|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-1304 |
0e+00 |
|
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: 875.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 6 TEVKPNPLQD--ANLCSRLFFWWLNPLFKAGHKRRLEEDDMFSVLPEDRSKHLGEELQGYWDKE----------VLRAKK 73
Cdd:TIGR00957 195 TNHDPNPCPEssASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKEckktrkqpvsAVYGKK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 74 DA--------------------------RKPSLTKAIVKCYWKSYLILGIFTLIEETTRVVQPIFLGKIIdyfeKYDSDD 127
Cdd:TIGR00957 275 DPskpkgssqldaneevealivksphkpRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLI----RFVNDP 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 128 SAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ 207
Cdd:TIGR00957 351 MAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 208 VTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIK 287
Cdd:TIGR00957 431 LATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 288 MYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTTYVLL--GNKITASHVFVAMTLYGAVRLTV 365
Cdd:TIGR00957 511 LYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVdeNNILDAEKAFVSLALFNILRFPL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 366 TLFfPSAIERVSEAVVSVRRIKNFLLLDELP----ERKAQEPSDGKAI-VHVQDFTafWDKAlDTPTLQGLSFTARPGEL 440
Cdd:TIGR00957 591 NIL-PMVISSIVQASVSLKRLRIFLSHEELEpdsiERRTIKPGEGNSItVHNATFT--WARD-LPPTLNGITFSIPEGAL 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 441 LAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAYVSQQPWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDLQLL 520
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEIL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 521 EDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQ--TLHEKITILVTHQLQYLK 598
Cdd:TIGR00957 747 PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTHGISYLP 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 599 AASHILILKDGEMVQKGTYTEFLKSGVDFGSLLK-----KENEEAEPSPV-----PGTPTLR---------------NRT 653
Cdd:TIGR00957 827 QVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRtyapdEQQGHLEDSWTalvsgEGKEAKLiengmlvtdvvgkqlQRQ 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 654 FSEASIWSQQSSR---PSLKDGVPDAQdaENTQAAQPEESRSEGRIGFKAYKNYfsAGASWFFIIFLVLLNLMGQ-VFYV 729
Cdd:TIGR00957 907 LSASSSDSGDQSRhhgSSAELQKAEAK--EETWKLMEADKAQTGQVELSVYWDY--MKAIGLFITFLSIFLFVCNhVSAL 982
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 730 LQDWWLSHWANrqGALNDTKNANGNVTgtldlswyLGIYTGLtavtvlfGIARSLLVF-YVL------VNASQTLHNRMF 802
Cdd:TIGR00957 983 ASNYWLSLWTD--DPMVNGTQNNTSLR--------LSVYGAL-------GILQGFAVFgYSMavsiggIQASRVLHQDLL 1045
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 803 ESILKAPVLFFDRNPieltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevlllalPGRILNRF 882
Cdd:TIGR00957 1046 HNKLRSPMSFFERTP---------------------------------------------------------SGNLVNRF 1068
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 883 SKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLESTTRSPVFSHLS 962
Cdd:TIGR00957 1069 SKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFN 1148
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 963 SSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGSLVLAKTLDAGQVGLALSY 1042
Cdd:TIGR00957 1149 ETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSY 1228
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1043 SLTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECRK-RPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTAL 1121
Cdd:TIGR00957 1229 SLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQEtAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVT 1308
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1122 IKSREKVGIVGRTGAGKSSLISALFRLSE-PEGKIWIDKILTTEIGLHDLRKKMSIIPQ--------------------- 1179
Cdd:TIGR00957 1309 IHGGEKVGIVGRTGAGKSSLTLGLFRINEsAEGEIIIDGLNIAKIGLHDLRFKITIIPQdpvlfsgslrmnldpfsqysd 1388
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ---------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKF 1250
Cdd:TIGR00957 1389 eevwwalelAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF 1468
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1251 AQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNpESLFYKMVQQLG 1304
Cdd:TIGR00957 1469 EDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ-RGIFYSMAKDAG 1521
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-1311 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 867.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 12 PLQDANLCSRLFFWWLNPLFKAGHKRRLEEDDMFSVLPEDRSKHLGEELQGYWDKEVLRAKkdarkPSLTKAIVKCYWKS 91
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPK-----PWLLRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 92 YLILGIFTLIEETTRVVQPIFLGKIIdyfEKYDSDDSAALhtAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMC 171
Cdd:PLN03130 303 FWLGGFFKIGNDLSQFVGPLLLNLLL---ESMQNGEPAWI--GYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQ 251
Cdd:PLN03130 378 AAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 252 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMasfFIANKVI 331
Cdd:PLN03130 458 TFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNS---FILNSIP 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 332 LFVT---FTTYVLLGNKITASHVFVAMTLYGAVRLTvtLF-FPSAIERVSEAVVSVRRIKNFLLLDEL-----PERKAQE 402
Cdd:PLN03130 535 VLVTvvsFGVFTLLGGDLTPARAFTSLSLFAVLRFP--LFmLPNLITQAVNANVSLKRLEELLLAEERvllpnPPLEPGL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 403 PSdgkaiVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTS-GLVSVHGRIAYVSQQ 481
Cdd:PLN03130 613 PA-----ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQV 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 482 PWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:PLN03130 688 SWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 562 LSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENEEAEPS 641
Cdd:PLN03130 768 LSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYV 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 642 PVPGTPTLrnrtfseasiwSQQSSRPSLKDGVPD-AQDAENTQAAQ-------PEESRSEGRIGFKAYKNYFSA-GASWF 712
Cdd:PLN03130 848 EENGEEED-----------DQTSSKPVANGNANNlKKDSSSKKKSKegksvliKQEERETGVVSWKVLERYKNAlGGAWV 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 713 FIIfLVLLNLMGQVFYVLQDWWLSHWANrQGALNDTKNAngnvtgtldlsWYLGIYTGLTAVTVLFGIARSLLVFYVLVN 792
Cdd:PLN03130 917 VMI-LFLCYVLTEVFRVSSSTWLSEWTD-QGTPKTHGPL-----------FYNLIYALLSFGQVLVTLLNSYWLIMSSLY 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 793 ASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevlll 872
Cdd:PLN03130 984 AAKRLHDAMLGSILRAPMSFFHTNPL------------------------------------------------------ 1009
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 873 alpGRILNRFSKDIGHMDDLLPL---TFLDFIQTLLLVVSVIAVAAAVIPWILIPLVplsIIFVVLRRYFLETSRDVKRL 949
Cdd:PLN03130 1010 ---GRIINRFAKDLGDIDRNVAVfvnMFLGQIFQLLSTFVLIGIVSTISLWAIMPLL---VLFYGAYLYYQSTAREVKRL 1083
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 950 ESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVA-FGSLVLA 1028
Cdd:PLN03130 1084 DSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTAsFAVMQNG 1163
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1029 KTLD----AGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECR-KRPPPGWPHEGVIVFDNV 1103
Cdd:PLN03130 1164 RAENqaafASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIEnNRPPPGWPSSGSIKFEDV 1243
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQ--- 1179
Cdd:PLN03130 1244 VLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQapv 1323
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ---------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATA 1232
Cdd:PLN03130 1324 lfsgtvrfnldpfnehndadlweslerAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1233 NVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLFYKMVQQLGKGEAAAL 1311
Cdd:PLN03130 1404 AVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQSTGAANAQYL 1482
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-1312 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 793.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 12 PLQDANLCSRLFFWWLNPLFKAGHKRRLEEDDMFSVLPEDRSKHLGEELQGYWDKEVLRAKkdarkPSLTKAIVKCYWKS 91
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPK-----PWLLRALNNSLGGR 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 92 YLILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSddsaaLHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMC 171
Cdd:PLN03232 303 FWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDP-----AWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQ 251
Cdd:PLN03232 378 AAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 252 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMasfFIANK-- 329
Cdd:PLN03232 458 TLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNS---FILNSip 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 330 -VILFVTFTTYVLLGNKITASHVFVAMTLYGAVRLTVTLFfPSAIERVSEAVVSVRRIKNFLLLDE--LPERKAQEPsdG 406
Cdd:PLN03232 535 vVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNML-PNLLSQVVNANVSLQRIEELLLSEEriLAQNPPLQP--G 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 407 KAIVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPT-SGLVSVHGRIAYVSQQPWVF 485
Cdd:PLN03232 612 APAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSWIF 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 486 SGTVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PLN03232 692 NATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 566 DAEVGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENEEAEPSPVPG 645
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNT 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 646 TPTLRNRTFSEASI-WSQQSSRPSLkdgvpdaQDAENTQAAQPEESRSEGRIGFKAYKNYFSAGASWFFIIFLVLLNLMG 724
Cdd:PLN03232 852 NDENILKLGPTVTIdVSERNLGSTK-------QGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTT 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 725 QVFYVLQDWWLSHWANRQGALNDTKnangnvtgtldlSWYLGIYT--GLTAVTVLFgiARSLLVFYVLVNASQTLHNRMF 802
Cdd:PLN03232 925 EVLRVSSSTWLSIWTDQSTPKSYSP------------GFYIVVYAllGFGQVAVTF--TNSFWLISSSLHAAKRLHDAML 990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 803 ESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevlllalpGRILNRF 882
Cdd:PLN03232 991 NSILRAPMLFFHTNPT---------------------------------------------------------GRVINRF 1013
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 883 SKDIGHMD----DLLPLtFLDFIQTLLLVVSVIAVAAAVIPWILIPLVplsIIFVVLRRYFLETSRDVKRLESTTRSPVF 958
Cdd:PLN03232 1014 SKDIGDIDrnvaNLMNM-FMNQLWQLLSTFALIGTVSTISLWAIMPLL---ILFYAAYLYYQSTSREVRRLDSVTRSPIY 1089
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 959 SHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVA-FGSLVLAKTLD----A 1033
Cdd:PLN03232 1090 AQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTAtFAVLRNGNAENqagfA 1169
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1034 GQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAP-WECRKRPPPGWPHEGVIVFDNVNFTYSLDGP 1112
Cdd:PLN03232 1170 STMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATaIIENNRPVSGWPSRGSIKFEDVHLRYRPGLP 1249
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1113 LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQ------------ 1179
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQspvlfsgtvrfn 1329
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDEL 1241
Cdd:PLN03232 1330 idpfsehndadlwealerAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 1242 IQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLFYKMVQQLGKGEAAALT 1312
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANAQYLS 1480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-1296 |
0e+00 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 762.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 11 NPLQDANLCSRLFFWWLNPLFKAGHKRRLEEDDMFSVLPEDRSKHLGEELQGYWDKEVLRAKKdarKPSLTKAIVKCYWK 90
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKK---NPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 91 SYLILGIFTLIEETTRVVQPIFLGKIIdyfEKYDSDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAM 170
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRII---ASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 171 CHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPL 250
Cdd:TIGR01271 158 FSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 251 QSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKV 330
Cdd:TIGR01271 238 QACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 331 ILFVTFTTYVLLgNKITASHVFVAMTLYGAVRLTVTLFFPSAIERVSEAVVSVRRIKNFLLLDElpeRKAQEPSDGKAIV 410
Cdd:TIGR01271 318 VVFLSVVPYALI-KGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEE---YKTLEYNLTTTEV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 411 HVQDFTAFWDKALD-------------------------------TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVL 459
Cdd:TIGR01271 394 EMVNVTASWDEGIGelfekikqnnkarkqpngddglffsnfslyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 460 GELPPTSGLVSVHGRIAYVSQQPWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQ 539
Cdd:TIGR01271 474 GELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 540 KARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:TIGR01271 554 RARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSE 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 620 FLKSGVDFGSLL-------------------------------------------------------------------K 632
Cdd:TIGR01271 634 LQAKRPDFSSLLlgleafdnfsaerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasaR 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 633 K----------------ENEEAEP-----SPVP----GTPTL------------------------------------RN 651
Cdd:TIGR01271 714 KfsfvqmgpqkaqattiEDAVREPserkfSLVPedeqGEESLprgnqyhhglqhqaqrrqsvlqlmthsnrgenrreqLQ 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 652 RTFSEASIWSQQS---------SRPSLKDGVPDAQDAENTQA-----AQPEESRSEgRIGFKAYKNYFSAGASWFFIIFL 717
Cdd:TIGR01271 794 TSFRKKSSITQQNelaseldiySRRLSKDSVYEISEEINEEDlkecfADERENVFE-TTTWNTYLRYITTNRNLVFVLIF 872
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 718 VLLNLMGQVFYVLQDWWLshwanrqgaLNDTKNANGNVTG----------------TLDLSWYL-GIYTGLTAVTVLFGI 780
Cdd:TIGR01271 873 CLVIFLAEVAASLLGLWL---------ITDNPSAPNYVDQqhanasspdvqkpviiTPTSAYYIfYIYVGTADSVLALGF 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 781 ARSLLVFYVLVNASQTLHNRMFESILKAPVLFFDrnpieltqlevfrvvdgaldshrhlshphpwpqngSLQAsvtsvtg 860
Cdd:TIGR01271 944 FRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLN-----------------------------------TMKA------- 981
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 861 sdvirfpevlllalpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFL 940
Cdd:TIGR01271 982 ---------------GRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFL 1046
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 941 ETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVV 1020
Cdd:TIGR01271 1047 RTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAV 1126
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1021 AFGSlVLAKTLDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPwECRKRPPPG--------- 1091
Cdd:TIGR01271 1127 TFIA-IGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEP-RPSGGGGKYqlstvlvie 1204
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1092 -------WPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTE 1164
Cdd:TIGR01271 1205 nphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNS 1284
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1165 IGLHDLRKKMSIIPQ------------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCL 1214
Cdd:TIGR01271 1285 VTLQTWRKAFGVIPQkvfifsgtfrknldpyeqwsdeeiwkvaeeVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCL 1364
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1215 ARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLqNPES 1294
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETS 1443
|
..
gi 1958679184 1295 LF 1296
Cdd:TIGR01271 1444 LF 1445
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
76-1309 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 603.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 76 RKPSLTKAIVKCYWKSYLILGIFTLIEETTRVVQPIflgkIIDYFEKYDSDDSAALHTAYGYAAVLSLCTLILAILHHLY 155
Cdd:PTZ00243 230 KRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPV----LLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRF 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 156 FYHVQCAGMRIRVAMCHMIYRKALRLSNSAMGK--TTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEI 233
Cdd:PTZ00243 306 YYISIRCGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLV 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 234 GISCLAGLAILVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISkilgs 313
Cdd:PTZ00243 386 GWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELR----- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 314 sYLRGM---NMASFFIAN---KVILFVTFTTYVLLGNKITASHVFVAMTLYGAVRLTVTLFfPSAIERVSEAVVSVRRIK 387
Cdd:PTZ00243 461 -YLRDVqlaRVATSFVNNatpTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMI-PWVFTTVLQFLVSIKRIS 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 388 NFLLLDE------------LPERKAQEPSDG-KAIVHVQDFTAFWDKAL----------------------DTPTLQGLS 432
Cdd:PTZ00243 539 TFLECDNatcstvqdmeeyWREQREHSTACQlAAVLENVDVTAFVPVKLprapkvktsllsralrmlcceqCRPTKRHPS 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 433 -------------------------------------------------FTARPGELL-------------AVVGPVGAG 450
Cdd:PTZ00243 619 psvvvedtdygspssasrhiveggtgggheatptsersaktpkmktddfFELEPKVLLrdvsvsvprgkltVVLGATGSG 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 451 KSSLLSAVLGELPPTSGLVSVHGRIAYVSQQPWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGD 530
Cdd:PTZ00243 699 KSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGE 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 531 RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGE 610
Cdd:PTZ00243 779 KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGR 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 611 MVQKGTYTEFLKSGVdFGSLLK--KENEEAEPSPVPGTPTLRNRTFSEASIWSQQSSRPSLKDGVPDAQDAEnTQAAQ-- 686
Cdd:PTZ00243 859 VEFSGSSADFMRTSL-YATLAAelKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALD-AAAGRlm 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 687 PEESRSEGRIGFKAYKNYFSA--GASWffIIFLVLLNLMGQVFYVLQDWWLSHWANRQGALNDTKNangnvtgtldLSWY 764
Cdd:PTZ00243 937 TREEKASGSVPWSTYVAYLRFcgGLHA--AGFVLATFAVTELVTVSSGVWLSMWSTRSFKLSAATY----------LYVY 1004
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 765 LGIytgltavtVLFGIA----RSLLVFYVLVNASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhls 840
Cdd:PTZ00243 1005 LGI--------VLLGTFsvplRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPL---------------------- 1054
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 841 hphpwpqngslqasvtsvtgsdvirfpevlllalpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPW 920
Cdd:PTZ00243 1055 -----------------------------------GRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPF 1099
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 921 ILIPLVPLSIIFVVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAY-KAEERCQELFdAHQDLHSEAWFLFL 999
Cdd:PTZ00243 1100 VLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYgKAHLVMQEAL-RRLDVVYSCSYLEN 1178
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1000 TTSRWFAVRLDAICAVFVIVVAF----GSLVLAKTLDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYTD 1075
Cdd:PTZ00243 1179 VANRWLGVRVEFLSNIVVTVIALigviGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTD 1258
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1076 -LEKEAPWECR-------KR-----------------PPPGWPH---EGVIVFDNVNFTYSLDGPLVLKHLTALIKSREK 1127
Cdd:PTZ00243 1259 eVPHEDMPELDeevdaleRRtgmaadvtgtvviepasPTSAAPHpvqAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREK 1338
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1128 VGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQ--------------------------- 1179
Cdd:PTZ00243 1339 VGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQdpvlfdgtvrqnvdpfleassaevwaa 1418
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ---VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILII-DEATANVDPRTDELIQQKIREKFAQCTV 1255
Cdd:PTZ00243 1419 lelVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTV 1498
|
1370 1380 1390 1400 1410
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1256 LTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLFYKMVQQLGKGEAA 1309
Cdd:PTZ00243 1499 ITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALGRSEAK 1552
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
710-1074 |
2.05e-173 |
|
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: 517.64 E-value: 2.05e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 710 SWFFIIFLVLLNLMGQVFYVLQDWWLSHWANRQGALNDTKNANGNVTGT------LDLSWYLGIYTGLTAVTVLFGIARS 783
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGENSTnvdiedLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 784 LLVFYVLVNASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdv 863
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPI--------------------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 864 irfpevlllalpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETS 943
Cdd:cd18601 116 ------------GRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTS 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 944 RDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFG 1023
Cdd:cd18601 184 REVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLATSRWLAVRLDALCALFVTVVAFG 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 1024 SLVLAKTLDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYT 1074
Cdd:cd18601 264 SLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
94-386 |
5.97e-161 |
|
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: 484.03 E-value: 5.97e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 94 ILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSDDSaaLHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHM 173
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSIS--LTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 174 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQSC 253
Cdd:cd18593 79 IYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVILF 333
Cdd:cd18593 159 FGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 334 VTFTTYVLLGNKITASHVFVAMTLYGAVRLTVTLFFPSAIERVSEAVVSVRRI 386
Cdd:cd18593 239 LTFLAYILLGNILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
94-386 |
1.64e-126 |
|
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: 392.77 E-value: 1.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 94 ILGIFTLIEETTRVVQPIFLGKIIDYFekydSDDSAALHT-AYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCH 172
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYF----VPDSTVTKTeAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 173 MIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQS 252
Cdd:cd18594 77 LIYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 253 CIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVIL 332
Cdd:cd18594 157 YLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 333 FVTFTTYVLLGNKITASHVFVAMTLYGAVRLTVTLFFPSAIERVSEAVVSVRRI 386
Cdd:cd18594 237 FATFVPYVLTGNTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
94-386 |
5.40e-115 |
|
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: 361.80 E-value: 5.40e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 94 ILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSDDsaaLHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHM 173
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEP---LSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 174 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQSC 253
Cdd:cd18579 78 IYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVILF 333
Cdd:cd18579 158 LAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 334 VTFTTYVLLGNKITASHVFVAMTLYGAVRlTVTLFFPSAIERVSEAVVSVRRI 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 |
1.38e-111 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 349.08 E-value: 1.38e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTAFWDKALDT--PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAYVSQQPWVFSG 487
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 TVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958679184 568 EVGKHLFQLCICQTL-HEKITILVTHQLQYLKAASHILILKDGE 610
Cdd:cd03250 161 HVGRHIFENCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1096-1285 |
5.26e-103 |
|
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: 326.37 E-value: 5.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 1174
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SIIPQ------------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRI 1224
Cdd:cd03244 81 SIIPQdpvlfsgtirsnldpfgeysdeelwqalerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 1225 LIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEP 1285
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
714-1074 |
2.57e-102 |
|
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: 327.54 E-value: 2.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 714 IIFLVLLNLMGQVFYVLQDWWLSHWAnrqgalndtknANGNVTGTLDLSWYLGIYTGLTAV-TVLFGIARSLLVFYVLVN 792
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWS-----------SDWSSSPNSSSGYYLGVYAALLVLaSVLLVLLRWLLFVLAGLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 793 ASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevlll 872
Cdd:cd18580 70 ASRRLHDKLLRSVLRAPMSFFDTTPS------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 873 alpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLEST 952
Cdd:cd18580 96 ---GRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 953 TRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGSLVLAKTLD 1032
Cdd:cd18580 173 SRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSSIS 252
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958679184 1033 AGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYT 1074
Cdd:cd18580 253 AGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
711-1301 |
1.71e-87 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 296.69 E-value: 1.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 711 WFFIIFLVLLNLMGQVFYVLQDWWLshwanrqGALNDTKNANGNVTGtldLSWYLGIYTGLTAVTVLFGIARSLLVFYVL 790
Cdd:COG1132 20 RGLLILALLLLLLSALLELLLPLLL-------GRIIDALLAGGDLSA---LLLLLLLLLGLALLRALLSYLQRYLLARLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 791 VNASQTLHNRMFESILKAPVLFFDRNPieltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevl 870
Cdd:COG1132 90 QRVVADLRRDLFEHLLRLPLSFFDRRR----------------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 871 llalPGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLE 950
Cdd:COG1132 117 ----TGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 951 STTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAV-FVIVVAFGS-LVLA 1028
Cdd:COG1132 193 QEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLgLALVLLVGGlLVLS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1029 KTLDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYTDLEKEAPWECRKRPPPgwPHEGVIVFDNVNFTYS 1108
Cdd:COG1132 273 GSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLP--PVRGEIEFENVSFSYP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1109 lDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQ-------- 1179
Cdd:COG1132 351 -GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPtSGRILIDGVDIRDLTLESLRRQIGVVPQdtflfsgt 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 -----------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDP 1236
Cdd:COG1132 430 irenirygrpdatdeeveeaakaAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDT 509
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 1237 RTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLRE---YDEpyvLLQNpESLFYKMVQ 1301
Cdd:COG1132 510 ETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEqgtHEE---LLAR-GGLYARLYR 573
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
94-386 |
1.86e-83 |
|
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: 274.73 E-value: 1.86e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 94 ILGIFTLIEETTRVVQPIFLGKIIDYFEkydsDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHM 173
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVE----DPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 174 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQSC 253
Cdd:cd18595 77 IYRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVILF 333
Cdd:cd18595 157 LARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 334 VTFTTYVLLG--NKITASHVFVAMTLYGAVRLTVTlFFPSAIERVSEAVVSVRRI 386
Cdd:cd18595 237 ATFATYVLSDpdNVLDAEKAFVSLSLFNILRFPLS-MLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
711-1074 |
6.05e-81 |
|
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: 267.80 E-value: 6.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 711 WFFIIFLVLLNlmgQVFYVLQDWWLSHWanrqgalndTKNANGNVTGTldlswYLGIYTGLTAVTVLFGIARSLLVFYVL 790
Cdd:cd18606 1 LPLLLLLLILS---QFAQVFTNLWLSFW---------TEDFFGLSQGF-----YIGIYAGLGVLQAIFLFLFGLLLAYLG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 791 VNASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevl 870
Cdd:cd18606 64 IRASKRLHNKALKRVLRAPMSFFDTTPL---------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 871 llalpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLE 950
Cdd:cd18606 92 -----GRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLE 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 951 STTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGSLVLAKT 1030
Cdd:cd18606 167 SILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRFS 246
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958679184 1031 LDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYT 1074
Cdd:cd18606 247 ISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
83-624 |
7.21e-81 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 277.82 E-value: 7.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 83 AIVKCYWKSYLILGIFTLIEETTRVVQPIFLGKIID-YFEKYDsddsaaLHTAYGYAAVLSLCTLILAILHHLYFYHVQC 161
Cdd:COG1132 14 RYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDaLLAGGD------LSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 162 AGMRIRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIGVTILLWV---EIGISC 237
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVidwRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 238 LAGLAILVILL-PLQSCIGKLFSSLRSKTAAFTdariRTMNEVITGMRIIKMYAWEKS----FADLITNLRKKEISKILG 312
Cdd:COG1132 168 LLVLPLLLLVLrLFGRRLRKLFRRVQEALAELN----GRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 313 SSYLRGMNMASFFIAnkVILFVTFTTYVLLGNKITAShVFVAMTLYgavrlTVTLFFP-----SAIERVSEAVVSVRRIk 387
Cdd:COG1132 244 SALFFPLMELLGNLG--LALVLLVGGLLVLSGSLTVG-DLVAFILY-----LLRLFGPlrqlaNVLNQLQRALASAERI- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 388 nFLLLDELPERK----AQEPSDGKAIVHVQDFTAFWDKalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELP 463
Cdd:COG1132 315 -FELLDEPPEIPdppgAVPLPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 464 PTSG-------------LVSVHGRIAYVSQQPWVFSGTVRSNILFGRK-YEKERYEKVIKACALKKDLQLLEDGDLTVIG 529
Cdd:COG1132 392 PTSGrilidgvdirdltLESLRRQIGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 530 DRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE----VGKHLFQLcicqtLHEKITILVTHQLQYLKAASHILI 605
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTEtealIQEALERL-----MKGRTTIVIAHRLSTIRNADRILV 546
|
570
....*....|....*....
