdgdlTV-IGDRG----ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG1126 97 NVTLAPIKVK----KMSKAEAEERAMELLE----RVgLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 567 ----AEVgkhlfqLCICQAL-HEKIT-ILVTHQLQY-LKAASHILILKDGEMVQKGTYTEFL 621
Cdd:COG1126 169 pelvGEV------LDVMRDLaKEGMTmVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
711-818 |
2.02e-15 |
|
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: 77.52 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 711 WFFIIFLVLLNmvgQVFYVLQDWWLSHWANKQGALNNTRnangnitetldlswYLGIYAGLTAVTVLFGIARSLLVFYIL 790
Cdd:cd18606 1 LPLLLLLLILS---QFAQVFTNLWLSFWTEDFFGLSQGF--------------YIGIYAGLGVLQAIFLFLFGLLLAYLG 63
|
90 100
....*....|....*....|....*...
gi 568987674 791 VNASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:cd18606 64 IRASKRLHNKALKRVLRAPMSFFDTTPL 91
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
160-577 |
3.09e-15 |
|
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: 79.79 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 160 QCAgMRLRVAMCHMIYRKAL------RLSNSamgKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVL-LWVE 232
Cdd:TIGR00954 161 ELK-LRFRVRLTRYLYSKYLsgftfyKVSNL---DSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFkLLTA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 233 IGISCLAGLAVLV-----ILLPLQSCIGKLfsslrSKTAAFTDARIRTMN-EVITGMRIIKMYAWEK--------SFADL 298
Cdd:TIGR00954 237 LGSVGPAGLFAYLfatgvVLTKLRPPIGKL-----TVEEQALEGEYRYVHsRLIMNSEEIAFYQGNKveketvmsSFYRL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 299 IANLRKKEISKIlgssylrGMNMASFFIANKV-----ILFVTFTSYVLLG-NEITASHVFVAMTLYGAVRLTVTLffPSA 372
Cdd:TIGR00954 312 VEHLNLIIKFRF-------SYGFLDNIVAKYTwsavgLVAVSIPIFDKTHpAFLEMSEEELMQEFYNNGRLLLKA--ADA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 373 IERGSEAIVSIRRIKNFLL-LDELPQ----------RKAHVPSD--------------GKAIVHVQD-FTAFWDKALDSP 426
Cdd:TIGR00954 383 LGRLMLAGRDMTRLAGFTArVDTLLQvlddvksgnfKRPRVEEIesgreggrnsnlvpGRGIVEYQDnGIKFENIPLVTP 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 427 T----LQGLSFIARPGELLAVVGPVGAGKSSLLSaVLGEL-PPASGLVSV--HGRIAYVSQQPWVFSGTVRSNILFGKKY 499
Cdd:TIGR00954 463 NgdvlIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELwPVYGGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIYPDSS 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 500 EkERYEKVIKACALKKDLQLL-------EDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 572
Cdd:TIGR00954 542 E-DMKRRGLSDKDLEQILDNVqlthileREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY 620
|
....*
gi 568987674 573 LFQLC 577
Cdd:TIGR00954 621 MYRLC 625
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
403-616 |
3.14e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.45 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 403 PSDGKAIVHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIayVSQQP 482
Cdd:PRK09452 8 PSSLSPLVELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--ITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 483 -------WVFSG-------TVRSNILFGKKYEK----ERYEKVIKACALKKdlqlLEDgdltvIGDRGAT-LSGGQKARV 543
Cdd:PRK09452 83 aenrhvnTVFQSyalfphmTVFENVAFGLRMQKtpaaEITPRVMEALRMVQ----LEE-----FAQRKPHqLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 544 NLARAVYQDADIYLLDDPLSAVDAEVGKHLfQLCIcQALHEK--IT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQM-QNEL-KALQRKlgITfVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
407-603 |
4.06e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.97 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 407 KAIVHVQDFTAFWDKaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAV--LGELPP---ASGLVSVHGR------- 474
Cdd:PRK14239 3 EPILQVSDLSVYYNK---KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHniysprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 475 --------IAYVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKAcALKKDLQ--LLEDGDLTVIGDRGATLSGGQKARVN 544
Cdd:PRK14239 80 dtvdlrkeIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKgaSIWDEVKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987674 545 LARAVYQDADIYLLDDPLSAVD----AEVGKHLFqlcicqALHEKITIL-VTHQLQylkAASHI 603
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDpisaGKIEETLL------GLKDDYTMLlVTRSMQ---QASRI 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
424-591 |
4.16e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQqpwvFSG---- 487
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQ----FDNldle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 -TVRSNIL-FGKKY--EKERYEKVIKAcalkkdlqLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK13536 129 fTVRENLLvFGRYFgmSTREIEAVIPS--------LLEFARLESKADaRVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180
....*....|....*....|....*....
gi 568987674 563 SAVDAEvGKHLFQLCICQALHEKITILVT 591
Cdd:PRK13536 201 TGLDPH-ARHLIWERLRSLLARGKTILLT 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
428-608 |
4.21e-15 |
|
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: 73.73 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLsAVLGEL-PPASGLVSVHGR--IAYVSQQPWVFSGTVRSNILfgkkYEKERy 504
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLwPWGSGRIGMPEGedLLFLPQRPYLPLGTLREQLI----YPWDD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 505 ekvikacalkkdlqlledgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCicqaLHE 584
Cdd:cd03223 91 -----------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KEL 137
|
170 180
....*....|....*....|....*
gi 568987674 585 KITIL-VTHQLQYLKAASHILILKD 608
Cdd:cd03223 138 GITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
93-386 |
5.63e-15 |
|
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: 76.44 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGIFTLIEEGTRVVQPLFLGKIIeyfekydpdDSVALHTAYG----YAAVLSMCTLILAILHHLYFYHVQCAGMRLRV 168
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLI---------DDVIPAGDLSlllwIALLLLLLALLRALLSYLRRYLAARLGQRVVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 169 AMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIAVTVLL----WVeigiscLAgLAV 243
Cdd:cd07346 73 DLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWK------LT-LVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 244 LVIlLPLQSCIGKLFSSLRSKtaAFTDARIR------TMNEVITGMRIIKMYAWEKS----FADLIANLRKKEISKILGS 313
Cdd:cd07346 146 LLL-LPLYVLILRYFRRRIRK--ASREVRESlaelsaFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLS 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 314 SYLRGMNMASFFIANkVILFVtFTSYVLLGNEITASHVFVAMT----LYGAVRLTVTLFfpSAIERgseAIVSIRRI 386
Cdd:cd07346 223 ALFSPLIGLLTALGT-ALVLL-YGGYLVLQGSLTIGELVAFLAylgmLFGPIQRLANLY--NQLQQ---ALASLERI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
276-637 |
5.76e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.69 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 276 MNEVITGMRIIKMYAWEKSFadlianLRKKEISKILGSSYLRGMN-MASFFIA--NKVILfVTFTSYVLLGNEI---TAS 349
Cdd:PTZ00265 239 IEEALVGIRTVVSYCGEKTI------LKKFNLSEKLYSKYILKANfMESLHIGmiNGFIL-ASYAFGFWYGTRIiisDLS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 350 HVFVAMTLYGAVRLTV-----------TLFFPSAIE--RGSEAIVSIRRIKNfllldelpqRKAHVPS--DGKAI----- 409
Cdd:PTZ00265 312 NQQPNNDFHGGSVISIllgvlismfmlTIILPNITEymKSLEATNSLYEIIN---------RKPLVENndDGKKLkdikk 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH--------------GRI 475
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwrSKI 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 476 AYVSQQPWVFSGTVRSNI---LFGKK---YEKERYEK--------------VIKACA-----------------LKKDLQ 518
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIkysLYSLKdleALSNYYNEdgndsqenknkrnsCRAKCAgdlndmsnttdsnelieMRKNYQ 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 519 LLEDGDL---------------------TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvGKHLFQLC 577
Cdd:PTZ00265 543 TIKDSEVvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKT 621
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 578 I--CQALHEKITILVTHQLQYLKAASHILILKDGEmvqKGTYTEFLKSGVDFGSLLKKENEE 637
Cdd:PTZ00265 622 InnLKGNENRITIIIAHRLSTIRYANTIFVLSNRE---RGSTVDVDIIGEDPTKDNKENNNK 680
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
412-613 |
5.86e-15 |
|
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: 76.05 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 412 VQDFTAFWDKAlDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLgELPPASGLVSVHG-----------RIAY--V 478
Cdd:cd03289 5 VKDLTAKYTEG-GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFgvI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 479 SQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLL 558
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 559 DDPLSAVDAeVGKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQ 613
Cdd:cd03289 163 DEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
415-628 |
7.19e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 7.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 415 FTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVSVHG----------RIAYVSQQ 481
Cdd:TIGR00955 28 RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemraISAYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 482 PWVF-SGTVRSNILF----------GKKYEKERYEKVIKACALKKDLQlledgdlTVIGDRGAT--LSGGQKARVNLARA 548
Cdd:TIGR00955 108 DLFIpTLTVREHLMFqahlrmprrvTKKEKRERVDEVLQALGLRKCAN-------TRIGVPGRVkgLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 549 VYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQY--LKAASHILILKDGEMVQKGTYTEFLKSGVD 626
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVPFFSD 260
|
..
gi 568987674 627 FG 628
Cdd:TIGR00955 261 LG 262
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
410-632 |
7.48e-15 |
|
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: 75.33 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDKALdSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIA 476
Cdd:cd03288 20 IKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 477 YVSQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIY 556
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 557 LLDDPLSAVDAEVgKHLFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFL--KSGVdFGSLLK 632
Cdd:cd03288 179 IMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaqEDGV-FASLVR 254
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
421-611 |
8.22e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.37 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSG 487
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 TVRSNILFGKKYEKERYEKVikacALKKDLQLLEDgDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDa 567
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPDPA----IFLDDLERFAL-PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568987674 568 EVGKHLFQLCICQALHEK-ITIL-VTHQLQYLKAASHILILKD--GEM 611
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQnIAVLwVTHDKDEINHADKVITLQPhaGEM 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
426-620 |
1.01e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVR 490
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILFGKKYEKERYEKVikaCALKKDLQLLEDGDLTvigdrGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:PRK15439 105 ENILFGLPKRQASMQKM---KQLLAALGCQLDLDSS-----AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568987674 571 KHLF-QLCICQALHEKItILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEF 620
Cdd:PRK15439 177 ERLFsRIRELLAQGVGI-VFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
428-612 |
1.03e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 72.46 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQqpwvfsgtvrsni 493
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevsfasprdarragIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 lfgkkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 573
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568987674 574 FQLcICQALHEKITIL-VTHQLQYLKA-ASHILILKDGEMV 612
Cdd:cd03216 122 FKV-IRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
409-615 |
1.23e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.16 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 409 IVHVQDFTAFWDKalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQQPW----- 483
Cdd:PRK13647 4 IIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 484 ----------VFSGTVRSNILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGAT-LSGGQKARVNL 545
Cdd:PRK13647 82 glvfqdpddqVFSSTVWDDVAFGpvnmgldKDEVERRVEEALKAVRMWD------------FRDKPPYhLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 546 ARAVYQDADIYLLDDPLSAVDAEVGKHLFQlcICQALHE--KITILVTHQLQY-LKAASHILILKDGEMVQKG 615
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
416-622 |
1.30e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.08 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 416 TAFWDKALDSptlqgLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------------RIAYVSQ 480
Cdd:PRK13637 16 TPFEKKALDN-----VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 481 QP--WVFSGTVRSNILFGKK----YEKERYEKVIKACALKKDlqlledgDLTVIGDRGA-TLSGGQKARVNLARAVYQDA 553
Cdd:PRK13637 91 YPeyQLFEETIEKDIAFGPInlglSEEEIENRVKRAMNIVGL-------DYEDYKDKSPfELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 554 DIYLLDDPLSAVDAEVGKHLFQLciCQALHEK---ITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLK 622
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNK--IKELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
424-619 |
1.44e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.73 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-IAY--------------VSQQP--WVFS 486
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYdkksllevrktvgiVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 487 GTVRSNILFGK---KYEKERYEKVIKAcALKKdlqlledgdltvIGDRGAT------LSGGQKARVNLARAVYQDADIYL 557
Cdd:PRK13639 94 PTVEEDVAFGPlnlGLSKEEVEKRVKE-ALKA------------VGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 558 LDDPLSAVDAEVGKHLFQLcicqaLH----EKITILV-THQLQYL-KAASHILILKDGEMVQKGTYTE 619
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKL-----LYdlnkEGITIIIsTHDVDLVpVYADKVYVMSDGKIIKEGTPKE 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
407-630 |
1.44e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.77 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 407 KAIVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------- 473
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 RIAYVSQQP-WVFSG-TVRSNILFGKKYE----KERYEKVIKAcalkkdLQLLedgDLTVIGDRG-ATLSGGQKARVNLA 546
Cdd:PRK13650 82 KIGMVFQNPdNQFVGaTVEDDVAFGLENKgiphEEMKERVNEA------LELV---GMQDFKEREpARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 547 RAVYQDADIYLLDDPLSAVDAEVGKHLFQlcICQALHEK--ITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIK--TIKGIRDDyqMTVIsITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
....*..
gi 568987674 624 GVDFGSL 630
Cdd:PRK13650 231 GNDLLQL 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
403-595 |
1.56e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 74.30 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 403 PSDGKAIVHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAV--LGELPP---ASGLVSVHG---- 473
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLDGediy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 -----------RIAYVSQQPWVFSGTVRSNILFG--------KKYEKERYEKVIKACAL----KKDLQlledgdltvigD 530
Cdd:COG1117 82 dpdvdvvelrrRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSELDEIVEESLRKAALwdevKDRLK-----------K 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 531 RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD-AEVGKhlfqlcICQALHE---KITI-LVTHQLQ 595
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK------IEELILElkkDYTIvIVTHNMQ 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
429-593 |
1.89e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 429 QGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIayVSQQPWVFsgtvRSNILF-----GKKYEKER 503
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDEY----HQDLLYlghqpGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 504 YEKVIKACALKkdlQLLEDGD----LTVIGDRG------ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 573
Cdd:PRK13538 92 LENLRFYQRLH---GPGDDEAlweaLAQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170 180
....*....|....*....|
gi 568987674 574 FQLCICQALHEKITILVTHQ 593
Cdd:PRK13538 169 EALLAQHAEQGGMVILTTHQ 188
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
410-615 |
2.08e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.08 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFT-AFWDKAldspTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------RIAYVS 479
Cdd:cd03269 1 LEVENVTkRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 480 QQPWVFSG-TVRSNILFgkkyeKERYEKVIKACALKKDLQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYL 557
Cdd:cd03269 77 EERGLYPKmKVIDQLVY-----LAQLKGLKKEEARRRIDEWLERLELSEYANkRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 558 LDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
428-590 |
2.17e-14 |
|
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: 73.92 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFG-------------------KKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQD 552
Cdd:COG0411 100 VLVAaharlgrgllaallrlpraRREEREARERA---------EELLERVGLADRADEPAgNLSYGQQRRLEIARALATE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568987674 553 ADIYLLDDPLSAVDAEVGKHLFQLcIcQALHE--KITILV 590
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAEL-I-RRLRDerGITILL 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
442-619 |
2.24e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 442 AVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------------IAYVSQQPWVFSG-TVRSNILFG-KKYEKE 502
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLFPHyKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 503 RYEKVIKACALKKdlqLLedgdltvigDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA----EVGKHLFQLc 577
Cdd:PRK11144 108 QFDKIVALLGIEP---LL---------DRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERL- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568987674 578 icqALHEKITIL-VTHQLQ-YLKAASHILILKDGEMVQKGTYTE 619
Cdd:PRK11144 175 ---AREINIPILyVSHSLDeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
428-616 |
2.46e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.11 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQpwvF----SG 487
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalserelraarrKIGMIFQH---FnllsSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 TVRSNILF-----GKKyEKERYEKVikacalkkdLQLLEdgdLTVIGDRG----ATLSGGQKARVNLARAVYQDADIYLL 558
Cdd:COG1135 98 TVAENVALpleiaGVP-KAEIRKRV---------AELLE---LVGLSDKAdaypSQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 559 DDPLSAVDAEVGKHLFQLciCQALHEK--ITI-LVTHQLQYLKA-ASHILILKDGEMVQKGT 616
Cdd:COG1135 165 DEATSALDPETTRSILDL--LKDINRElgLTIvLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
410-594 |
3.36e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.76 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDKAldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------IAYVS 479
Cdd:PRK15056 7 IVVNDVTVTWRNG--HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 480 QQP---WVFSGTVRSNILFGK-------KYEKERYEKVIKACALKKDLQLLEDGDltvIGDrgatLSGGQKARVNLARAV 549
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568987674 550 YQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITILV-THQL 594
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISL-LRELRDEGKTMLVsTHNL 202
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
409-626 |
4.16e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.59 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 409 IVHVQDFTAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RI 475
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrrKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 476 AYVSQQP--WVFSGTVRSNILFGKKYEKERYEKVIKacalKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDA 553
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 554 DIYLLDDPLSAVDAeVGKHLfqlcICQALHE-----KITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVD 626
Cdd:PRK13642 160 EIIILDESTSMLDP-TGRQE----IMRVIHEikekyQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
431-623 |
4.20e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.33 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 431 LSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPwVFSGTVRSNI---- 493
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrckHIRMIFQDP-NTSLNPRLNIgqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 -----LFGKKYEKERYEKVIKAcaLKKdLQLLEDGDLTVIgdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:COG4167 111 eeplrLNTDLTAEEREERIFAT--LRL-VGLLPEHANFYP----HMLSSGQKQRVALARALILQPKIIIADEALAALDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 569 VGKHLFQLCIcqALHEKIT---ILVTHQLQYLKAAS-HILILKDGEMVQKGTYTEFLKS 623
Cdd:COG4167 184 VRSQIINLML--ELQEKLGisyIYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
428-615 |
4.76e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.08 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------------------------RIAYVSQQ 481
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 482 --PWVFSgTVRSNIL--------FGKKYEKERYEKVIKACALKKDLQlledgdltviGDRGATLSGGQKARVNLARAVYQ 551
Cdd:PRK10619 101 fnLWSHM-TVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 552 DADIYLLDDPLSAVDAE-VGKhlfQLCICQALHE--KITILVTHQLQYLK-AASHILILKDGEMVQKG 615
Cdd:PRK10619 170 EPEVLLFDEPTSALDPElVGE---VLRIMQQLAEegKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEG 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
428-615 |
5.71e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.48 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV--------------HGRIAYVSQQ-PWVFSG----- 487
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQLRQHvGFVFQNfnlfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 --TVRSNILFGKKYEKeryeKVIKACALKKDLQLLEDGDLTviGDRGA---TLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK11264 99 hrTVLENIIEGPVIVK----GEPKEEATARARELLAKVGLA--GKETSyprRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 563 SAVDAE-VGKHLfqLCICQALHEKIT-ILVTHQLQYLK-AASHILILKDGEMVQKG 615
Cdd:PRK11264 173 SALDPElVGEVL--NTIRQLAQEKRTmVIVTHEMSFARdVADRAIFMDQGRIVEQG 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
416-654 |
7.49e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.94 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 416 TAFWDKALDSptlqgLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYV 478
Cdd:PRK13641 16 TPMEKKGLDN-----ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 479 SQQP--WVFSGTVRSNILFGKK----YEKERYEKVIKAcaLKKdLQLLEDgdltVIGDRGATLSGGQKARVNLARAVYQD 552
Cdd:PRK13641 91 FQFPeaQLFENTVLKDVEFGPKnfgfSEDEAKEKALKW--LKK-VGLSED----LISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 553 ADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSgvdfGSLL 631
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSD----KEWL 239
|
250 260
....*....|....*....|...
gi 568987674 632 KKENeEAEPSTAPGTPTLRKRTF 654
Cdd:PRK13641 240 KKHY-LDEPATSRFASKLEKGGF 261
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
403-613 |
1.41e-13 |
|
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: 70.93 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 403 PSDGKAIVHVQDFTafwdKALDSPT-----LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---- 473
Cdd:COG4181 2 SSSSAPIIELRGLT----KTVGTGAgeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 ----------RIAYVSqqpWVF-------SGTVRSNI-----LFGKKYEKERYEKVIKACALkkdlqlledgdltviGDR 531
Cdd:COG4181 78 aldedararlRARHVG---FVFqsfqllpTLTALENVmlpleLAGRRDARARARALLERVGL---------------GHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 532 G----ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH----LFQLcicQALHEKITILVTHQLQYLKAASHI 603
Cdd:COG4181 140 LdhypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidlLFEL---NRERGTTLVLVTHDPALAARCDRV 216
|
250
....*....|
gi 568987674 604 LILKDGEMVQ 613
Cdd:COG4181 217 LRLRAGRLVE 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
438-620 |
1.47e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLL----SAVLGELPPASGL------VSVHGRIA-----------YVSQQ-PWVFSGTVRSNILF 495
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIellgrtVQREGRLArdirksrantgYIFQQfNLVNRLSVLENVLI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 496 GKKYEKERYEKVIKACALKKDLQLLEDgdLTVIG------DRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK09984 110 GALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPES 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568987674 570 GKHLFQLCICQALHEKITILVT-HQLQY-LKAASHILILKDGEMVQKGTYTEF 620
Cdd:PRK09984 188 ARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
426-621 |
1.79e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.77 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVFSGTVRSN 492
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 I-LFGKKYEKERYEK--------VIKACALKKDLQLLEDGDltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:PLN03130 1333 LdPFNEHNDADLWESlerahlkdVIRRNSLGLDAEVSEAGE---------NFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 564 AVDaeVGKH-LFQLCICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:PLN03130 1404 AVD--VRTDaLIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
428-616 |
2.21e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELpPASGLVSVHGRI-------------AYVSQQ-PWVFSGTVRSNI 493
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPlsdwsaaelarhrAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 -LFGkkYEKERYEKVIKACAlkkdlQLLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQ-------DADIYLLDDPLSA 564
Cdd:COG4138 91 aLHQ--PAGASSEAVEQLLA-----QLAEALGLEDKLSRPLTqLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 565 VD----AEVGKHLFQLCICQalhekITILV-THQLQY-LKAASHILILKDGEMVQKGT 616
Cdd:COG4138 164 LDvaqqAALDRLLRELCQQG-----ITVVMsSHDLNHtLRHADRVWLLKQGKLVASGE 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
424-591 |
4.43e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------------RIAYVSQqpwvFSG---- 487
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQ----FDNldpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 -TVRSNIL-FGkkyekeRYEKVIKACALKKDLQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13537 95 fTVRENLLvFG------RYFGLSAAAARALVPPLLEFAKLENKADaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180
....*....|....*....|....*..
gi 568987674 565 VDAEvGKHLFQLCICQALHEKITILVT 591
Cdd:PRK13537 169 LDPQ-ARHLMWERLRSLLARGKTILLT 194
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
478-621 |
6.06e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 478 VSQQPWVFSGTVRSNILFGKkyEKERYEKVIKAC---ALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDAD 554
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGK--EDATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 555 IYLLDDPLSAVDAEVGKHLFQLCI-CQALHEKITILVTHQLQYLKAASHILIL----KDGEMVQ-KGTYTEFL 621
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELL 1451
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
393-645 |
6.30e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.40 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 393 DELPQRKAHVPSDGKAIVHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH 472
Cdd:PRK11607 3 DAIPRPQAKTRKALTPLLEIRNLTKSFD---GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 473 GR-IAYVS--QQP--WVFSG-------TVRSNILFGKKyeKERYEKVIKACALKKDLQLLEDGDLTviGDRGATLSGGQK 540
Cdd:PRK11607 80 GVdLSHVPpyQRPinMMFQSyalfphmTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQEFA--KRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 541 ARVNLARAVYQDADIYLLDDPLSAVDAEVgKHLFQLCICQALhEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKL-RDRMQLEVVDIL-ERVgvtCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568987674 617 ------------YTEFLKSGVDFGSLLKKENEEAEPSTAPG 645
Cdd:PRK11607 234 peeiyehpttrySAEFIGSVNVFEGVLKERQEDGLVIDSPG 274
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
392-612 |
6.95e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 6.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 392 LDELPQRKAHVPsdGKAIVHVQDFTAfwdkaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV 471
Cdd:COG1129 241 LEDLFPKRAAAP--GEVVLEVEGLSV-------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 472 HGR--------------IAYVS----QQPWVFSGTVRSNI------------LFGKKYEKERYEKVIKACALKkdlqlLE 521
Cdd:COG1129 312 DGKpvrirsprdairagIAYVPedrkGEGLVLDLSIRENItlasldrlsrggLLDRRRERALAEEYIKRLRIK-----TP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 522 DGDLTVigdrgATLSGG--QKarVNLARAVYQDADIYLLDDPLSAVDaeVG-KH-LFQLcICQALHEKITILV-THQLQY 596
Cdd:COG1129 387 SPEQPV-----GNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGID--VGaKAeIYRL-IRELAAEGKAVIViSSELPE 456
|
250
....*....|....*..
gi 568987674 597 LKAASH-ILILKDGEMV 612
Cdd:COG1129 457 LLGLSDrILVMREGRIV 473
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
407-622 |
9.37e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 69.73 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 407 KAIVHVQDFTAFWD-KALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV---------------- 469
Cdd:PRK13651 6 KNIVKIFNKKLPTElKALD-----NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 470 ---------------------SVHGRIAYVSQ--QPWVFSGTVRSNILFG-------KKYEKERYEKVIKACALkkDLQL 519
Cdd:PRK13651 81 ekvleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 520 LEDGDLTvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLfqLCICQALHE--KITILVTHQLQY- 596
Cdd:PRK13651 159 LQRSPFE--------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI--LEIFDNLNKqgKTIILVTHDLDNv 228
|
250 260 270
....*....|....*....|....*....|..
gi 568987674 597 LKAASHILILKDGEMVQKG-TY-----TEFLK 622
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGdTYdilsdNKFLI 260
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
426-615 |
1.27e-12 |
|
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: 68.13 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIayvsqqPWVFSGTVRSNI--LFGKK----- 498
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV------PWKRRKKFLRRIgvVFGQKtqlww 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 499 --------------Y--EKERYEKVIKACAlkkdlQLLEDGDLTVIGDRgaTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:cd03267 109 dlpvidsfyllaaiYdlPPARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 563 SAVDA----EVGKHLFQLCicqALHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03267 182 IGLDVvaqeNIRNFLKEYN---RERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
428-619 |
1.79e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.68 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQP--WVFSGTVRSN 492
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFG-------KKYEKERYEKVIKACALKKdlqlledgdltvIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13652 100 IAFGpinlgldEETVAHRVSSALHMLGLEE------------LRDRVPhHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 565 VDAEVGKHLFQLciCQALHEK---ITILVTHQLQYL-KAASHILILKDGEMVQKGTYTE 619
Cdd:PRK13652 168 LDPQGVKELIDF--LNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEE 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
428-625 |
2.99e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-------------IAYVSQQ-PWVFSGTVRSNI 493
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFGK-----------KYEKERYEKVIKACALKKDLQLLEDgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK10575 107 AIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 563 SAVDaeVGKHLFQLCICQALHEKITILVTHQLQYLKAAS----HILILKDGEMVQKGTYTEFLKSGV 625
Cdd:PRK10575 176 SALD--IAHQVDVLALVHRLSQERGLTVIAVLHDINMAArycdYLVALRGGEMIAQGTPAELMRGET 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
424-611 |
3.54e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 66.66 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG---------RIAYVSQQ-PWVFSG------ 487
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKiGVVFQDfrllpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 -TVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGdltvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:cd03292 93 rNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHK----HRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568987674 567 AEVGKHLFQLciCQALHEK-ITILV-THQLQYLKAASH-ILILKDGEM 611
Cdd:cd03292 169 PDTTWEIMNL--LKKINKAgTTVVVaTHAKELVDTTRHrVIALERGKL 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
428-650 |
3.98e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGKkyEKER-----YEKVIKACAlkkdlQLLEDGDLTV-IGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSA-V 565
Cdd:COG1129 100 IFLGR--EPRRgglidWRAMRRRAR-----ELLARLGLDIdPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASlT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 566 DAEVgKHLFQlcICQALHEK-ITIL-VTHQLQYLKA-ASHILILKDGEMVqkgtyTEFLKSGVDFGSLLKK------ENE 636
Cdd:COG1129 173 EREV-ERLFR--IIRRLKAQgVAIIyISHRLDEVFEiADRVTVLRDGRLV-----GTGPVAELTEDELVRLmvgrelEDL 244
|
250
....*....|....