gi 1958679184 606 LKDGEMVQKGTYTEFLKSG 624
Cdd:COG1132 547 LDDGRIVEQGTHEELLARG 565
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
711-1074 |
3.34e-80 |
|
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: 266.74 E-value: 3.34e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 711 WFFIIFLVLLNLMGQVFyvlQDWWLSHWANrQGALNDTKNAN------GNVTGTLDLSWYLGIYTGLTAVTVLFGIARSL 784
Cdd:cd18599 5 FLFVLLLFILSVGSTVF---SDWWLSYWLK-QGSGNTTNNVDnstvdsGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 785 LVFYVLVNASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvi 864
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPT---------------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 865 rfpevlllalpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSR 944
Cdd:cd18599 115 -----------GRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 945 DVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGS 1024
Cdd:cd18599 184 ELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLV 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1025 LVLAKTLDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYT 1074
Cdd:cd18599 264 VLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
711-1074 |
1.45e-79 |
|
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: 264.33 E-value: 1.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 711 WFFIIFLVLLnlmGQVFYVLQDWWLSHWANRQGALNDTKNANGNVtgtldlSWYLGIYTGLTAVTVLFGIARSLLVFYVL 790
Cdd:cd18604 1 WALLLLLFVL---SQLLSVGQSWWLGIWASAYETSSALPPSEVSV------LYYLGIYALISLLSVLLGTLRYLLFFFGS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 791 VNASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevl 870
Cdd:cd18604 72 LRASRKLHERLLHSVLRAPLRWLDTTPV---------------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 871 llalpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLE 950
Cdd:cd18604 100 -----GRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 951 STTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGsLVLAKT 1030
Cdd:cd18604 175 SVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAAL-LVYGPG 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958679184 1031 LDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYT 1074
Cdd:cd18604 254 IDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
96-386 |
1.56e-78 |
|
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: 261.23 E-value: 1.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 96 GIFTLIEETTRVVQPIFLGKIIDYFE-KYDSDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHMI 174
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEdAYLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 175 YRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQ-AIGVTILLWVeIGISCLAGLAILVILLPLQSC 253
Cdd:cd18597 83 YRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQiIIAIALLIVN-LGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVILF 333
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 334 VTFTTYVLLGNKITASHVFVAMTLYGAVRLTVTlFFPSAIERVSEAVVSVRRI 386
Cdd:cd18597 242 LSFITYYATGHTLDPANIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
714-1074 |
2.44e-78 |
|
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: 260.49 E-value: 2.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 714 IIFLVLLNLMGQVFYVLQDWWLSHWANrqgalndtKNANGNVTGTLDLSWYLGIYTGLTAVTVLFGIARSLLVFYVLVNA 793
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSD--------DPALNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 794 SQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevllla 873
Cdd:cd18603 73 SRNLHNKLLHNILRAPMSFFDTTPL------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 874 lpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLESTT 953
Cdd:cd18603 98 --GRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVS 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 954 RSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAvfvIVVAFGSL--VLAK-T 1030
Cdd:cd18603 176 RSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGN---LIVLFAALfaVLSRdS 252
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958679184 1031 LDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYT 1074
Cdd:cd18603 253 LSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
714-1074 |
9.21e-74 |
|
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: 248.29 E-value: 9.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 714 IIFLVLLNLMGQVFYVLQDWWLSHWANRQGALNDTKNANGNVTGT-LDLSWYLGIYTGLTAVTVLFGIARSLLVFYVLVN 792
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEdDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 793 ASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevlll 872
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPI------------------------------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 873 alpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLEST 952
Cdd:cd18602 107 ---GRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 953 TRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGSLV--LAKT 1030
Cdd:cd18602 184 TKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTaaLAGY 263
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958679184 1031 LDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYT 1074
Cdd:cd18602 264 ISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1092-1285 |
8.22e-71 |
|
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: 235.77 E-value: 8.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1092 WPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL 1170
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAeEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSIIPQ---------------------VQLKEAIEdlpgkmdteLAESGSNFSVGQRQLVCLARAILKKNRILIIDE 1229
Cdd:cd03369 81 RSSLTIIPQdptlfsgtirsnldpfdeysdEEIYGALR---------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1230 ATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEP 1285
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
92-386 |
1.88e-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: 223.59 E-value: 1.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 92 YLILGIFTLIeettrvVQPIFLGKIIDYFEKYDSDdsaaLHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMC 171
Cdd:cd18592 6 LLISLIFGFI------GPTILIRKLLEYLEDSDSS----VWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 172 HMIYRKALRLSNSamGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQ 251
Cdd:cd18592 76 GLLYKKILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 252 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVI 331
Cdd:cd18592 154 AFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 332 LFVTFTTYVLLGNKITASHVFVAMTLYGAVRLTVTlFFPSAIERVSEAVVSVRRI 386
Cdd:cd18592 234 SVVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLR-MLPYAVKALAEAKVALQRI 287
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
755-1302 |
5.97e-65 |
|
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: 235.11 E-value: 5.97e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 755 VTGTLDLSWYLGI-YTGLTAVTVLFGIARSLLVFYVLVNASQTLHNRMFESILKAPVLFFDRNPI-ELTQlevfRVVDga 832
Cdd:COG2274 188 PNQDLSTLWVLAIgLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVgDLAS----RFRD-- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 833 ldshrhlshphpwpqNGSLQASVTSVTGSdvirfpevLLLALPgrilnrFSkdighmddLLPLTFLDFIQTLLlvvsvia 912
Cdd:COG2274 262 ---------------VESIREFLTGSLLT--------ALLDLL------FV--------LIFLIVLFFYSPPL------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 913 vaaavipwILIPLVpLSIIFVVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHS 992
Cdd:COG2274 298 --------ALVVLL-LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 993 EA---WFLFLTTSRWFAVRLDAICAVFVIVVAfGSLVLAKTLDAGQ-------VGLALSYSLTLMGMFQwsvrqsaEVEN 1062
Cdd:COG2274 369 NArfkLRRLSNLLSTLSGLLQQLATVALLWLG-AYLVIDGQLTLGQliafnilSGRFLAPVAQLIGLLQ-------RFQD 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1063 MMISVERVIEYTDLEKEAPWECRKRPPPgwPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLI 1142
Cdd:COG2274 441 AKIALERLDDILDLPPEREEGRSKLSLP--RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1143 SALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQ-------------------------------VQLKEAIEDLP 1190
Cdd:COG2274 519 KLLLGLYEPtSGRILIDGIDLRQIDPASLRRQIGVVLQdvflfsgtirenitlgdpdatdeeiieaarlAGLHDFIEALP 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1191 GKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDK 1270
Cdd:COG2274 599 MGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADR 678
|
570 580 590
....*....|....*....|....*....|..
gi 1958679184 1271 IMVLDSGRLREyDEPYVLLQNPESLFYKMVQQ 1302
Cdd:COG2274 679 IIVLDKGRIVE-DGTHEELLARKGLYAELVQQ 709
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
394-631 |
8.89e-65 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 221.27 E-value: 8.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 394 ELPERKAQEPSDGKAivHVQDFTAFWDK--ALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSV 471
Cdd:cd03291 19 ELLEKAKQENNDRKH--SSDDNNLFFSNlcLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 472 HGRIAYVSQQPWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQ 551
Cdd:cd03291 97 SGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 552 DADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLL 631
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
94-386 |
9.12e-65 |
|
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: 221.66 E-value: 9.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 94 ILGIFTLIEETTRVVQPIFLGKIIDYFEkydsDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHM 173
Cdd:cd18598 1 PLGLLKLLADVLGFAGPLLLNKLVEFLE----DSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 174 IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQSC 253
Cdd:cd18598 77 VYRKALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 254 IGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMnMASFFIANKVIL- 332
Cdd:cd18598 157 IAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL-CVYFWATTPVLIs 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 333 FVTFTTYVLLGNKITASHVFVAMTLYGavRLTVTL-FFPSAIERVSEAVVSVRRI 386
Cdd:cd18598 236 ILTFATYVLMGNTLTAAKVFTSLALFN--MLIGPLnAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
94-386 |
3.68e-63 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 217.75 E-value: 3.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 94 ILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSDdsaALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHM 173
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLEDPGED---ATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 174 IYRKALRLSNSA-------------------MGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIG 234
Cdd:cd18596 78 IFEKALRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 235 ISCLAGLAILVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSS 314
Cdd:cd18596 158 WSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRF 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 315 YLRGMNMASFFIANKVILFVTFTTYVLL-GNKITASHVFVAMTLYGAVRLTVTlFFPSAIERVSEAVVSVRRI 386
Cdd:cd18596 238 LLDLLLSLLWFLIPILVTVVTFATYTLVmGQELTASVAFTSLALFNMLRGPLN-VLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
713-1074 |
1.22e-62 |
|
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: 215.86 E-value: 1.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 713 FIIFLVLLNLMgQVFYVLQDWWLSHWanrqgaLNDTKNANGNvTGTLDLSWYLGIYTGLTAVTVLFGIARSLLVFYVLVN 792
Cdd:cd18605 1 LILILLSLILM-QASRNLIDFWLSYW------VSHSNNSFFN-FINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 793 ASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevlll 872
Cdd:cd18605 73 AARRLHNKLLSSILFAKMSFFDKTPV------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 873 alpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLEST 952
Cdd:cd18605 99 ---GRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 953 TRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGSLVLA---K 1029
Cdd:cd18605 176 NLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQHffgL 255
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958679184 1030 TLDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEYT 1074
Cdd:cd18605 256 SIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
701-1073 |
5.70e-62 |
|
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: 215.05 E-value: 5.70e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 701 YKNYFSAGASWFFIIFLVLLNLMGQVFYVLQDWWL---SHWANRQGALNDTKNANGNVTGTLDLSWYLGIYTGLTAVTVL 777
Cdd:cd18600 6 YLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLlrsQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVADSLLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 778 FGIARSLLVFYVLVNASQTLHNRMFESILKAPVLFFDrnpieltqlevfrvvdgaldshrhlshphpwpqngSLQasvts 857
Cdd:cd18600 86 MGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFN-----------------------------------TMK----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 858 vtgsdvirfpevlllalPGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRR 937
Cdd:cd18600 126 -----------------AGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 938 YFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFV 1017
Cdd:cd18600 189 YFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFF 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1018 IVVAFGSlVLAKTLDAGQVGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEY 1073
Cdd:cd18600 269 TAVTFIS-IGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRIFKF 323
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
58-635 |
1.49e-58 |
|
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: 215.85 E-value: 1.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 58 EELQGYWDKEVL------RAKKDARKPSLTKAI---VKCYWKSYLILGIFTLIEETTRVVQPIFLGKIIDYFEKydsddS 128
Cdd:COG2274 115 EEFAESWTGVALlleptpEFDKRGEKPFGLRWFlrlLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLP-----N 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 129 AALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLsNDVNKFDQV 208
Cdd:COG2274 190 QDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREF 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 209 --TIFLHFLWAGPLQAIGVTILL-------WVEIGISCLAGLAILVILLPLQSCIGKLFSsLRSKTAAFtdarirtMNEV 279
Cdd:COG2274 269 ltGSLLTALLDLLFVLIFLIVLFfyspplaLVVLLLIPLYVLLGLLFQPRLRRLSREESE-ASAKRQSL-------LVET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 280 ITGMRIIKMYA--------WEKSFADLI-TNLRKKEISKILGssylrgmNMASFFIANKVILFVTFTTYVLLGNKITASH 350
Cdd:COG2274 341 LRGIETIKALGaesrfrrrWENLLAKYLnARFKLRRLSNLLS-------TLSGLLQQLATVALLWLGAYLVIDGQLTLGQ 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 351 VFVAMTLYGAVRLTVTLFFpSAIERVSEAVVSVRRIKNFLLL--DELPERKAQEPSDGKAIVHVQDFTaFWDKALDTPTL 428
Cdd:COG2274 414 LIAFNILSGRFLAPVAQLI-GLLQRFQDAKIALERLDDILDLppEREEGRSKLSLPRLKGDIELENVS-FRYPGDSPPVL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 429 QGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILF 495
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITL 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 496 GRKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 574
Cdd:COG2274 572 GDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 575 QLcICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKEN 635
Cdd:COG2274 652 EN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
162-622 |
1.70e-57 |
|
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: 209.62 E-value: 1.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 162 AGMRIRVamchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVtiFLHFL---WAGPLQAIGVTILLWV---EIGI 235
Cdd:COG4987 88 ADLRVRL------YRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL--YLRVLlplLVALLVILAAVAFLAFfspALAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 236 SCLAGLAILVILLPLqscigkLFSSL-----RSKTAAFTDARIRTMnEVITGMRIIKMY----AWEKSFADLITNLRKKE 306
Cdd:COG4987 160 VLALGLLLAGLLLPL------LAARLgrragRRLAAARAALRARLT-DLLQGAAELAAYgaldRALARLDAAEARLAAAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 307 --ISKILGSSylRGMNMASFFIAnkVILFVTFTTYVLLGNKITASH----VFVAMTLYGAVrltVTLffPSAIERVSEAV 380
Cdd:COG4987 233 rrLARLSALA--QALLQLAAGLA--VVAVLWLAAPLVAAGALSGPLlallVLAALALFEAL---APL--PAAAQHLGRVR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 381 VSVRRIKNflLLDELP---ERKAQEPSDGKAIVHVQDFTAFWDKAlDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSA 457
Cdd:COG4987 304 AAARRLNE--LLDAPPavtEPAEPAPAPGGPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 458 VLGELPPTSGLV-------------SVHGRIAYVSQQPWVFSGTVRSNILFGRKYEKEryEKVIKACA---LKKDLQLLE 521
Cdd:COG4987 381 LLRFLDPQSGSItlggvdlrdldedDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD--EELWAALErvgLGDWLAALP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 522 DGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQTLHEKITILVTHQLQYLKAAS 601
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMD 537
|
490 500
....*....|....*....|.
gi 1958679184 602 HILILKDGEMVQKGTYTEFLK 622
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLA 558
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
90-624 |
2.82e-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: 208.84 E-value: 2.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 90 KSYLILGI-FTLIEETTRVVQPIFLGKIIDYFekydSDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRV 168
Cdd:COG4988 16 RRWLALAVlLGLLSGLLIIAQAWLLASLLAGL----IIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 169 AMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVnkfDQVTIFL-HFLwagP--LQAIGVTILLWVEI-GISCLAGLaIL 244
Cdd:COG4988 92 RLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV---EALDGYFaRYL---PqlFLAALVPLLILVAVfPLDWLSGL-IL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 245 VILLPL----QSCIGKlfsslrsKTAAFTDARIRTMN-------EVITGMRIIKMY----AWEKSFADLITNLRKK--EI 307
Cdd:COG4988 165 LVTAPLiplfMILVGK-------GAAKASRRQWRALArlsghflDRLRGLTTLKLFgrakAEAERIAEASEDFRKRtmKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 308 SKI--LGSSYLRGMnmASFFIAnKVILFVTFTtyvLLGNKITASHVFVAMTL----YGAVRLTVTLFFPSAiervsEAVV 381
Cdd:COG4988 238 LRVafLSSAVLEFF--ASLSIA-LVAVYIGFR---LLGGSLTLFAALFVLLLapefFLPLRDLGSFYHARA-----NGIA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 382 SVRRIKNFLlldELPERKAQE-----PSDGKAIVHVQDFTAFWDKalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLS 456
Cdd:COG4988 307 AAEKIFALL---DAPEPAAPAgtaplPAAGPPSIELEDVSFSYPG--GRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 457 AVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGR-KYEKERYEKVIKACALKKDLQLLED 522
Cdd:COG4988 382 LLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPD 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 523 GDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQTLHEKITILVTHQLQYLKAASH 602
Cdd:COG4988 462 GLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADR 540
|
570 580
....*....|....*....|..
gi 1958679184 603 ILILKDGEMVQKGTYTEFLKSG 624
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
96-386 |
2.02e-56 |
|
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: 198.23 E-value: 2.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 96 GIFTLIEETTRVVQPIFLGKIIDYFEK--YDSDDSAALHTAY----------GY--AAVLSLCTLILAILHHLYFYHVQC 161
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEEntYSSSNSTDKLSVSyvtveeffsnGYvlAVILFLALLLQATFSQASYHIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 162 AGMRIRVAMCHMIYRKALRLS--NSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLA 239
Cdd:cd18591 83 EGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 240 GLAILVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGM 319
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 320 NMASFFIANKVILFVTFTTYVLLGNK-ITASHVFVAMTLYGavRLTVTLF-FPSAIERVSEAVVSVRRI 386
Cdd:cd18591 243 MTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFN--QLTVPLFiFPVVIPILINAVVSTRRL 309
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1096-1290 |
1.98e-55 |
|
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: 192.44 E-value: 1.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTYSLDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKM 1174
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SIIPQ-------------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNR 1223
Cdd:cd03254 80 GVVLQdtflfsgtimenirlgrpnatdeevieaakeAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1224 ILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQ 1290
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1098-1278 |
2.05e-55 |
|
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: 190.29 E-value: 2.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1176
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQ-VQLkeaiedlpgkMDTELAEsgsN-FSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCT 1254
Cdd:cd03228 81 VPQdPFL----------FSGTIRE---NiLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKT 147
|
170 180
....*....|....*....|....
gi 1958679184 1255 VLTIAHRLNTIIDSDKIMVLDSGR 1278
Cdd:cd03228 148 VIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
707-1291 |
1.22e-53 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 198.06 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 707 AGASWFFIIFLVLLNLMGQVFYVLQDWWLSHWAnrQGALNDTKNANgnvtgtlDLSWYLGIYTGLTAVTVLFGIARSLLV 786
Cdd:COG4988 12 ARGARRWLALAVLLGLLSGLLIIAQAWLLASLL--AGLIIGGAPLS-------ALLPLLGLLLAVLLLRALLAWLRERAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 787 FYVLVNASQTLHNRMFESILKAPVLFFDRNPI-ELTQLevfrVVDG--ALDSH--RHLshphpwPQngSLQASVTSVTgs 861
Cdd:COG4988 83 FRAAARVKRRLRRRLLEKLLALGPAWLRGKSTgELATL----LTEGveALDGYfaRYL------PQ--LFLAALVPLL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 862 dvirfpevLLLALpgrilnrfskdighmddllplTFLDFIQTLLLVvsviavaaavipwILIPLVPLSIIFV------VL 935
Cdd:COG4988 149 --------ILVAV---------------------FPLDWLSGLILL-------------VTAPLIPLFMILVgkgaakAS 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 936 RRYFLETSRdvkrlesttrspVFSHLSSSLQGLWTIRAYKAEER-CQELFDAHQDLHSE-------AwflFLTTsrwfAV 1007
Cdd:COG4988 187 RRQWRALAR------------LSGHFLDRLRGLTTLKLFGRAKAeAERIAEASEDFRKRtmkvlrvA---FLSS----AV 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1008 rLDAICAVFVIVVAFGslvlaktldagqVGLALSY-SLTLMGMF------------------QWSVRQSAevenmMISVE 1068
Cdd:COG4988 248 -LEFFASLSIALVAVY------------IGFRLLGgSLTLFAALfvlllapefflplrdlgsFYHARANG-----IAAAE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1069 RVIEYTDLEKEAPWECRKRPPpgWPHEGVIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRL 1148
Cdd:COG4988 310 KIFALLDAPEPAAPAGTAPLP--AAGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1149 SEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQ-------------------------------VQLKEAIEDLPGKMDTE 1196
Cdd:COG4988 387 LPPySGSILINGVDLSDLDPASWRRQIAWVPQnpylfagtirenlrlgrpdasdeeleaaleaAGLDEFVAALPDGLDTP 466
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1197 LAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDS 1276
Cdd:COG4988 467 LGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDD 546
|
650
....*....|....*
gi 1958679184 1277 GRLREYDEPYVLLQN 1291
Cdd:COG4988 547 GRIVEQGTHEELLAK 561
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1096-1301 |
1.13e-51 |
|
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: 182.80 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 1174
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SIIPQ------------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRI 1224
Cdd:cd03288 98 SIILQdpilfsgsirfnldpeckctddrlwealeiAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1225 LIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLFYKMVQ 1301
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
412-609 |
1.12e-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: 178.68 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 412 VQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLV-----------------SVHGR 474
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 475 IAYVSQQPWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDAD 554
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 555 IYLLDDPLSAVDAEVGKHLFQLCICQTLHE--KITILVTHQLQYLKAASHILILKDG 609
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1098-1281 |
8.37e-48 |
|
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: 170.87 E-value: 8.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1176
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQ-------------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRIL 1225
Cdd:cd03251 81 VSQdvflfndtvaeniaygrpgatreeveeaaraANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1226 IIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLRE 1281
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1098-1302 |
1.75e-47 |
|
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: 170.10 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1176
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVsSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQ-------------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRIL 1225
Cdd:cd03253 80 VPQdtvlfndtigynirygrpdatdeevieaakaAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1226 IIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLqNPESLFYKMVQQ 1302
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKA 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
424-624 |
5.11e-43 |
|
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: 157.00 E-value: 5.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSG-------------LVSVHGRIAYVSQQPWVFSGTVR 490
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirdisRKSLRSMIGVVLQDTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFGRKYEKEryEKVIKACALKKDLQL---LEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03254 95 ENIRLGRPNATD--EEVIEAAKEAGAHDFimkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 568 EVGKhLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:cd03254 173 ETEK-LIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
127-606 |
3.92e-42 |
|
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: 163.23 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 127 DSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFD 206
Cdd:TIGR02857 36 AGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 207 qvTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLaILVILLPL----QSCIGklfsslrSKTAAFTDARIRTMN----- 277
Cdd:TIGR02857 116 --GYFARYLPQLVLAVIVPLAILAAVFPQDWISGL-ILLLTAPLipifMILIG-------WAAQAAARKQWAALSrlsgh 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 278 --EVITGMRIIKMYAWEKSFADLIT----NLRKKEISkILGSSYLRGMNMaSFFIANKVILFVTFTTYVLLGNKITASHV 351
Cdd:TIGR02857 186 flDRLRGLPTLKLFGRAKAQAAAIRrsseEYRERTMR-VLRIAFLSSAVL-ELFATLSVALVAVYIGFRLLAGDLDLATG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 352 FVAMTL----YGAVRLTVTLFFPSAiervsEAVVSVRRIKNFLLLDELPErKAQEPSDGK---AIVHVQDFTAFWDKald 424
Cdd:TIGR02857 264 LFVLLLapefYLPLRQLGAQYHARA-----DGVAAAEALFAVLDAAPRPL-AGKAPVTAApasSLEFSGVSVAYPGR--- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 425 TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTVRS 491
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFGRKYEKE-RYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:TIGR02857 415 NIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
490 500 510
....*....|....*....|....*....|....*...
gi 1958679184 571 KHLFQ--LCICQTlheKITILVTHQLQYLKAASHILIL 606
Cdd:TIGR02857 495 AEVLEalRALAQG---RTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
424-610 |
1.67e-41 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 150.23 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTVR 490
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNIlfgrkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:cd03228 94 ENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958679184 571 KHLFQLcICQTLHEKITILVTHQLQYLKAASHILILKDGE 610
Cdd:cd03228 133 ALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
96-624 |
3.06e-41 |
|
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: 161.41 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 96 GIFTLIEETTRVVQPIFLGKIIDyfEKYDSDDSAALHTaygYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHMIY 175
Cdd:TIGR02204 24 LVALLITAAATLSLPYAVRLMID--HGFSKDSSGLLNR---YFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 176 RKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQV-----TIFLHFLwagpLQAIG-VTILLWVEIGISCLAGLAILVILLP 249
Cdd:TIGR02204 99 AHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVigsslSMALRNA----LMCIGgLIMMFITSPKLTSLVLLAVPLVLLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 250 LqSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRG-MNMASFFIAN 328
Cdd:TIGR02204 175 I-LLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRAlLTAIVIVLVF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 329 KVILFVTFT-TYVLLGNKITASHVfVAMTLYgavrltvTLFFPSAIERVSEAVVSVRRIKN-----FLLLDELPERKAQE 402
Cdd:TIGR02204 254 GAIVGVLWVgAHDVIAGKMSAGTL-GQFVFY-------AVMVAGSIGTLSEVWGELQRAAGaaerlIELLQAEPDIKAPA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 403 -----PSDGKAIVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG---- 473
Cdd:TIGR02204 326 hpktlPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlr 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 ---------RIAYVSQQPWVFSGTVRSNILFGRKYEKEryEKVIKACALKKD---LQLLEDGDLTVIGDRGATLSGGQKA 541
Cdd:TIGR02204 406 qldpaelraRMALVPQDPVLFAASVMENIRYGRPDATD--EEVEAAARAAHAhefISALPEGYDTYLGERGVTLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 542 RVNLARAVYQDADIYLLDDPLSAVDAEvGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAE-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELI 562
|
...
gi 1958679184 622 KSG 624
Cdd:TIGR02204 563 AKG 565
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1096-1296 |
1.37e-40 |
|
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: 151.55 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMS 1175
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 IIPQ------------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRIL 1225
Cdd:cd03289 81 VIPQkvfifsgtfrknldpygkwsdeeiwkvaeeVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 1226 IIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLqNPESLF 1296
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL-NEKSHF 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1098-1302 |
2.61e-40 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 149.23 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTY-SLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMS 1175
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPtSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 IIPQ----------------------VQLKEA---------IEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRI 1224
Cdd:cd03249 81 LVSQepvlfdgtiaenirygkpdatdEEVEEAakkanihdfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1225 LIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLRE---YDEpyvLLQNPEsLFYKMVQ 1301
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEqgtHDE---LMAQKG-VYAKLVK 236
|
.
gi 1958679184 1302 Q 1302
Cdd:cd03249 237 A 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
89-631 |
1.28e-39 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 158.35 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 89 WKsYLILGIFTL-IEETTRVVQPIFLGKIIDyfekydsddsaALHTAYGYAAvLSLCTLILAILHHLYFYHVQCAGMRIR 167
Cdd:TIGR00958 160 WP-WLISAFVFLtLSSLGEMFIPFYTGRVID-----------TLGGDKGPPA-LASAIFFMCLLSIASSVSAGLRGGSFN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 168 VAMCHM-------IYRKALRLSNSAMGKTTTGQIVNLLSNDVNKF-DQVTIFLH-FLWAGPLQAIGVTILLWVEIGISCL 238
Cdd:TIGR00958 227 YTMARInlriredLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsRSLSLNVNvLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 239 AGLAI-LVILLPlqSCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKS----FADLITNL----RKKEISK 309
Cdd:TIGR00958 307 TLINLpLVFLAE--KVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETlqlnKRKALAY 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 310 ILGSSYLRGMNMASFFIankvILFvtFTTYVLLGNKITA----SHVFVAMTLYGAVRLTVTLFfpsaiERVSEAVVSVRR 385
Cdd:TIGR00958 385 AGYLWTTSVLGMLIQVL----VLY--YGGQLVLTGKVSSgnlvSFLLYQEQLGEAVRVLSYVY-----SGMMQAVGASEK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 386 IknFLLLDelpeRKAQEPSDG-------KAIVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAV 458
Cdd:TIGR00958 454 V--FEYLD----RKPNIPLTGtlaplnlEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 459 LGELPPTSGLV-------------SVHGRIAYVSQQPWVFSGTVRSNILFG-RKYEKERYEKVIKACALKKDLQLLEDGD 524
Cdd:TIGR00958 528 QNLYQPTGGQVlldgvplvqydhhYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGY 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 525 LTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVgKHLFQLCICQtlHEKITILVTHQLQYLKAASHIL 604
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC-EQLLQESRSR--ASRTVLLIAHRLSTVERADQIL 684
|
570 580
....*....|....*....|....*..
gi 1958679184 605 ILKDGEMVQKGTYTEFLKSGVDFGSLL 631
Cdd:TIGR00958 685 VLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
123-386 |
6.25e-39 |
|
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: 147.36 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 123 YDSDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDV 202
Cdd:cd18559 26 FDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 203 NKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGISCLAGLAILVILLPLQSCIGKLFSSLRSKTAAFTDARIRTMNEVITG 282
Cdd:cd18559 106 DRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 283 MRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVILFVTFTTYVLLG--NKITASHVFVAMTLYGA 360
Cdd:cd18559 186 ISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHslAGLVALKVFYSLALTTY 265
|
250 260
....*....|....*....|....*.
gi 1958679184 361 VRLTVTLfFPSAIERVSEAVVSVRRI 386
Cdd:cd18559 266 LNWPLNM-SPEVITNIVAAEVSLERS 290
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
162-594 |
7.30e-39 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 153.29 E-value: 7.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 162 AGMRIRVamchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTIL----LWVEIGISC 237
Cdd:TIGR02868 86 GALRVRV------YERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAaiavLSVPAALIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 238 LAGLAILVILLPLqscigklFSSLRSKTAAFTDARIRtmnevitGMRIIKMYAWEKSFADLITNLRKKEI---SKILGSS 314
Cdd:TIGR02868 160 AAGLLLAGFVAPL-------VSLRAARAAEQALARLR-------GELAAQLTDALDGAAELVASGALPAAlaqVEEADRE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 315 YLRGMNMASFFIA---NKVILFVTFTTY--VLLGNKITASHVFVAMTLYGAVRLTVTLF-----FPSAIERVSEAVVSVR 384
Cdd:TIGR02868 226 LTRAERRAAAATAlgaALTLLAAGLAVLgaLWAGGPAVADGRLAPVTLAVLVLLPLAAFeafaaLPAAAQQLTRVRAAAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 385 RIkNFLLLDELPERKAQEPSDG-----KAIVHVQDFTAFWDKalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVL 459
Cdd:TIGR02868 306 RI-VEVLDAAGPVAEGSAPAAGavglgKPTLELRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 460 GELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGRK-YEKERYEKVIKACALKKDLQLLEDGDL 525
Cdd:TIGR02868 383 GLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLD 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 526 TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQTLHEKITILVTHQL 594
Cdd:TIGR02868 463 TVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHHL 530
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
424-624 |
8.55e-39 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 145.07 E-value: 8.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-------------IAYVSQQPWVFSGTVR 490
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFGRKYE-KERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEv 569
Cdd:cd03251 94 ENIAYGRPGAtREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTE- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 570 GKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:cd03251 173 SERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
424-624 |
8.66e-39 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 144.99 E-value: 8.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTVR 490
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlrwlrsQIGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFGRKYEK-ERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:cd03249 95 ENIRYGKPDATdEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 570 GKhLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:cd03249 175 EK-LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
424-615 |
1.91e-38 |
|
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: 143.50 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTVR 490
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFGRKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:cd03245 96 DNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958679184 570 GKHLFQlCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKG 615
Cdd:cd03245 176 EERLKE-RLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1095-1281 |
2.15e-38 |
|
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: 153.05 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1095 EGVIVFDNVNFTYSLDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKK 1173
Cdd:COG5265 355 GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVtSGRILIDGQDIRDVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1174 MSIIPQ-------------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKN 1222
Cdd:COG5265 434 IGIVPQdtvlfndtiayniaygrpdaseeeveaaaraAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1223 RILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLRE 1281
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
386-637 |
3.05e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 152.31 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 386 IKNFLLLDEL-PERKAQEPSDGKAI-VHVQDFTAFwdkALDTPTLQG-LSFTARPGELLAVVGPVGAGKSSLLSAVLGEL 462
Cdd:PRK11174 324 LVTFLETPLAhPQQGEKELASNDPVtIEAEDLEIL---SPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 463 PPTsGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGRK-YEKERYEKVIKACALKKDLQLLEDGDLTVI 528
Cdd:PRK11174 401 PYQ-GSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPI 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 529 GDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAevgkHLFQLcICQTLHE----KITILVTHQLQYLKAASHIL 604
Cdd:PRK11174 480 GDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA----HSEQL-VMQALNAasrrQTTLMVTHQLEDLAQWDQIW 554
|
250 260 270
....*....|....*....|....*....|...
gi 1958679184 605 ILKDGEMVQKGTYTEFLKSGVDFGSLLKKENEE 637
Cdd:PRK11174 555 VMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
922-1281 |
4.60e-38 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 151.79 E-value: 4.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 922 LIPLVPLSIIFVVLRRY---FLETSRDVKRLESTTRSPVfshlSSSLQGLWTIRAYKAEERCQELFDAHQDlhseawflf 998
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVskrLRRISKEIQNSMGQVTTVA----EETLQGYRVVKLFGGQAYETRRFDAVSN--------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 999 ltTSRWFAVRLDAICAV------FVIVVAFGSLVLAKTLDAG----QVGLALSYsLTLMGMFQWSVRQSAEVENMM---- 1064
Cdd:TIGR02203 225 --RNRRLAMKMTSAGSIsspitqLIASLALAVVLFIALFQAQagslTAGDFTAF-ITAMIALIRPLKSLTNVNAPMqrgl 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1065 ISVERVIEYTDLEKEApwECRKRPPPgwPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISA 1144
Cdd:TIGR02203 302 AAAESLFTLLDSPPEK--DTGTRAIE--RARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1145 LFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQ--------------------------------VQLKEAIEDLPG 1191
Cdd:TIGR02203 378 IPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQdvvlfndtianniaygrteqadraeieralaaAYAQDFVDKLPL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1192 KMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKI 1271
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
410
....*....|
gi 1958679184 1272 MVLDSGRLRE 1281
Cdd:TIGR02203 538 VVMDDGRIVE 547
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1051-1313 |
2.43e-37 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 149.87 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1051 QWSVRQSAEVenmmiSVERVIEYTDLEKEaPWECRKRPPPGwpheGVIVFDNVNFTYsLDGPLVLKHLTALIKSREKVGI 1130
Cdd:PRK10790 304 QQSMLQQAVV-----AGERVFELMDGPRQ-QYGNDDRPLQS----GRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVAL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1131 VGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQ------------------------------ 1179
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLtEGEIRLDGRPLSSLSHSVLRQGVAMVQQdpvvladtflanvtlgrdiseeqvwqalet 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIA 1259
Cdd:PRK10790 453 VQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1260 HRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNpESLFYKM--VQQLGKGEAAALTE 1313
Cdd:PRK10790 533 HRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMyqLQLAGEELAASVRE 587
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
403-611 |
3.73e-37 |
|
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: 139.91 E-value: 3.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 403 PSDGKAIVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSV----------- 471
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpisqyehk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 472 --HGRIAYVSQQPWVFSGTVRSNILFGrkYEKERYEKViKACALKKD----LQLLEDGDLTVIGDRGATLSGGQKARVNL 545
Cdd:cd03248 85 ylHSKVSLVGQEPVLFARSLQDNIAYG--LQSCSFECV-KEAAQKAHahsfISELASGYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 546 ARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQtlHEKITILV-THQLQYLKAASHILILKDGEM 611
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDW--PERRTVLViAHRLSTVERADQILVLDGGRI 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
408-623 |
9.51e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 9.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 408 AIVHVQDFTAFWDkalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--------RIAYVS 479
Cdd:COG1121 5 PAIELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 480 QQ---PWVFSGTVR--------SNILFGRKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLAR 547
Cdd:COG1121 82 QRaevDWDFPITVRdvvlmgryGRRGLFRRPSRADREAVDEA---------LERVGLEDLADRPiGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 548 AVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQTLHEKITIL-VTHQLQYL-KAASHILILkDGEMVQKGTYTEFLKS 623
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYEL-LRELRREGKTILvVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEVLTP 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1098-1301 |
2.65e-36 |
|
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: 138.00 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSI 1176
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEnGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQVQL-------------------------------KEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRIL 1225
Cdd:cd03252 81 VLQENVlfnrsirdnialadpgmsmervieaaklagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1226 IIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLRE---YDEpyvlLQNPESLFYKMVQ 1301
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEqgsHDE----LLAENGLYAYLYQ 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
424-623 |
3.16e-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: 146.05 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-------------IAYVSQQPWVFSGTVR 490
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNIlfGRkYEKERYEKVIKACALK--KDLQL-LEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:COG4618 424 ENI--AR-FGDADPEKVVAAAKLAgvHEMILrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 568 EVGKHLFQlCIcQTLHE--KITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:COG4618 501 EGEAALAA-AI-RALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
426-607 |
4.69e-36 |
|
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: 136.12 E-value: 4.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--------RIAYVSQQ---PWVFSGTVR---- 490
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRrsiDRDFPISVRdvvl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 ----SNILFGRKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:cd03235 93 mglyGHKGLFRRLSKADKAKV---------DEALERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958679184 566 DAEVGKHLFQLciCQTLHEK-ITIL-VTHQL-QYLKAASHILILK 607
Cdd:cd03235 164 DPKTQEDIYEL--LRELRREgMTILvVTHDLgLVLEYFDRVLLLN 206
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
373-617 |
7.62e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 144.86 E-value: 7.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 373 IERVSEAVVSVRRiknflLLDELPERK--AQEPSDGKAIVHVqDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAG 450
Cdd:PRK10789 280 VERGSAAYSRIRA-----MLAEAPVVKdgSEPVPEGRGELDV-NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 451 KSSLLSAVLGELPPTSGLVSVH-------------GRIAYVSQQPWVFSGTVRSNILFGR-KYEKERYEKVIKACALKKD 516
Cdd:PRK10789 354 KSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 517 LQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlCICQTLHEKITILVTHQLQY 596
Cdd:PRK10789 434 ILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILH-NLRQWGEGRTVIISAHRLSA 512
|
250 260
....*....|....*....|.
gi 1958679184 597 LKAASHILILKDGEMVQKGTY 617
Cdd:PRK10789 513 LTEASEILVMQHGHIAQRGNH 533
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
965-1303 |
1.20e-34 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 142.79 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 965 LQGLWTIRAYKAEERCqelFDAHQDLHSEAWFLFLTTSRW--FAVRLDAICAVFVIVVAFGSLVLAKTLDAGQVGLALSY 1042
Cdd:TIGR03797 321 INGISKLRVAGAENRA---FARWAKLFSRQRKLELSAQRIenLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAF 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1043 SlTLMGMFQWSVRQSAeveNMMISVERVI---EYTDLEKEAPWECR-KRPPPGwPHEGVIVFDNVNFTYSLDGPLVLKHL 1118
Cdd:TIGR03797 398 N-TAFGSFSGAVTQLS---NTLISILAVIplwERAKPILEALPEVDeAKTDPG-KLSGAIEVDRVTFRYRPDGPLILDDV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1119 TALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQ------------------ 1179
Cdd:TIGR03797 473 SLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPEsGSVFYDGQDLAGLDVQAVRRQLGVVLQngrlmsgsifeniaggap 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIr 1247
Cdd:TIGR03797 553 ltldeaweaarmAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL- 631
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1248 EKFaQCTVLTIAHRLNTIIDSDKIMVLDSGRLRE---YDEpyvlLQNPESLFYKMVQ-QL 1303
Cdd:TIGR03797 632 ERL-KVTRIVIAHRLSTIRNADRIYVLDAGRVVQqgtYDE----LMAREGLFAQLARrQL 686
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
876-1300 |
1.33e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 142.94 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 876 GRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWI-LIPLVPLSIIFVVLRRY---FLETSRDVKrlES 951
Cdd:TIGR00958 258 GELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLtMVTLINLPLVFLAEKVFgkrYQLLSEELQ--EA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 952 TTRSPVFSHlsSSLQGLWTIRAYKAEE-RCQELFDAHQDLHSEAW------FLFLTTSRWFAVrldaicAVFVIVVAFGS 1024
Cdd:TIGR00958 336 VAKANQVAE--EALSGMRTVRSFAAEEgEASRFKEALEETLQLNKrkalayAGYLWTTSVLGM------LIQVLVLYYGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1025 -LVLAKTLDAGQVglaLSYSLTLMGMFQwSVRQSAEVEN-MMISV---ERVIEYTDLEKEAPWECRKRPPPgwpHEGVIV 1099
Cdd:TIGR00958 408 qLVLTGKVSSGNL---VSFLLYQEQLGE-AVRVLSYVYSgMMQAVgasEKVFEYLDRKPNIPLTGTLAPLN---LEGLIE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1100 FDNVNFTYSL--DGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1176
Cdd:TIGR00958 481 FQDVSFSYPNrpDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPtGGQVLLDGVPLVQYDHHYLHRQVAL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQVQL--------------------------KEA-----IEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRIL 1225
Cdd:TIGR00958 560 VGQEPVlfsgsvreniaygltdtpdeeimaaaKAAnahdfIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVL 639
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1226 IIDEATANVDPRTDELIQQKirEKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPeSLFYKMV 1300
Cdd:TIGR00958 640 ILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
424-616 |
5.72e-34 |
|
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: 131.70 E-value: 5.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWV-FSGTV 489
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEPPApFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 490 RSNILFGR--------KYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:COG1120 93 RELVALGRyphlglfgRPSAEDREAVEEA---------LERTGLEHLADRPvDELSGGERQRVLIARALAQEPPLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 561 PLSAVD----AEVGKHLFQLCicqTLHEKITILVTHQL-QYLKAASHILILKDGEMVQKGT 616
Cdd:COG1120 164 PTSHLDlahqLEVLELLRRLA---RERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
426-634 |
7.47e-34 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 130.81 E-value: 7.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-------------IAYVSQQPWVFSGTVRSN 492
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrraIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGR-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:cd03253 95 IRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 572 HLFQlCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLKKE 634
Cdd:cd03253 175 EIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
424-636 |
8.19e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 130.57 E-value: 8.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQQPWVFSG-TVR 490
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILF-------GRKYEKERYEKVIKACALKKdlqlledgdltVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:COG1131 92 ENLRFfarlyglPRKEARERIDELLELFGLTD-----------AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 564 AVDAEVGKHLFQLcICQTLHEKITILV-THQLQYL-KAASHILILKDGEMVQKGTYTEFLKSGVD--FGSLLKKENE 636
Cdd:COG1131 161 GLDPEARRELWEL-LRELAAEGKTVLLsTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARLLEdvFLELTGEEAR 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1096-1279 |
2.42e-33 |
|
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: 128.86 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM 1174
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPtSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SIIPQ----------------------VQLKEAIE---------DLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNR 1223
Cdd:cd03245 81 GYVPQdvtlfygtlrdnitlgapladdERILRAAElagvtdfvnKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1224 ILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRL 1279
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
276-1276 |
3.77e-33 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 140.16 E-value: 3.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 276 MNEVITGMRIIKMYAWEKsfadliTNLRKKEISKILGSSYLRGMN-MASFFIA--NKVILfVTFTTYVLLGNKI---TAS 349
Cdd:PTZ00265 239 IEEALVGIRTVVSYCGEK------TILKKFNLSEKLYSKYILKANfMESLHIGmiNGFIL-ASYAFGFWYGTRIiisDLS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 350 HVFVAMTLYGAVRLTV------TLFFPSAI-ERVSEAVVSVRRIKNfllLDELPERK--AQEPSDGKAI-----VHVQDF 415
Cdd:PTZ00265 312 NQQPNNDFHGGSVISIllgvliSMFMLTIIlPNITEYMKSLEATNS---LYEIINRKplVENNDDGKKLkdikkIQFKNV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 416 TAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVH--------------GRIAYVSQQ 481
Cdd:PTZ00265 389 RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwrSKIGVVSQD 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 482 PWVFSGTVRSNI---LFGRK---YEKERYEK--------------VIKACA-----------------LKKDLQLLEDGD 524
Cdd:PTZ00265 469 PLLFSNSIKNNIkysLYSLKdleALSNYYNEdgndsqenknkrnsCRAKCAgdlndmsnttdsnelieMRKNYQTIKDSE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 525 L---------------------TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvGKHLFQLCI--CQT 581
Cdd:PTZ00265 549 VvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTInnLKG 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 582 LHEKITILVTHQLQYLKAASHILILKDGEmvqKGTYTEFLKSGVDFGSLLKKENEEAEPSPVPGTPTLRNRTFSEA-SIW 660
Cdd:PTZ00265 628 NENRITIIIAHRLSTIRYANTIFVLSNRE---RGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAgSYI 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 661 SQQSSRPSL---KDGV---------------------------------------PD--------------AQDAENTQA 684
Cdd:PTZ00265 705 IEQGTHDALmknKNGIyytminnqkvsskkssnndndkdsdmkssaykdsergydPDemngnskhenesasNKKSCKMSD 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 685 AQPEESRSEGRIGF---------KA-------YKNYFSAGASwFFIIFLVLLNLMG--QVFYVLqdwwlshWANRQGALN 746
Cdd:PTZ00265 785 ENASENNAGGKLPFlrnlfkrkpKApnnlrivYREIFSYKKD-VTIIALSILVAGGlyPVFALL-------YAKYVSTLF 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 747 DTKNANGNvtgtldlSWYLGIYTGLTAVTVLfgIARSLLVFYVLV---NASQTLHNRMFESILKAPVLFFDRNpieltql 823
Cdd:PTZ00265 857 DFANLEAN-------SNKYSLYILVIAIAMF--ISETLKNYYNNVigeKVEKTMKRRLFENILYQEISFFDQD------- 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 824 evfRVVDGALDSHrhlshphpwpQNGSLQASVTSVTGSDVIrFPEVLLLALPGRILNRFSKDIghMDDLLPLTFLDFIQt 903
Cdd:PTZ00265 921 ---KHAPGLLSAH----------INRDVHLLKTGLVNNIVI-FTHFIVLFLVSMVMSFYFCPI--VAAVLTGTYFIFMR- 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 904 lllvvsviavaaavipwiliplvplsiIFVVLRRyfLETSRDVKRLESTTRSPVFSH-------------LSSSLQGLWT 970
Cdd:PTZ00265 984 ---------------------------VFAIRAR--LTANKDVEKKEINQPGTVFAYnsddeifkdpsflIQEAFYNMNT 1034
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 971 IRAYKAEERCQELFDAHQDLHSEAW-FLFLTTSRWFAVRLDAICAVFVIVVAFGSLVLAK-TLDAGQVGLAL-------S 1041
Cdd:PTZ00265 1035 VIIYGLEDYFCNLIEKAIDYSNKGQkRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRgTILVDDFMKSLftflftgS 1114
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1042 YSLTLMGMfqwsvrqSAEVENMMISVERVieYTDLEKEAPWECRK----RPPPGWPHEGVIVFDNVNFTY-SLDGPLVLK 1116
Cdd:PTZ00265 1115 YAGKLMSL-------KGDSENAKLSFEKY--YPLIIRKSNIDVRDnggiRIKNKNDIKGKIEIMDVNFRYiSRPNVPIYK 1185
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1117 HLTALIKSREKVGIVGRTGAGKSSLISALFR------------------------------------------------- 1147
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1148 ------LSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQ-------------------------------VQLKEAIEDLP 1190
Cdd:PTZ00265 1266 sgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQepmlfnmsiyenikfgkedatredvkrackfAAIDEFIESLP 1345
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1191 GKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQK---IREKfAQCTVLTIAHRLNTIID 1267
Cdd:PTZ00265 1346 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTivdIKDK-ADKTIITIAHRIASIKR 1424
|
....*....
gi 1958679184 1268 SDKIMVLDS 1276
Cdd:PTZ00265 1425 SDKIVVFNN 1433
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1100-1278 |
4.74e-33 |
|
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: 125.43 E-value: 4.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1100 FDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIP 1178
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPtSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1179 QvqlkeaiedlpgkmdtelaesgsnFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLT 1257
Cdd:cd00267 80 Q------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVII 135
|
170 180
....*....|....*....|..
gi 1958679184 1258 IAHRLNTIID-SDKIMVLDSGR 1278
Cdd:cd00267 136 VTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
428-563 |
5.79e-33 |
|
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: 125.07 E-value: 5.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSG-TVRSNI 493
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 494 LFGRkyEKERYEKVIKACALKKDLQLLEDGDL--TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
925-1284 |
1.98e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 134.70 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 925 LVPLSIIFVVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAY-KAEERCQELFDAHQDLHSeAWFLFLTtsr 1003
Cdd:PRK13657 162 LVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnRIEAETQALRDIADNLLA-AQMPVLS--- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1004 WFAV-----RLDAICAVFVIVVAFGSLVLAKTLDAGQVGLALSYSLTLMGMFQwsvRQSAEVENMMISVERVIEYTDLEK 1078
Cdd:PRK13657 238 WWALasvlnRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLD---QVVAFINQVFMAAPKLEEFFEVED 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1079 EAPwecRKRPPPGWPH----EGVIVFDNVNFTYSLDGPLVlKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-G 1153
Cdd:PRK13657 315 AVP---DVRDPPGAIDlgrvKGAVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQsG 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1154 KIWIDKILTTEIGLHDLRKKMSIIPQ----------------------VQLKEA---------IEDLPGKMDTELAESGS 1202
Cdd:PRK13657 391 RILIDGTDIRTVTRASLRRNIAVVFQdaglfnrsiednirvgrpdatdEEMRAAaeraqahdfIERKPDGYDTVVGERGR 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1203 NFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLRE- 1281
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEs 550
|
....*
gi 1958679184 1282 --YDE 1284
Cdd:PRK13657 551 gsFDE 555
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
93-365 |
3.49e-32 |
|
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: 126.99 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSDDSAALhtaYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCH 172
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAL---NVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 173 MIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVEIGIS-CLAGLAILVILLPLQ 251
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 252 SCIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKSFADLITNLRKKEISKILGSSYLRG-MNMASFFIANKV 330
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGlSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958679184 331 ILFVTFT-TYVLLGNKITASHVFVAMTLYGAVRLTV 365
Cdd:pfam00664 239 YALALWFgAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
921-1274 |
7.46e-32 |
|
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: 132.03 E-value: 7.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 921 ILIPLVPLSIIFVVLRRYFLEtSRDVKRLESTTRspVFSHLSSSLQGLWTIRAYKAEERCQE-LFDAHQDLHSEAW---- 995
Cdd:TIGR02857 149 ILLLTAPLIPIFMILIGWAAQ-AAARKQWAALSR--LSGHFLDRLRGLPTLKLFGRAKAQAAaIRRSSEEYRERTMrvlr 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 996 FLFLTTsrwFAVRLDAICAVFVIVVAFGSLVLAKTLDAgQVGLalsYSLTLMGMFQWSVRQ-------SAEVENMMISVE 1068
Cdd:TIGR02857 226 IAFLSS---AVLELFATLSVALVAVYIGFRLLAGDLDL-ATGL---FVLLLAPEFYLPLRQlgaqyhaRADGVAAAEALF 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1069 RVIEytdlekEAPWECRKRPPPGWPHEGVIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRL 1148
Cdd:TIGR02857 299 AVLD------AAPRPLAGKAPVTAAPASSLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1149 SEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQ-------------------------------VQLKEAIEDLPGKMDTE 1196
Cdd:TIGR02857 372 VDPtEGSIAVNGVPLADADADSWRDQIAWVPQhpflfagtiaenirlarpdasdaeirealerAGLDEFVAALPQGLDTP 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 1197 LAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVL 1274
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
410-616 |
8.41e-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: 8.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTAFWDKALDtPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIA 476
Cdd:cd03244 3 IEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 477 YVSQQPWVFSGTVRSNI-LFGRKYEKERYEkVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADI 555
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 556 YLLDDPLSAVDAEVGKHLFQLcICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGT 616
Cdd:cd03244 161 LVLDEATASVDPETDALIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
426-638 |
1.96e-31 |
|
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: 123.81 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQQPWVFSG-TVRSN 492
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 I-LFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeVGK 571
Cdd:COG4555 95 IrYFAELYGLFDEELKKRIEELIELLGLEEFLDRRV-----GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV-MAR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 572 HLFQLCICQTLHEKITILV-THQLQYLKA-ASHILILKDGEMVQKGTYTEFLKSGVD------FGSLLKKENEEA 638
Cdd:COG4555 169 RLLREILRALKKEGKTVLFsSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEenledaFVALIGSEEGEA 243
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
428-615 |
6.58e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 120.23 E-value: 6.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-------------IAYVSQqpwvfsgtvrsnil 494
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 495 fgrkyekeryekvikacalkkdlqLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEV 569
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958679184 570 GKHLFQLCicqTLHEKITILVTHQL-QYLKAASHILILKDGEMVQKG 615
Cdd:cd03214 137 LELLRRLA---RERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
714-1048 |
9.41e-31 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 123.14 E-value: 9.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 714 IIFLVLLNLMGQVFYVLQDWWLSHWANrqgalndtKNANGNVTGTLDLSWYLGIYTGLTAVTVLFGIARSLLVFYVLVNA 793
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD--------VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 794 SQTLHNRMFESILKAPVLFFDRNPieltqlevfrvvdgaldshrhlshphpwpqngslqasvtsvtgsdvirfpevllla 873
Cdd:pfam00664 73 SRRLRRKLFKKILRQPMSFFDTNS-------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 874 lPGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLESTT 953
Cdd:pfam00664 97 -VGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 954 RSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAF--GSLVLAKTL 1031
Cdd:pfam00664 176 VAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWfgAYLVISGEL 255
|
330
....*....|....*..
gi 1958679184 1032 DAGQVGLALSYSLTLMG 1048
Cdd:pfam00664 256 SVGDLVAFLSLFAQLFG 272
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
404-609 |
1.71e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.74 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 404 SDGKAIVHVQDFT-AFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--------R 474
Cdd:COG1116 2 SAAAPALELRGVSkRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 475 IAYVSQQ----PWVfsgTVRSNILFG----RKYEKERYEKVikacalkkdLQLLEDGDLTviGDRGA---TLSGGQKARV 543
Cdd:COG1116 82 RGVVFQEpallPWL---TVLDNVALGlelrGVPKAERRERA---------RELLELVGLA--GFEDAyphQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 544 NLARAVYQDADIYLLDDPLSAVDA----EVGKHLFQLCicqtLHEKITIL-VTHQLQ---YLkaASHILILKDG 609
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDAltreRLQDELLRLW----QETGKTVLfVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
428-606 |
2.02e-30 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 120.27 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------IAYVSQQ----PWVfsgTVRSNILF 495
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQdallPWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 496 G----RKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA--- 567
Cdd:cd03293 97 GlelqGVPKAEARERA---------EELLELVGLSGFENAyPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltr 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958679184 568 -EVGKHLFQlcICQTlHEKITILVTHQLQ---YLkaASHILIL 606
Cdd:cd03293 168 eQLQEELLD--IWRE-TGKTVLLVTHDIDeavFL--ADRVVVL 205
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
389-647 |
2.18e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 128.54 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 389 FLLLDELPERkaQEPSDGKAIVHVQDFTAFWDKALD----TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPP 464
Cdd:PRK13657 310 FEVEDAVPDV--RDPPGAIDLGRVKGAVEFDDVSFSydnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 465 TSGLVSVHG-------------RIAYVSQQPWVFSGTVRSNILFGRK--YEKERYEKVIKACALkkDLQLL-EDGDLTVI 528
Cdd:PRK13657 388 QSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEMRAAAERAQAH--DFIERkPDGYDTVV 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 529 GDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLfQLCICQTLHEKITILVTHQLQYLKAASHILILKD 608
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958679184 609 GEMVQKGTYTEFLKSGVDFGSLLK-----KENEEAEPSPVPGTP 647
Cdd:PRK13657 545 GRVVESGSFDELVARGGRFAALLRaqgmlQEDERRKQPAAEGAN 588
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
424-616 |
2.85e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.72 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAYVSQQP------WVFSG-------TVR 490
Cdd:COG1118 14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvgFVFQHyalfphmTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFG---RKYEKERyekvIKACALkkdlQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG1118 94 ENIAFGlrvRPPSKAE----IRARVE----ELLELVQLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 567 AEVGKHLFQLCIcqTLHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:COG1118 166 AKVRKELRRWLR--RLHDELggtTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
426-606 |
3.65e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.49 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--RIAYVSQQ---PWVFSGTVRSNILFG---- 496
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGrwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 497 ----RKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:NF040873 86 rglwRRLTRDDRAAVDDA---------LERVGLADLAGRQlGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958679184 572 HLFQLcICQTLHEKITIL-VTHQLQYLKAASHILIL 606
Cdd:NF040873 157 RIIAL-LAEEHARGATVVvVTHDLELVRRADPCVLL 191
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1098-1279 |
5.47e-30 |
|
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: 117.32 E-value: 5.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1176
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPtSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQ-VQLkeaiedLPGKmdteLAEsgsN-FSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE-KFAQC 1253
Cdd:cd03246 81 LPQdDEL------FSGS----IAE---NiLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlKAAGA 147
|
170 180
....*....|....*....|....*.