gi 568987674 637 EAEPSTAPGTPTLR 650
Cdd:COG1129 245 FPKRAAAPGEVVLE 258
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
427-624 |
4.04e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.47 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 427 TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASG-------------LVSVHGRIAYVSQQP---WVFSgTVR 490
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaitddnFEKLRKHIGIVFQNPdnqFVGS-IVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILFGKKYEKERYEKVIKACAlkkdlQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVS-----EALKQVDMLERADyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 570 GKHLFQLCICQALHEKITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIIsITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
426-619 |
4.06e-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: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQ----PWVfsgTVR 490
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyalyPHM---SVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILFG---KKYEKERYEKVIKACAlkkdlQLLEDGDLTvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK11650 95 ENMAYGlkiRGMPKAEIEERVAEAA-----RILELEPLL---DRKpRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 567 AevgKHLFQLCI-CQALHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:PRK11650 167 A---KLRVQMRLeIQRLHRRLkttSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
428-657 |
5.70e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.37 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSaVLGEL-PPASGLVSVHGR-----------------IAYVSQQPWVFSG-T 488
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQdvatldadalaqlrrehFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 489 VRSNILFGKKYE-KERYEKVIKACALKKDLQLLEDgdltvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PRK10535 103 AAQNVEVPAVYAgLERKQRLLRAQELLQRLGLEDR-----VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 568 EVGKHLfqLCICQALHEK--ITILVTHQLQYLKAASHILILKDGEMVQkgtyteflksgvDFGSLLKKENEEAEPSTAPG 645
Cdd:PRK10535 178 HSGEEV--MAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIVR------------NPPAQEKVNVAGGTEPVVNT 243
|
250
....*....|....
gi 568987674 646 TPTLRKRT--FSEA 657
Cdd:PRK10535 244 ASGWRQFVsgFREA 257
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
410-637 |
6.59e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDKALDSPTLQGLSFIarpgellavvGPVGAGKSSLLSAV--LGELPP---ASGLVSVHG----------- 473
Cdd:PRK14243 18 VYYGSFLAVKNVWLDIPKNQITAFI----------GPSGCGKSTILRCFnrLNDLIPgfrVEGKVTFHGknlyapdvdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 ----RIAYVSQQPWVFSGTVRSNILFGKK---YE---KERYEKVIKACAL----KKDLQlledgdltvigDRGATLSGGQ 539
Cdd:PRK14243 88 evrrRIGMVFQKPNPFPKSIYDNIAYGARingYKgdmDELVERSLRQAALwdevKDKLK-----------QSGLSLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 540 KARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQALHEKITI-LVTHQLQYLKAASHILILKDGEMVQKGTYT 618
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEEL--MHELKEQYTIiIVTHNMQQAARVSDMTAFFNVELTEGGGRY 234
|
250 260
....*....|....*....|...
gi 568987674 619 ----EFLKSGVDFGSLLKKENEE 637
Cdd:PRK14243 235 gylvEFDRTEKIFNSPQQQATRD 257
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
425-616 |
7.60e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 425 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWV-FSG-T 488
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklVGIVFQNPETqFVGrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 489 VRSNILFGKKyekeryekviKACALKKDLQLLEDGDLTVIG------DRGATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK13644 95 VEEDLAFGPE----------NLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 563 SAVDAEVGKHLFQLciCQALHE--KITILVTHQLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK13644 165 SMLDPDSGIAVLER--IKKLHEkgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
397-616 |
8.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.18 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 397 QRKAHVPSD--GKAIVHVQDFTAFWDKALDSP--TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH 472
Cdd:PRK13631 7 KKKLKVPNPlsDDIILRVKNLYCVFDEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 473 G-----------------------------RIAYVSQQP--WVFSGTVRSNILFG------KKYE-KERYEKVIKACALK 514
Cdd:PRK13631 87 DiyigdkknnhelitnpyskkiknfkelrrRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 515 KDLqlLEDGDLTvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQL 594
Cdd:PRK13631 167 DSY--LERSPFG--------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTM 236
|
250 260
....*....|....*....|...
gi 568987674 595 -QYLKAASHILILKDGEMVQKGT 616
Cdd:PRK13631 237 eHVLEVADEVIVMDKGKILKTGT 259
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
426-568 |
1.33e-11 |
|
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: 65.15 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH---------------------GRIAYVSQ---- 480
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 481 -----------QPWVFSGTvrsnilfgkkyekERYEKVIKACALKKDLQLLEdgdltvigdR-----GATLSGGQKARVN 544
Cdd:COG4778 105 iprvsaldvvaEPLLERGV-------------DREEARARARELLARLNLPE---------RlwdlpPATFSGGEQQRVN 162
|
170 180
....*....|....*....|....
gi 568987674 545 LARAVYQDADIYLLDDPLSAVDAE 568
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
431-621 |
1.48e-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: 67.65 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 431 LSFIarPGELLAVVGPVGAGKSSLL-------SAVLGELPPASGLvsvhgRIAYVSQQPWV-FSGTVRSNILFG------ 496
Cdd:TIGR03719 26 LSFF--PGAKIGVLGLNGAGKSTLLrimagvdKDFNGEARPQPGI-----KVGYLPQEPQLdPTKTVRENVEEGvaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 497 --KKY-------------------EKERYEKVIKAC-ALKKDLQL--------LEDGDLTVigdrgATLSGGQKARVNLA 546
Cdd:TIGR03719 99 alDRFneisakyaepdadfdklaaEQAELQEIIDAAdAWDLDSQLeiamdalrCPPWDADV-----TKLSGGERRRVALC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 547 RAVYQDADIYLLDDPLSAVDAE----VGKHL--FQLCIcqalhekitILVTHQLQYL-KAASHILILKDGEMVQ-KGTYT 618
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAEsvawLERHLqeYPGTV---------VAVTHDRYFLdNVAGWILELDRGRGIPwEGNYS 244
|
...
gi 568987674 619 EFL 621
Cdd:TIGR03719 245 SWL 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
428-618 |
1.72e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.84 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQPWV---FSG 487
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLlpdFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 --TVRSNILFGKKYEKERYEK---VIKACALKKDLQlledgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK11629 105 leNVAMPLLIGKKKPAEINSRaleMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 563 SAVDAEVGKHLFQLC-ICQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYT 618
Cdd:PRK11629 174 GNLDARNADSIFQLLgELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLM 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
420-623 |
1.83e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.98 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 420 DKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQP 482
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 483 WVFSG-TVRSNILFGKKYE----KERYEKVIKAcalkkdlqLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYL 557
Cdd:PRK10070 116 ALMPHmTVLDNTAFGMELAginaEERREKALDA--------LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 558 LDDPLSAVDAEVGKHLF-QLCICQALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
428-593 |
2.07e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPAS--GLVSVHG---------RIAYVSQQPWVFSG-TVRSNILF 495
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrkptkqilkRTGFVTQDDILYPHlTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 496 ------GKKYEKEryEKVIKACALKKDLQLLEDGDlTVIGD---RGatLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PLN03211 164 csllrlPKSLTKQ--EKILVAESVISELGLTKCEN-TIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180
....*....|....*....|....*..
gi 568987674 567 AEVGKHLFQLCICQALHEKITILVTHQ 593
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
438-624 |
3.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.19 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQP--WVFSGTVRSNILFGKK 498
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFPesQLFEDTVEREIIFGPK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 499 YEKERYEKViKACALKKDLQLLEDGDltVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCI 578
Cdd:PRK13646 113 NFKMNLDEV-KNYAHRLLMDLGFSRD--VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLK 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568987674 579 -CQALHEKITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:PRK13646 190 sLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
436-610 |
3.84e-11 |
|
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: 63.97 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 436 RPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-RIAYVSQQPWV-FSGTVRSnILFGK---KYEKERYEKVIKa 510
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKAdYEGTVRD-LLSSItkdFYTHPYFKTEIA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 511 calkKDLQL--LEDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-------VGKHLfqlcicqA 581
Cdd:cd03237 101 ----KPLQIeqILDREVP-------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmaskVIRRF-------A 162
|
170 180 190
....*....|....*....|....*....|
gi 568987674 582 LHEKITILVT-HQLQYLKAASHILILKDGE 610
Cdd:cd03237 163 ENNEKTAFVVeHDIIMIDYLADRLIVFEGE 192
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
438-621 |
7.06e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQ----------QPWVFSGTVRSNIL 494
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLAQnattpgditvQELVARGRYPHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 FgKKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 573
Cdd:PRK10253 113 F-TRWRKEDEEAVTKA---------MQATGITHLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568987674 574 FQLcICQALHEKITIL--VTHQL-QYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK10253 183 LEL-LSELNREKGYTLaaVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
406-611 |
7.21e-11 |
|
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: 61.68 E-value: 7.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 406 GKAIVHVQDFTAfwdkaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------- 474
Cdd:cd03215 1 GEPVLEVRGLSV-------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdai 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 475 ---IAYVS----QQPWVFSGTVRSNILFGkkyekeryekvikacalkkdlqlledgdltvigdrgATLSGG--QKarVNL 545
Cdd:cd03215 74 ragIAYVPedrkREGLVLDLSVAENIALS------------------------------------SLLSGGnqQK--VVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 546 ARAVYQDADIYLLDDPLSAVDaeVG--KHLFQLCICQALHEKITILVTHQLQYLKA-ASHILILKDGEM 611
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVD--VGakAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
424-621 |
9.27e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.80 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAV--LGELPPASGLV---SVHGRIA----------YVSQQPWVFSG- 487
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDLIVdglKVNDPKVderlirqeagMVFQQFYLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 TVRSNILFGKKyekeRYEKVIKACALKKDLQLLEDGDLtviGDRG----ATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:PRK09493 93 TALENVMFGPL----RVRGASKEEAEKQARELLAKVGL---AERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 564 AVDAEVGKHLfqLCICQALHEK--ITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK09493 166 ALDPELRHEV--LKVMQDLAEEgmTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
424-591 |
1.03e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------IAYVSQQPwvfsgtvrsni 493
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLP----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 lfGKKYEKERYEKVIKACALK-KDLQLLEDGDLTVIGDRGAT------LSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13543 92 --GLKADLSTLENLHFLCGLHgRRAKQMPGSALAIVGLAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*
gi 568987674 567 AEvGKHLFQLCICQALHEKITILVT 591
Cdd:PRK13543 170 LE-GITLVNRMISAHLRGGGAALVT 193
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
426-612 |
1.14e-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: 61.89 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVS------------VHGRIAYVSQQPWVFSG-TV 489
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHyngipykefaekYPGEIIYVSEEDVHFPTlTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 490 RSNILFgkkyekeryekvikACALKkdlqlledGDLTVigdRGatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:cd03233 101 RETLDF--------------ALRCK--------GNEFV---RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568987674 570 GKHLFQlCICQALHE-KITILVThqlqyLKAAS--------HILILKDGEMV 612
Cdd:cd03233 154 ALEILK-CIRTMADVlKTTTFVS-----LYQASdeiydlfdKVLVLYEGRQI 199
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
428-619 |
1.49e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.67 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR----------------IAYVSQQpwvF----SG 487
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrkarrqIGMIFQH---FnllsSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 TVRSNILFGKKYEKERYEKvIKacalKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK11153 98 TVFDNVALPLELAGTPKAE-IK----ARVTELLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 567 AEVGKHLFQLC--ICQALHekITI-LVTHQLQYLKA-ASHILILKDGEMVQKGTYTE 619
Cdd:PRK11153 173 PATTRSILELLkdINRELG--LTIvLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSE 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
428-616 |
1.52e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELP--PASGLVSVHGRI-------------------AYVSQ--QPwV 484
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVtlngeplaaidaprlarlrAVLPQaaQP-A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 485 FSGTVRSNILFGkkyekeRYEKVIKACALKKdlqllEDGDL-----------TVIGDRGATLSGGQKARVNLARAVYQ-- 551
Cdd:PRK13547 96 FAFSAREIVLLG------RYPHARRAGALTH-----RDGEIawqalalagatALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 552 -------DADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITIL-VTHQLQYlkAASH---ILILKDGEMVQKGT 616
Cdd:PRK13547 165 pphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNL--AARHadrIAMLADGAIVAHGA 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
438-616 |
1.59e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.59 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNILFGKKYEK---- 501
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHmSLGENVGYGLKMLGvpke 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 502 ERYEKVIKACALKkdlqlledgDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKhlfqlcicq 580
Cdd:PRK11432 112 ERKQRVKEALELV---------DLAGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR--------- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568987674 581 ALHEKI----------TILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK11432 174 SMREKIrelqqqfnitSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGS 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
441-585 |
1.64e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.88 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 441 LAVVGPVGAGKSSLLSAVLGELPPASGLV--SVHGRIAYVSQQPwVFSGTVRSNILFgkkYEKERYEKVIKAcALKKDLq 518
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMAVFSQHH-VDGLDLSSNPLL---YMMRCFPGVPEQ-KLRAHL- 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 519 lledGDLTVIGDRGA----TLSGGQKARVNLARAVYQDADIYLLDDP-----LSAVDAEV-GKHLFQLCICQALHEK 585
Cdd:PLN03073 612 ----GSFGVTGNLALqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPsnhldLDAVEALIqGLVLFQGGVLMVSHDE 684
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-616 |
1.73e-10 |
|
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: 64.32 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 391 LLDELPQR-KAHVPSDGKAIVHVQDF-------------TAFWDKALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLS 456
Cdd:COG4172 256 LLAAEPRGdPRPVPPDAPPLLEARDLkvwfpikrglfrrTVGHVKAVD-----GVSLTLRRGETLGLVGESGSGKSTLGL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 457 AVLGeLPPASGLVSVHG----------------RIAYVSQQPwvFSG-----TVRS------NILFGKKYEKERYEKVIk 509
Cdd:COG4172 331 ALLR-LIPSEGEIRFDGqdldglsrralrplrrRMQVVFQDP--FGSlsprmTVGQiiaeglRVHGPGLSAAERRARVA- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 510 acalkkdlQLLEDGDLtvigDRGAT------LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQALH 583
Cdd:COG4172 407 --------EALEEVGL----DPAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDL--LRDLQ 472
|
250 260 270
....*....|....*....|....*....|....*..
gi 568987674 584 EK--IT-ILVTHQLQYLKAASH-ILILKDGEMVQKGT 616
Cdd:COG4172 473 REhgLAyLFISHDLAVVRALAHrVMVMKDGKVVEQGP 509
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
410-626 |
1.99e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDKaldSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAvLGELPPASGLVSVHGRIAYVSQ--------- 480
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQniyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 481 ------------QPWVFSGTVRSNILFGKK----YEKERYEKVIKACALKKDLQlleDGDLTVIGDRGATLSGGQKARVN 544
Cdd:PRK14258 84 nrlrrqvsmvhpKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDADLW---DEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 545 LARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITI-LVTHQLQYLKAASHILIL------KDGEMVQKGTY 617
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMvIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEFGLT 240
|
....*....