gi 1958679184 1254 TVLTIAHRLNTIIDSDKIMVLDSGRL 1279
Cdd:cd03246 148 TRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
410-615 |
7.19e-30 |
|
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: 118.39 E-value: 7.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTAFWDkalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------IAYV 478
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 479 SQQPWVFSG-TVRSNILFGRKYEKERYEKVIKACalkkdLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIY 556
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGLKLRGVPKAEIRARV-----RELLELVGLEGLLNRyPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 557 LLDDPLSAVDAEVGKHLF-QLCICQTLHEKITILVTH-QLQYLKAASHILILKDGEMVQKG 615
Cdd:cd03259 153 LLDEPLSALDAKLREELReELKELQRELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
424-624 |
7.98e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 119.13 E-value: 7.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTP-TLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTV 489
Cdd:cd03252 13 DGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 490 RSNILFGRkyEKERYEKVIKACALKKD---LQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:cd03252 93 RDNIALAD--PGMSMERVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 567 AEvGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:cd03252 171 YE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1095-1279 |
2.76e-29 |
|
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: 117.19 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1095 EGVIVFDNVNFTY-SLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRK 1172
Cdd:cd03248 9 KGIVKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KMSIIPQ----------------------VQLKEA---------IEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKK 1221
Cdd:cd03248 89 KVSLVGQepvlfarslqdniayglqscsfECVKEAaqkahahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 1222 NRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRL 1279
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
424-611 |
4.00e-29 |
|
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: 115.01 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTVR 490
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnelgdHVGYLPQDDELFSGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILfgrkyekeryekvikacalkkdlqlledgdltvigdrgatlSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:cd03246 94 ENIL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958679184 571 KHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEM 611
Cdd:cd03246 133 RALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
424-619 |
7.61e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.41 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------IAYVSQQPWVF-SGTVRS 491
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQSYALYpHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFG---RKYEK-ERYEKVIKACALkkdLQLLEdgdltvIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG3839 95 NIAFPlklRKVPKaEIDRRVREAAEL---LGLED------LLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 567 A----EVGKHLFQlcicqtLHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:COG3839 166 AklrvEMRAEIKR------LHRRLgttTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
412-610 |
1.64e-28 |
|
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: 114.49 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 412 VQDFTAFWDKAlDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYV 478
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 479 SQQP--WVFSGTVRSNILFGRKYEKERYEKVIkacalKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADI 555
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIE-----ERVEEALELVGLEGLRDRSpFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 556 YLLDDPLSAVDAEVGKHLFQLcICQTLHEKITIL-VTHQLQYLKA-ASHILILKDGE 610
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLEL-LKKLKAEGKTIIiVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1096-1289 |
2.02e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 122.43 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE-PEGKIWIDKILTTEIGLHDLRKKM 1174
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SIIPQ-VQL------------------KEAIE---------DLPGKM----DTELAESGSNFSVGQRQLVCLARAILKKN 1222
Cdd:PRK11176 420 ALVSQnVHLfndtianniayarteqysREQIEeaarmayamDFINKMdnglDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1223 RILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLL 1289
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
424-611 |
3.23e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.37 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSGTVR 490
Cdd:COG4619 12 GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWGGTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFGRKYEKERYEKViKACALKKDLQLledgDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE-- 568
Cdd:COG4619 92 DNLPFPFQLRERKFDRE-RALELLERLGL----PPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEnt 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958679184 569 --VGKHLFQLCicqtLHEKITIL-VTH-QLQYLKAASHILILKDGEM 611
Cdd:COG4619 167 rrVEELLREYL----AEEGRAVLwVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
424-620 |
7.26e-28 |
|
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: 113.43 E-value: 7.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG----------------RIAYVSQQPW---- 483
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMIFQQFNlier 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 484 ------VFSG------TVRSniLFGRKYEKERYekviKACALKKDLQLLEDgdltvIGDRGATLSGGQKARVNLARAVYQ 551
Cdd:cd03256 93 lsvlenVLSGrlgrrsTWRS--LFGLFPKEEKQ----RALAALERVGLLDK-----AYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 552 DADIYLLDDPLSAVD---AEVGKHLFqLCICQtlHEKITILVT-HQLQYLKA-ASHILILKDGEMVQKGTYTEF 620
Cdd:cd03256 162 QPKLILADEPVASLDpasSRQVMDLL-KRINR--EEGITVIVSlHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1098-1281 |
7.75e-28 |
|
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: 111.25 E-value: 7.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFR-LSEPEGKIWIDKILTTEIGlHDLRKKMSI 1176
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQVqlkeaiedlPGKMDTELAES-GSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTD----ELIQQKIREKfa 1251
Cdd:cd03247 80 LNQR---------PYLFDTTLRNNlGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITErqllSLIFEVLKDK-- 148
|
170 180 190
....*....|....*....|....*....|
gi 1958679184 1252 qcTVLTIAHRLNTIIDSDKIMVLDSGRLRE 1281
Cdd:cd03247 149 --TLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
424-623 |
1.30e-27 |
|
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: 112.60 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG----------------RIAYVSQQPWVFSG 487
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -TVRSNILFGRKYEKERYEKVIKACALKKdLQ---LLEDGDLtvigdRGATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:cd03261 92 lTVFENVAFPLREHTRLSEEEIREIVLEK-LEavgLRGAEDL-----YPAELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 564 AVDAeVGKHLFQLCIcQTLHEKI---TILVTHQLQ-YLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:cd03261 166 GLDP-IASGVIDDLI-RSLKKELgltSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1098-1295 |
1.45e-27 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 112.43 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSI 1176
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPtSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 I---PQVQL---------------------------KEAIEDLpgKMDtELAE------SGsnfsvGQRQLVCLARAILK 1220
Cdd:COG1122 80 VfqnPDDQLfaptveedvafgpenlglpreeirervEEALELV--GLE-HLADrpphelSG-----GQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1221 KNRILIIDEATANVDPR-TDELIQ--QKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPESL 1295
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRgRRELLEllKRLNKE--GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1104-1279 |
2.05e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 110.22 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQVqL 1182
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSsGEILLDGKDLASLSPKELARKIAYVPQA-L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1183 KEA-IEDLPGKMDTELaeSGsnfsvGQRQLVCLARAILKKNRILIIDEATANVDP----RTDELIQQKIREKfaQCTVLT 1257
Cdd:cd03214 83 ELLgLAHLADRPFNEL--SG-----GERQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARER--GKTVVM 153
|
170 180
....*....|....*....|...
gi 1958679184 1258 IAHRLNTIID-SDKIMVLDSGRL 1279
Cdd:cd03214 154 VLHDLNLAARyADRVILLKDGRI 176
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
424-615 |
3.23e-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: 109.71 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQQPWVFSGTVRS 491
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NIlfgrkyekeryekvikacalkkdlqlledgdltvigdrGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:cd03247 94 NL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958679184 572 HLFQLcICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKG 615
Cdd:cd03247 136 QLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
425-623 |
5.07e-27 |
|
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: 111.24 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 425 TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSG-TVR 490
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFGRKYEKERYEKVIKacalkKDLQLLEDGDLTVIGDRG---ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03295 94 ENIALVPKLLKWPKEKIRE-----RADELLALVGLDPAEFADrypHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 568 EVGKHLFQ--LCICQTLHEKItILVTHQLQ-YLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:cd03295 169 ITRDQLQEefKRLQQELGKTI-VFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
424-622 |
7.11e-27 |
|
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: 110.50 E-value: 7.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPW--VFSGT 488
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQNPDdqLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 489 VRSNILFG---RKYEKERYEKVIKacalkkdlQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:COG1122 93 VEEDVAFGpenLGLPREEIRERVE--------EALELVGLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 565 VDAEVGKHLFQlcICQTLHEK-IT-ILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLK 622
Cdd:COG1122 165 LDPRGRRELLE--LLKRLNKEgKTvIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
424-616 |
8.56e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 113.65 E-value: 8.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------IAYVSQqpwvfSG----- 487
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQ-----DYalfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -TVRSNILFG---RKYEK-ERYEKVIKACALkkdLQLledGDLtviGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:COG3842 92 lTVAENVAFGlrmRGVPKaEIRARVAELLEL---VGL---EGL---ADRYpHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 562 LSAVDAEVGKHLfQLCICQTLHE-KIT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:COG3842 163 LSALDAKLREEM-REELRRLQRElGITfIYVTHdQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
426-619 |
1.17e-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: 110.12 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNI 493
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 LFGRKyEKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 572
Cdd:cd03296 96 AFGLR-VKPRSERPPEAEIRAKVHELLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 573 LFQLciCQTLHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:cd03296 175 LRRW--LRRLHDELhvtTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1066-1303 |
2.32e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 115.69 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1066 SVERVIEYTDLEKEAPWECRKRPPPGwphEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISAL 1145
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD---QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1146 FRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQ-------------------------------VQLKEAIEDLPGkM 1193
Cdd:PRK11160 387 TRAWDPQqGEILLNGQPIADYSEAALRQAISVVSQrvhlfsatlrdnlllaapnasdealievlqqVGLEKLLEDDKG-L 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1194 DTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMV 1273
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260 270
....*....|....*....|....*....|
gi 1958679184 1274 LDSGRLREYDEPYVLLQNpESLFYKMVQQL 1303
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQ-QGRYYQLKQRL 574
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
409-619 |
2.96e-26 |
|
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: 108.82 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 409 IVHVQDFT-AFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------- 473
Cdd:cd03258 1 MIELKNVSkVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 --RIAYVSQQPWVFSG-TVRSNILF----GRKYEKERYEKVikacalkkdLQLLEDGDLTVIGDR-GATLSGGQKARVNL 545
Cdd:cd03258 81 rrRIGMIFQHFNLLSSrTVFENVALpleiAGVPKAEIEERV---------LELLELVGLEDKADAyPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 546 ARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQTLHEK--ITI-LVTHQLQYLKA-ASHILILKDGEMVQKGTYTE 619
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILAL--LRDINRElgLTIvLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
424-605 |
8.22e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.41 E-value: 8.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQQPWVFSG-TVR 490
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILF-----GRKYEKERYEKVIKAcalkkdLQLLEDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:COG4133 94 ENLRFwaalyGLRADREAIDEALEA------VGLAGLADLPV-----RQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958679184 566 DAEvGKHLFQLCICQTLHE-KITILVTHQLQYLKAASHILI 605
Cdd:COG4133 163 DAA-GVALLAELIAAHLARgGAVLLTTHQPLELAAARVLDL 202
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1107-1302 |
1.55e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 113.40 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1107 YSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMS----------- 1175
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSwvgqnpqlphg 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 --------------------IIPQVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVD 1235
Cdd:PRK11174 438 tlrdnvllgnpdasdeqlqqALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1236 PRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLRE---YDEpyvlLQNPESLFYKMVQQ 1302
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
389-625 |
2.42e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 112.80 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 389 FLLLDELPERK--AQEPSDGKAIVHVQDFTAFWDKAlDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTS 466
Cdd:PRK11176 319 FAILDLEQEKDegKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 467 G-------------LVSVHGRIAYVSQQPWVFSGTVRSNILFGR--KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDR 531
Cdd:PRK11176 398 GeilldghdlrdytLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINKMDNGLDTVIGEN 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 532 GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvGKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEM 611
Cdd:PRK11176 478 GVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
250
....*....|....*
gi 1958679184 612 VQKGTYTEFL-KSGV 625
Cdd:PRK11176 557 VERGTHAELLaQNGV 571
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
426-621 |
2.70e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.61 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-------------IAYVSQQPWVFSGTVRSN 492
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGR-KYEKERYEKVIKACALKKdlqLLEDGD-L-TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK11160 434 LLLAApNASDEALIEVLQQVGLEK---LLEDDKgLnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 570 GKHLFQLcICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK11160 511 ERQILEL-LAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
876-1262 |
4.09e-25 |
|
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: 111.30 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 876 GRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAA-VIPWILIPLVPLSIIFVVLRRYFLETSRDVKRLESTTR 954
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVlSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 955 SPVFSHLSSSLQGLWTIRAYKAEERCQ-ELFDAHQDLH----SEAWFLFLTTSrwfAVRLDAICAVFVIVVAFGSLVLAK 1029
Cdd:TIGR02868 190 GELAAQLTDALDGAAELVASGALPAALaQVEEADRELTraerRAAAATALGAA---LTLLAAGLAVLGALWAGGPAVADG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1030 TLDAgqVGLALSYSLTL-----MGMFQWSVRQSAEVEnmmISVERVIEYTDLEKEAPWECRKRPPPGWPHEGVIVFDNVN 1104
Cdd:TIGR02868 267 RLAP--VTLAVLVLLPLaafeaFAALPAAAQQLTRVR---AAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1105 FTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIPQ---- 1179
Cdd:TIGR02868 342 AGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPlQGEVTLDGVPVSSLDQDEVRRRVSVCAQdahl 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ---------------------------VQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATA 1232
Cdd:TIGR02868 421 fdttvrenlrlarpdatdeelwaalerVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
410 420 430
....*....|....*....|....*....|
gi 1958679184 1233 NVDPRTDELIQQKIREKFAQCTVLTIAHRL 1262
Cdd:TIGR02868 501 HLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
191-630 |
4.35e-25 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 112.53 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 191 TGQIVNLLSnDVNKF-DQV--TIFLHFLWAGPLQAIGvTILLWVEIGISCLAGLAIlvillPLQSCIGKLFSSLRSKTAA 267
Cdd:TIGR01193 252 TGEIVSRFT-DASSIiDALasTILSLFLDMWILVIVG-LFLVRQNMLLFLLSLLSI-----PVYAVIIILFKRTFNKLNH 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 268 FTDARIRTMN----EVITGMRIIKMYAWE----KSFADLITNLRKKEISKILGSSYLRGMNMASFFIANKVILFvtFTTY 339
Cdd:TIGR01193 325 DAMQANAVLNssiiEDLNGIETIKSLTSEaerySKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILW--TGAY 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 340 VLLGNKITASHVFVAMTLYGavrltvtlFFPSAIE-------RVSEAVVSVRRIKNFLLLDELPERKAQ--EPSDGKAIV 410
Cdd:TIGR01193 403 LVMRGKLTLGQLITFNALLS--------YFLTPLEniinlqpKLQAARVANNRLNEVYLVDSEFINKKKrtELNNLNGDI 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 411 HVQDFTafWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-------------IAY 477
Cdd:TIGR01193 475 VINDVS--YSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINY 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 478 VSQQPWVFSGTVRSNILFGRKyEKERYEKVIKACAL---KKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDAD 554
Cdd:TIGR01193 553 LPQEPYIFSGSILENLLLGAK-ENVSQDEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 555 IYLLDDPLSAVDAEVGKHLFQLCIcqTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSL 630
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
407-650 |
4.82e-25 |
|
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: 111.15 E-value: 4.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 407 KAIVHVQDFTaFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPT---SGLVSVHG---------- 473
Cdd:COG1123 2 TPLLEVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 ---RIAYVSQQPWV--FSGTVRSNILFGRkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLAR 547
Cdd:COG1123 81 rgrRIGMVFQDPMTqlNPVTVGDQIAEAL-----ENLGLSRAEARARVLELLEAVGLERRLDRYpHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 548 AVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITIL-VTHQLQY-LKAASHILILKDGEMVQKGTYTEFLKSGV 625
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLlITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260
....*....|....*....|....*..
gi 1958679184 626 DFGSL--LKKENEEAEPSPVPGTPTLR 650
Cdd:COG1123 236 ALAAVprLGAARGRAAPAAAAAEPLLE 262
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
428-610 |
8.08e-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: 102.65 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG---------------RIAYVSQQPWVFSG-TVRS 491
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFGrkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958679184 572 HLFQLciCQTLHEK--IT-ILVTHQLQYL-KAASHILILKDGE 610
Cdd:cd03229 138 EVRAL--LKSLQAQlgITvVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
424-610 |
1.07e-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: 101.55 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQqpwvfsgtvr 490
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkdiaklpleelrrRIGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 snilfgrkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:cd00267 81 --------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958679184 571 KHLFQLCICQTLHEKITILVTHQLQYL-KAASHILILKDGE 610
Cdd:cd00267 117 ERLLELLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
425-610 |
1.09e-24 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 103.72 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 425 TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------------IAYVSQQPWVFSG 487
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -TVRSNILFGrkyekERYEKVIKACALKKDLQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:cd03255 97 lTALENVELP-----LLLAGVPKKERRERAEELLERVGLGdRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958679184 566 DAEVGKHLFQLcICQTLHEKIT--ILVTHQLQYLKAASHILILKDGE 610
Cdd:cd03255 172 DSETGKEVMEL-LRELNKEAGTtiVVVTHDPELAEYADRIIELRDGK 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
407-612 |
1.13e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 103.97 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 407 KAIVHVQDFT-AFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------ 473
Cdd:COG1136 2 SPLLELRNLTkSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 -----RIAYVSQQPWVFSG-TVRSNI----LFGRKYEKERYEKVikacalkkdLQLLED-GdltvIGDRG----ATLSGG 538
Cdd:COG1136 82 rlrrrHIGFVFQFFNLLPElTALENValplLLAGVSRKERRERA---------RELLERvG----LGDRLdhrpSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 539 QKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQTLHEK--ITIL-VTHQLQYLKAASHILILKDGEMV 612
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL--LRELNRElgTTIVmVTHDPELAARADRVIRLRDGRIV 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
424-606 |
1.44e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.95 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPP---TSGLVSVHG-----------RIAYVSQQPWVFSG-T 488
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltalpaeqrRIGILFQDDLLFPHlS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 489 VRSNILFG---RKYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:COG4136 93 VGENLAFAlppTIGRAQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958679184 565 VDAEVGKHLFQLCICQTLHEKI-TILVTHQLQYLKAASHILIL 606
Cdd:COG4136 164 LDAALRAQFREFVFEQIRQRGIpALLVTHDEEDAPAAGRVLDL 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1099-1278 |
2.18e-24 |
|
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: 102.55 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1099 VFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSII 1177
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPtSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1178 PQ-------------------VQLKEAIEDLPGKMDTELAESG---------SNFSVGQRQLVCLARAILKKNRILIIDE 1229
Cdd:cd03225 81 FQnpddqffgptveeevafglENLGLPEEEIEERVEEALELVGleglrdrspFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 1230 ATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGR 1278
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
432-621 |
2.31e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.30 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 432 SFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNILFGR-- 497
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQENNLFPHlTVAQNIGLGLrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 498 --KYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEVG 570
Cdd:COG3840 99 glKLTAEQRAQVEQA---------LERVGLAGLLDRlPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 571 KHLFQLCicqtLHEKITIL-VTHQLQ-YLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:COG3840 170 DLVDELC----RERGLTVLmVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1100-1232 |
2.46e-24 |
|
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: 100.41 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1100 FDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMSIIP 1178
Cdd:pfam00005 1 LKNVSLT---------------LNPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTILLDGQDLTDDERKSLRKEIGYVF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1179 Q-----------------------------VQLKEAIE--DLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILII 1227
Cdd:pfam00005 66 QdpqlfprltvrenlrlglllkglskrekdARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLL 145
|
....*
gi 1958679184 1228 DEATA 1232
Cdd:pfam00005 146 DEPTA 150
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
425-621 |
3.83e-24 |
|
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: 103.49 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 425 TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------------RIAYVSQQPWVFSG 487
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -TVRSNILFG-------RKYEKERYEKVIKACALKKDLQLLEDgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:cd03294 117 rTVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 560 DPLSAVD----AEVGKHLFQLcicQTLHEKITILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:cd03294 186 EAFSALDplirREMQDELLRL---QAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
428-623 |
4.33e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 102.41 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------RIAYVSQQPWVFSG-TVRSNILF 495
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 496 G---RKYEK-ERYEKVIKACALKKDLQLLedgdltvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:cd03299 95 GlkkRKVDKkEIERKVLEIAEMLGIDHLL---------NRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 571 KHLFQLciCQTLHEK--ITIL-VTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKS 623
Cdd:cd03299 166 EKLREE--LKKIRKEfgVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
428-616 |
4.61e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.89 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRiAYVSQQPWV---------------FSGTVRSN 492
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR-PLAAWSPWElarrravlpqhsslaFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGR---KYEKERYEKVIKACALKKDLQLLEDGDLTvigdrgaTLSGGQKARVNLARA---VYQDAD----IYLLDDPL 562
Cdd:COG4559 96 VALGRaphGSSAAQDRQIVREALALVGLAHLAGRSYQ-------TLSGGEQQRVQLARVlaqLWEPVDggprWLFLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 563 SAVDAevgKHlfQLCICQTL----HEKITIL-VTHQL----QYlkaASHILILKDGEMVQKGT 616
Cdd:COG4559 169 SALDL---AH--QHAVLRLArqlaRRGGGVVaVLHDLnlaaQY---ADRILLLHQGRLVAQGT 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1097-1282 |
6.85e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 101.81 E-value: 6.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGLHDL 1170
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPtSGSIIFDgKDLLKlsRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSIIPQ-------------VQLKEAIEDLPGKMDTELAESGSN-------------------FSVGQRQLVCLARAI 1218
Cdd:cd03257 81 RKEIQMVFQdpmsslnprmtigEQIAEPLRIHGKLSKKEARKEAVLlllvgvglpeevlnrypheLSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 1219 LKKNRILIIDEATANVDPRT-DELIQ--QKIREKFaQCTVLTIAHRLNTI-IDSDKIMVLDSGRLREY 1282
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVaKIADRVAVMYAGKIVEE 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
424-611 |
7.83e-24 |
|
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: 99.78 E-value: 7.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQQPWVFSG-TVR 490
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEEPSLYENlTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNIlfgrkyekeryekvikacalkkdlqlledgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:cd03230 92 ENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958679184 571 KHLFQLCICQTLHEKITILVTHQLQYLKA-ASHILILKDGEM 611
Cdd:cd03230 132 REFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
409-615 |
1.35e-23 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 100.66 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 409 IVHVQDFT-AFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------- 473
Cdd:cd03257 1 LLEVKNLSvSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 --RIAYVSQQPwvFSG-----TVRSNILFG-RKYEKERYEKVIKACALKKDLQLLEDGDltVIGDRGATLSGGQKARVNL 545
Cdd:cd03257 81 rkEIQMVFQDP--MSSlnprmTIGEQIAEPlRIHGKLSKKEARKEAVLLLLVGVGLPEE--VLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 546 ARAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQTLHE-----KITIL-VTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKlqeelGLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
410-615 |
1.59e-23 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 100.02 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTAFWDKaldTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------IAYV 478
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 479 SQQPWVFSG-TVRSNILFG---RKYEKERYEKVIKACAlkKDLQLLEdgdltVIGDRGATLSGGQKARVNLARAVYQDAD 554
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGlklRKVPKDEIDERVREVA--ELLQIEH-----LLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 555 IYLLDDPLSAVDA----EVGKHLFQLcicQTLHEKITILVTH-QLQYLKAASHILILKDGEMVQKG 615
Cdd:cd03301 151 VFLMDEPLSNLDAklrvQMRAELKRL---QQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
427-612 |
2.61e-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: 99.25 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 427 TLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR----------IAYVSQQP--WVFSGTVRSNIL 494
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrksIGYVMQDVdyQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 495 FGRKYEKERYEKVikACALKK-DLQLLEDgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE----V 569
Cdd:cd03226 95 LGLKELDAGNEQA--ETVLKDlDLYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958679184 570 GKHLFQLcicqTLHEKITILVTHQLQYL-KAASHILILKDGEMV 612
Cdd:cd03226 166 GELIREL----AAQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
428-623 |
4.55e-23 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 99.67 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG----------------RIAYVSQQPWVFSG-TVR 490
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGMLFQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFG-RKY----EKERYEKVikacalkkdLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:COG1127 101 ENVAFPlREHtdlsEAEIRELV---------LEKLELVGLPGAADKMpSELSGGMRKRVALARALALDPEILLYDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 565 VDAEVGKHLFQLcIcQTLHEKI---TILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKS 623
Cdd:COG1127 172 LDPITSAVIDEL-I-RELRDELgltSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1097-1295 |
5.04e-23 |
|
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: 104.60 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRL----SEPEGKIWIDKILTTEIGLHDLRK 1172
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphgGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KMSIIPQ------------VQLKEAIE--DLPGK--------------MDTELAESGSNFSVGQRQLVCLARAILKKNRI 1224
Cdd:COG1123 84 RIGMVFQdpmtqlnpvtvgDQIAEALEnlGLSRAeararvlelleavgLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1225 LIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPESL 1295
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
89-621 |
1.25e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 104.03 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 89 WKSYLILGIFTL-IEETTRVVQPIflgkIIDYFekydSDDSAALHT-----AYGYAAVLSLCTLILAILHH---LYFYH- 158
Cdd:PRK10790 21 WRKPLGLAVLMLwVAAAAEVSGPL----LISYF----IDNMVAKGNlplglVAGLAAAYVGLQLLAAGLHYaqsLLFNRa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 159 ----VQcaGMRIRVAmchmiyRKALRLSNSAMGKTTTGQIVNLLSND--VNKFDQVTIFLHFLWAGPLqaIGVTI----- 227
Cdd:PRK10790 93 avgvVQ--QLRTDVM------DAALRQPLSAFDTQPVGQLISRVTNDteVIRDLYVTVVATVLRSAAL--IGAMLvamfs 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 228 LLWVEIGISCLAGLAILVILLPLQSCIGKLFSSLRSKTAAFTDArirtMNEVITGMRIIKMYAWEKSFADlitnlRKKEI 307
Cdd:PRK10790 163 LDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDG----FNEVINGMSVIQQFRQQARFGE-----RMGEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 308 SKilgSSYLRGMN---MASFFIANkviLFVTFTTYVLLGnkitashvfvAMTLYG-----AVRLTVTLFFPSAIERVSE- 378
Cdd:PRK10790 234 SR---SHYMARMQtlrLDGFLLRP---LLSLFSALILCG----------LLMLFGfsasgTIEVGVLYAFISYLGRLNEp 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 379 -------------AVVSVRRIknFLLLDElpeRKAQEPSDGKAI----VHVQDFTAFWDKalDTPTLQGLSFTARPGELL 441
Cdd:PRK10790 298 lielttqqsmlqqAVVAGERV--FELMDG---PRQQYGNDDRPLqsgrIDIDNVSFAYRD--DNLVLQNINLSVPSRGFV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 442 AVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-------------IAYVSQQPWVFSGTVRSNILFGRKYEKERYEKVI 508
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvlrqgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQAL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 509 KACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlcICQTLHEKITI 588
Cdd:PRK10790 451 ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ--ALAAVREHTTL 528
|
570 580 590
....*....|....*....|....*....|....