gi 568987674 618 TEFLKSGVD 626
Cdd:PRK14258 241 KKIFNSPHD 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
424-623 |
2.04e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.32 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQP-WVFSG-T 488
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeirkKIGIIFQNPdNQFIGaT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 489 VRSNILFG---KKYEKERYEKVIKACALKKDLQLLEDGDltvigdrGATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PRK13632 101 VEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDYLDKE-------PQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 566 DA----EVGKHLFQLcicQALHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK13632 174 DPkgkrEIKKIMVDL---RKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
410-636 |
2.13e-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: 64.05 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 410 VHVQDFTAFWDkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLG--ELPPASGLVSVH----------GRIAY 477
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyvERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 478 VSQQP--------------WVFSGTVRSN------ILFGKK---YEKER-YEKVIKAC---------ALKKDLQLLEDGD 524
Cdd:TIGR03269 78 VGEPCpvcggtlepeevdfWNLSDKLRRRirkriaIMLQRTfalYGDDTvLDNVLEALeeigyegkeAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 525 LT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVT-HQLQYL-KAAS 601
Cdd:TIGR03269 158 LShRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIeDLSD 237
|
250 260 270
....*....|....*....|....*....|....*
gi 568987674 602 HILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENE 636
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECE 272
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
435-568 |
2.25e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 435 ARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSQqpWV---FSGTVRSNI-----LFGKKYEKEryeK 506
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLLrsitdDLGSSYYKS---E 436
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 507 VIKACALKKdlqlLEDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:PRK13409 437 IIKPLQLER----LLDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
438-615 |
2.64e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.12 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLG-----------------ELPPASGLVSVhgriayvsqqpwVFSG-------TVRSNI 493
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGleditsgdlfigekrmnDVPPAERGVGM------------VFQSyalyphlSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFGKKYEK----ERYEKVIKACALKKDLQLLEDgdltvigdRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA-- 567
Cdd:PRK11000 97 SFGLKLAGakkeEINQRVNQVAEVLQLAHLLDR--------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAal 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 568 ------EVGKhlfqlcicqaLHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKG 615
Cdd:PRK11000 169 rvqmriEISR----------LHKRLgrtMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
428-612 |
2.77e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.64 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV----------SVHGRIAYVSQqpwVF---------SGT 488
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklPEYKRAKYIGR---VFqdpmmgtapSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 489 VRSNILF----GKKY---------EKERY-EKVikacalkKDLQL-LEDGdltvIGDRGATLSGGQKARVNLARAVYQDA 553
Cdd:COG1101 99 IEENLALayrrGKRRglrrgltkkRRELFrELL-------ATLGLgLENR----LDTKVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 554 DIYLLDDPLSAVD----AEVgkhlfqlcicQALHEKI-------TILVTHQLQY-LKAASHILILKDGEMV 612
Cdd:COG1101 168 KLLLLDEHTAALDpktaALV----------LELTEKIveennltTLMVTHNMEQaLDYGNRLIMMHEGRII 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
428-612 |
3.09e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 IL------FGKKYEKERYEKVIKACALKKDLQLledgDL-TVIGDrgatLSGGQKARVNLARAVYQDADIYLLDDPlSAV 565
Cdd:COG3845 101 IVlgleptKGGRLDRKAARARIRELSERYGLDV----DPdAKVED----LSVGEQQRVEILKALYRGARILILDEP-TAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568987674 566 --DAEVgKHLFQlcICQAL-HEKITIL-VTHQLQYLKAASH-ILILKDGEMV 612
Cdd:COG3845 172 ltPQEA-DELFE--ILRRLaAEGKSIIfITHKLREVMAIADrVTVLRRGKVV 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
424-623 |
3.21e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.60 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAY-------------------VSQQPWV 484
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiklrkevgmVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 485 FSG-TVRSNILFGKKY----EKERYEKVIKACalkkdlqLLEDGDLTVIGDR----GATLSGGQKARVNLARAVYQDADI 555
Cdd:PRK14246 102 FPHlSIYDNIAYPLKShgikEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 556 YLLDDPLSAVDAeVGKHLFQLCICQALHEKITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK14246 175 LLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
428-615 |
3.54e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLgELPPASG----------------LVSVHGRIAYVSQQPWVfSGTVRS 491
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGeiwfdgqplhnlnrrqLLPVRHRIQVVFQDPNS-SLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NIL----------FGKKYEKERYEKVIKAcalkkdlqLLEDG-DLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK15134 380 NVLqiieeglrvhQPTLSAAQREQQVIAV--------MEEVGlDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 561 PLSAVDAEVGKHLFQLC-ICQALHEKITILVTHQLQYLKAASH-ILILKDGEMVQKG 615
Cdd:PRK15134 452 PTSSLDKTVQAQILALLkSLQQKHQLAYLFISHDLHVVRALCHqVIVLRQGEVVEQG 508
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
428-625 |
4.25e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.10 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR------IAYVSQQ--------PWvfsGTVRSNI 493
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdLYALSEAerrrllrtEW---GFVHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFGKKYE-------KERYEKV-------IKACALKKdLQLLEDgDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK11701 99 RDGLRMQvsaggniGERLMAVgarhygdIRATAGDW-LERVEI-DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 560 DPLSAVDAEVGKHLFQLC--ICQALHEKItILVTHQLQYLKAASH-ILILKDGEMVQKG-----------TYTEFLKSGV 625
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLrgLVRELGLAV-VIVTHDLAVARLLAHrLLVMKQGRVVESGltdqvlddpqhPYTQLLVSSV 255
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
434-604 |
4.62e-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: 60.84 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 434 IARPGELLAVVGPVGAGKSSLLSAVLGELPPASGL------------------------------VSVHGRIAYVSQQPW 483
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkllegdVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 484 VFSGTVRSniLFGKKYEKERYEKVIKACALKKDLqlledgdltvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:cd03236 102 AVKGKVGE--LLKKKDERGKLDELVDQLELRHVL------------DRNiDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568987674 563 SAVDaeVGKHLFQLCICQAL--HEKITILVTHQ---LQYLKAASHIL 604
Cdd:cd03236 168 SYLD--IKQRLNAARLIRELaeDDNYVLVVEHDlavLDYLSDYIHCL 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
436-616 |
4.73e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 436 RPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-----------------IAYVSQQP--WVFSGTVRSNILFG 496
Cdd:PRK13634 31 PSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkknkklkplrkkVGIVFQFPehQLFEETVEKDICFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 497 -------KKYEKERYEKVIKACALKKDLQlledgdltvigDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:PRK13634 111 pmnfgvsEEDAKQKAREMIELVGLPEELL-----------ARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 569 VGKHLFQLciCQALHEK---ITILVTHQL----QYlkaASHILILKDGEMVQKGT 616
Cdd:PRK13634 180 GRKEMMEM--FYKLHKEkglTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGT 229
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
424-623 |
4.88e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLV--SVHGRIAYVSQQPwvfsgtvrsnilfgkkyek 501
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQDH------------------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 502 eryekvikACALKKDLQLLE---------DGDLTVIGDRG-------------ATLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK15064 392 --------AYDFENDLTLFDwmsqwrqegDDEQAVRGTLGrllfsqddikksvKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 560 DPLSAVDAEVGKHLfqlciCQAL--HEKITILVTHQLQYLKA-ASHILILKDGEMVQ-KGTYTEFLKS 623
Cdd:PRK15064 464 EPTNHMDMESIESL-----NMALekYEGTLIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYLRS 526
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
435-568 |
5.20e-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: 62.88 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 435 ARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAY----VSQQpwvFSGTVRSNI-------LFGKKYEKEr 503
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyISPD---YDGTVEEFLrsantddFGSSYYKTE- 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 504 yekVIKACALKKdlqlLEDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:COG1245 439 ---IIKPLGLEK----LLDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
426-622 |
5.27e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPP---ASGLVSVHG-------------RIAYVSQQP-WVFSG- 487
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGitltaktvwdireKVGIVFQNPdNQFVGa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 TVRSNILFGKKYEKERYEKVIKACAlkkdlQLLED-GDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKIVR-----DVLADvGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 567 AEVGKHLFQLCICQALHEKITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLK 622
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVIsITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
428-599 |
5.34e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--RIAYVSQQ-------PWVFS-------GTVRS 491
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQKlyldttlPLTVNrflrlrpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILfgkkyekERYEKVIKACALKKDLQlledgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:PRK09544 100 DIL-------PALKRVQAGHLIDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|
gi 568987674 572 HLFQLcICQALHEK--ITILVTHQLQYLKA 599
Cdd:PRK09544 158 ALYDL-IDQLRRELdcAVLMVSHDLHLVMA 186
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
428-616 |
7.04e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.89 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRiayvsqqPwvFSGTVRSNIlfGkkY--EkER-- 503
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-------P--LDPEDRRRI--G--YlpE-ERgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 504 Y--EKVI-------------KACALKKDLQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:COG4152 83 YpkMKVGeqlvylarlkglsKAEAKRRADEWLERLGLGdRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 568 eVGKHLFQlcicQALHE-----KITILVTHQLQYLKA-ASHILILKDGEMVQKGT 616
Cdd:COG4152 163 -VNVELLK----DVIRElaakgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
406-620 |
8.24e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 8.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 406 GKAIVHVQDFT-AFWDKALdsptLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVhG---RIAYVSQQ 481
Cdd:TIGR03719 319 GDKVIEAENLTkAFGDKLL----IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GetvKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 482 pwvfsgtvRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGDR--------------GA-------TLSGGQ 539
Cdd:TIGR03719 394 --------RDAL----DPNKTVWEEI-------------SGGlDIIKLGKReipsrayvgrfnfkGSdqqkkvgQLSGGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 540 KARVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfqlciCQALHEKI------TILVTHQLQYL-KAASHILILK-DGEM 611
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVET---------LRALEEALlnfagcAVVISHDRWFLdRIATHILAFEgDSHV 519
|
250
....*....|
gi 568987674 612 VQ-KGTYTEF 620
Cdd:TIGR03719 520 EWfEGNFSEY 529
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
428-615 |
8.60e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGK--------------KYEKERYEKVIKACALKKDLqlledgDLTVigdrgATLSGGQKARVNLARAVYQDADIYLL 558
Cdd:PRK09700 101 LYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDL------DEKV-----ANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 559 DDPLSAV-DAEVgKHLFqLCICQALHE-KITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:PRK09700 170 DEPTSSLtNKEV-DYLF-LIMNQLRKEgTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
428-566 |
9.05e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASG----------LVSVHGR----IAYVSQQPWVFSgtvRSNI 493
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedisLLPLHARarrgIGYLPQEASIFR---RLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 lfgkkyekerYEKVIKACALKKDL----------QLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK10895 96 ----------YDNLMAVLQIRDDLsaeqredranELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
....
gi 568987674 563 SAVD 566
Cdd:PRK10895 166 AGVD 169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
416-616 |
9.59e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.41 E-value: 9.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 416 TAFWDKALDSPTLQglsfiARPGELLAVVGPVGAGKSSLLS------------AVLGELPPASGLVSV------HGRIAY 477
Cdd:PRK13645 20 TPFEFKALNNTSLT-----FKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIkevkrlRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 478 VSQQP--WVFSGTVRSNILFGKKYEKERYEKVIKACA-LKKDLQLLEDgdltVIGDRGATLSGGQKARVNLARAVYQDAD 554
Cdd:PRK13645 95 VFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPeLLKLVQLPED----YVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568987674 555 IYLLDDPLSAVDAEVGKHLFQLCI-CQALHEKITILVTHQL-QYLKAASHILILKDGEMVQKGT 616
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFErLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
440-615 |
1.39e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.47 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 440 LLAVVGPVGAGKSSLLSAV-----LGELPPASGLVSVHGRIAY---------------VSQQPWVFSG-TVRSNILFGKK 498
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpievrrevgmVFQYPNPFPHlTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 499 YEK---------ERYEKVIKACALKKDLQlledgdlTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeV 569
Cdd:PRK14267 112 LNGlvkskkeldERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-V 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568987674 570 GKHLFQLCICQALHEKITILVTHQ-LQYLKAASHILILKDGEMVQKG 615
Cdd:PRK14267 184 GTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
421-623 |
2.24e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 59.68 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPP---ASGLVSVHG-----------------RIAYVSQ 480
Cdd:COG0444 19 KAVD-----GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedllklsekelrkirgrEIQMIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 481 QPW-----VFsgTVRSNI-----LFGKKYEKERYEKVIkacalkkdlQLLEDGDLTVIGDRGA----TLSGGQKARVNLA 546
Cdd:COG0444 94 DPMtslnpVM--TVGDQIaeplrIHGGLSKAEARERAI---------ELLERVGLPDPERRLDryphELSGGMRQRVMIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 547 RAVYQDADIYLLDDPLSAVDAEVgkhlfqlcicQA--------LHEKI---TILVTHQL---QYLkaASHILILKDGEMV 612
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTI----------QAqilnllkdLQRELglaILFITHDLgvvAEI--ADRVAVMYAGRIV 230
|
250
....*....|.
gi 568987674 613 QKGTYTEFLKS 623
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
431-623 |
2.24e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.03 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 431 LSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------------RIAYVSQQPWVfSGTVRSNI---- 493
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqRIRMIFQDPST-SLNPRQRIsqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 ----LFGKKYEKERYEKVIKAcALKKdLQLLEDGdltvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK15112 111 dfplRLNTDLEPEQREKQIIE-TLRQ-VGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 570 GKHLFQLCI-CQALHEKITILVTHQLQYLKAAS-HILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK15112 185 RSQLINLMLeLQEKQGISYIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
425-622 |
2.52e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 425 SPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGeLPPASGLVSVHGRI-------------AYVSQQ-PWVFSGTVr 490
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelarhrAYLSQQqTPPFAMPV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 snilF-------GKKYEKERYEKVIKACAlkkdlQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQ-------DADIY 556
Cdd:PRK03695 87 ----FqyltlhqPDKTRTEAVASALNEVA-----EALGLDDK--LGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 557 LLDDPLSAVDAEVGKHLFQLC--ICQAlheKITILVT-HQLQY-LKAASHILILKDGEMVQKGTYTEFLK 622
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLseLCQQ---GIAVVMSsHDLNHtLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
93-358 |
2.94e-09 |
|
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: 58.94 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGI-FTLIEEGTRVVQPLFLGKII-EYFEKYDPDDSVALHTAYGYAAVLsmctLILAILHHLYFYHVQCAGMR----L 166
Cdd:cd18544 1 FILALlLLLLATALELLGPLLIKRAIdDYIVPGQGDLQGLLLLALLYLGLL----LLSFLLQYLQTYLLQKLGQRiiydL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 167 RVAmchmIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ--VTIFLHFLWAGPLQAIAVTVLLWVEIGISCLAgLAVL 244
Cdd:cd18544 77 RRD----LFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNElfTSGLVTLIGDLLLLIGILIAMFLLNWRLALIS-LLVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 245 VILLPL----QSCIGKLFSSLRSKTA---AFtdarirtMNEVITGMRIIKMYAWEKS----FADLIANLRK---KEIskI 310
Cdd:cd18544 152 PLLLLAtylfRKKSRKAYREVREKLSrlnAF-------LQESISGMSVIQLFNREKRefeeFDEINQEYRKanlKSI--K 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568987674 311 LGSSYLRGMNMASFFIankVILFVTFTSYVLLGNEITAShVFVAMTLY 358
Cdd:cd18544 223 LFALFRPLVELLSSLA---LALVLWYGGGQVLSGAVTLG-VLYAFIQY 266
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
436-627 |
4.17e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 436 RPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV-----------------HGRIAYVSQQP--WVFSGTVRSNILFG 496
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeikpvRKKVGVVFQFPesQLFEETVLKDVAFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 497 KK---YEKERYEKV----IKACALKKdlQLLEDGDLTvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK13643 110 PQnfgIPKEKAEKIaaekLEMVGLAD--EFWEKSPFE--------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 570 GKHLFQLciCQALHE--KITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSgVDF 627
Cdd:PRK13643 180 RIEMMQL--FESIHQsgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE-VDF 237
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
714-817 |
6.29e-09 |
|
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: 58.04 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 714 IIFLVLLNMVGQVFYVLQDWWLSHWANKqgalnntrNANGNITETLDLSWYLGIYAGLTAVTVLFGIARSLLVFYILVNA 793
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDV--------LLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERL 72
|
90 100
....*....|....*....|....
gi 568987674 794 SQTLHNRMFESILKAPVLFFDRNP 817
Cdd:pfam00664 73 SRRLRRKLFKKILRQPMSFFDTNS 96
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
424-566 |
7.12e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 7.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------RIAYvsQQPWVFSG---------T 488
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTY--QKQLCFVGhrsginpylT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 489 VRSNILFGKKYEKERYEkVIKACALKKDLQLLedgDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-ITELCRLFSLEHLI---DYPC-----GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
438-610 |
7.18e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASG--------LVSVHGRIAYVSQQ----PWvfsGTVRSNILFGKKYE-KERY 504
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtapLAEAREDTRLMFQDarllPW---KKVIDNVGLGLKGQwRDAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 505 EKVIKACALkkdlqlledgdltviGDRG----ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQ 580
Cdd:PRK11247 115 LQALAAVGL---------------ADRAnewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESL 179
|
170 180 190
....*....|....*....|....*....|..
gi 568987674 581 ALHEKITI-LVTHQLQYLKA-ASHILILKDGE 610
Cdd:PRK11247 180 WQQHGFTVlLVTHDVSEAVAmADRVLLIEEGK 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
428-619 |
8.78e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.55 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR---------------IAYVSQQP--WVFSGTVR 490
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklresVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 491 SNILFG----KKYEKERYEKVIKACAlKKDLQLLEDGDLtvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13636 102 QDVSFGavnlKLPEDEVRKRVDNALK-RTGIEHLKDKPT-------HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 567 AEVGKHLFQLCICQALHEKITILV-THQLQYLKA-ASHILILKDGEMVQKGTYTE 619
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIaTHDIDIVPLyCDNVFVMKEGRVILQGNPKE 228
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
428-593 |
9.24e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELP--PASGLVSVhgriayvsqqPWVFSGTVRSNI-LFGKKYEKERY 504
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV----------PDNQFGREASLIdAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 505 EKVIKACALkkdlqlledGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD---AEVGKHLFQLcICQA 581
Cdd:COG2401 116 VELLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQK-LARR 185
|
170
....*....|...
gi 568987674 582 LheKIT-ILVTHQ 593
Cdd:COG2401 186 A--GITlVVATHH 196
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
437-618 |
1.05e-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: 55.06 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 437 PGELLAVVGPVGAGKSSLLSAVLgelppasglvsvhgriayvsqqpWVFSGtvRSNILFGKKYEKERYekvIKACAlkkD 516
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG-----------------------LALGG--AQSATRRRSGVKAGC---IVAAV---S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 517 LQLLedgdLTVIGdrgatLSGGQKARVNLARAV----YQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTH 592
Cdd:cd03227 69 AELI----FTRLQ-----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
170 180
....*....|....*....|....*.
gi 568987674 593 QLQYLKAASHILILKdgeMVQKGTYT 618
Cdd:cd03227 140 LPELAELADKLIHIK---KVITGVYK 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
428-613 |
1.13e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQ-PWVFSGTVRSN 492
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAIIYQElHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGK--------KYEKERYEKVIKACALKKDLqlleDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK11288 100 LYLGQlphkggivNRRLLNYEAREQLEHLGVDI----DPDTPL-----KYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568987674 565 VDAEVGKHLFQLcICQALHE-KITILVTHQLQYLKAASH-ILILKDGEMVQ 613
Cdd:PRK11288 171 LSAREIEQLFRV-IRELRAEgRVILYVSHRMEEIFALCDaITVFKDGRYVA 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
426-655 |
1.30e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.87 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 426 PTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR------------IAYVSQQPWVFSG-TVRSN 492
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILF-----GKKYEKERYEkvIKAcalkkdlqLLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:TIGR01257 1024 ILFyaqlkGRSWEEAQLE--MEA--------MLEDTGLHHKRNEEAQdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 567 AEVGKHLFQLcICQALHEKITILVTHQLQYLKA-ASHILILKDGEMVQKGTyTEFLKSGVDFGSLL----KKENEEAEPS 641
Cdd:TIGR01257 1094 PYSRRSIWDL-LLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT-PLFLKNCFGTGFYLtlvrKMKNIQSQRG 1171
|
250
....*....|....
gi 568987674 642 TAPGTPTLRKRTFS 655
Cdd:TIGR01257 1172 GCEGTCSCTSKGFS 1185
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
428-612 |
1.58e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-IAYVSQQPWVFsgtVRSNI--LFGKKY---EK 501
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITRLKNREVPF---LRRQIgmIFQDHHllmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 502 ERYEKV----IKACALKKDLQLLEDGDLTVIG--DRGAT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:PRK10908 95 TVYDNVaiplIIAGASGDDIRRRVSAALDKVGllDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568987674 572 HLFQLcicqaLHE----KITILV-THQLQYLKAASH-ILILKDGEMV 612
Cdd:PRK10908 175 GILRL-----FEEfnrvGVTVLMaTHDIGLISRRSYrMLTLSDGHLH 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
437-612 |
1.87e-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: 53.92 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 437 PGELLAVVGPVGAGKSSLLSAVLGELPPASGlvsvhgriayvsqqpwvfsgtvrsnilfgkkyekeryeKVIKACALKKD 516
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--------------------------------------GVIYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 517 LQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQAL-----HEKITILVT 591
Cdd:smart00382 43 EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILT 122
|
170 180
....*....|....*....|.
gi 568987674 592 HQLQYLKAASHILILKDGEMV 612
Cdd:smart00382 123 TNDEKDLGPALLRRRFDRRIV 143
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
428-616 |
1.95e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.04 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimreaVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 493 ILFGKKY-EKERYEKVIKACAlkkDL--QLLEDGdltviGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWVY---ELfpRLHERR-----IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568987674 570 GKHLFQLcICQALHEKITILVTHQ--LQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK11614 173 IQQIFDT-IEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDT 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
434-566 |
2.24e-08 |
|
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: 57.49 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 434 IARPGELLAVVGPVGAGKSSLLSAVLGELPP------------------------------ASGLVSVHGRIAYVSQQPW 483
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPnlgdydeepswdevlkrfrgtelqdyfkklANGEIKVAHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 484 VFSGTVRSnILfgKKY-EKERYEKVIKACALKKDLqlleDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:COG1245 175 VFKGTVRE-LL--EKVdERGKLDELAEKLGLENIL----DRDIS-------ELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
....
gi 568987674 563 SAVD 566
Cdd:COG1245 241 SYLD 244
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
431-623 |
2.75e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 431 LSFIARPgeLLAVVGPVGAGKSSLLSAVLGELPPASG-------------------LVSVHGRIAYVSQQPWVFSGTVRS 491
Cdd:PRK14271 42 MGFPARA--VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyrdVLEFRRRVGMLFQRPNPFPMSIMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILFGKKYEKERYEKVIKACALKKdlqLLEDGDLTVIGDRGAT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PRK14271 120 NVLAGVRAHKLVPRKEFRGVAQAR---LTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 568 EVGKHLFQLciCQALHEKIT-ILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK14271 197 TTTEKIEEF--IRSLADRLTvIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
424-566 |
2.98e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA-SGLVSVHGR--------------IAYVSQQ---PWVF 485
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRrrgsgetiwdikkhIGYVSSSlhlDYRV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 486 SGTVRSNILFGKKYEKERYEKVIKAcalkkdLQLLEDGDLTVIGDRGAT-------LSGGQKARVNLARAVYQDADIYLL 558
Cdd:PRK10938 352 STSVRNVILSGFFDSIGIYQAVSDR------QQKLAQQWLDILGIDKRTadapfhsLSWGQQRLALIVRALVKHPTLLIL 425
|
....*...
gi 568987674 559 DDPLSAVD 566
Cdd:PRK10938 426 DEPLQGLD 433
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
421-612 |
3.28e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELP-----------------------PASGLVSVHGRIAY 477
Cdd:TIGR02633 15 KALD-----GIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiywsgsplkasnirdtERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 478 VSQQpwvfsgTVRSNILFGK----KYEKERYEKVIKAC-ALKKDLQLLEDGDLTVIGDRGatlsGGQKARVNLARAVYQD 552
Cdd:TIGR02633 90 VPEL------SVAENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 553 ADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQLQYLKAASH-ILILKDGEMV 612
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDtICVIRDGQHV 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
394-611 |
3.74e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 394 ELPQR---KAHVPsdGKAIVHVQDFTAfwdkaLDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVS 470
Cdd:PRK10982 234 SLTQRfpdKENKP--GEVILEVRNLTS-----LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTIT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 471 VHGR--------------IAYVSQQ----------PWVFSGTVrSNIlfgKKYeKERYeKVIKACALKKDLQLLED---- 522
Cdd:PRK10982 307 LHGKkinnhnaneainhgFALVTEErrstgiyaylDIGFNSLI-SNI---RNY-KNKV-GLLDNSRMKSDTQWVIDsmrv 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 523 ---GDLTVIGdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQL-QYLK 598
Cdd:PRK10982 381 ktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLG 456
|
250
....*....|...
gi 568987674 599 AASHILILKDGEM 611
Cdd:PRK10982 457 ITDRILVMSNGLV 469
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
438-619 |
3.79e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.54 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASG----------------LVSVHGRIAYVSQQPWVFSG-TVRSNILFGKKYE 500
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGeilfdgenipamsrsrLYTVRKRMSMLFQSGALFTDmNVFDNVAYPLREH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 501 KERYEKVIKACALKKdlqlledgdLTVIGDRGAT------LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 574
Cdd:PRK11831 113 TQLPAPLLHSTVMMK---------LEAVGLRGAAklmpseLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568987674 575 QLcICQALHE-KIT-ILVTHQL-QYLKAASHILILKDGEMVQKGTYTE 619
Cdd:PRK11831 184 KL-ISELNSAlGVTcVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQA 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
434-566 |
4.29e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 434 IARPGELLAVVGPVGAGKSSLLSAVLGELPP------------------------------ASGLVSVHGRIAYVSQQPW 483
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdyeeepswdevlkrfrgtelqnyfkklYNGEIKVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 484 VFSGTVRSniLFGKKYEKERYEKVIKACALKKDLqlleDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:PRK13409 175 VFKGKVRE--LLKKVDERGKLDEVVERLGLENIL----DRDIS-------ELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
...
gi 568987674 564 AVD 566
Cdd:PRK13409 242 YLD 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
421-612 |
4.47e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDsptlqGLSFIARPGELLAVVGPVGAGKSSL---LSAVL------GEL--------------PPASGLVSVHGRIAY 477
Cdd:PRK13549 19 KALD-----NVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYphgtyeGEIifegeelqasnirdTERAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 478 VSQQpwvfsgTVRSNILFGKKYEKE---RYEKVIKAC-ALKKDLQLLEDGDLTViGDrgatLSGGQKARVNLARAVYQDA 553
Cdd:PRK13549 94 VKEL------SVLENIFLGNEITPGgimDYDAMYLRAqKLLAQLKLDINPATPV-GN----LGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 554 DIYLLDDPLSAVDAEVGKHLFQLcICQALHEKIT-ILVTHQLQYLKAAS-HILILKDGEMV 612
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDI-IRDLKAHGIAcIYISHKLNEVKAISdTICVIRDGRHI 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
428-611 |
4.63e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------RIAYVSQQ-PWVFSG-------TV 489
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeeaRAKLRAKHvGFVFQSfmliptlNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 490 RSNI-----LFGkkyEKERYEKViKACALKKDLQLledgdltviGDR----GATLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK10584 106 LENVelpalLRG---ESSRQSRN-GAKALLEQLGL---------GKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 561 PLSAVDAEVGKH----LFQLcicQALHEKITILVTHQLQYLKAASHILILKDGEM 611
Cdd:PRK10584 173 PTGNLDRQTGDKiadlLFSL---NREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
418-619 |
5.66e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.48 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 418 FWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-IAYVSQQPWVfsgTVRSNI--- 493
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWR---AVRSDIqmi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 -----------------------LFGKKYEKERYEKVIKACALKkdLQLLEDgdltVIGDRGATLSGGQKARVNLARAVY 550
Cdd:PRK15079 104 fqdplaslnprmtigeiiaeplrTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 551 QDADIYLLDDPLSAVDAEVGKHLFQLciCQALHEKI---TILVTHQLQYLKAAS-HILILKDGEMVQKGTYTE 619
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNL--LQQLQREMglsLIFIAHDLAVVKHISdRVLVMYLGHAVELGTYDE 248
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
424-619 |
9.25e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAV--LGELPP---ASGLVSVHG-------------RIAYVSQQP-WV 484
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPearVSGEVYLDGqdifkmdvielrrRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 485 FSGTVRSNILFGKKY------EKERYEKVIKAcaLKKdLQLLEDgdltvIGDR----GATLSGGQKARVNLARAVYQDAD 554
Cdd:PRK14247 95 PNLSIFENVALGLKLnrlvksKKELQERVRWA--LEK-AQLWDE-----VKDRldapAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 555 IYLLDDPLSAVDAEVGKHLFQLCIcqALHEKITI-LVTH-QLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFL--ELKKDMTIvLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
406-561 |
1.79e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 406 GKAIVHVQDFT-AFWDKALdsptLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVhG---RIAYVSQQ 481
Cdd:PRK11819 321 GDKVIEAENLSkSFGDRLL----IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GetvKLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 482 pwvfsgtvRSNIlfgkKYEKERYEKVikacalkkdlqllEDG-DLTVIGDR--------------GA-------TLSGGQ 539
Cdd:PRK11819 396 --------RDAL----DPNKTVWEEI-------------SGGlDIIKVGNReipsrayvgrfnfkGGdqqkkvgVLSGGE 450
|
170 180
....*....|....*....|..