gi 1958679184 589 LV-THQLQYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK10790 529 VViAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
421-615 |
1.49e-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: 97.37 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 421 KALDTPTLQgLSFTArPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------------RIAYVSQQPW 483
Cdd:cd03297 8 KRLPDFTLK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 484 VFSG-TVRSNILFGRKYeKERYEKVIKACALkkdLQLLedgDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:cd03297 86 LFPHlNVRENLAFGLKR-KRNREDRISVDEL---LDLL---GLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 562 LSAVDAEVGKHLFQLciCQTLHEKI---TILVTH---QLQYLkaASHILILKDGEMVQKG 615
Cdd:cd03297 159 FSALDRALRLQLLPE--LKQIKKNLnipVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
428-615 |
1.79e-22 |
|
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: 97.60 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAyvsqqpWVF---SG-----TVRSNILFG--- 496
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS------SLLglgGGfnpelTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 497 ----RKYEKERYEKVIKACALKKDLqlledgDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvgkh 572
Cdd:cd03220 112 lglsRKEIDEKIDEIIEFSELGDFI------DLPV-----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA---- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958679184 573 lFQL-CI----CQTLHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03220 177 -FQEkCQrrlrELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1097-1295 |
2.09e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 98.52 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMS 1175
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPqSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 II---PQVQ-----------------------LKEAIEDLPGKMDTE--LAESGSNFSVGQRQLVCLARAILKKNRILII 1227
Cdd:PRK13632 87 IIfqnPDNQfigatveddiafglenkkvppkkMKDIIDDLAKKVGMEdyLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1228 DEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESL 1295
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
425-616 |
2.61e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 425 TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------RIAYVSQQPWVFSG-TVRSN 492
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGRKYeKERYEKVIKACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:PRK10851 95 IAFGLTV-LPRRERPNAAAIKAKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958679184 572 HLFQLciCQTLHE--KIT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK10851 174 ELRRW--LRQLHEelKFTsVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
417-623 |
2.61e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 97.57 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 417 AFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQP- 482
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrRVQMVFQDPy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 483 ------WvfsgTVRSNI-----LFGRKYEKERYEKVIKACALKKDLQlledgdltvigDR-GATLSGGQKARVNLARAVY 550
Cdd:COG1124 90 aslhprH----TVDRILaeplrIHGLPDREERIAELLEQVGLPPSFL-----------DRyPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 551 QDADIYLLDDPLSAVDAEVGKHLFQLciCQTLHE--KIT-ILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKS 623
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNL--LKDLREerGLTyLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
424-647 |
3.19e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSG-TV 489
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 490 RSNILFGR--------KYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK11231 94 RELVAYGRspwlslwgRLSAEDNARVNQA---------MEQTRINHLADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 561 PLSAVD----AEVGKHLFQLcicqTLHEKITILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFLKSGvdfgsLLKKE- 634
Cdd:PRK11231 165 PTTYLDinhqVELMRLMREL----NTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPG-----LLRTVf 235
|
250
....*....|....*
gi 1958679184 635 NEEAE--PSPVPGTP 647
Cdd:PRK11231 236 DVEAEihPEPVSGTP 250
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
428-610 |
3.38e-22 |
|
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: 96.44 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG---------------RIAYVSQQPWVFSG-TVRS 491
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFGRKYEKeryeKVIKACALKKDLQLLED-GDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:cd03262 96 NITLAPIKVK----GMSKAEAEERALELLEKvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958679184 571 KHLFQLcICQTLHEKIT-ILVTHQLQY-LKAASHILILKDGE 610
Cdd:cd03262 172 GEVLDV-MKDLAEEGMTmVVVTHEMGFaREVADRVIFMDDGR 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
428-621 |
5.20e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWV-FSGTVRSNI 493
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 LFGRkyekeryekVIKACALKKDLQL----LEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDAD------IYLLDDPL 562
Cdd:PRK13548 98 AMGR---------APHGLSRAEDDALvaaaLAQVDLAHLAGRDyPQLSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 563 SAVDAEVGKHLFQLCICQTLHEKITIL-VTHQL----QYlkaASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLAHERGLAVIvVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEVL 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
392-616 |
7.78e-22 |
|
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: 101.13 E-value: 7.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 392 LDELPERKAQEPSDGKAIVHVQDFTA--FWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLV 469
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVRNLSKryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 470 SVHG----------------RIAYVSQQPwvFSG-----TVRSNI-----LFGRKYEKERYEKVikacalkkdLQLLEDG 523
Cdd:COG1123 323 LFDGkdltklsrrslrelrrRVQMVFQDP--YSSlnprmTVGDIIaeplrLHGLLSRAERRERV---------AELLERV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 524 DL--TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQTLHEK--ITIL-VTHQL---Q 595
Cdd:COG1123 392 GLppDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL--LRDLQRElgLTYLfISHDLavvR 469
|
250 260
....*....|....*....|.
gi 1958679184 596 YLkaASHILILKDGEMVQKGT 616
Cdd:COG1123 470 YI--ADRVAVMYDGRIVEDGP 488
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
424-624 |
9.07e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 101.44 E-value: 9.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLV-------------SVHGRIAYVSQQPWVFSGTVR 490
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvtqaSLRAAIGIVPQDTVLFNDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFGR-KYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD--- 566
Cdd:COG5265 450 YNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDsrt 529
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 567 -AEVGKHLFQLCICQTlhekiTILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:COG5265 530 eRAIQAALREVARGRT-----TLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQG 583
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
412-621 |
1.02e-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: 95.19 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 412 VQDFTAFWDKaldTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAY 477
Cdd:cd03224 3 VENLNAGYGK---SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 478 VSQQPWVFSG-TVRSNILFG-----RKYEKERYEKVikacalkkdLQL---LEDgdltVIGDRGATLSGGQKARVNLARA 548
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGayarrRAKRKARLERV---------YELfprLKE----RRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 549 VYQDADIYLLDDP---LS-AVDAEVGKHLFQLCicqtlHEKITILVTHqlQYLKAASHI----LILKDGEMVQKGTYTEF 620
Cdd:cd03224 147 LMSRPKLLLLDEPsegLApKIVEEIFEAIRELR-----DEGVTILLVE--QNARFALEIadraYVLERGRVVLEGTAAEL 219
|
.
gi 1958679184 621 L 621
Cdd:cd03224 220 L 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1098-1279 |
1.67e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 92.85 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGlHDLRKKMSI 1176
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQVqlkeaiEDLPGKMdtelaeSGS---NFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE-KFAQ 1252
Cdd:cd03230 78 LPEE------PSLYENL------TVRenlKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRElKKEG 145
|
170 180
....*....|....*....|....*...
gi 1958679184 1253 CTVLTIAHRLNTIID-SDKIMVLDSGRL 1279
Cdd:cd03230 146 KTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1098-1278 |
4.88e-21 |
|
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: 92.53 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTY---SLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALfrLSE---PEGKI-------------WI- 1157
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGElekLSGSVsvpgsiayvsqepWIq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1158 -----DKILtteiGLHDLRKKM--SIIPQVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEA 1230
Cdd:cd03250 79 ngtirENIL----FGKPFDEERyeKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1231 TANVDPRT-DELIQQKIREKFAQC-TVLTIAHRLNTIIDSDKIMVLDSGR 1278
Cdd:cd03250 155 LSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
424-649 |
6.42e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 6.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWV-FSGTV 489
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 490 RSNILFGRKYEKERYEKVIKACALKKDlQLLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVDae 568
Cdd:PRK09536 95 RQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 569 VGKHLFQLCICQTLHE--KITILVTHQLQYlkAASH---ILILKDGEMVQKGTYTEFLKSGVDFGSLlkkeneEAEP--- 640
Cdd:PRK09536 172 INHQVRTLELVRRLVDdgKTAVAAIHDLDL--AARYcdeLVLLADGRVRAAGPPADVLTADTLRAAF------DARTavg 243
|
250
....*....|
gi 1958679184 641 -SPVPGTPTL 649
Cdd:PRK09536 244 tDPATGAPTV 253
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
432-631 |
7.25e-21 |
|
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: 95.94 E-value: 7.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 432 SFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------------RIAYVSQQPWVFSG-TVRSNI 493
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFPHlSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 LFGRKYE-----KERYEKVIkacalkkdlQLLEDGDLTvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD- 566
Cdd:COG4148 99 LYGRKRApraerRISFDEVV---------ELLGIGHLL---DRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDl 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 567 ---AEVGKHLfqlcicQTLHEKITI---LVTHQL---QYLkaASHILILKDGEMVQKGTYTEFLkSGVDFGSLL 631
Cdd:COG4148 167 arkAEILPYL------ERLRDELDIpilYVSHSLdevARL--ADHVVLLEQGRVVASGPLAEVL-SRPDLLPLA 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1098-1285 |
7.73e-21 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 92.63 E-value: 7.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYsldGPL-VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE------PEGKIWID--KILTTEIGLH 1168
Cdd:cd03260 1 IELRDLNVYY---GDKhALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgapDEGEVLLDgkDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1169 DLRKK------------MSI---------IPQVQLKEAIED----------LPGKMDTELAESGsnFSVGQRQLVCLARA 1217
Cdd:cd03260 78 ELRRRvgmvfqkpnpfpGSIydnvayglrLHGIKLKEELDErveealrkaaLWDEVKDRLHALG--LSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1218 ILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEP 1285
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPT 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1097-1284 |
9.03e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.42 E-value: 9.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEI---GLHDLRK 1172
Cdd:COG2884 1 MIRFENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KMSIIPQ-------------------------VQLKEAIED------LPGKMDT---ELaeSGsnfsvGQRQLVCLARAI 1218
Cdd:COG2884 80 RIGVVFQdfrllpdrtvyenvalplrvtgksrKEIRRRVREvldlvgLSDKAKAlphEL--SG-----GEQQRVAIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 1219 LKKNRILIIDEATANVDPRT-DELIQ--QKIREkfAQCTVLtIA-HRLNtIIDS--DKIMVLDSGRLREYDE 1284
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETsWEIMEllEEINR--RGTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVRDEA 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
428-616 |
1.13e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAyvsqqpWVF---SG-----TVRSNILFG--- 496
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS------ALLelgAGfhpelTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 497 ----RKYEKERYEKVIkacalkkdlqlledgDLTVIGD------RgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG1134 116 lglsRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 567 AEvgkhlFQL-CIcQTLHE-----KITILVTHQLQYLKA-ASHILILKDGEMVQKGT 616
Cdd:COG1134 179 AA-----FQKkCL-ARIRElresgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
428-620 |
1.34e-20 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 92.24 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAV-----LGELPPTSGLVSVHG---------------RIAYVSQQPWVFSG 487
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 TVRSNILFGRKYEKERYEKVIKAcalkKDLQLLEDGDLT-VIGDR--GATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:cd03260 96 SIYDNVAYGLRLHGIKLKEELDE----RVEEALRKAALWdEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 565 VDAeVGKHLFQLCIcQTLHEKITIL-VTHQL-QYLKAASHILILKDGEMVQKGTYTEF 620
Cdd:cd03260 172 LDP-ISTAKIEELI-AELKKEYTIViVTHNMqQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
405-624 |
1.47e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 405 DGKAIVHVQDFTAFWDKAlDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG----------- 473
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 --RIAYVSQQP-WVFSG-TVRSNILFG-------RKYEKERYEKVIKACALKKDLQlledgdltvigDRGATLSGGQKAR 542
Cdd:PRK13635 80 rrQVGMVFQNPdNQFVGaTVQDDVAFGlenigvpREEMVERVDQALRQVGMEDFLN-----------REPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 543 VNLARAVYQDADIYLLDDPLSAVD----AEVgkhlfqLCICQTLHEK--ITIL-VTHQLQYLKAASHILILKDGEMVQKG 615
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDprgrREV------LETVRQLKEQkgITVLsITHDLDEAAQADRVIVMNKGEILEEG 222
|
....*....
gi 1958679184 616 TYTEFLKSG 624
Cdd:PRK13635 223 TPEEIFKSG 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
424-616 |
1.48e-20 |
|
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: 92.30 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRI-----AYVSQQPWVFSG-------TVRS 491
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRPVNTVFQNyalfphlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFG----RKYEKERYEKVIKACALkkdLQLLEDGDltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03300 92 NIAFGlrlkKLPKAEIKERVAEALDL---VQLEGYAN-----RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 568 EVGKHLfQLCIcQTLHEK--IT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:cd03300 164 KLRKDM-QLEL-KRLQKElgITfVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
428-619 |
1.98e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 91.73 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFG--------------RKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYL 557
Cdd:cd03219 96 VMVAaqartgsglllaraRREEREARERA---------EELLERVGLADLADRPAgELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 558 LDDPLSAVDAEVGKHLFQLcICQTLHEKITILVT-HQLQYLKA-ASHILILKDGEMVQKGTYTE 619
Cdd:cd03219 167 LDEPAAGLNPEETEELAEL-IRELRERGITVLLVeHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
424-622 |
2.69e-20 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 91.03 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQQPWVFSG-TVR 490
Cdd:cd03263 14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNI-LFGR---KYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:cd03263 94 EHLrFYARlkgLPKSEIKEEV---------ELLLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 566 DAeVGKHLfqlcICQTLHEKIT----ILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEfLK 622
Cdd:cd03263 165 DP-ASRRA----IWDLILEVRKgrsiILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQE-LK 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
428-623 |
4.99e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 90.68 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLV----------SVHGR----IAYVSQQPWVFSG-TVRSN 492
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklPMHKRarlgIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 I---LFGRKYEKERYEKVIKacalkkdlQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD-- 566
Cdd:cd03218 96 IlavLEIRGLSKKEREEKLE--------ELLEEFHITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpi 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 567 --AEVGKhlfqlcICQTLHEK-ITILVT-HQL-QYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:cd03218 168 avQDIQK------IIKILKDRgIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1098-1278 |
6.83e-20 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 88.40 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSldGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID--KILTTEIGLHDLRKKM 1174
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPdSGSILIDgeDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SIIPQ----VQLKEAIEDLpgkmdtELAESGsnfsvGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKF 1250
Cdd:cd03229 79 GMVFQdfalFPHLTVLENI------ALGLSG-----GQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQ 147
|
170 180 190
....*....|....*....|....*....|.
gi 1958679184 1251 AQ--CTVLTIAHRLNTIID-SDKIMVLDSGR 1278
Cdd:cd03229 148 AQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
424-567 |
7.77e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.69 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRI--------AYVSQQ----PWVfsgTVRS 491
Cdd:COG4525 19 PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPWL---NVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFGRKY----EKERYEKvikACALkkdLQL--LEDgdltVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:COG4525 96 NVAFGLRLrgvpKAERRAR---AEEL---LALvgLAD----FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGAL 165
|
..
gi 1958679184 566 DA 567
Cdd:COG4525 166 DA 167
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1093-1292 |
7.81e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 95.16 E-value: 7.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1093 PHE-GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE-PEGKIWIDKILTTEIGLHDL 1170
Cdd:PRK10789 308 PEGrGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSW 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSIIPQV----------------------QLKEA---------IEDLPGKMDTELAESGSNFSVGQRQLVCLARAIL 1219
Cdd:PRK10789 388 RSRLAVVSQTpflfsdtvannialgrpdatqqEIEHVarlasvhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALL 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 1220 KKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNP 1292
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
368-609 |
8.31e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 368 FFPSAIERVSEAVVSVRRIKNFLllDELpERKAQEPSDGKAIVHVQDFT-AFWDKALDTPT----LQGLSFTARPGELLA 442
Cdd:COG4178 317 WFVDNYQSLAEWRATVDRLAGFE--EAL-EAADALPEAASRIETSEDGAlALEDLTLRTPDgrplLEDLSLSLKPGERLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 443 VVGPVGAGKSSLLSAVLGELPPTSGLVSV--HGRIAYVSQQPWVFSGTVRSNILF---GRKYEKERYEKVIKACALKKDL 517
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGHLA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 518 QLLEDGDltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLcICQTLHEKITILVTHQLQYL 597
Cdd:COG4178 474 ERLDEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPGTTVISVGHRSTLA 547
|
250
....*....|..
gi 1958679184 598 KAASHILILKDG 609
Cdd:COG4178 548 AFHDRVLELTGD 559
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
431-615 |
9.41e-20 |
|
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: 89.09 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNILFGR- 497
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGLs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 498 ---KYEKERYEKVIKACAlKKDLQLLEDgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 574
Cdd:cd03298 97 pglKLTAEDRQAIEVALA-RVGLAGLEK-------RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958679184 575 QLCICQTLHEKITIL-VTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03298 169 DLVLDLHAETKMTVLmVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
424-623 |
1.34e-19 |
|
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: 89.76 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGL-VSVHG-------------RIAYVS---QQPWVFS 486
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGerrggedvwelrkRIGLVSpalQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 487 GTVRSNILFG--------RKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYL 557
Cdd:COG1119 95 ETVLDVVLSGffdsiglyREPTDEQRERA---------RELLELLGLAHLADRPfGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 558 LDDPLSAVDAEvGKHLF-----QLCicqTLHEKITILVTHQLQYLKAA-SHILILKDGEMVQKGTYTEFLKS 623
Cdd:COG1119 166 LDEPTAGLDLG-ARELLlalldKLA---AEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
403-616 |
2.23e-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: 87.85 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 403 PSDGKaiVHVQDFTAFWDKALdTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--------- 473
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDL-PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistiple 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 ----RIAYVSQQPWVFSGTVRSNI-LFGRKYEKERYEkvikacALKkdlqlledgdltvIGDRGATLSGGQKARVNLARA 548
Cdd:cd03369 79 dlrsSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIYG------ALR-------------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 549 VYQDADIYLLDDPLSAVDAEVgKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGT 616
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYAT-DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1097-1293 |
2.95e-19 |
|
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: 88.41 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGLHDL 1170
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPtSGSVLVDgTDLTLlsGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSII-------------------------PQVQLKEAIEDLPGKMD-TELAES-GSNFSVGQRQLVCLARAILKKNR 1223
Cdd:cd03258 81 RRRIGMIfqhfnllssrtvfenvalpleiagvPKAEIEERVLELLELVGlEDKADAyPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1224 ILIIDEATANVDPRTDELIQQ---KIREKFAqCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPE 1293
Cdd:cd03258 161 VLLCDEATSALDPETTQSILAllrDINRELG-LTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1096-1279 |
3.58e-19 |
|
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: 85.94 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTTEIGLHDLRKK 1173
Cdd:cd03216 12 GVKALDGVSLS---------------VRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVDgKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1174 MSIIPQvqlkeaiedlpgkmdtelaesgsnFSVGQRQLVCLARAILKKNRILIIDEATANVDPR-TDELIQQkIREKFAQ 1252
Cdd:cd03216 77 IAMVYQ------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERLFKV-IRRLRAQ 131
|
170 180
....*....|....*....|....*....
gi 1958679184 1253 -CTVLTIAHRLNTIID-SDKIMVLDSGRL 1279
Cdd:cd03216 132 gVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
417-639 |
4.61e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 417 AFWDKALdtptLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--RIAYVSQQPWVFSG-TVRSNI 493
Cdd:COG0488 7 SFGGRPL----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 L--FGRKYE-KERYEKVIKACALKKDL------------------------QLL-------EDGDLTVigdrgATLSGGQ 539
Cdd:COG0488 83 LdgDAELRAlEAELEELEAKLAEPDEDlerlaelqeefealggweaearaeEILsglgfpeEDLDRPV-----SELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 540 KARVNLARAVYQDADIYLLDDP---LsavDAE-VG---KHLfqlcicqtLHEKIT-ILVTHQLQYL-KAASHILILKDGE 610
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPtnhL---DLEsIEwleEFL--------KNYPGTvLVVSHDRYFLdRVATRILELDRGK 226
|
250 260 270
....*....|....*....|....*....|
gi 1958679184 611 MVQ-KGTYTEFLKSgvdfgsllKKENEEAE 639
Cdd:COG0488 227 LTLyPGNYSAYLEQ--------RAERLEQE 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
424-625 |
7.81e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 7.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSG-TV 489
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQENHINSRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 490 RSNILFGR------KYEKERYEKVIKAcalkkdLQLLedgDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:COG4604 93 RELVAFGRfpyskgRLTAEDREIIDEA------IAYL---DLEDLADRYLdELSGGQRQRAFIAMVLAQDTDYVLLDEPL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 563 SAVD----AEVGKHLFQLCicqtlHE--KITILVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKSGV 625
Cdd:COG4604 164 NNLDmkhsVQMMKLLRRLA-----DElgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPEV 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1088-1282 |
7.84e-19 |
|
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: 92.12 E-value: 7.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1088 PPPgwphEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKIlttEIG 1166
Cdd:COG4618 325 PRP----KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPtAGSVRLDGA---DLS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1167 LHDLRKKMSII---PQ-VQL-----------------------------KEAIEDLPGKMDTELAESGSNFSVGQRQLVC 1213
Cdd:COG4618 398 QWDREELGRHIgylPQdVELfdgtiaeniarfgdadpekvvaaaklagvHEMILRLPDGYDTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1214 LARAILKKNRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREY 1282
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
432-631 |
8.31e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 432 SFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG---RIAYVSQQPW--------VFSG-TVRSNILFG--- 496
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRPVsmlfqennLFSHlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 497 ----RKYEKERYEKVIKACALKKDLQLLEdgdltvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 572
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 573 LFQLC--ICQTlhEKITIL-VTHQLQ-YLKAASHILILKDGEMVQKGTYTEFLKSGVDFGSLL 631
Cdd:PRK10771 168 MLTLVsqVCQE--RQLTLLmVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1097-1292 |
9.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.12 E-value: 9.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIG-LHDLRKKM 1174
Cdd:PRK13644 1 MIRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SII---PQVQL--KEAIEDLP--------------GKMDTELAESG---------SNFSVGQRQLVCLARAILKKNRILI 1226
Cdd:PRK13644 80 GIVfqnPETQFvgRTVEEDLAfgpenlclppieirKRVDRALAEIGlekyrhrspKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1227 IDEATANVDPRTDELIQQKIREKFAQC-TVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNP 1292
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1090-1296 |
9.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.18 E-value: 9.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1090 PGWPHEGViVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTE--IG 1166
Cdd:PRK13637 14 EGTPFEKK-ALDNVNIE---------------IEDGEFVGLIGHTGSGKSTLIQHLNGLLKPtSGKIIIDGVDITDkkVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1167 LHDLRKKMSII---PQVQL---------------------------KEAIEDLPGKMDTELAESGSNFSVGQRQLVCLAR 1216
Cdd:PRK13637 78 LSDIRKKVGLVfqyPEYQLfeetiekdiafgpinlglseeeienrvKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1217 AILKKNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLreydepyVLLQNPE 1293
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKC-------ELQGTPR 230
|
...
gi 1958679184 1294 SLF 1296
Cdd:PRK13637 231 EVF 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
424-612 |
1.62e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.87 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG----------------RIAYVSQQPWVFSG 487
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -TVRSNILF-----GRKyEKERYEKVIKacALKKdlqlledgdltV-IGDRG----ATLSGGQKARVNLARAVYQDADIY 556
Cdd:COG2884 94 rTVYENVALplrvtGKS-RKEIRRRVRE--VLDL-----------VgLSDKAkalpHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 557 LLDDPLSAVDAEVGKHLFQLcicqtLHE----KITILV-THQLQYLKAASH-ILILKDGEMV 612
Cdd:COG2884 160 LADEPTGNLDPETSWEIMEL-----LEEinrrGTTVLIaTHDLELVDRMPKrVLELEDGRLV 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
409-615 |
1.64e-18 |
|
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: 85.88 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 409 IVHVQDFT-AFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGriAYVSQQPW---- 483
Cdd:cd03266 1 MITADALTkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAearr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 484 ---VFSG--------TVRSNIL-FGRKYEKERYEkvIKAcALKKDLQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQ 551
Cdd:cd03266 79 rlgFVSDstglydrlTARENLEyFAGLYGLKGDE--LTA-RLEELADRLGMEEL--LDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 552 DADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1097-1295 |
1.77e-18 |
|
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: 90.73 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGPlvlKHLTAL------IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG--- 1166
Cdd:COG1123 260 LLEVRNLSKRYPVRGK---GGVRAVddvsltLRRGETLGLVGESGSGKSTLARLLLGLLRPtSGSILFDGKDLTKLSrrs 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1167 LHDLRKKMSIIPQ----------------------------VQLKEAIEDLPGK--MDTELAE-SGSNFSVGQRQLVCLA 1215
Cdd:COG1123 337 LRELRRRVQMVFQdpysslnprmtvgdiiaeplrlhgllsrAERRERVAELLERvgLPPDLADrYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1216 RAILKKNRILIIDEATANVDPRTD----ELIqQKIREKFaQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQ 1290
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQaqilNLL-RDLQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
....*
gi 1958679184 1291 NPESL 1295
Cdd:COG1123 495 NPQHP 499
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
425-593 |
3.61e-18 |
|
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: 84.33 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 425 TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR------------IAYVSQQPWVFSG-TVRS 491
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFGRKyekeryekvIKACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvG 570
Cdd:TIGR01189 93 NLHFWAA---------IHGGAQRTIEDALAAVGLTGFEDLpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-G 162
|
170 180
....*....|....*....|....
gi 1958679184 571 KHLFQLCICQTLHEK-ITILVTHQ 593
Cdd:TIGR01189 163 VALLAGLLRAHLARGgIVLLTTHQ 186
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1097-1304 |
3.75e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.32 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGP-LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKM 1174
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SI--------------------------IPQVQLKEAIE---DLPGKMDTELAESgSNFSVGQRQLVCLARAILKKNRIL 1225
Cdd:PRK13650 84 GMvfqnpdnqfvgatveddvafglenkgIPHEEMKERVNealELVGMQDFKEREP-ARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1226 IIDEATANVDPRTD-ELIQ--QKIREKFaQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLfykmvQQ 1302
Cdd:PRK13650 163 ILDEATSMLDPEGRlELIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDL-----LQ 236
|
..
gi 1958679184 1303 LG 1304
Cdd:PRK13650 237 LG 238
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1097-1281 |
4.21e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 85.14 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIwidKILTTEIGLHdlRKKMS 1175
Cdd:COG1121 6 AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPtSGTV---RLFGKPPRRA--RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 IIPQ---------------VQL----------------KEAIEDLPGKMD-TELAE------SGsnfsvGQRQLVCLARA 1217
Cdd:COG1121 79 YVPQraevdwdfpitvrdvVLMgrygrrglfrrpsradREAVDEALERVGlEDLADrpigelSG-----GQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1218 ILKKNRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLRE 1281
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
428-567 |
5.17e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.16 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG----------RIAYVSQQ----PwvfSGTVRSNI 493
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLGHRnamkP---ALTVAENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 494 LFGRKYeKERYEKVIKACALKKDLQLLEDgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PRK13539 95 EFWAAF-LGGEELDIAAALEAVGLAPLAH-------LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
424-622 |
9.50e-18 |
|
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: 83.57 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQQPWVFSG-TVR 490
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNI-LFGRKY------EKERYEKVIKAcalkkdLQLLEDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:cd03265 92 ENLyIHARLYgvpgaeRRERIDELLDF------VGLLEAADRLV-----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 564 AVDAEVGKHLFQlcICQTLHEK--ITILVThqLQYL----KAASHILILKDGEMVQKGTYTEfLK 622
Cdd:cd03265 161 GLDPQTRAHVWE--YIEKLKEEfgMTILLT--THYMeeaeQLCDRVAIIDHGRIIAEGTPEE-LK 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
410-610 |
1.05e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 80.96 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTAFWDkalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--RIAYVSQqpwvfsg 487
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 tvrsnilfgrkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:cd03221 71 -----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958679184 568 EvGKHLFQlcicQTL--HEKITILVTHQLQYLKA-ASHILILKDGE 610
Cdd:cd03221 104 E-SIEALE----EALkeYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
431-620 |
1.29e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTARPGELLAVVGPVGAGKSSLLSaVLGELP-PTSGLVSVHGRIAYVSQQP-------------WVFSG-------TV 489
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIAGNHFDFSKTPsdkairelrrnvgMVFQQynlwphlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 490 RSNILfgrkyekERYEKVI---KACALKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PRK11124 100 QQNLI-------EAPCRVLglsKDQALARAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 566 DAEVGKHLFQlcICQTLHE-KIT-ILVTHQLQYL-KAASHILILKDGEMVQKGTYTEF 620
Cdd:PRK11124 173 DPEITAQIVS--IIRELAEtGITqVIVTHEVEVArKTASRVVYMENGHIVEQGDASCF 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
428-615 |
1.58e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 82.65 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------RIAYVSQQPWVFSG-TVRSNILF 495
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkniealrRIGALIEAPGFYPNlTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 496 GRKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 574
Cdd:cd03268 96 LARLLGIRKKRI---------DEVLDVVGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958679184 575 QLcICQTLHEKITILV-THQLQYL-KAASHILILKDGEMVQKG 615
Cdd:cd03268 167 EL-ILSLRDQGITVLIsSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
428-615 |
1.81e-17 |
|
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: 83.09 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPP---TSGLVSVHG----------RIAYVSQQP-WVFSGTVR--- 490
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqprkpdqfqkCVAYVRQDDiLLPGLTVRetl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 --SNILFGRKYEKERYEKVIKACALKKDLqlledGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA- 567
Cdd:cd03234 103 tyTAILRLPRKSSDAIRKKRVEDVLLRDL-----ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSf 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 568 ---EVGKHLFQLCicqtlHEKITILVT-HQ--LQYLKAASHILILKDGEMVQKG 615
Cdd:cd03234 178 talNLVSTLSQLA-----RRNRIVILTiHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
428-615 |
2.04e-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: 82.24 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGeLLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQQPwvfsgTVRSNIlf 495
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEF-----GVYPNF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 496 gRKYEKERYEKVIKACALKKD----LQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEvG 570
Cdd:cd03264 88 -TVREFLDYIAWLKGIPSKEVkarvDEVLELVNLGdRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE-E 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958679184 571 KHLFQLCICQTLHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03264 166 RIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1098-1296 |
2.08e-17 |
|
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: 83.12 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKM-- 1174
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPtSGEIFIDGEDIREQDPVELRRKIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 -----------------SIIPQV------QLKEAIEDLPGKMDTELAESG----SNFSVGQRQLVCLARAILKKNRILII 1227
Cdd:cd03295 80 viqqiglfphmtveeniALVPKLlkwpkeKIRERADELLALVGLDPAEFAdrypHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 1228 DEATANVDPRTDELIQQ---KIREKFAQcTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPESLF 1296
Cdd:cd03295 160 DEPFGALDPITRDQLQEefkRLQQELGK-TIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSPANDF 231
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
876-1073 |
2.08e-17 |
|
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: 84.19 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 876 GRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPWILIpLVPLSIIFVVLRRYFLETSRDVKRLESTTRS 955
Cdd:cd18559 95 GELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV-GIPLGLLYVPVNRVYAASSRQLKRLESVSKD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 956 PVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDlHSEAWFLFLTTSRWFAVRLDAICAVFVIVVAFGSLVLAKTLdAGQ 1035
Cdd:cd18559 174 PRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSL-AGL 251
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958679184 1036 VGLALSYSLTLMGMFQWSVRQSAEVENMMISVERVIEY 1073
Cdd:cd18559 252 VALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
424-621 |
2.81e-17 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 82.73 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG---------------RIAYVSQQPWVFSG- 487
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedltdskkdinklrrKVGMVFQQFNLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 TVRSNILFGRKYEKeryeKVIKACALKKDLQLLEdgdlTV-IGDRG----ATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:COG1126 93 TVLENVTLAPIKVK----KMSKAEAEERAMELLE----RVgLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 563 SAVD----AEVgkhlfqLCICQTL-HEKIT-ILVTHQLQY-LKAASHILILKDGEMVQKGTYTEFL 621
Cdd:COG1126 165 SALDpelvGEV------LDVMRDLaKEGMTmVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
385-622 |
3.14e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 385 RIKNF--LLLDELPERKA-------QEPSDGKAIVHVQDFTAFWDkalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLL 455
Cdd:COG0488 282 RIKALekLEREEPPRRDKtveirfpPPERLGKKVLELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 456 SAVLGELPPTSGLVsVHG---RIAYVSQQPWVFSG--TVRSNIlfgRKYEKERYEKVIKacalkkdlQLLED----GD-- 524
Cdd:COG0488 359 KLLAGELEPDSGTV-KLGetvKIGYFDQHQEELDPdkTVLDEL---RDGAPGGTEQEVR--------GYLGRflfsGDda 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 525 LTVIGDrgatLSGGQKARVNLARAVYQDADIYLLDDP-----LSAVDAevgkhL------FQLCIcqtlhekitILVTHQ 593
Cdd:COG0488 427 FKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA-----LeealddFPGTV---------LLVSHD 488
|
250 260 270
....*....|....*....|....*....|.