gi 568987674 540 KARVNLARAVYQDADIYLLDDP 561
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEP 472
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
416-615 |
2.14e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.09 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 416 TAFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPAS---------------GLVSVHGRIAYVSQ 480
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKgavlwqgkpldyskrGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 481 QP--WVFSGTVRSNILFGKK----YEKERYEKVIKACALkKDLQLLEDGDLTVigdrgatLSGGQKARVNLARAVYQDAD 554
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRnlgvPEAEITRRVDEALTL-VDAQHFRHQPIQC-------LSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 555 IYLLDDPLSAVDAEVGKHLFQL---CICQALHekiTILVTHQLQYLKAASH-ILILKDGEMVQKG 615
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIirrIVAQGNH---VIISSHDIDLIYEISDaVYVLRQGQILTHG 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
431-621 |
2.87e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 431 LSFIarPGELLAVVGPVGAGKSSLLS--AVL-----GELPPASGLvsvhgRIAYVSQQPWV-FSGTVRSNILFG---KKY 499
Cdd:PRK11819 28 LSFF--PGAKIGVLGLNGAGKSTLLRimAGVdkefeGEARPAPGI-----KVGYLPQEPQLdPEKTVRENVEEGvaeVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 500 EKERYEKV------------------------IKAC-ALKKDLQL--------LEDGDLTVigdrgATLSGGQKARVNLA 546
Cdd:PRK11819 101 ALDRFNEIyaayaepdadfdalaaeqgelqeiIDAAdAWDLDSQLeiamdalrCPPWDAKV-----TKLSGGERRRVALC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 547 RAVYQDADIYLLDDPLSAVDAE----VGKHL--FQLCIcqalhekitILVTHQLQYL-KAASHILILKDGEMVQ-KGTYT 618
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAEsvawLEQFLhdYPGTV---------VAVTHDRYFLdNVAGWILELDRGRGIPwEGNYS 246
|
...
gi 568987674 619 EFL 621
Cdd:PRK11819 247 SWL 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
428-632 |
6.24e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.61 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR-IAYVSQQPW-VFSGTVRsnILF----GKKYEK 501
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEpLAKLNRAQRkAFRRDIQ--MVFqdsiSAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 502 ERYEKVI-----------KACALKKDLQLLE--DGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAe 568
Cdd:PRK10419 106 KTVREIIreplrhllsldKAERLARASEMLRavDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL- 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 569 vgkhLFQLCICQ---ALHEKITI---LVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLK 632
Cdd:PRK10419 185 ----VLQAGVIRllkKLQQQFGTaclFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVLQ 251
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
394-561 |
6.72e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 394 ELPQRKAHVPSdGKAIVHVQDFTAFWDKALdsPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG 473
Cdd:COG3845 243 LLRVEKAPAEP-GEVVLEVENLSVRDDRGV--PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 474 R--------------IAYVSQQPW----VFSGTVRSNILFGkKYEKERYEK--VIKACALKKD-LQLLEDGDL--TVIGD 530
Cdd:COG3845 320 EditglsprerrrlgVAYIPEDRLgrglVPDMSVAENLILG-RYRRPPFSRggFLDRKAIRAFaEELIEEFDVrtPGPDT 398
|
170 180 190
....*....|....*....|....*....|...
gi 568987674 531 RGATLSGG--QKarVNLARAVYQDADIYLLDDP 561
Cdd:COG3845 399 PARSLSGGnqQK--VILARELSRDPKLLIAAQP 429
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
93-342 |
1.13e-06 |
|
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: 51.26 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGIFTLI-EEGTRVVQPLFLGKIIEYFEKYDPDDSVALHtaygYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMC 171
Cdd:cd18541 1 YLLGILFLIlVDLLQLLIPRIIGRAIDALTAGTLTASQLLR----YALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIF--LHFLWAGPLQAIAVTVLLWVEIGISCLAglavlVILLP 249
Cdd:cd18541 77 NDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPgiLYLVDALFLGVLVLVMMFTISPKLTLIA-----LLPLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 250 LQSCIGKLFSSL---RSKTA--AFTDarirtMN----EVITGMRIIKMYAWE----KSFADLIANLRKKEIS-------- 308
Cdd:cd18541 152 LLALLVYRLGKKihkRFRKVqeAFSD-----LSdrvqESFSGIRVIKAFVQEeaeiERFDKLNEEYVEKNLRlarvdalf 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568987674 309 -----KILGSSYLRGMNMASFFIANKVIL---FVTFTSYVLL 342
Cdd:cd18541 227 fpligLLIGLSFLIVLWYGGRLVIRGTITlgdLVAFNSYLGM 268
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
405-613 |
1.93e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 405 DGKAIVHVQDFTAFwdkalDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR---------- 474
Cdd:PRK09700 261 AHETVFEVRNVTSR-----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsplda 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 475 ----IAYVSQ---QPWVFSG-TVRSNILFGKKYEKERYEKVIKACALKKDLQLLED--GDLTV----IGDRGATLSGGQK 540
Cdd:PRK09700 336 vkkgMAYITEsrrDNGFFPNfSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqrELLALkchsVNQNITELSGGNQ 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 541 ARVNLARAVYQDADIYLLDDPLSAVD----AEVGKHLFQLcicqALHEKITILVTHQL-QYLKAASHILILKDGEMVQ 613
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQL----ADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
421-612 |
2.05e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDSPTLQglsfiARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQ-PWVF 485
Cdd:PRK10982 12 KALDNVNLK-----VRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQElNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 486 SGTVRSNILFGkkyekeRYEK----VIKACALKKDLQLLEDGDLTV-IGDRGATLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK10982 87 QRSVMDNMWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIDIdPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 561 PLSAVDAEVGKHLFQlcICQALHEK--ITILVTHQL-QYLKAASHILILKDGEMV 612
Cdd:PRK10982 161 PTSSLTEKEVNHLFT--IIRKLKERgcGIVYISHKMeEIFQLCDEITILRDGQWI 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
423-616 |
2.20e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.13 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 423 LDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-----------------RIAYVSQQP--W 483
Cdd:PRK13649 18 FEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdikqirkKVGLVFQFPesQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 484 VFSGTVRSNILFGKK---YEKERYEKVikacALKKdlqlledgdLTVIG------DRGA-TLSGGQKARVNLARAVYQDA 553
Cdd:PRK13649 98 LFEETVLKDVAFGPQnfgVSQEEAEAL----AREK---------LALVGiseslfEKNPfELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 554 DIYLLDDPLSAVDAEVGKHLFQLciCQALHEK-ITI-LVTHQLQYL-KAASHILILKDGEMVQKGT 616
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTL--FKKLHQSgMTIvLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
428-615 |
4.70e-06 |
|
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: 48.29 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGElppaSGLVSVHGRIAYVSQqpwvfsgtvrsNILFGKKYEKER---- 503
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----PKYEVTEGEILFKGE-----------DITDLPPEERARlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 504 ----YEKVIKACALKKDLQLLEDGdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlcIC 579
Cdd:cd03217 81 lafqYPPEIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE--VI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568987674 580 QALHEKIT--ILVTHQ---LQYLKaASHILILKDGEMVQKG 615
Cdd:cd03217 148 NKLREEGKsvLIITHYqrlLDYIK-PDRVHVLYDGRIVKSG 187
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
701-814 |
6.47e-06 |
|
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: 49.03 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 701 YKNYFSAGASWFFIIFLVLLNMVGQVFYVLQDWWL---SHWANKQGALNNTRNANGNITETLDLSWYLGIYAGLTAVTVL 777
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLlrsQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVADSLLA 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 568987674 778 FGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFD 814
Cdd:cd18600 86 MGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFN 122
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
442-610 |
6.54e-06 |
|
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: 47.60 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 442 AVVGPVGAGKSSLLSAVL----GELPPASGLVSVHGRIAyvsqqpwvFSGTVRSNI------LFGKKYEKERYEKVIKAC 511
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLI--------REGEVRAQVklafenANGKKYTITRSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 512 AlkkdlqLLEDGDLTVIGDRG-ATLSGGQKA------RVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfqlcICQALHE 584
Cdd:cd03240 98 I------FCHQGESNWPLLDMrGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN--------IEESLAE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 568987674 585 KIT----------ILVTHQLQYLKAASHIL-ILKDGE 610
Cdd:cd03240 164 IIEerksqknfqlIVITHDEELVDAADHIYrVEKDGR 200
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
191-612 |
7.27e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.41 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 191 TGQIVNLLSNDVnkfDQVTIFLHFLwAGPLQAIAVTV-----LLWVEIGIsCLAGLAVLVILLPL-QSCIGKLFSSLRsK 264
Cdd:COG4615 104 AARLLAALTEDV---RTISQAFVRL-PELLQSVALVLgclayLAWLSPPL-FLLTLVLLGLGVAGyRLLVRRARRHLR-R 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 265 TAAFTDARIRTMNEVITGMRIIKMYAwEKSFA----DLIANLRKKEISKILG-SSYLRGMNMAS--FFIANKVILFVtFT 337
Cdd:COG4615 178 AREAEDRLFKHFRALLEGFKELKLNR-RRRRAffdeDLQPTAERYRDLRIRAdTIFALANNWGNllFFALIGLILFL-LP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 338 SYVLLGNEITASHVFVAMTLYGAVrLTVTLFFPSAIErgseAIVSIRRIKNfllLDELPQRKAHVPSDGKAIVHVQDFT- 416
Cdd:COG4615 256 ALGWADPAVLSGFVLVLLFLRGPL-SQLVGALPTLSR----ANVALRKIEE---LELALAAAEPAAADAAAPPAPADFQt 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 417 --------AFWDKALDSP-TLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-------RIAYVSQ 480
Cdd:COG4615 328 lelrgvtyRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpvtadnREAYRQL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 481 qpwvFSgTVRSNI-LFGKKYEKERYEKVIKACALKKDLQLleDGDLTVIGDRGAT--LSGGQKARVNLARAVYQDADIYL 557
Cdd:COG4615 408 ----FS-AVFSDFhLFDRLLGLDGEADPARARELLERLEL--DHKVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPILV 480
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 558 LD------DPlsavdaeVGKHLFQLCICQALHE--KITILVTHQLQYLKAASHILILKDGEMV 612
Cdd:COG4615 481 FDewaadqDP-------EFRRVFYTELLPELKArgKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
424-615 |
8.58e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPasGLVSVHGRIAY--VSQQPWVFSGTVRSNIL------F 495
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLdgKPVAPCALRGRKIATIMqnprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 496 G-----KKYEKERYEKVIKACALKKDLQLLEDGDLtviGDRGATL-------SGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:PRK10418 93 NplhtmHTHARETCLALGKPADDATLTAALEAVGL---ENAARVLklypfemSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 564 AVDAEVGKHLFQLCicqalhEKIT-------ILVTHQLQYL-KAASHILILKDGEMVQKG 615
Cdd:PRK10418 170 DLDVVAQARILDLL------ESIVqkralgmLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
438-622 |
1.07e-05 |
|
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: 46.80 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-RIAYVSQQpwvfsgtvrsnilfgkkyekeryekvikacalkkd 516
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY----------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 517 lqlledgdltvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVT-HQLQ 595
Cdd:cd03222 70 ----------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVeHDLA 133
|
170 180
....*....|....*....|....*..
gi 568987674 596 YLKAASHILILKDGEmvqKGTYTEFLK 622
Cdd:cd03222 134 VLDYLSDRIHVFEGE---PGVYGIASQ 157
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
164-386 |
1.28e-05 |
|
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: 47.80 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 164 MRLRVAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIA-VTVLLWVEIGISCLAGL 241
Cdd:cd18552 72 RDLRNDL----FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGlLGVLFYLDWKLTLIALV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 242 AVLVILLPLQScIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKS----FADLIANLRKKEISKILGSSYLR 317
Cdd:cd18552 148 VLPLAALPIRR-IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSS 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568987674 318 GMN--MASFFIAnkVILFvtFTSYVLLGNEITASHvFVA-----MTLYGAVRLTVTLFfpSAIERGseaIVSIRRI 386
Cdd:cd18552 227 PLMelLGAIAIA--LVLW--YGGYQVISGELTPGE-FISfitalLLLYQPIKRLSNVN--ANLQRG---LAAAERI 292
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
428-593 |
1.29e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA---SGLVSVHGR---------IAYVSQQPwVFSG--TVRSNI 493
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNGRpldssfqrsIGYVQQQD-LHLPtsTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFG---------KKYEKERY-EKVIKacalkkdlqLLEDGDL--TVIGDRGATLSGGQKARVNLA-RAVYQDADIYLLDD 560
Cdd:TIGR00956 858 RFSaylrqpksvSKSEKMEYvEEVIK---------LLEMESYadAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDE 928
|
170 180 190
....*....|....*....|....*....|....
gi 568987674 561 PLSAVDAEVGKHLFQLCICQALHEKiTILVT-HQ 593
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQ-AILCTiHQ 961
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
93-310 |
1.45e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 47.86 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGI-FTLIEEGTRVVQPLFLGKIIeyfekydpDDSVALHTAYG---YAAVLsmctLILAILHHLYFY----------- 157
Cdd:cd18543 1 LILALlAALLATLAGLAIPLLTRRAI--------DGPIAHGDRSAlwpLVLLL----LALGVAEAVLSFlrrylagrlsl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 158 HVQcAGMRLRvamchmIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIAVTVLLWVeigISC 237
Cdd:cd18543 69 GVE-HDLRTD------LFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLV---LSP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 238 LAGLAVLVILLPLqscigkLFSSLRSKTAAFTDARI---------RTMNEVITGMRIIKMYAWEKS----FADLIANLRK 304
Cdd:cd18543 139 PLALVALASLPPL------VLVARRFRRRYFPASRRaqdqagdlaTVVEESVTGIRVVKAFGRERReldrFEAAARRLRA 212
|
....*.