gi 1958679184 594 LQYLKA-ASHILILKDGEMVQK-GTYTEFLK 622
Cdd:COG0488 489 RYFLDRvATRILEFEDGGVREYpGGYDDYLE 519
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
93-386 |
3.31e-17 |
|
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: 83.75 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIFTLIEETTRVVQPIFLGKIIDYFEKydsddSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCH 172
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIP-----AGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 173 MIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIGVTILL----WVeigisclagLAILV-I 246
Cdd:cd07346 77 DLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWK---------LTLVAlL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 247 LLPLQSCIGKLFSSLRSKtaAFTDARIR------TMNEVITGMRIIKMYAWEKS----FADLITNLRKKEISKILGSSYL 316
Cdd:cd07346 148 LLPLYVLILRYFRRRIRK--ASREVRESlaelsaFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALF 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 317 RGMNMASFFIANkVILFVtFTTYVLLGNKITAShVFVAMTLYgavrlTVTLFFPsaIERVSE-------AVVSVRRI 386
Cdd:cd07346 226 SPLIGLLTALGT-ALVLL-YGGYLVLQGSLTIG-ELVAFLAY-----LGMLFGP--IQRLANlynqlqqALASLERI 292
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1095-1285 |
3.93e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.14 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1095 EGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKK 1173
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1174 MSIIPQ----------VQ--------------------LKEAIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILKKNR 1223
Cdd:PRK13635 83 VGMVFQnpdnqfvgatVQddvafglenigvpreemverVDQALRQV--GMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1224 ILIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEP 1285
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
402-616 |
4.14e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.00 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 402 EPSDGKAIVHVQDFTAFWDkalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIayVSQQ 481
Cdd:PRK09452 7 QPSSLSPLVELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD--ITHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 482 P-------WVFSG-------TVRSNILFGRKYEK----ERYEKVIKACALKKdlqlLEDgdltvIGDRGAT-LSGGQKAR 542
Cdd:PRK09452 82 PaenrhvnTVFQSyalfphmTVFENVAFGLRMQKtpaaEITPRVMEALRMVQ----LEE-----FAQRKPHqLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 543 VNLARAVYQDADIYLLDDPLSAVDAEVGKHLfQLCICQtLHEK--IT-ILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQM-QNELKA-LQRKlgITfVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1104-1275 |
4.67e-17 |
|
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: 81.43 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKIltteiGLHDLRKKMSIIPQ--- 1179
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtSGSIRVFGK-----PLEKERKRIGYVPQrrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ------------VQL----------------KEAIEDLPGKMD-TELAESG-SNFSVGQRQLVCLARAILKKNRILIIDE 1229
Cdd:cd03235 79 idrdfpisvrdvVLMglyghkglfrrlskadKAKVDEALERVGlSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958679184 1230 ATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIIDS-DKIMVLD 1275
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLN 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1093-1305 |
5.71e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.93 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1093 PHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSS---LISALFRLSE-PEGKIWIDKILTTEIGLH 1168
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDnPNSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1169 DLRKKMSII--------------------------PQVQLKEAIEDL---PGKMDTELAESgSNFSVGQRQLVCLARAIL 1219
Cdd:PRK13640 81 DIREKVGIVfqnpdnqfvgatvgddvafglenravPRPEMIKIVRDVladVGMLDYIDSEP-ANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1220 KKNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESL-- 1295
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKlkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLke 239
|
250
....*....|....*..
gi 1958679184 1296 -------FYKMVQQLGK 1305
Cdd:PRK13640 240 igldipfVYKLKNKLKE 256
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
418-616 |
6.15e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.97 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 418 FWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG----------------RIAYVSQQ 481
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalserelraarrKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 482 pwvF----SGTVRSNILF-----GRKyEKERYEKVikacalkkdLQLLEdgdLTVIGDRG----ATLSGGQKARVNLARA 548
Cdd:COG1135 91 ---FnllsSRTVAENVALpleiaGVP-KAEIRKRV---------AELLE---LVGLSDKAdaypSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 549 VYQDADIYLLDDPLSAVDAEVGKHLFQLciCQTLHEK--ITI-LVTHQLQYLKA-ASHILILKDGEMVQKGT 616
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDL--LKDINRElgLTIvLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1094-1304 |
7.15e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.11 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1094 HEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRK 1172
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVkSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KMSII---PQVQ---------------------------LKEAIEDLpGKMDTELAESGSnFSVGQRQLVCLARAILKKN 1222
Cdd:PRK13648 84 HIGIVfqnPDNQfvgsivkydvafglenhavpydemhrrVSEALKQV-DMLERADYEPNA-LSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1223 RILIIDEATANVDP--RTD--ELIQQKIREKfaQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLF-- 1296
Cdd:PRK13648 162 SVIILDEATSMLDPdaRQNllDLVRKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELTri 239
|
250
....*....|....*
gi 1958679184 1297 -------YKMVQQLG 1304
Cdd:PRK13648 240 gldlpfpIKINQMLG 254
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1097-1285 |
7.30e-17 |
|
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: 82.01 E-value: 7.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMS 1175
Cdd:COG1120 1 MLEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPsSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 IIPQVQlkEAIEDL-------------------PGKMDTELAE-------------------SGsnfsvGQRQLVCLARA 1217
Cdd:COG1120 79 YVPQEP--PAPFGLtvrelvalgryphlglfgrPSAEDREAVEealertglehladrpvdelSG-----GERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 1218 ILKKNRILIIDEATANVDPR----TDELIQQKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEP 1285
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAhqleVLELLRRLARER--GRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPP 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
426-595 |
8.15e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.67 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRI--------AYVSQQ----PWVfsgTVRSNI 493
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNegllPWR---NVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 LFGRkyekeRYEKVIKACALKKDLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 572
Cdd:PRK11248 92 AFGL-----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*
gi 1958679184 573 LfQLCICQTLHE--KITILVTHQLQ 595
Cdd:PRK11248 167 M-QTLLLKLWQEtgKQVLLITHDIE 190
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
428-593 |
9.12e-17 |
|
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: 80.23 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR------------IAYVSQQPWVFSG-TVRSNIL 494
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIKTTlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 495 FGRKYekeryekvikaCALKKDLQLLEDGDLTVIGDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 573
Cdd:cd03231 96 FWHAD-----------HSDEQVEEALARVGLNGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 1958679184 574 FQLCICQTLHEKITILVTHQ 593
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQ 184
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1098-1279 |
1.01e-16 |
|
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: 80.61 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGP--LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL---- 1170
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSIIPQ-----------------------------VQLKEAIE--DLPGKMD---TELaesgsnfSVGQRQLVCLAR 1216
Cdd:cd03255 81 RRHIGFVFQsfnllpdltalenvelplllagvpkkerrERAEELLErvGLGDRLNhypSEL-------SGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1217 AILKKNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRL 1279
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
421-611 |
1.07e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 421 KALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVFSG 487
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 TVRSNILFGRKYEKERYEKVikacALKKDLQLLEDgDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDa 567
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPDPA----IFLDDLERFAL-PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958679184 568 EVGKHLFQLCICQTLHEK-ITIL-VTHQLQYLKAASHILILKD--GEM 611
Cdd:PRK10247 170 ESNKHNVNEIIHRYVREQnIAVLwVTHDKDEINHADKVITLQPhaGEM 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
424-612 |
1.18e-16 |
|
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: 78.62 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQqpwvfsgtv 489
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevsfasprdarragIAMVYQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 490 rsnilfgrkyekeryekvikacalkkdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:cd03216 83 ---------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958679184 570 GKHLFQLcICQTLHEKITIL-VTHQLQYLKA-ASHILILKDGEMV 612
Cdd:cd03216 118 VERLFKV-IRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
428-590 |
1.44e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 81.24 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFG-------------------RKYEKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQD 552
Cdd:COG0411 100 VLVAaharlgrgllaallrlpraRREEREARERA---------EELLERVGLADRADEPAgNLSYGQQRRLEIARALATE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958679184 553 ADIYLLDDPLSAVDAEVGKHLFQLcIcQTLHE--KITILV 590
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAEL-I-RRLRDerGITILL 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1091-1281 |
1.59e-16 |
|
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: 80.62 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1091 GWPHEGVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHD 1169
Cdd:COG1124 12 GQGGRRVPVLKDVSLE---------------VAPGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 LRKKMSIIPQ-----------VQ--LKE--AIEDLPGKMDT--ELAES---GSNF--------SVGQRQLVCLARAILKK 1221
Cdd:COG1124 77 FRRRVQMVFQdpyaslhprhtVDriLAEplRIHGLPDREERiaELLEQvglPPSFldryphqlSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1222 NRILIIDEATANVDPRT-DELIQ--QKIREKFaQCTVLTIAHRLNtIID--SDKIMVLDSGRLRE 1281
Cdd:COG1124 157 PELLLLDEPTSALDVSVqAEILNllKDLREER-GLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVE 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
424-591 |
2.74e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQqpwvFSG---- 487
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQ----FDNldle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -TVRSNIL-FGRKY--EKERYEKVIKAcalkkdlqLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK13536 129 fTVRENLLvFGRYFgmSTREIEAVIPS--------LLEFARLESKADaRVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180
....*....|....*....|....*....
gi 1958679184 563 SAVDAEvGKHLFQLCICQTLHEKITILVT 591
Cdd:PRK13536 201 TGLDPH-ARHLIWERLRSLLARGKTILLT 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
407-603 |
3.56e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.82 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 407 KAIVHVQDFTAFWDKaldTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAV--LGELPP---TSGLVSVHGR------- 474
Cdd:PRK14239 3 EPILQVSDLSVYYNK---KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHniysprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 475 --------IAYVSQQPWVFSGTVRSNILFGRKYEKERYEKVIKAcALKKDLQ--LLEDGDLTVIGDRGATLSGGQKARVN 544
Cdd:PRK14239 80 dtvdlrkeIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKgaSIWDEVKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 545 LARAVYQDADIYLLDDPLSAVDA-EVGKhlfqlcICQTLH---EKITIL-VTHQLQylkAASHI 603
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPiSAGK------IEETLLglkDDYTMLlVTRSMQ---QASRI 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
400-595 |
3.95e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 79.70 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 400 AQEPSDGKAIVHVQDFTAFWDkalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAV--LGELPP---TSGLVSVHG- 473
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLDGe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 --------------RIAYVSQQPWVFSGTVRSNILFG--------RKYEKERYEKVIKACAL----KKDLQlledgdltv 527
Cdd:COG1117 79 diydpdvdvvelrrRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSELDEIVEESLRKAALwdevKDRLK--------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 528 igDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD-AEVGKhlfqlcICQTLHE---KITI-LVTHQLQ 595
Cdd:COG1117 150 --KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK------IEELILElkkDYTIvIVTHNMQ 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
428-566 |
4.35e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.30 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 493 IL----FGRKYEKERYEKVIkacalkkdlQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:COG1137 99 ILavleLRKLSKKEREERLE---------ELLEEFGITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
160-577 |
4.41e-16 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 83.64 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 160 QCAgMRIRVAMCHMIYRKAL------RLSNSamgKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTI------ 227
Cdd:TIGR00954 161 ELK-LRFRVRLTRYLYSKYLsgftfyKVSNL---DSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSfkllta 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 228 LLWVEIGISCLAGLAILVILLPLQSCIGKLfsslrSKTAAFTDARIRTMN-EVITGMRIIKMYAWEK--------SFADL 298
Cdd:TIGR00954 237 LGSVGPAGLFAYLFATGVVLTKLRPPIGKL-----TVEEQALEGEYRYVHsRLIMNSEEIAFYQGNKveketvmsSFYRL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 299 ITNLRKKEISKIlgssylrGMNMASFFIA----NKVILFVTFTTYVLLGNK--ITASHVFVAMTLYGAVRLTVTLffPSA 372
Cdd:TIGR00954 312 VEHLNLIIKFRF-------SYGFLDNIVAkytwSAVGLVAVSIPIFDKTHPafLEMSEEELMQEFYNNGRLLLKA--ADA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 373 IERVSEAVVSVRRIKNFLL-LDEL----------PERKAQEPSD--------------GKAIVHVQD-FTAFWDKALDTP 426
Cdd:TIGR00954 383 LGRLMLAGRDMTRLAGFTArVDTLlqvlddvksgNFKRPRVEEIesgreggrnsnlvpGRGIVEYQDnGIKFENIPLVTP 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 427 T----LQGLSFTARPGELLAVVGPVGAGKSSLLSaVLGELPPT-SGLVSV--HGRIAYVSQQPWVFSGTVRSNILFGRKY 499
Cdd:TIGR00954 463 NgdvlIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVyGGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIYPDSS 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 500 EkERYEKVIKACALKKDLQLL-------EDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH 572
Cdd:TIGR00954 542 E-DMKRRGLSDKDLEQILDNVqlthileREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY 620
|
....*
gi 1958679184 573 LFQLC 577
Cdd:TIGR00954 621 MYRLC 625
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
431-623 |
5.31e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 79.50 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR------IAYVSQQpwvfsgtVR-----SNILFGRKY 499
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdYKYRCKH-------IRmifqdPNTSLNPRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 500 -----------------EKERYEKVIKAcaLKKdLQLLEDGDLTVIgdrgATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:COG4167 105 nigqileeplrlntdltAEEREERIFAT--LRL-VGLLPEHANFYP----HMLSSGQKQRVALARALILQPKIIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 563 SAVDAEVGKHLFQLCIcqTLHEKIT---ILVTHQLQYLKAAS-HILILKDGEMVQKGTYTEFLKS 623
Cdd:COG4167 178 AALDMSVRSQIINLML--ELQEKLGisyIYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1098-1278 |
7.44e-16 |
|
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: 75.95 E-value: 7.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILtteiglhdlrkKMSI 1176
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPdEGIVTWGSTV-----------KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQvqlkeaiedlpgkmdtelaesgsnFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKfaQCTVL 1256
Cdd:cd03221 68 FEQ------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY--PGTVI 121
|
170 180
....*....|....*....|....*
gi 1958679184 1257 TIAH-R--LNTIIdsDKIMVLDSGR 1278
Cdd:cd03221 122 LVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1104-1287 |
8.57e-16 |
|
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: 78.31 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKI---LTTEIGLHDLRKKMSIIPQ 1179
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEdisGLSEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 -------------VQL---------KEAIED----------LPG---KMDTELaeSGsnfsvGQRQLVCLARAILKKNRI 1224
Cdd:cd03261 85 sgalfdsltvfenVAFplrehtrlsEEEIREivlekleavgLRGaedLYPAEL--SG-----GMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1225 LIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIID-SDKIMVLDSGR---------LREYDEPYV 1287
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKivaegtpeeLRASDDPLV 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
416-622 |
9.65e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 79.32 E-value: 9.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 416 TAFWDKALDTptlqgLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG---------------RIAYVSQ 480
Cdd:PRK13637 16 TPFEKKALDN-----VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 481 QP--WVFSGTVRSNILFGRK----YEKERYEKVIKACALKKDlqlledgDLTVIGDRGA-TLSGGQKARVNLARAVYQDA 553
Cdd:PRK13637 91 YPeyQLFEETIEKDIAFGPInlglSEEEIENRVKRAMNIVGL-------DYEDYKDKSPfELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 554 DIYLLDDPLSAVDAEVGKHLFQLciCQTLHEK---ITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLK 622
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNK--IKELHKEynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
424-619 |
1.27e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.58 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-IAY--------------VSQQP--WVFS 486
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYdkksllevrktvgiVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 487 GTVRSNILFG---RKYEKERYEKVIKAcALKKdlqlledgdltvIGDRGAT------LSGGQKARVNLARAVYQDADIYL 557
Cdd:PRK13639 94 PTVEEDVAFGplnLGLSKEEVEKRVKE-ALKA------------VGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 558 LDDPLSAVDAEVGKHLFQLcicqtLH----EKITILV-THQLQYL-KAASHILILKDGEMVQKGTYTE 619
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKL-----LYdlnkEGITIIIsTHDVDLVpVYADKVYVMSDGKIIKEGTPKE 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1098-1295 |
1.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.72 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPLVLKHLTAL---IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI-DKILTTEIG---LHD 1169
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNIsfeLEEGSFVALVGHTGSGKSTLMQHFNALLKPsSGTITIaGYHITPETGnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 LRKKMSII---PQVQLKE--AIEDL---PGK--------------------MDTELAE-SGSNFSVGQRQLVCLARAILK 1220
Cdd:PRK13641 83 LRKKVSLVfqfPEAQLFEntVLKDVefgPKNfgfsedeakekalkwlkkvgLSEDLISkSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1221 KNRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPESL 1295
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
428-615 |
1.69e-15 |
|
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: 76.44 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPP--TSGLVSVHGR----------IAYVSQQPWVFSG-TVRSNIL 494
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrkiIGYVPQDDILHPTlTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 495 FgrkyekeryekvikACALKKdlqlledgdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLF 574
Cdd:cd03213 105 F--------------AAKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958679184 575 QLC--ICQTlhEKITILVTHQLQYL--KAASHILILKDGEMVQKG 615
Cdd:cd03213 152 SLLrrLADT--GRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
424-619 |
1.92e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.50 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------IAYVSQQ----PWVfsgT 488
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyalyPHM---S 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 489 VRSNILFG---RKYEKERYEKVIKACAlkkdlQLLEDGDLTvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK11650 93 VRENMAYGlkiRGMPKAEIEERVAEAA-----RILELEPLL---DRKpRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 565 VDAevgKHLFQLCI-CQTLHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:PRK11650 165 LDA---KLRVQMRLeIQRLHRRLkttSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
412-613 |
2.01e-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: 77.97 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 412 VQDFTAFWDKAlDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLgELPPTSGLVSVHG-----------RIAY--V 478
Cdd:cd03289 5 VKDLTAKYTEG-GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFgvI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 479 SQQPWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLL 558
Cdd:cd03289 83 PQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 559 DDPLSAVDA-------EVGKHLFQLCicqtlhekITILVTHQLQYLKAASHILILKDGEMVQ 613
Cdd:cd03289 163 DEPSAHLDPityqvirKTLKQAFADC--------TVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1098-1261 |
2.45e-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: 74.88 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFtYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALfrlsepeGKIWidKILTTEIGLHDLRKKMSI- 1176
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AGLW--PWGSGRIGMPEGEDLLFLp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 ----IPQVQLKEAIedlpgkmdteLAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAq 1252
Cdd:cd03223 71 qrpyLPLGTLREQL----------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI- 139
|
....*....
gi 1958679184 1253 cTVLTIAHR 1261
Cdd:cd03223 140 -TVISVGHR 147
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
410-615 |
2.50e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 76.17 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTafwdKALDTPT-LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG---------RIAYVS 479
Cdd:cd03269 1 LEVENVT----KRFGRVTaLDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 480 QQPWVFSG-TVRSNIL-FGRKYEKERYEkvikacALKKDLQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIY 556
Cdd:cd03269 77 EERGLYPKmKVIDQLVyLAQLKGLKKEE------ARRRIDEWLERLELSEYANkRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 557 LLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
403-613 |
3.25e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 76.70 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 403 PSDGKAIVHVQDFTafwdKALDTPT-----LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG---- 473
Cdd:COG4181 2 SSSSAPIIELRGLT----KTVGTGAgeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 ----------RIAYVSqqpWVF-------SGTVRSNI-----LFGRKYEKERYEKVIKACALkkdlqlledgdltviGDR 531
Cdd:COG4181 78 aldedararlRARHVG---FVFqsfqllpTLTALENVmlpleLAGRRDARARARALLERVGL---------------GHR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 532 G----ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKH----LFQLCICQ--TLhekitILVTHQLQYLKAAS 601
Cdd:COG4181 140 LdhypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQiidlLFELNRERgtTL-----VLVTHDPALAARCD 214
|
250
....*....|..
gi 1958679184 602 HILILKDGEMVQ 613
Cdd:COG4181 215 RVLRLRAGRLVE 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
424-608 |
4.53e-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: 74.11 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLsAVLGEL-PPTSGLVSVHGR--IAYVSQQPWVFSGTVRSNILfgrkYE 500
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLwPWGSGRIGMPEGedLLFLPQRPYLPLGTLREQLI----YP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 501 KERyekvikacalkkdlqlledgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCicq 580
Cdd:cd03223 88 WDD------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL--- 134
|
170 180
....*....|....*....|....*....
gi 1958679184 581 tLHEKITIL-VTHQLQYLKAASHILILKD 608
Cdd:cd03223 135 -KELGITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
409-615 |
6.77e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.70 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 409 IVHVQDFTAFWDKalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAYVSQQPW----- 483
Cdd:PRK13647 4 IIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvrskv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 484 ----------VFSGTVRSNILFG-------RKYEKERYEKVIKACALKKdlqlledgdltvIGDRGAT-LSGGQKARVNL 545
Cdd:PRK13647 82 glvfqdpddqVFSSTVWDDVAFGpvnmgldKDEVERRVEEALKAVRMWD------------FRDKPPYhLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 546 ARAVYQDADIYLLDDPLSAVDAEVGKHLFQlcICQTLHE--KITILVTHQLQY-LKAASHILILKDGEMVQKG 615
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
426-620 |
8.31e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQPWVFSG-TVR 490
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 SNILFGRKYEKERYEKVikaCALKKDLQLLEDGDLTvigdrGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVG 570
Cdd:PRK15439 105 ENILFGLPKRQASMQKM---KQLLAALGCQLDLDSS-----AGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 571 KHLFQLcICQTLHEKITIL-VTHQLQYLKA-ASHILILKDGEMVQKGTYTEF 620
Cdd:PRK15439 177 ERLFSR-IRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
429-593 |
1.10e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 429 QGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIayVSQQPWVFsgtvRSNILF-----GRKYEKER 503
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--IRRQRDEY----HQDLLYlghqpGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 504 YEKVIKACALKkdlQLLEDGD----LTVIGDRG------ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEV 569
Cdd:PRK13538 92 LENLRFYQRLH---GPGDDEAlweaLAQVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvARL 168
|
170 180
....*....|....*....|....*.
gi 1958679184 570 GKHLFQLCicqtlhEK--ITILVTHQ 593
Cdd:PRK13538 169 EALLAQHA------EQggMVILTTHQ 188
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
428-620 |
1.41e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLL----SAVLGELPPTSGL------VSVHGRIA-----------YVSQQ-PWVF 485
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIellgrtVQREGRLArdirksrantgYIFQQfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 486 SGTVRSNILFG------------RKYEKERYEKVIKAcalkkdlqlledgdLTVIG------DRGATLSGGQKARVNLAR 547
Cdd:PRK09984 100 RLSVLENVLIGalgstpfwrtcfSWFTREQKQRALQA--------------LTRVGmvhfahQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 548 AVYQDADIYLLDDPLSAVDAEVGKhlfqlCICQTLH-----EKITILVT-HQLQY-LKAASHILILKDGEMVQKGTYTEF 620
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESAR-----IVMDTLRdinqnDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
428-594 |
1.44e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR----------IAYVSQQP---WVFSGTVRSNIL 494
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 495 FGR-------KYEKERYEKVIKACALKKDLQLLEDGDltvIGDrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PRK15056 103 MGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*...