gi 568987674 305 KEISKI 310
Cdd:cd18543 213 TRLRAA 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
421-612 |
1.46e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDSPTL-QGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG-RIAYVSQQPWVFSG----------- 487
Cdd:PRK11288 261 DGLKGPGLrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkae 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 ------TVRSNI-------------LFGKKYEKERYEKVIKACALKKdlqllEDGDlTVIGdrgaTLSGGQKARVNLARA 548
Cdd:PRK11288 341 giipvhSVADNInisarrhhlragcLINNRWEAENADRFIRSLNIKT-----PSRE-QLIM----NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568987674 549 VYQDADIYLLDDPLSAVDaeVG-KHLfqlcICQALHE----KITIL-VTHQL-QYLKAASHILILKDGEMV 612
Cdd:PRK11288 411 LSEDMKVILLDEPTRGID--VGaKHE----IYNVIYElaaqGVAVLfVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
421-569 |
1.49e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG----------------RIAYVSQQPWV 484
Cdd:PRK11308 29 KALD-----GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllkadpeaqkllrqKIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 485 fSGTVRSNIlfGKKYE-----------KERYEKVikacalkkdLQLLEDGDL-TVIGDRGATL-SGGQKARVNLARAVYQ 551
Cdd:PRK11308 104 -SLNPRKKV--GQILEepllintslsaAERREKA---------LAMMAKVGLrPEHYDRYPHMfSGGQRQRIAIARALML 171
|
170
....*....|....*...
gi 568987674 552 DADIYLLDDPLSAVDAEV 569
Cdd:PRK11308 172 DPDVVVADEPVSALDVSV 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
421-609 |
1.68e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--------------IAYVSQQP---- 482
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISEDRkrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 483 WVFSGTVRSNI------LFGKKY-------EKERYEKVIKACALK---KDLQlledgdltvIGdrgaTLSGGQKARVNLA 546
Cdd:PRK10762 341 LVLGMSVKENMsltalrYFSRAGgslkhadEQQAVSDFIRLFNIKtpsMEQA---------IG----LLSGGNQQKVAIA 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 547 RAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQALHEKITI-LVTHQL-QYLKAASHILILKDG 609
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQL-INQFKAEGLSIiLVSSEMpEVLGMSDRILVMHEG 471
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
417-623 |
2.10e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 417 AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVS-------------------------- 470
Cdd:PRK10261 21 AFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvielseqsaaqmrh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 471 VHGR-IAYVSQQPW-----VFsgTVRSNILFGKKYEK--ERYEKVIKAcalKKDLQLLEDGDLTVIGDR-GATLSGGQKA 541
Cdd:PRK10261 101 VRGAdMAMIFQEPMtslnpVF--TVGEQIAESIRLHQgaSREEAMVEA---KRMLDQVRIPEAQTILSRyPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 542 RVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLC-ICQALHEKITILVTHQLQYL-KAASHILILKDGEMVQKGTYTE 619
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQ 255
|
....
gi 568987674 620 FLKS 623
Cdd:PRK10261 256 IFHA 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
421-621 |
2.10e-05 |
|
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: 47.87 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 421 KALDsptlqGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV----------------HGR----IAYVSQ 480
Cdd:TIGR03269 298 KAVD-----NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRakryIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 481 QPWVFS-GTVRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:TIGR03269 373 EYDLYPhRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 560 DPLSAVDAeVGKHLFQLCICQALHE--KITILVTHQLQY-LKAASHILILKDGEMVQKGTYTEFL 621
Cdd:TIGR03269 453 EPTGTMDP-ITKVDVTHSILKAREEmeQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
394-611 |
2.45e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 394 ELPQRKaHVPSDGKAIVHVQDFTA--FWDkaldsptlqgLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSV 471
Cdd:PRK15439 254 ELPGNR-RQQAAGAPVLTVEDLTGegFRN----------ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIML 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 472 HGR--------------IAYVS---QQP---------W-VFSGTVRSNILFGK-KYEKERYEKVIKACALKkdlqlLEDG 523
Cdd:PRK15439 323 NGKeinalstaqrlargLVYLPedrQSSglyldaplaWnVCALTHNRRGFWIKpARENAVLERYRRALNIK-----FNHA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 524 DLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILVTHQL-QYLKAASH 602
Cdd:PRK15439 398 EQAA-----RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLeEIEQMADR 472
|
....*....
gi 568987674 603 ILILKDGEM 611
Cdd:PRK15439 473 VLVMHQGEI 481
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
93-334 |
2.67e-05 |
|
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: 47.01 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILG-IFTLIEEGTRVVQPLFLGKIIEYFEKYDpDDSVALHTAyGYAAVLSMCTLILAILHHLYFYHV-QCAGMRLRvam 170
Cdd:cd18548 1 AILApLFKLLEVLLELLLPTLMADIIDEGIANG-DLSYILRTG-LLMLLLALLGLIAGILAGYFAAKAsQGFGRDLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 171 cHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIAVTVLLwveIGISclAGLA-VLVILL 248
Cdd:cd18548 76 -KDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNfVMMLLRMLVRAPIMLIGAIIMA---FRIN--PKLAlILLVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 249 PLQSCI--------GKLFSSLRSKtaafTDARIRTMNEVITGMRIIKMYAWE----KSFADLIANLRKKEIS--KILGSs 314
Cdd:cd18548 150 PILALVvflimkkaIPLFKKVQKK----LDRLNRVVRENLTGIRVIRAFNREdyeeERFDKANDDLTDTSLKagRLMAL- 224
|
250 260
....*....|....*....|
gi 568987674 315 ylrgMNMASFFIANKVILFV 334
Cdd:cd18548 225 ----LNPLMMLIMNLAIVAI 240
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
428-612 |
2.99e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 45.70 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSaVL---GELPPASGLVSVHGR---------IAYVSQQPwVFSG--TVRSNI 493
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLD-VLagrKTAGVITGEILINGRpldknfqrsTGYVEQQD-VHSPnlTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 494 LFgkkyekeryekvikACALkkdlqlledgdltvigdRGatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGkhl 573
Cdd:cd03232 101 RF--------------SALL-----------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA--- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568987674 574 fqLCICQALhEKI-----TILVT-HQ--LQYLKAASHILILK-DGEMV 612
Cdd:cd03232 145 --YNIVRFL-KKLadsgqAILCTiHQpsASIFEKFDRLLLLKrGGKTV 189
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
93-389 |
3.03e-05 |
|
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: 46.73 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDSvaLHTAYGYAAVLSMCTLILAILHHLYFYHvqcagMRLRVAmcH 172
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSS--GYYLGVYAALLVLASVLLVLLRWLLFVL-----AGLRAS--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 173 MIYRKALR-LSNSAMG---KTTTGQIVNLLSNDVNKFDQV--TIFLHFLWAGpLQAIAVTVLlwveIGISCLAGLAVLVI 246
Cdd:cd18580 73 RLHDKLLRsVLRAPMSffdTTPSGRILNRFSKDIGLIDEElpLALLDFLQSL-FSVLGSLIV----IAIVSPYFLIVLPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 247 LLPLQSCIGKLFSS----LR-----SKTAAFTdarirTMNEVITGMRIIKMYAWEKSFADLiaNLRKKEISkiLGSSYLr 317
Cdd:cd18580 148 LLVVYYLLQRYYLRtsrqLRrleseSRSPLYS-----HFSETLSGLSTIRAFGWQERFIEE--NLRLLDAS--QRAFYL- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 318 gMNMASF-------FIANKVILFVTFTSyVLLGNEITASHVFVAMTLygAVRLTVTLFFpsAIERGSE---AIVSIRRIK 387
Cdd:cd18580 218 -LLAVQRwlglrldLLGALLALVVALLA-VLLRSSISAGLVGLALTY--ALSLTGSLQW--LVRQWTEletSMVSVERIL 291
|
..
gi 568987674 388 NF 389
Cdd:cd18580 292 EY 293
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
93-342 |
3.65e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 46.38 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGIF-TLIEEGTRVVQPLFLGKIIEYFEkydpDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMC 171
Cdd:cd18778 1 LILTLLcALLSTLLGLVPPWLIRELVDLVT----IGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVtiFLHflwAGP------LQAIAVTVLLwveIGISCLagLAVLV 245
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERL--IAD---GIPqgitnvLTLVGVAIIL---FSINPK--LALLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 246 IL-LPLQSCIGKLFsslrSKTA--AFTDARIRT--MNEV----ITGMRIIKMYAWEKSFADlianlRKKEISKILGSSYL 316
Cdd:cd18778 147 LIpIPFLALGAWLY----SKKVrpRYRKVREALgeLNALlqdnLSGIREIQAFGREEEEAK-----RFEALSRRYRKAQL 217
|
250 260
....*....|....*....|....*.
gi 568987674 317 RGMNMASFFiaNKVILFVTFTSYVLL 342
Cdd:cd18778 218 RAMKLWAIF--HPLMEFLTSLGTVLV 241
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
93-369 |
4.82e-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: 45.92 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGIFTLIEEGTRVVQPLFLGKIIEyfeKYDPD-DSVALHTaygYAAVLSMCTLILAILHHLYFYHVQCAGMRLRVAMC 171
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAID---EYIPNgDLSGLLI---IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNK----FDQ--VTIFLHFLwagPLQAIAVTVLLW-VEIGISCLAGLAVL 244
Cdd:cd18545 77 QDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSlsdlLSNglINLIPDLL---TLVGIVIIMFSLnVRLALVTLAVLPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 245 VILL-PLQSCIGKLFSSLRSKTAAFTDArirtMNEVITGMRIIKMYAWEK----SFADLIANLRKkeiskilgsSYLRGM 319
Cdd:cd18545 154 VLVVfLLRRRARKAWQRVRKKISNLNAY----LHESISGIRVIQSFAREDeneeIFDELNRENRK---------ANMRAV 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 320 NMASFF---------IANKVILFvtFTSYVLLGNEITAShVFVAMTLYgavrltVTLFF 369
Cdd:cd18545 221 RLNALFwplvelisaLGTALVYW--YGGKLVLGGAITVG-VLVAFIGY------VGRFW 270
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
428-637 |
6.90e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRIAYVSqqpwVFSG-----TVRSNILFgKKYEKE 502
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIA----ISAGlsgqlTGIENIEF-KMLCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 503 RYEKVIKACaLKKDLQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSavdaeVGKHLF-QLCIcQA 581
Cdd:PRK13546 115 FKRKEIKAM-TPKIIEFSELGEF--IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS-----VGDQTFaQKCL-DK 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 582 LHE-----KITILVTHQL-QYLKAASHILILKDGEMVQKG-------TYTEFLKsgvDFGSLLKKENEE 637
Cdd:PRK13546 186 IYEfkeqnKTIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGelddvlpKYEAFLN---DFKKKSKAEQKE 251
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
93-364 |
7.16e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 45.50 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGIF-TLIEEGTRVVQPLFLGKIIeyfekydpDDSVALHTAYGYAAVLSMCTLILAILHHLYFYHVQCAG----MRLR 167
Cdd:cd18551 1 LILALLlSLLGTAASLAQPLLVKNLI--------DALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGervvLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 168 vamcHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQV--TIFLHFLwAGPLQAIAVTVLL----WVEIGISCLAGL 241
Cdd:cd18551 73 ----RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELitSGLPQLV-TGVLTVVGAVVLMflldWVLTLVTLAVVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 242 AVLVILLPLQSCIGKLFSSLRSKTAAFTDArirtMNEVITGMRIIKMYAWEKSFAdlianlrkKEISKILGSSYLRGMNM 321
Cdd:cd18551 148 LAFLIILPLGRRIRKASKRAQDALGELSAA----LERALSAIRTVKASNAEERET--------KRGGEAAERLYRAGLKA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568987674 322 ASFF-IANKVILFVTFTSyvllgneitashvFVAMTLYGAVRLT 364
Cdd:cd18551 216 AKIEaLIGPLMGLAVQLA-------------LLVVLGVGGARVA 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
394-576 |
8.33e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.08 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 394 ELPQRKAHVPSD-GKAIVHVQDFTAfWDKalDSPTLQ---GLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPAS-GL 468
Cdd:PRK13549 243 ELTALYPREPHTiGEVILEVRNLTA-WDP--VNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 469 VSVHGR--------------IAYVS----QQPWVFSGTVRSNIL--------FGKKYEKERYEKVIkacalKKDLQLLE- 521
Cdd:PRK13549 320 IFIDGKpvkirnpqqaiaqgIAMVPedrkRDGIVPVMGVGKNITlaaldrftGGSRIDDAAELKTI-----LESIQRLKv 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 522 ---DGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEVGKHLFQL 576
Cdd:PRK13549 395 ktaSPELAI-----ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYEIYKLINQL 451
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
428-622 |
1.01e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.08 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG------RIAYVSQQPWVFsG---------TVR-S 491
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrRKEFARRIGVVF-GqrsqlwwdlPAIdS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 492 NILFGKKYE--KERYEKVIKACAlkkdlQLLEDGDLTVIGDRgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:COG4586 117 FRLLKAIYRipDAEYKKRLDELV-----ELLDLGELLDTPVR--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 570 gkhlfQLCICQALHE-----KITILVT-HQLQYLKA-ASHILILKDGEMVQKGTYTEFLK 622
Cdd:COG4586 190 -----KEAIREFLKEynrerGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
435-472 |
1.26e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 43.64 E-value: 1.26e-04
10 20 30
....*....|....*....|....*....|....*...
gi 568987674 435 ARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVH 472
Cdd:COG3709 2 SGPGRLIYVVGPSGAGKDSLLAAARARLAADPRLVFAR 39
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
428-493 |
1.28e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 1.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGRI--AY-----------VSQQPWVFSGTVRSNI 493
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREigAYglrelrrqfsmIPQDPVLFDGTVRQNV 1404
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
535-623 |
1.64e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 535 LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKIT-ILVTHQLQYL-KAASHILILKDGEMV 612
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlVLITHDLALVaEAAHKIIVMYAGQVV 233
|
90
....*....|.
gi 568987674 613 QKGTYTEFLKS 623
Cdd:PRK11022 234 ETGKAHDIFRA 244
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
168-356 |
1.86e-04 |
|
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: 44.39 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 168 VAMCHMIYRKALRLSNSAMGK----------TT-TGQIVNLLSNDVNKFD-----QVTIFLHFLwagpLQAIAVTVLL-- 229
Cdd:cd18606 57 LLLAYLGIRASKRLHNKALKRvlrapmsffdTTpLGRILNRFSKDTDVLDnelpdSLRMFLYTL----SSIIGTFILIii 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 230 ---WVEIGISCLAGLAVLVILLPLQSC--IGKLFSSLRSKT-AAFtdarirtmNEVITGMRIIKMYAWEKSFadlIANLR 303
Cdd:cd18606 133 ylpWFAIALPPLLVLYYFIANYYRASSreLKRLESILRSFVyANF--------SESLSGLSTIRAYGAQDRF---IKKNE 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568987674 304 KkeiskilgssYLRGMNMASF--------------FIANKVILFVTFTSyVLLGNEITASHVFVAMT 356
Cdd:cd18606 202 K----------LIDNMNRAYFltianqrwlairldLLGSLLVLIVALLC-VTRRFSISPSSTGLVLS 257
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
92-386 |
1.92e-04 |
|
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: 44.34 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 92 YLILGIFTLIEEGTRVVQPLFLGKIIeyfekydpdDSVALHTAYGYAAVLSMCTLILAILH------HLYFYHV--QCAG 163
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII---------DSVIGGGLRELLWLLALLILGVALLRgvfrylQGYLAEKasQKVA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 164 MRLRVAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVnkfDQVTIFLHFLWAGPLQAI-----AVTVLLW--VEIGIS 236
Cdd:cd18542 72 YDLRNDL----YDHLQRLSFSFHDKARTGDLMSRCTSDV---DTIRRFLAFGLVELVRAVllfigALIIMFSinWKLTLI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 237 CLAGLAVLVIL-LPLQSCIGKLFSSLRSKTAAFTdariRTMNEVITGMRIIKMYAWEKS----FADLIANLRKKEISkil 311
Cdd:cd18542 145 SLAIIPFIALFsYVFFKKVRPAFEEIREQEGELN----TVLQENLTGVRVVKAFAREDYeiekFDKENEEYRDLNIK--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 312 gSSYLRGMNMA-SFFIANKVILFVT-FTSYVLLGNEITAShVFVAMTLYgavrlTVTLFFP--------SAIERgseAIV 381
Cdd:cd18542 218 -LAKLLAKYWPlMDFLSGLQIVLVLwVGGYLVINGEITLG-ELVAFISY-----LWMLIWPvrqlgrliNDMSR---ASA 287
|
....*
gi 568987674 382 SIRRI 386
Cdd:cd18542 288 SAERI 292
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
711-818 |
2.12e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 44.77 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 711 WFFIIFLVLLNMVGQVFYVLQDWWLSHWANkqgALNNTRNANGnitetldLSWYLGIYAGLTAVTVLFGIARSLLVFYIL 790
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLLGRIID---ALLAGGDLSA-------LLLLLLLLLGLALLRALLSYLQRYLLARLA 89
|
90 100
....*....|....*....|....*...
gi 568987674 791 VNASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:COG1132 90 QRVVADLRRDLFEHLLRLPLSFFDRRRT 117
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
422-566 |
3.93e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 422 ALDSPTLQglsfIARpGELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHG--------------RIAYVSQqpwvfsG 487
Cdd:NF033858 16 ALDDVSLD----IPA-GCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrravcpRIAYMPQ------G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 ---------TVRSNI-----LFGKKyEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQD 552
Cdd:NF033858 85 lgknlyptlSVFENLdffgrLFGQD-AAERRRRI---------DELLRATGLAPFADRPAgKLSGGMKQKLGLCCALIHD 154
|
170
....*....|....
gi 568987674 553 ADIYLLDDPLSAVD 566
Cdd:NF033858 155 PDLLILDEPTTGVD 168
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
438-568 |
5.54e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASGLVSVHGR--IAYVSQ-----QPwvfSGTVRSNILFGKKyekeryekvika 510
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKleVAYFDQhraelDP---EKTVMDNLAEGKQ------------ 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 511 calkkdlqlledgDLTVIG----------------DRGAT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:PRK11147 410 -------------EVMVNGrprhvlgylqdflfhpKRAMTpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
424-618 |
9.96e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLG--ELPPASGLVSVHGR--------------IAYVSQQPWVFSG 487
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdllelspedragegIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 488 TvrSNILF-------GKKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK09580 93 V--SNQFFlqtalnaVRSYrGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568987674 560 DPLSAVDAEVGKHLFQLCICQALHEKITILVTHQ---LQYLKaASHILILKDGEMVQKGTYT 618
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDFT 231
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
93-341 |
1.15e-03 |
|
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: 41.62 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGIFTLIEEGTRVVQPLFLGKII-EYFEKYDPDDSVALHTAYGYAAVLSMCTLILAILHHLYFY---HV-QCAGMRLR 167
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIdLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRlmaRVsQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 168 VAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQV--TIFLHFLwAGPLQAIAVTVLLWVeigISCLAGLAVLV 245
Cdd:cd18547 82 KDL----FEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQAlsQSLTQLI-SSILTIVGTLIMMLY---ISPLLTLIVLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 246 ILlPLQSCIGKLFSSlrsKTAAFTDARIRT-------MNEVITGMRIIKMYAWE----KSFADLIANLRKkeiskilgSS 314
Cdd:cd18547 154 TV-PLSLLVTKFIAK---RSQKYFRKQQKAlgelngyIEEMISGQKVVKAFNREeeaiEEFDEINEELYK--------AS 221
|
250 260
....*....|....*....|....*....
gi 568987674 315 YlrgmnMASFF--IANKVILFVTFTSYVL 341
Cdd:cd18547 222 F-----KAQFYsgLLMPIMNFINNLGYVL 245
|
|
| TraA_Ti |
TIGR02768 |
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a ... |
434-567 |
1.37e-03 |
|
Ti-type conjugative transfer relaxase TraA; This protein contains domains distinctive of a single strand exonuclease (N-terminus, MobA/MobL, pfam03389) as well as a helicase domain (central region, homologous to the corresponding region of the F-type relaxase TraI, TIGR02760). This protein likely fills the same role as TraI(F), nicking (at the oriT site) and unwinding the coiled plasmid prior to conjugative transfer.
Pssm-ID: 274289 [Multi-domain] Cd Length: 744 Bit Score: 42.10 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 434 IARPGELLAVVGPVGAGKSSLLSAVlgelppasglvsvhgRIAYVSQqpwvfSGTVRSNILFGKKYEKERYEKVIKA--- 510
Cdd:TIGR02768 364 VTGSGDIAVVVGRAGTGKSTMLKAA---------------REAWEAA-----GYRVIGAALSGKAAEGLQAESGIESrtl 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568987674 511 ----CALKKDLQLLEDGDLTVIGDRGATLSgGQKARVnLARAVYQDADIYLLDDP--LSAVDA 567
Cdd:TIGR02768 424 asleYAWANGRDLLSDKDVLVIDEAGMVGS-RQMARV-LKEAEEAGAKVVLVGDPeqLQPIEA 484
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
93-250 |
1.53e-03 |
|
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: 41.30 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 93 LILGIFTLIEEGTRVVQPLFLGKIIEYFEKYDPDDSVALHTAY---GYAAvLSMCTLILAILHHLYFYHvqcAGMRlrva 169
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYylgIYAL-ISLLSVLLGTLRYLLFFF---GSLR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 170 MCHMIYRkalRLSNSAMG-------KTTTGQIVNLLSNDVNKFDqvtiflhflwagplQAIAVTVLLWVEIGISCLAGLA 242
Cdd:cd18604 74 ASRKLHE---RLLHSVLRaplrwldTTPVGRILNRFSKDIETID--------------SELADSLSSLLESTLSLLVILI 136
|
....*...
gi 568987674 243 VLVILLPL 250
Cdd:cd18604 137 AIVVVSPA 144
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
428-567 |
1.79e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELppASGLVSVHGRIAY-----------------------------V 478
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNT--DGFHIGVEGVITYdgitpeeikkhyrgdvvynaetdvhfphlT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 479 SQQPWVFSGTVRSNILFGKKYEKERYEKVIKACALKK-DLQLLEDgdlTVIGD---RGatLSGGQKARVNLARAVYQDAD 554
Cdd:TIGR00956 155 VGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMATyGLSHTRN---TKVGNdfvRG--VSGGERKRVSIAEASLGGAK 229
|
170
....*....|...
gi 568987674 555 IYLLDDPLSAVDA 567
Cdd:TIGR00956 230 IQCWDNATRGLDS 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
438-611 |
1.93e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 438 GELLAVVGPVGAGKSSLLSAVLGELPPASG-------LVSVHGRIAYVSQQPWVFSGTVrsniLF-------GKKYEKER 503
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGeilldgkPVTAEQPEDYRKLFSAVFTDFH----LFdqllgpeGKPANPAL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 504 YEKVIKACALKKDLQLlEDGDLTVIgdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQALH 583
Cdd:PRK10522 425 VEKWLERLKMAHKLEL-EDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQE 498
|
170 180
....*....|....*....|....*....
gi 568987674 584 EKITIL-VTHQLQYLKAASHILILKDGEM 611
Cdd:PRK10522 499 MGKTIFaISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
424-650 |
2.03e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 424 DSPTLQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPASG-LVSVHGRIAYVS---QQPWV--------------- 484
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGeRQSQFSHITRLSfeqLQKLVsdewqrnntdmlspg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 485 ---FSGTVRSNILFGKKyEKERYEKVIKACALKKdlqLLEdgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:PRK10938 95 eddTGRTTAEIIQDEVK-DPARCEQLAQQFGITA---LLD--------RRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 562 LSAVDAEVGKHLFQLcICQALHEKITI-LVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKSGVdFGSLLKKENEEAE 639
Cdd:PRK10938 163 FDGLDVASRQQLAEL-LASLHQSGITLvLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQAL-VAQLAHSEQLEGV 240
|
250
....*....|.
gi 568987674 640 PSTAPGTPTLR 650
Cdd:PRK10938 241 QLPEPDEPSAR 251
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
761-818 |
2.30e-03 |
|
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: 40.83 E-value: 2.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 568987674 761 LSWYLGIYAGLTAVTVLFGIARSLLVFYILVNASQTLHNRMFESILKAPVLFFDRNPI 818
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPV 97
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
405-477 |
3.20e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.82 E-value: 3.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568987674 405 DGKAIVHVQDFT-AFWDKALDSPTLQGLSFIARPGELLAVVGPVGAGKS-SLLSaVLGELPPasGLVSVHGRIAY 477
Cdd:COG4172 2 MSMPLLSVEDLSvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRLLPD--PAAHPSGSILF 73
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
164-358 |
5.00e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 39.80 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 164 MRLRVAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVnkfDQVTIFLHFLwagpLQAIAVTVLLWVEIGISCL---AG 240
Cdd:cd18563 76 ADLRRDL----YEHLQRLSLSFFDKRQTGSLMSRVTSDT---DRLQDFLSDG----LPDFLTNILMIIGIGVVLFslnWK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 241 LAVLVIL-LPLQSCIGKLFS-SLRSKTAAFTDARIR---TMNEVITGMRIIKMYAWEKS----FADLIANLRkkEISKIL 311
Cdd:cd18563 145 LALLVLIpVPLVVWGSYFFWkKIRRLFHRQWRRWSRlnsVLNDTLPGIRVVKAFGQEKReikrFDEANQELL--DANIRA 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568987674 312 GSSYLRGMNMASFFIANKVILFVTFTSYVLLGNEITAShVFVAMTLY 358
Cdd:cd18563 223 EKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLSY 268
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
90-347 |
5.54e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 39.50 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 90 KSYLILGIFTLIEEGTRVVQPLFLGKIIEyfeKYDPDDSVALHTAYGyaAVLSMCTLILAILHHLYFYHVQCAGMRLRVA 169
Cdd:cd18782 2 RALIEVLALSFVVQLLGLANPLLFQVIID---KVLVQQDLATLYVIG--VVMLVAALLEAVLTALRTYLFTDTANRIDLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 170 MCHMIYRKALRLSNSAMGKTTTGQIVNLLSnDVNKFDQ------VTIFLHFLWAgplqAIAVTVLLWveigISCLAGLAV 243
Cdd:cd18782 77 LGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGfltgtaLTTLLDVLFS----VIYIAVLFS----YSPLLTLVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 244 LvILLPLQSCIGKLFS-SLRSKTAAFTDARIRT---MNEVITGMRIIK--------MYAWEKSFADLIANLRKKEISKIL 311
Cdd:cd18782 148 L-ATVPLQLLLTFLFGpILRRQIRRRAEASAKTqsyLVESLTGIQTVKaqnaelkaRWRWQNRYARSLGEGFKLTVLGTT 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 568987674 312 GSSYLRGMNMASffiankVILFVTFTSYVLLGNEIT 347
Cdd:cd18782 227 SGSLSQFLNKLS------SLLVLWVGAYLVLRGELT 256
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
442-601 |
5.54e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 442 AVVGPVGAGKSSLLSA---VLGE----LPPASGLVSVHGRIayvsqQPWVFSGTVRsnILFGKKYekeryekvikacalk 514
Cdd:cd03239 26 AIVGPNGSGKSNIVDAicfVLGGkaakLRRGSLLFLAGGGV-----KAGINSASVE--ITFDKSY--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 515 kdlQLLEDGDLTVIgdrgatLSGGQKARVNLARAV----YQDADIYLLDDPLSAVDAEVGKHLFQLCICQALHEKITILV 590
Cdd:cd03239 84 ---FLVLQGKVEQI------LSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVI 154
|
170
....*....|.
gi 568987674 591 THQLQYLKAAS 601
Cdd:cd03239 155 TLKKEMFENAD 165
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
442-473 |
7.89e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 38.00 E-value: 7.89e-03
10 20 30
....*....|....*....|....*....|...
gi 568987674 442 AVVGPVGAGKSSLLSAVLGElppASGLVS-VHG 473
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQ---NVGIVSpIPG 30
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| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
428-567 |
8.02e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.83 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 428 LQGLSFIARPGELLAVVGPVGAGKSSLLSAVLGELPPA--SGLVSVHG---------RIAYVSQQPWVFSG--TVRSNIL 494
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkkqetfaRISGYCEQNDIHSPqvTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 495 FGK--KYEKE--RYEKVIkacALKKDLQLLEDGDL--TVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PLN03140 976 YSAflRLPKEvsKEEKMM---FVDEVMELVELDNLkdAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
98-358 |
8.46e-03 |
|
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: 39.06 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 98 FTLIEEGTRVVQPLFLGKIIeyfekydpdDSVAL----HTAYGYAAVLSMCTLILAILHHL--YFYHVqcAGMRLRVAMC 171
Cdd:cd18572 4 FLVVAALSELAIPHYTGAVI---------DAVVAdgsrEAFYRAVLLLLLLSVLSGLFSGLrgGCFSY--AGTRLVRRLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKF-DQVTIFLHFLWAGPLQAIAVTVLLWV---EIGISCLAGLAVLVIl 247
Cdd:cd18572 73 RDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVsDPLSTNLNVFLRNLVQLVGGLAFMFSlswRLTLLAFITVPVIAL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568987674 248 lplqscIGKLFSSLRSKTAAFTDARI----RTMNEVITGMRIIKMYAWEKS----FADLIANLRKKEISKILGSSYLRGM 319
Cdd:cd18572 152 ------ITKVYGRYYRKLSKEIQDALaeanQVAEEALSNIRTVRSFATEERearrYERALDKALKLSVRQALAYAGYVAV 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 568987674 320 NMASFFIANKVILFVtfTSYVLLGNEITAsHVFVAMTLY 358
Cdd:cd18572 226 NTLLQNGTQVLVLFY--GGHLVLSGRMSA-GQLVTFMLY 261
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