gi 1958679184 568 EVGKHLFQLcICQTLHEKITILV-THQL 594
Cdd:PRK15056 176 KTEARIISL-LRELRDEGKTMLVsTHNL 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1098-1278 |
1.65e-14 |
|
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: 74.53 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG---LHDLRKK 1173
Cdd:cd03256 1 IEVENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPtSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1174 MSIIPQ-VQLKE---AIED-----------------LPGKMDTELA-----ESG---------SNFSVGQRQLVCLARAI 1218
Cdd:cd03256 80 IGMIFQqFNLIErlsVLENvlsgrlgrrstwrslfgLFPKEEKQRAlaaleRVGlldkayqraDQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 1219 LKKNRILIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGR 1278
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAREyADRIVGLKDGR 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
428-612 |
1.82e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGRkyEKER-----YEKVIKACAlkkdlQLLEDGDLTV-IGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSA-V 565
Cdd:COG1129 100 IFLGR--EPRRgglidWRAMRRRAR-----ELLARLGLDIdPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASlT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958679184 566 DAEVgKHLFQlcICQTLHEK-ITIL-VTHQLQYLKA-ASHILILKDGEMV 612
Cdd:COG1129 173 EREV-ERLFR--IIRRLKAQgVAIIyISHRLDEVFEiADRVTVLRDGRLV 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1097-1279 |
1.93e-14 |
|
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: 73.35 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVnfTYSLDGPL------VLKHLTALIKSREKVGIVGRTGAGKSSLISALF-RLSEP--EGKIWIDKIlttEIGL 1167
Cdd:cd03213 3 TLSFRNL--TVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLgvSGEVLINGR---PLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1168 HDLRKKM-------SIIPQVQLKEAIEdlpgkMDTELaesgSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDE 1240
Cdd:cd03213 78 RSFRKIIgyvpqddILHPTLTVRETLM-----FAAKL----RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958679184 1241 LIQQKIReKFAQ--CTVLTIAHRLNTIIDS--DKIMVLDSGRL 1279
Cdd:cd03213 149 QVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQGRV 190
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
409-626 |
2.14e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.13 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 409 IVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RI 475
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrrKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 476 AYVSQQP--WVFSGTVRSNILFGRKYEKERYEKVIKacalKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDA 553
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 554 DIYLLDDPLSAVDAeVGKHLfqlcICQTLHE-----KITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSGVD 626
Cdd:PRK13642 160 EIIILDESTSMLDP-TGRQE----IMRVIHEikekyQLTVLsITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1097-1281 |
2.66e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.54 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL--- 1170
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 -RKKMSIIPQ-------------VQL----------------KEAIE--DLPGKMD---TELaesgsnfSVGQRQLVCLA 1215
Cdd:COG1136 84 rRRHIGFVFQffnllpeltalenVALplllagvsrkerreraRELLErvGLGDRLDhrpSQL-------SGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1216 RAILKKNRILIIDEATANVDPRT-DELIQ--QKIREKFaQCTVLTIAHRLNTIIDSDKIMVLDSGRLRE 1281
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTgEEVLEllRELNREL-GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
392-561 |
2.84e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 392 LDELPERKAQEPsdGKAIVHVQDFTAfwdkaldTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSV 471
Cdd:COG1129 241 LEDLFPKRAAAP--GEVVLEVEGLSV-------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 472 HGR--------------IAYVS----QQPWVFSGTVRSNI------------LFGRKYEKERYEKVIKACALKkdlqlLE 521
Cdd:COG1129 312 DGKpvrirsprdairagIAYVPedrkGEGLVLDLSIRENItlasldrlsrggLLDRRRERALAEEYIKRLRIK-----TP 386
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958679184 522 DGDLTVigdrgATLSGG--QKarVNLARAVYQDADIYLLDDP 561
Cdd:COG1129 387 SPEQPV-----GNLSGGnqQK--VVLAKWLATDPKVLILDEP 421
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1098-1294 |
3.14e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.50 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPLVlkhlTAL------IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGL 1167
Cdd:COG1135 2 IELENLSKTFPTKGGPV----TALddvsltIEKGEIFGIIGYSGAGKSTLIRCINLLERPtSGSVLVDgVDLTAlsEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1168 HDLRKKMSIIPQ-------------VQL--------KEAIE----------DLPGKMDTELAE-SGsnfsvGQRQLVCLA 1215
Cdd:COG1135 78 RAARRKIGMIFQhfnllssrtvaenVALpleiagvpKAEIRkrvaellelvGLSDKADAYPSQlSG-----GQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1216 RAILKKNRILIIDEATANVDPRTD----ELIqQKIREKFaQCTVLTIAHRLNTI--IdSDKIMVLDSGRLREYDEPYVLL 1289
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTrsilDLL-KDINREL-GLTIVLITHEMDVVrrI-CDRVAVLENGRIVEQGPVLDVF 229
|
....*
gi 1958679184 1290 QNPES 1294
Cdd:COG1135 230 ANPQS 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
428-615 |
3.39e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.02 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSV--------------HGRIAYVSQQ-PWVFSG----- 487
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQLRQHvGFVFQNfnlfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 --TVRSNILFGRKYEKeryeKVIKACALKKDLQLLEDGDLTviGDRGA---TLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK11264 99 hrTVLENIIEGPVIVK----GEPKEEATARARELLAKVGLA--GKETSyprRLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 563 SAVDAE-VGKHLfqLCICQTLHEKIT-ILVTHQLQYLK-AASHILILKDGEMVQKG 615
Cdd:PRK11264 173 SALDPElVGEVL--NTIRQLAQEKRTmVIVTHEMSFARdVADRAIFMDQGRIVEQG 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
428-625 |
5.43e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.67 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-------------IAYVSQQ-PWVFSGTVRSNI 493
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 LFGR-----------KYEKERYEKVIKACALKKDLQLLEDgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK10575 107 AIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 563 SAVDaeVGKHLFQLCICQTLHEKITILVTHQLQYLKAAS----HILILKDGEMVQKGTYTEFLKSGV 625
Cdd:PRK10575 176 SALD--IAHQVDVLALVHRLSQERGLTVIAVLHDINMAArycdYLVALRGGEMIAQGTPAELMRGET 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1093-1261 |
6.49e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.38 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1093 PHEGVIVFDNVNFtYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSePEGkiwidkilTTEIGLHDLRK 1172
Cdd:COG4178 358 SEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW-PYG--------SGRIARPAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KM-----SIIPQVQLKEAI-----------------------EDLPGKMDTElAESGSNFSVGQRQLVCLARAILKKNRI 1224
Cdd:COG4178 428 VLflpqrPYLPLGTLREALlypataeafsdaelrealeavglGHLAERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958679184 1225 LIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHR 1261
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
393-638 |
6.89e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.26 E-value: 6.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 393 DELPERKAQEPSDGKAIVHVQDFTAFWDkalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVH 472
Cdd:PRK11607 3 DAIPRPQAKTRKALTPLLEIRNLTKSFD---GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 473 GR-IAYVS--QQP--WVFSG-------TVRSNILFGRKyeKERYEKVIKACALKKDLQLLEDGDLTviGDRGATLSGGQK 540
Cdd:PRK11607 80 GVdLSHVPpyQRPinMMFQSyalfphmTVEQNIAFGLK--QDKLPKAEIASRVNEMLGLVHMQEFA--KRKPHQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 541 ARVNLARAVYQDADIYLLDDPLSAVDAEVgKHLFQLCICQTLhEKI---TILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKL-RDRMQLEVVDIL-ERVgvtCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGE 233
|
250 260 270
....*....|....*....|....*....|....
gi 1958679184 617 ------------YTEFLKSGVDFGSLLKKENEEA 638
Cdd:PRK11607 234 peeiyehpttrySAEFIGSVNVFEGVLKERQEDG 267
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1101-1277 |
7.12e-14 |
|
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: 73.74 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1101 DNVNFT-YSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKI-------------WI------DK 1159
Cdd:cd03291 38 NNLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPsEGKIkhsgrisfssqfsWImpgtikEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1160 ILtteIGL-HDLRKKMSIIPQVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRT 1238
Cdd:cd03291 118 II---FGVsYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958679184 1239 DELIQQKIREKF-AQCTVLTIAHRLNTIIDSDKIMVLDSG 1277
Cdd:cd03291 195 EKEIFESCVCKLmANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1098-1295 |
7.36e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.90 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGP---LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI-DKILTTEI---GLHD 1169
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPtSGTVTIgERVITAGKknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 LRKKMSII---PQVQL---------------------------KEAIEdLPGKMDTELAESGSNFSVGQRQLVCLARAIL 1219
Cdd:PRK13634 83 LRKKVGIVfqfPEHQLfeetvekdicfgpmnfgvseedakqkaREMIE-LVGLPEELLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1220 KKNRILIIDEATANVDPRTdeliQQKIREKFAQC------TVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNP 1292
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKG----RKEMMEMFYKLhkekglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
...
gi 1958679184 1293 ESL 1295
Cdd:PRK13634 238 DEL 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1113-1280 |
7.92e-14 |
|
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: 72.02 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1113 LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTE--------IGLHD----LRKKMSIIPQ 1179
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDaGFATVDGFDVVKepaearrrLGFVSdstgLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 V------------QLKEAIEDLPGKMDTE--LAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQK 1245
Cdd:cd03266 99 LeyfaglyglkgdELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958679184 1246 IRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLR 1280
Cdd:cd03266 179 IRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
407-630 |
8.55e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.23 E-value: 8.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 407 KAIVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------- 473
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 RIAYVSQQP-WVFSG-TVRSNILFGRKYE----KERYEKVIKAcalkkdLQLLedgDLTVIGDRG-ATLSGGQKARVNLA 546
Cdd:PRK13650 82 KIGMVFQNPdNQFVGaTVEDDVAFGLENKgiphEEMKERVNEA------LELV---GMQDFKEREpARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 547 RAVYQDADIYLLDDPLSAVDAEVGKHLFQlcICQTLHEK--ITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIK--TIKGIRDDyqMTVIsITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
....*..
gi 1958679184 624 GVDFGSL 630
Cdd:PRK13650 231 GNDLLQL 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
442-619 |
9.06e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.53 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 442 AVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------------IAYVSQQPWVFSG-TVRSNILFG-RKYEKE 502
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQDARLFPHyKVRGNLRYGmAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 503 RYEKVIKACALKKdlqLLedgdltvigDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA----EVGKHLfqlc 577
Cdd:PRK11144 108 QFDKIVALLGIEP---LL---------DRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYL---- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958679184 578 icQTLHE--KITIL-VTHQLQ-YLKAASHILILKDGEMVQKGTYTE 619
Cdd:PRK11144 172 --ERLAReiNIPILyVSHSLDeILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
428-616 |
1.05e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.57 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPtSGLVSVHGRI-------------AYVSQQ-PWVFSGTVRSNI 493
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPlsdwsaaelarhrAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 LFGRkYEKERYEKVIKACAlkkdlQLLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQ-------DADIYLLDDPLSAV 565
Cdd:COG4138 91 ALHQ-PAGASSEAVEQLLA-----QLAEALGLEDKLSRPLTqLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 566 D----AEVGKHLFQLCICQtlhekITILV-THQLQY-LKAASHILILKDGEMVQKGT 616
Cdd:COG4138 165 DvaqqAALDRLLRELCQQG-----ITVVMsSHDLNHtLRHADRVWLLKQGKLVASGE 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
424-611 |
1.17e-13 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 71.67 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG---------RIAYVSQQ-PWVFSG------ 487
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKiGVVFQDfrllpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -TVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGdltvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:cd03292 93 rNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHK----HRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958679184 567 AEVGKHLFQLciCQTLHEK-ITILV-THQLQYLKAASH-ILILKDGEM 611
Cdd:cd03292 169 PDTTWEIMNL--LKKINKAgTTVVVaTHAKELVDTTRHrVIALERGKL 214
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
410-632 |
1.39e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 72.25 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTAFWDKALdTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIA 476
Cdd:cd03288 20 IKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 477 YVSQQPWVFSGTVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIY 556
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 557 LLDDPLSAVDAEVgKHLFQLCICQTLHEKITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFL--KSGVdFGSLLK 632
Cdd:cd03288 179 IMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaqEDGV-FASLVR 254
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
428-615 |
1.75e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.92 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--------------------------RIAYVSQQ 481
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 482 --PWVFSgTVRSNIL--------FGRKYEKERYEKVIKACALKKDLQlledgdltviGDRGATLSGGQKARVNLARAVYQ 551
Cdd:PRK10619 101 fnLWSHM-TVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 552 DADIYLLDDPLSAVDAE-VGKhlfQLCICQTLHE--KITILVTHQLQYLK-AASHILILKDGEMVQKG 615
Cdd:PRK10619 170 EPEVLLFDEPTSALDPElVGE---VLRIMQQLAEegKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEG 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1104-1265 |
1.77e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWID--------KILTTEIGLHDLRKKMS 1175
Cdd:PRK14258 12 NLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgrveffnqNIYERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 II-------------------------PQVQLKEAIE------DLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRI 1224
Cdd:PRK14258 92 MVhpkpnlfpmsvydnvaygvkivgwrPKLEIDDIVEsalkdaDLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958679184 1225 LIIDEATANVDP----RTDELIQQ-KIRekfAQCTVLTIAHRLNTI 1265
Cdd:PRK14258 172 LLMDEPCFGLDPiasmKVESLIQSlRLR---SELTMVIVSHNLHQV 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1095-1279 |
1.89e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1095 EGVIVFDNVNFTYSLDG----PLVLKHLTALIKSREKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWIDKILTTEIG- 1166
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSE--GKVYVDGLDTSDEEn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1167 LHDLRKKMSII---PQVQLKEAI--EDL----------PGKMDTELAESGSN-------------FSVGQRQLVCLARAI 1218
Cdd:PRK13633 80 LWDIRNKAGMVfqnPDNQIVATIveEDVafgpenlgipPEEIRERVDESLKKvgmyeyrrhaphlLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 1219 LKKNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIIDSDKIMVLDSGRL 1279
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
423-642 |
1.96e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.55 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 423 LDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------------RIAYVSQQP--W 483
Cdd:PRK13641 18 MEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFPeaQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 484 VFSGTVRSNILFGRK----YEKERYEKVIKacALKKdLQLLEDgdltVIGDRGATLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK13641 98 LFENTVLKDVEFGPKnfgfSEDEAKEKALK--WLKK-VGLSED----LISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 560 DPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSgvdfGSLLKKENeEA 638
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSD----KEWLKKHY-LD 245
|
....
gi 1958679184 639 EPSP 642
Cdd:PRK13641 246 EPAT 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1093-1293 |
1.99e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.99 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1093 PHEGVIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE--P----EGKIWIDK--ILTTE 1164
Cdd:COG1117 7 TLEPKIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarvEGEILLDGedIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1165 IGLHDLRKK------------MSI-------------IPQVQLKEAIED------LPGKMDTELAESGSNFSVGQRQLVC 1213
Cdd:COG1117 85 VDVVELRRRvgmvfqkpnpfpKSIydnvayglrlhgiKSKSELDEIVEEslrkaaLWDEVKDRLKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1214 LARAILKKNRILIIDEATANVDP----RTDELIQQkIREKFaqcTVLTIAH------RLntiidSDKIMVLDSGRLREYD 1283
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPistaKIEELILE-LKKDY---TIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFG 235
|
250
....*....|
gi 1958679184 1284 EPYVLLQNPE 1293
Cdd:COG1117 236 PTEQIFTNPK 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
426-615 |
2.23e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.21 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIayvsqqPWVFSGTVRSNI--LFGRK----- 498
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV------PWKRRKKFLRRIgvVFGQKtqlww 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 499 --------------Y--EKERYEKVIKACAlkkdlQLLEDGDLTVIGDRgaTLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:cd03267 109 dlpvidsfyllaaiYdlPPARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 563 SAVDA----EVGKHLFQLCicqTLHEKITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:cd03267 182 IGLDVvaqeNIRNFLKEYN---RERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1098-1283 |
2.31e-13 |
|
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: 70.63 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHD------- 1169
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPdSGEILIDGRDVTGVPPERrnigmvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 ------------------LRKKMSIIPQVQ--LKEAIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDE 1229
Cdd:cd03259 79 qdyalfphltvaeniafgLKLRGVPKAEIRarVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1230 ATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYD 1283
Cdd:cd03259 157 PLSALDAKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
276-621 |
2.31e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 276 MNEVITGMRIIKMYAWEKSFADLITNL----RKKEISKILGSSYLRGMNM-ASFFIANKVILFVTF-----TTYV----- 340
Cdd:PTZ00265 1025 IQEAFYNMNTVIIYGLEDYFCNLIEKAidysNKGQKRKTLVNSMLWGFSQsAQLFINSFAYWFGSFlirrgTILVddfmk 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 341 -LLGNKITASHVFVAMTLYG---AVRLTVTLFFPSAIERvseAVVSVR-----RIKNfllldelperkaqePSDGKAIVH 411
Cdd:PTZ00265 1105 sLFTFLFTGSYAGKLMSLKGdseNAKLSFEKYYPLIIRK---SNIDVRdnggiRIKN--------------KNDIKGKIE 1167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 412 VQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVL-------------------------------- 459
Cdd:PTZ00265 1168 IMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqgdee 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 460 ----------------GELPPTSGLVSVHGRI-------------------AYVSQQPWVFSGTVRSNILFGRkyEKERY 504
Cdd:PTZ00265 1248 qnvgmknvnefsltkeGGSGEDSTVFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLFNMSIYENIKFGK--EDATR 1325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 505 EKVIKAC---ALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCI-CQ 580
Cdd:PTZ00265 1326 EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdIK 1405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1958679184 581 TLHEKITILVTHQLQYLKAASHILIL----KDGEMVQ-KGTYTEFL 621
Cdd:PTZ00265 1406 DKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELL 1451
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
424-591 |
5.25e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.37 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQqpwvFSG---- 487
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQ----FDNldpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -TVRSNIL-FGrkyekeRYEKVIKACALKKDLQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13537 95 fTVRENLLvFG------RYFGLSAAAARALVPPLLEFAKLENKADaKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180
....*....|....*....|....*..
gi 1958679184 565 VDAEvGKHLFQLCICQTLHEKITILVT 591
Cdd:PRK13537 169 LDPQ-ARHLMWERLRSLLARGKTILLT 194
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
407-622 |
5.68e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 407 KAIVHVQDFTAFWD-KALDtptlqGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLV---------------- 469
Cdd:PRK13651 6 KNIVKIFNKKLPTElKALD-----NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 470 ---------------------SVHGRIAYVSQ--QPWVFSGTVRSNILFG------RKYE-KERYEKVIKACALkkDLQL 519
Cdd:PRK13651 81 ekvleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvSKEEaKKRAAKYIELVGL--DESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 520 LEDGDLTvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLfqLCICQTLHE--KITILVTHQLQY- 596
Cdd:PRK13651 159 LQRSPFE--------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEI--LEIFDNLNKqgKTIILVTHDLDNv 228
|
250 260 270
....*....|....*....|....*....|..
gi 1958679184 597 LKAASHILILKDGEMVQKG-TY-----TEFLK 622
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGdTYdilsdNKFLI 260
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
415-628 |
5.74e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.54 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 415 FTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPP---TSGLVSVHG----------RIAYVsQQ 481
Cdd:TIGR00955 28 RGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGmpidakemraISAYV-QQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 482 PWVFSG--TVRSNILF------GRKYEK----ERYEKVIKACALKKDLQlledgdlTVIGDRGAT--LSGGQKARVNLAR 547
Cdd:TIGR00955 107 DDLFIPtlTVREHLMFqahlrmPRRVTKkekrERVDEVLQALGLRKCAN-------TRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 548 AVYQDADIYLLDDPLSAVDAEVGKHLFQLC--ICQTlhEKITILVTHQLQY--LKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLkgLAQK--GKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
....*
gi 1958679184 624 GVDFG 628
Cdd:TIGR00955 258 FSDLG 262
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
426-568 |
5.82e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 69.77 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVH---------------------GRIAYVSQ---- 480
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 481 QPWVFSGTVRSNILFGRKYEKERYEKviKACALKKDLQLLEdgdltvigdR-----GATLSGGQKARVNLARAVYQDADI 555
Cdd:COG4778 105 IPRVSALDVVAEPLLERGVDREEARA--RARELLARLNLPE---------RlwdlpPATFSGGEQQRVNIARGFIADPPL 173
|
170
....*....|...
gi 1958679184 556 YLLDDPLSAVDAE 568
Cdd:COG4778 174 LLLDEPTASLDAA 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1162-1292 |
6.88e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1162 TTEIGLHDLRKKMSII---------PQVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATA 1232
Cdd:PTZ00265 529 TDSNELIEMRKNYQTIkdsevvdvsKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 1233 NVDPRTDELIQQKIREKFAQCTVLT--IAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNP 1292
Cdd:PTZ00265 609 SLDNKSEYLVQKTINNLKGNENRITiiIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1114-1282 |
8.24e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 68.85 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTTEIGLH--------DLRKKMSIIPQV--- 1180
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDgKPLDIAARNRigylpeerGLYPKMKVIDQLvyl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1181 -QLK-----EA---IEDLPGKMD-TELAESG-SNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE- 1248
Cdd:cd03269 95 aQLKglkkeEArrrIDEWLERLElSEYANKRvEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREl 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1958679184 1249 KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREY 1282
Cdd:cd03269 175 ARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLY 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
428-666 |
8.62e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSaVLGEL-PPTSGLVSVHGR-----------------IAYVSQQ-------- 481
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQdvatldadalaqlrrehFGFIFQRyhllshlt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 482 -------PWVFSGTvrsnilfGRKYEKERyekvikACALKKDLQLLEDgdltvIGDRGATLSGGQKARVNLARAVYQDAD 554
Cdd:PRK10535 103 aaqnvevPAVYAGL-------ERKQRLLR------AQELLQRLGLEDR-----VEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 555 IYLLDDPLSAVDAEVGKHLfqLCICQTLHEK--ITILVTHQLQYLKAASHILILKDGEMVQkgtyteflksgvDFGSllk 632
Cdd:PRK10535 165 VILADEPTGALDSHSGEEV--MAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIVR------------NPPA--- 227
|
250 260 270
....*....|....*....|....*....|....
gi 1958679184 633 KENEEAEPSPVPGTPTlrnrtfseASIWSQQSSR 666
Cdd:PRK10535 228 QEKVNVAGGTEPVVNT--------ASGWRQFVSG 253
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
424-624 |
9.66e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.17 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTP-TLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSG-------------LVSVHGRIAYVSQQP---WVFS 486
Cdd:PRK13648 20 DASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaitddnFEKLRKHIGIVFQNPdnqFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 487 gTVRSNILFGRKYEKERYEKVIKACAlkkdlQLLEDGDLTVIGD-RGATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PRK13648 100 -IVKYDVAFGLENHAVPYDEMHRRVS-----EALKQVDMLERADyEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 566 DAEVGKHLFQLCICQTLHEKITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIIsITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1097-1281 |
1.27e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.60 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI-LTT--EIGLHDL 1170
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPtSGRVLVDGQdLTAlsEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSIIPQ-------------VQL--------KEAIE-------DLPG---KMDTELAesgsNFSVGQRQLVCLARAIL 1219
Cdd:PRK11153 81 RRQIGMIFQhfnllssrtvfdnVALplelagtpKAEIKarvtellELVGlsdKADRYPA----QLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1220 KKNRILIIDEATANVDPRTDELIQQ---KIREKFAqCTVLTIAHRLNTI--IdSDKIMVLDSGRLRE 1281
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILEllkDINRELG-LTIVLITHEMDVVkrI-CDRVAVIDAGRLVE 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1095-1283 |
1.63e-12 |
|
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: 68.33 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1095 EGVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLH----- 1168
Cdd:cd03220 33 GEFWALKDVSFE---------------VPRGERIGLIGRNGAGKSTLLRLLAGIYPPdSGTVTVRGRVSSLLGLGggfnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1169 DL------RKKMSI--IPQVQLKEAIEDLpgkmdTELAESG-------SNFSVGQRQLVCLARAILKKNRILIIDEATAN 1233
Cdd:cd03220 98 ELtgreniYLNGRLlgLSRKEIDEKIDEI-----IEFSELGdfidlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 1234 VDPRTDELIQQKIREKFAQC-TVLTIAHRLNTIID-SDKIMVLDSGRLREYD 1283
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
423-618 |
1.74e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 423 LDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------------RIAYVSQQPWV- 484
Cdd:PRK11629 20 VQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 485 --FSG--TVRSNILFGRKYEKERYEK---VIKACALKKDLQlledgdltvigDRGATLSGGQKARVNLARAVYQDADIYL 557
Cdd:PRK11629 100 pdFTAleNVAMPLLIGKKKPAEINSRaleMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 558 LDDPLSAVDAEVGKHLFQLCICQTLHEKITIL-VTHQLQYLKAASHILILKDGEMVQKGTYT 618
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLvVTHDLQLAKRMSRQLEMRDGRLTAELSLM 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
428-619 |
1.77e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.21 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR----------------IAYVSQQpwvF----SG 487
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrkarrqIGMIFQH---FnllsSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 TVRSNILFGRKYEKERYEKvIKacalKKDLQLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK11153 98 TVFDNVALPLELAGTPKAE-IK----ARVTELLELVGLSDKADRyPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 567 AEVGKHLFQLC--ICQTLHekITI-LVTHQLQYLKA-ASHILILKDGEMVQKGTYTE 619
Cdd:PRK11153 173 PATTRSILELLkdINRELG--LTIvLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSE 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
425-616 |
2.46e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 425 TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQPWV-FSG-T 488
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklVGIVFQNPETqFVGrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 489 VRSNILFGRKyekeryekviKACALKKDLQLLEDGDLTVIG------DRGATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK13644 95 VEEDLAFGPE----------NLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 563 SAVDAEVGKHLFQLciCQTLHE--KITILVTHQLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK13644 165 SMLDPDSGIAVLER--IKKLHEkgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
424-621 |
3.31e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.81 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSG--LV---SVHGRIA----------YVSQQPWVFSG- 487
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlIVdglKVNDPKVderlirqeagMVFQQFYLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 TVRSNILFG----RKYEKERYEKVIKACALKKDLqlledgdltviGDRG----ATLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK09493 93 TALENVMFGplrvRGASKEEAEKQARELLAKVGL-----------AERAhhypSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 560 DPLSAVDAEVGKHLfqLCICQTLHEK--ITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK09493 162 EPTSALDPELRHEV--LKVMQDLAEEgmTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
410-655 |
4.13e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTAFWDkalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLG--ELPPTSGLVSVH----------GRIAY 477
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyvERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 478 VSQQP--------------WVFSGTVRSN------ILFGRK---YEKER-YEKVIKAC---------ALKKDLQLLEDGD 524
Cdd:TIGR03269 78 VGEPCpvcggtlepeevdfWNLSDKLRRRirkriaIMLQRTfalYGDDTvLDNVLEALeeigyegkeAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 525 LT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVT-HQLQYL-KAAS 601
Cdd:TIGR03269 158 LShRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTsHWPEVIeDLSD 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 602 HILILKDGEMVQKGTYTEFLKSGVDFGSLLKKENEEAEPSPVPGTPTLRNRTFS 655
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYIS 291
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
428-612 |
4.19e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGR------KYEKERYEKVIKACALKKDLQLleDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPlSAV- 565
Cdd:COG3845 101 IVLGLeptkggRLDRKAARARIRELSERYGLDV--DPDAKV-----EDLSVGEQQRVEILKALYRGARILILDEP-TAVl 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 566 -DAEVgKHLFQlcICQTL-HEKITIL-VTHQLQYLKAASH-ILILKDGEMV 612
Cdd:COG3845 173 tPQEA-DELFE--ILRRLaAEGKSIIfITHKLREVMAIADrVTVLRRGKVV 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
428-624 |
4.38e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 68.27 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------------RIAYVSQQP--WVFSGT 488
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 489 VRSNILFGRKYEKERYEKViKACALKKDLQLLEDGDltVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEV-KNYAHRLLMDLGFSRD--VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 569 VGKHLFQLCI-CQTLHEKITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSG 624
Cdd:PRK13646 180 SKRQVMRLLKsLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
397-616 |
4.88e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 397 ERKAQEPSDGKAIVHVQDFTAFWDKALDTP--TLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG- 473
Cdd:PRK13631 9 KLKVPNPLSDDIILRVKNLYCVFDEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 ----------------------------RIAYVSQQP--WVFSGTVRSNILFG------RKYE-KERYEKVIKACALKKD 516
Cdd:PRK13631 89 yigdkknnhelitnpyskkiknfkelrrRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 517 LqlLEDGDLTvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQL-Q 595
Cdd:PRK13631 169 Y--LERSPFG--------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMeH 238
|
250 260
....*....|....*....|.
gi 1958679184 596 YLKAASHILILKDGEMVQKGT 616
Cdd:PRK13631 239 VLEVADEVIVMDKGKILKTGT 259
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1097-1286 |
5.62e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKilTTEIG-----LHDL 1170
Cdd:COG0488 315 VLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPdSGTVKLGE--TVKIGyfdqhQEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSIIpqvqlkEAIEDL-PGKMDTELAE-------SG-------SNFSVGQRQLVCLARAILKKNRILIIDEATANVD 1235
Cdd:COG0488 391 DPDKTVL------DELRDGaPGGTEQEVRGylgrflfSGddafkpvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1236 PRTDELIQQKIREkFaQCTVLTIAH-R--LNTIidSDKIMVLDSGRLREYDEPY 1286
Cdd:COG0488 465 IETLEALEEALDD-F-PGTVLLVSHdRyfLDRV--ATRILEFEDGGVREYPGGY 514
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1109-1279 |
5.90e-12 |
|
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: 65.92 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1109 LDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHD-LRKKMSIIPQVQLKEAI 1186
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAsGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKREGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1187 -EDLPGKMDTELAE--SGSNfsvgQrQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLTIAHRL 1262
Cdd:cd03215 90 vLDLSVAENIALSSllSGGN----Q-QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSEL 164
|
170
....*....|....*...
gi 1958679184 1263 NTIID-SDKIMVLDSGRL 1279
Cdd:cd03215 165 DELLGlCDRILVMYEGRI 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
428-619 |
6.04e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-------------IAYVSQQP--WVFSGTVRSN 492
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPddQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFG-------RKYEKERYEKVIKACALKKdlqlledgdltvIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13652 100 IAFGpinlgldEETVAHRVSSALHMLGLEE------------LRDRVPhHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 565 VDAEVGKHLFQLCICQTLHEKIT-ILVTHQLQYL-KAASHILILKDGEMVQKGTYTE 619
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTvIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEE 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1098-1238 |
7.24e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 66.28 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTeiGLHD-----LR 1171
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPtSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1172 KKMSII--------------------------PQV---QLKEAIE--DLPGKMDTELAEsgsnFSVGQRQLVCLARAILK 1220
Cdd:cd03292 78 RKIGVVfqdfrllpdrnvyenvafalevtgvpPREirkRVPAALElvGLSHKHRALPAE----LSGGEQQRVAIARAIVN 153
|
170
....*....|....*...
gi 1958679184 1221 KNRILIIDEATANVDPRT 1238
Cdd:cd03292 154 SPTILIADEPTGNLDPDT 171
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1098-1277 |
9.34e-12 |
|
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: 66.20 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALF-RLSEPEGKIWIDKILTTEIGLHDLRKK--- 1173
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgEMQTLEGKVHWSNKNESEPSFEATRSRnry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1174 -------------------------------MSIIPQVQLKEAIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILKKN 1222
Cdd:cd03290 80 svayaaqkpwllnatveenitfgspfnkqryKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1223 RILIIDEATANVDPR-TDELIQQKIReKFAQ---CTVLTIAHRLNTIIDSDKIMVLDSG 1277
Cdd:cd03290 160 NIVFLDDPFSALDIHlSDHLMQEGIL-KFLQddkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
431-616 |
1.22e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.82 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------IAYVSQQPWVFSG-TVRSNILFGRK 498
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHmSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 499 YEK----ERYEKVIKACALKkdlqlledgDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKhl 573
Cdd:PRK11432 105 MLGvpkeERKQRVKEALELV---------DLAGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR-- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 574 fqlcicqTLHEKI----------TILVTH-QLQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK11432 174 -------SMREKIrelqqqfnitSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGS 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
428-616 |
1.88e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 66.67 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRiayvsqqPwvFSGTVRSNIlfGrkY--EkER-- 503
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-------P--LDPEDRRRI--G--YlpE-ERgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 504 Y--EKVI-------------KACALKKDLQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:COG4152 83 YpkMKVGeqlvylarlkglsKAEAKRRADEWLERLGLGdRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 568 eVGKHLFQlcicQTLHE-----KITILVTHQLQYLKA-ASHILILKDGEMVQKGT 616
Cdd:COG4152 163 -VNVELLK----DVIRElaakgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1098-1293 |
1.99e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.55 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYsldgPLVLKHLTALIKSREKVGIVGRTGAGKSSLISAL--FrLSEPEGKIWID--------------KIL 1161
Cdd:COG3840 2 LRLDDLTYRY----GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIagF-LPPDSGRILWNgqdltalppaerpvSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1162 TTE--------------IGLH-DLR-------KKMSIIPQVQLKEAIEDLPGKMdtelaeSGsnfsvGQRQLVCLARAIL 1219
Cdd:COG3840 77 FQEnnlfphltvaqnigLGLRpGLKltaeqraQVEQALERVGLAGLLDRLPGQL------SG-----GQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1220 KKNRILIIDEATANVDP--RTD--ELIQQKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGRLrEYDEPYVLLQNPE 1293
Cdd:COG3840 146 RKRPILLLDEPFSALDPalRQEmlDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRI-AADGPTAALLDGE 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
410-637 |
1.99e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTAFWDKALDTPTLQglsftarpgeLLAVVGPVGAGKSSLLSAV--LGELPPT---SGLVSVHG----------- 473
Cdd:PRK14243 18 VYYGSFLAVKNVWLDIPKNQ----------ITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGknlyapdvdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 ----RIAYVSQQPWVFSGTVRSNILFGRK---YE---KERYEKVIKACAL----KKDLQlledgdltvigDRGATLSGGQ 539
Cdd:PRK14243 88 evrrRIGMVFQKPNPFPKSIYDNIAYGARingYKgdmDELVERSLRQAALwdevKDKLK-----------QSGLSLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 540 KARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQTLHEKITI-LVTHQLQYLKAASHILILKDGEMVQKGTYT 618
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEEL--MHELKEQYTIiIVTHNMQQAARVSDMTAFFNVELTEGGGRY 234
|
250 260
....*....|....*....|...
gi 1958679184 619 ----EFLKSGVDFGSLLKKENEE 637
Cdd:PRK14243 235 gylvEFDRTEKIFNSPQQQATRD 257
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1064-1285 |
2.68e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1064 MISVERV-IEY------TDLEKEAPWECRKRPppgwpHEGVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGA 1136
Cdd:COG1134 4 MIEVENVsKSYrlyhepSRSLKELLLRRRRTR-----REEFWALKDVSFE---------------VERGESVGIIGRNGA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1137 GKSSLISALFRLSEP-EGKIWIDKILTT--EIG------------------LHDLRKKM--SIIPQV----QLKEAIeDL 1189
Cdd:COG1134 64 GKSTLLKLIAGILEPtSGRVEVNGRVSAllELGagfhpeltgreniylngrLLGLSRKEidEKFDEIvefaELGDFI-DQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1190 PGK-----MDTELAesgsnFSVgqrqlvclarAILKKNRILIIDEATAnVdprTDELIQQKIREKFAQ-----CTVLTIA 1259
Cdd:COG1134 143 PVKtyssgMRARLA-----FAV----------ATAVDPDILLVDEVLA-V---GDAAFQKKCLARIRElresgRTVIFVS 203
|
250 260
....*....|....*....|....*..
gi 1958679184 1260 HRLNTIID-SDKIMVLDSGRLREYDEP 1285
Cdd:COG1134 204 HSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1098-1296 |
2.76e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 66.64 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWIDKILTTEIGLHD----- 1169
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmIAGLEDPTS--GEILIGGRDVTDLPPKDrniam 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 --------------------LR-KKMS---IIPQVqlKEA-----IEDLPGKMDTELaeSGsnfsvGQRQLVCLARAILK 1220
Cdd:COG3839 80 vfqsyalyphmtvyeniafpLKlRKVPkaeIDRRV--REAaellgLEDLLDRKPKQL--SG-----GQRQRVALGRALVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1221 KNRILIIDEATANVDP------RTdELiqQKIREKFAQCTV---------LTIAhrlntiidsDKIMVLDSGRLREYDEP 1285
Cdd:COG3839 151 EPKVFLLDEPLSNLDAklrvemRA-EI--KRLHRRLGTTTIyvthdqveaMTLA---------DRIAVMNDGRIQQVGTP 218
|
250
....*....|.
gi 1958679184 1286 YVLLQNPESLF 1296
Cdd:COG3839 219 EELYDRPANLF 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1101-1292 |
2.77e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 66.23 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1101 DNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP----EGKIWIDKILTTEIGLHDLR----K 1172
Cdd:COG0444 22 DGVSFD---------------VRRGETLGLVGESGSGKSTLARAILGLLPPpgitSGEILFDGEDLLKLSEKELRkirgR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KMSIIPQ-----------V--QLKEAI---EDLPGKMDTELAE----------------------SGsnfsvGQRQLVCL 1214
Cdd:COG0444 87 EIQMIFQdpmtslnpvmtVgdQIAEPLrihGGLSKAEARERAIellervglpdperrldryphelSG-----GMRQRVMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1215 ARAILKKNRILIIDEATANVDPrtdeLIQ-------QKIREKFaQCTVLTIAHRLNTI--IdSDKIMVLDSGRLREYDEP 1285
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDV----TIQaqilnllKDLQREL-GLAILFITHDLGVVaeI-ADRVAVMYAGRIVEEGPV 235
|
....*..
gi 1958679184 1286 YVLLQNP 1292
Cdd:COG0444 236 EELFENP 242
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
428-625 |
2.79e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR----------------------IAYVSQQPW-- 483
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyalseaerrrllrteWGFVHQHPRdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 484 ----VFSGtvrSNI---LFG---RKYEKeryekvIKACALKKdLQLLEDgDLTVIGDRGATLSGGQKARVNLARAVYQDA 553
Cdd:PRK11701 102 lrmqVSAG---GNIgerLMAvgaRHYGD------IRATAGDW-LERVEI-DAARIDDLPTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 554 DIYLLDDPLSAVDAEVGKHLFQLC--ICQTLHEKItILVTHQLQYLKAASH-ILILKDGEMVQKG-----------TYTE 619
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAV-VIVTHDLAVARLLAHrLLVMKQGRVVESGltdqvlddpqhPYTQ 249
|
....*.
gi 1958679184 620 FLKSGV 625
Cdd:PRK11701 250 LLVSSV 255
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
428-615 |
2.81e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGR--------------KYEKERYEKVIKACALKKDLqlledgDLTVigdrgATLSGGQKARVNLARAVYQDADIYLL 558
Cdd:PRK09700 101 LYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDL------DEKV-----ANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 559 DDPLSAV-DAEVgKHLFqLCICQTLHE-KITILVTHQLQYLKA-ASHILILKDGEMVQKG 615
Cdd:PRK09700 170 DEPTSSLtNKEV-DYLF-LIMNQLRKEgTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1098-1291 |
3.10e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.99 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYsldgplvlKHL----TALIKSREKVGIVGRTGAGKSSLIS--ALFrLSEPEGKIWIDKI----------- 1160
Cdd:PRK10771 2 LKLTDITWLY--------HHLpmrfDLTVERGERVAILGPSGAGKSTLLNliAGF-LTPASGSLTLNGQdhtttppsrrp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1161 -------------LTTE--IGL---------HDLRKKM-SIIPQVQLKEAIEDLPGKMdtelaeSGsnfsvGQRQLVCLA 1215
Cdd:PRK10771 73 vsmlfqennlfshLTVAqnIGLglnpglklnAAQREKLhAIARQMGIEDLLARLPGQL------SG-----GQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1216 RAILKKNRILIIDEATANVDP--RTD--ELIQQKIREKfaQCTVLTIAHRLNtiiDSDKI----MVLDSGRLrEYDEPYV 1287
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDPalRQEmlTLVSQVCQER--QLTLLMVSHSLE---DAARIaprsLVVADGRI-AWDGPTD 215
|
....
gi 1958679184 1288 LLQN 1291
Cdd:PRK10771 216 ELLS 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
432-623 |
3.25e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.98 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 432 SFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------------RIAYVSQQPWVFSG-TVRSNI 493
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 LFGRKYE----KERYEKVIKAcalkkdlqLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK10070 128 AFGMELAginaEERREKALDA--------LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 570 GKHLF-QLCICQTLHEKITILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK10070 200 RTEMQdELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
424-623 |
5.08e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.01 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQP-WVFSG-T 488
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeirkKIGIIFQNPdNQFIGaT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 489 VRSNILFG---RKYEKERYEKVIKACALKKDLQLLEDGDltvigdrGATLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PRK13632 101 VEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDYLDKE-------PQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 566 DAEVGKHLFQlcICQTLHE---KITILVTHQLQYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK13632 174 DPKGKREIKK--IMVDLRKtrkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1098-1279 |
5.19e-11 |
|
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: 63.70 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYsldGPL-VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID--KILTTEIGLHDLRKK 1173
Cdd:cd03262 1 IEIKNLHKSF---GDFhVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTIIIDglKLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1174 MSII------------------PQVQLK-----EAIEdlpgKMDTELAESG---------SNFSVGQRQLVCLARAILKK 1221
Cdd:cd03262 78 VGMVfqqfnlfphltvlenitlAPIKVKgmskaEAEE----RALELLEKVGladkadaypAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 1222 NRILIIDEATANVDPrtdELIQQ--KIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRL 1279
Cdd:cd03262 154 PKVMLFDEPTSALDP---ELVGEvlDVMKDLAEegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
406-566 |
5.45e-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: 62.83 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 406 GKAIVHVQDFTAfwdkaldTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR----------- 474
Cdd:cd03215 1 GEPVLEVRGLSV-------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdai 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 475 ---IAYVS----QQPWVFSGTVRSNILFGRkyekeryekvikacalkkdlqlledgdltvigdrgaTLSGG--QKarVNL 545
Cdd:cd03215 74 ragIAYVPedrkREGLVLDLSVAENIALSS------------------------------------LLSGGnqQK--VVL 115
|
170 180
....*....|....*....|.
gi 1958679184 546 ARAVYQDADIYLLDDPLSAVD 566
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVD 136
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1097-1295 |
5.74e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.73 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGPL-VLKHLTALIKSREKVGIVGRTGAGKSS---LISALFRlsEPEGKIWIDKILTTEIGLHDLRK 1172
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KMSII---PQVQLKEAI----------------EDLPGKMDTEL---------AESGSNFSVGQRQLVCLARAILKKNRI 1224
Cdd:PRK13642 82 KIGMVfqnPDNQFVGATveddvafgmenqgiprEEMIKRVDEALlavnmldfkTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1225 LIIDEATANVDP--RTDEL-IQQKIREKFaQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESL 1295
Cdd:PRK13642 162 IILDESTSMLDPtgRQEIMrVIHEIKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
421-647 |
5.99e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 65.46 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 421 KALDtptlqGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPP---TSGLVSVHG-----------------RIAYVSQ 480
Cdd:COG0444 19 KAVD-----GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedllklsekelrkirgrEIQMIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 481 QPW-----VFsgTVRSNI-----LFGRKYEKERYEKVIkacalkkdlQLLEDGDLTVIGDRGA----TLSGGQKARVNLA 546
Cdd:COG0444 94 DPMtslnpVM--TVGDQIaeplrIHGGLSKAEARERAI---------ELLERVGLPDPERRLDryphELSGGMRQRVMIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 547 RAVYQDADIYLLDDPLSAVDAEVgkhlfQLCICQTLHE-----KITIL-VTHQL---QYLkaASHILILKDGEMVQKGT- 616
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTI-----QAQILNLLKDlqrelGLAILfITHDLgvvAEI--ADRVAVMYAGRIVEEGPv 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958679184 617 ----------YTEFLksgvdFGSLLKKENEEAEPSPVPGTP 647
Cdd:COG0444 236 eelfenprhpYTRAL-----LSSIPRLDPDGRRLIPIPGEP 271
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
425-612 |
6.06e-11 |
|
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: 63.44 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 425 TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPT---SGLVS------------VHGRIAYVSQQPWVFSG-T 488
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHyngipykefaekYPGEIIYVSEEDVHFPTlT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 489 VRSNILFgrkyekeryekvikACALKkdlqlledGDLTVigdRGatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:cd03233 100 VRETLDF--------------ALRCK--------GNEFV---RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 569 VGKHLFQlCICQTLHE-KITILVThqlqyLKAAS--------HILILKDGEMV 612
Cdd:cd03233 153 TALEILK-CIRTMADVlKTTTFVS-----LYQASdeiydlfdKVLVLYEGRQI 199
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1130-1293 |
6.30e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.26 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1130 IVGRTGAGKSSLISALFRLSEPE-GKIWIDKI---------------LTTEI-GLHDLRKKMSII---PQVQL-KEAIE- 1187
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKyGTIQVGDIyigdkknnhelitnpYSKKIkNFKELRRRVSMVfqfPEYQLfKDTIEk 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1188 ------------------------DLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQ 1243
Cdd:PRK13631 137 dimfgpvalgvkkseakklakfylNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 1244 QKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPE 1293
Cdd:PRK13631 217 QLILDaKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
429-621 |
6.53e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 429 QGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQ----------QPWVF 485
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLAQnattpgditvQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 486 SGTVRSNILFGRkYEKERYEKVIKAcalkkdlqlLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK10253 104 RGRYPHQPLFTR-WRKEDEEAVTKA---------MQATGITHLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 565 VDAEVGKHLFQLcICQTLHEKITIL--VTHQL-QYLKAASHILILKDGEMVQKGTYTEFL 621
Cdd:PRK10253 174 LDISHQIDLLEL-LSELNREKGYTLaaVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
436-568 |
6.60e-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: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 436 RPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-RIAYVSQQPWV-FSGTVRSnILFG---RKYEKERYEKVIKa 510
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKAdYEGTVRD-LLSSitkDFYTHPYFKTEIA- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 511 calkKDLQL--LEDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:cd03237 101 ----KPLQIeqILDREVP-------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
428-599 |
7.03e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--RIAYVSQQ-------PWVFS-------GTVRS 491
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQKlyldttlPLTVNrflrlrpGTKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFGRKyekeryeKVIKACALKKDLQlledgdltvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:PRK09544 100 DILPALK-------RVQAGHLIDAPMQ---------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|
gi 1958679184 572 HLFQLcICQTLHEK--ITILVTHQLQYLKA 599
Cdd:PRK09544 158 ALYDL-IDQLRRELdcAVLMVSHDLHLVMA 186
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
424-591 |
7.54e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR----------IAYVSQQPwvfsgtvrsni 493
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLP----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 lfGRKYEKERYEKVIKACALK-KDLQLLEDGDLTVIGDRGAT------LSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13543 92 --GLKADLSTLENLHFLCGLHgRRAKQMPGSALAIVGLAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*
gi 1958679184 567 AEvGKHLFQLCICQTLHEKITILVT 591
Cdd:PRK13543 170 LE-GITLVNRMISAHLRGGGAALVT 193
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
434-616 |
7.61e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.66 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 434 TARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----------------IAYVSQQP--WVFSGTVRSNIL 494
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitagkknkklkplrkkVGIVFQFPehQLFEETVEKDIC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 495 FG-------RKYEKERYEKVIKACALKKDLQlledgdltvigDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13634 109 FGpmnfgvsEEDAKQKAREMIELVGLPEELL-----------ARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 567 AEVGKHLFQLciCQTLHEK---ITILVTHQL----QYlkaASHILILKDGEMVQKGT 616
Cdd:PRK13634 178 PKGRKEMMEM--FYKLHKEkglTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGT 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1103-1293 |
9.92e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.35 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1103 VNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE-------------------------------- 1150
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrysgdvllggrsifnyrdvlefrrrvg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1151 -------PEGKIWIDKILTTeIGLHDL--RKKMSIIPQVQLKEAieDLPGKMDTELAESGSNFSVGQRQLVCLARAILKK 1221
Cdd:PRK14271 105 mlfqrpnPFPMSIMDNVLAG-VRAHKLvpRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 1222 NRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPE 1293
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
434-568 |
1.11e-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: 65.96 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 434 TARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAY----VSQQpwvFSGTVRSNIlfgRKYEKER------ 503
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyISPD---YDGTVEEFL---RSANTDDfgssyy 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 504 YEKVIKACALKKdlqlLEDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAE 568
Cdd:COG1245 436 KTEIIKPLGLEK----LLDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
394-568 |
1.12e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 394 ELPERKAQEPSDGKAIVHVQDFTafwdKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG 473
Cdd:PRK13409 325 EFEERPPRDESERETLVEYPDLT----KKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 RIAYVSQqpWV---FSGTVRSNI-----LFGRKYEKeryEKVIKACALKKdlqlLEDGDLTvigdrgaTLSGGQKARVNL 545
Cdd:PRK13409 401 KISYKPQ--YIkpdYDGTVEDLLrsitdDLGSSYYK---SEIIKPLQLER----LLDKNVK-------DLSGGELQRVAI 464
|
170 180
....*....|....*....|...
gi 1958679184 546 ARAVYQDADIYLLDDPLSAVDAE 568
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDVE 487
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1096-1295 |
1.14e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTYSLDGPLVLKHL--TALIKSREKVG-IVGRTGAGKSSLISAL--FRLSEPEGKIWIDKILTTEIG---- 1166
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFKALnnTSLTFKKNKVTcVIGTTGSGKSTMIQLTngLIISETGQTIVGDYAIPANLKkike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1167 LHDLRKKMSII---PQVQL--------------------KEAIEDLPGKMD-TELAE-----SGSNFSVGQRQLVCLARA 1217
Cdd:PRK13645 85 VKRLRKEIGLVfqfPEYQLfqetiekdiafgpvnlgenkQEAYKKVPELLKlVQLPEdyvkrSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1218 ILKKNRILIIDEATANVDPRTDE-LIQQKIR-EKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPES 1294
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEdFINLFERlNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
.
gi 1958679184 1295 L 1295
Cdd:PRK13645 245 L 245
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
441-585 |
1.70e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.65 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 441 LAVVGPVGAGKSSLLSAVLGELPPTSGLV--SVHGRIAYVSQQPwVFSGTVRSNILFgrkYEKERYEKVIKAcALKKDLq 518
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMAVFSQHH-VDGLDLSSNPLL---YMMRCFPGVPEQ-KLRAHL- 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 519 lledGDLTVIGDRGA----TLSGGQKARVNLARAVYQDADIYLLDDP-----LSAVDAEV-GKHLFQLCICQTLHEK 585
Cdd:PLN03073 612 ----GSFGVTGNLALqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPsnhldLDAVEALIqGLVLFQGGVLMVSHDE 684
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
428-593 |
1.98e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTS--GLVSVHG---------RIAYVSQQPWVFSG-TVRSNILF 495
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrkptkqilkRTGFVTQDDILYPHlTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 496 ------GRKYEKEryEKVIKACALKKDLQLLEDGDlTVIGD---RGatLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PLN03211 164 csllrlPKSLTKQ--EKILVAESVISELGLTKCEN-TIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180
....*....|....*....|....*....
gi 1958679184 567 AEVGKHLFQLCIcqTLHEKITILVT--HQ 593
Cdd:PLN03211 239 ATAAYRLVLTLG--SLAQKGKTIVTsmHQ 265
|
|
| 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: 63.13 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 410 VHVQDFTAFWDKaldTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAvLGELPPTSGLVSVHGRIAYVSQ--------- 480
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQniyerrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 481 ------------QPWVFSGTVRSNILFGRK----YEKERYEKVIKACALKKDLQlleDGDLTVIGDRGATLSGGQKARVN 544
Cdd:PRK14258 84 nrlrrqvsmvhpKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDADLW---DEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 545 LARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITI-LVTHQLQYLKAASHILIL------KDGEMVQKGTY 617
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMvIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEFGLT 240
|
....*....
gi 1958679184 618 TEFLKSGVD 626
Cdd:PRK14258 241 KKIFNSPHD 249
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1098-1280 |
2.18e-10 |
|
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: 62.14 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI-LTTEIglHDLRKKMS 1175
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtSGTAYINGYsIRTDR--KAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 IIPQ-------------------------VQLKEAIE------DLPGKMDTELaesgSNFSVGQRQLVCLARAILKKNRI 1224
Cdd:cd03263 79 YCPQfdalfdeltvrehlrfyarlkglpkSEIKEEVElllrvlGLTDKANKRA----RTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1225 LIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTI-IDSDKIMVLDSGRLR 1280
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLR 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
431-621 |
2.26e-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: 64.96 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTarPGELLAVVGPVGAGKSSLL-------SAVLGELPPTSGLvsvhgRIAYVSQQPWV-FSGTVRSNILFG------ 496
Cdd:TIGR03719 26 LSFF--PGAKIGVLGLNGAGKSTLLrimagvdKDFNGEARPQPGI-----KVGYLPQEPQLdPTKTVRENVEEGvaeikd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 497 ---------RKY------------EKERYEKVIKAC-ALKKDLQL--------LEDGDLTVigdrgATLSGGQKARVNLA 546
Cdd:TIGR03719 99 aldrfneisAKYaepdadfdklaaEQAELQEIIDAAdAWDLDSQLeiamdalrCPPWDADV-----TKLSGGERRRVALC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 547 RAVYQDADIYLLDDPLSAVDAE----VGKHL--FQLCIcqtlhekitILVTHQLQYL-KAASHILILKDGEMVQ-KGTYT 618
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAEsvawLERHLqeYPGTV---------VAVTHDRYFLdNVAGWILELDRGRGIPwEGNYS 244
|
...
gi 1958679184 619 EFL 621
Cdd:TIGR03719 245 SWL 247
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1097-1295 |
2.54e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSLDGPLVLKHLTAL---IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG----LH 1168
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIdleVKKGSYTALIGHTGSGKSTLLQHLNGLLQPtEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1169 DLRKKMSII---PQVQL-------------------KEAIEDLPGK------MDTELAE-SGSNFSVGQRQLVCLARAIL 1219
Cdd:PRK13643 81 PVRKKVGVVfqfPESQLfeetvlkdvafgpqnfgipKEKAEKIAAEklemvgLADEFWEkSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1220 KKNRILIIDEATANVDPRTdELIQQKIREKFAQC--TVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPESL 1295
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKA-RIEMMQLFESIHQSgqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEVDFL 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
428-566 |
2.80e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSG----------LVSVHGR----IAYVSQQPWVFSgtvRSNI 493
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedisLLPLHARarrgIGYLPQEASIFR---RLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 lfgrkyekerYEKVIKACALKKDL----------QLLEDGDLTVIGDR-GATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:PRK10895 96 ----------YDNLMAVLQIRDDLsaeqredranELMEEFHIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
....
gi 1958679184 563 SAVD 566
Cdd:PRK10895 166 AGVD 169
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
431-623 |
2.95e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------------RIAYVSQQPWVfSGTVRSNI---- 493
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqRIRMIFQDPST-SLNPRQRIsqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 ----LFGRKYEKERYEKVIKAcALKKdLQLLEDGdltvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK15112 111 dfplRLNTDLEPEQREKQIIE-TLRQ-VGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 570 GKHLFQLCI-CQTLHEKITILVTHQLQYLKAAS-HILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK15112 185 RSQLINLMLeLQEKQGISYIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
406-623 |
3.04e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 406 GKAIVHVQDFTAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAY-------- 477
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 478 -----------VSQQPWVFSG-TVRSNILFGRKY----EKERYEKVIKACalkkdlqLLEDGDLTVIGDR----GATLSG 537
Cdd:PRK14246 84 daiklrkevgmVFQQPNPFPHlSIYDNIAYPLKShgikEKREIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 538 GQKARVNLARAVYQDADIYLLDDPLSAVDAeVGKHLFQLCICQTLHEKITILVTHQLQYL-KAASHILILKDGEMVQKGT 616
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGS 235
|
....*..
gi 1958679184 617 YTEFLKS 623
Cdd:PRK14246 236 SNEIFTS 242
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
428-616 |
3.41e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELP--PTSGLVSVHGRIAY----------------------VSQQPW 483
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVTLngeplaaidaprlarlravlpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 484 VFSgtVRSNILFG------RKYEKERYEKVIKACALKK-DLQLLEDGDLTvigdrgaTLSGGQKARVNLARAVYQ----- 551
Cdd:PRK13547 97 AFS--AREIVLLGrypharRAGALTHRDGEIAWQALALaGATALVGRDVT-------TLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 552 ----DADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITIL-VTHQLQYlkAASH---ILILKDGEMVQKGT 616
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNL--AARHadrIAMLADGAIVAHGA 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
438-615 |
3.86e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 438 GELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-RIAYVsqQP------WVFSG-------TVRSNILFGRKYEK-- 501
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkRMNDV--PPaergvgMVFQSyalyphlSVAENMSFGLKLAGak 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 502 --ERYEKVIKACALKKDLQLLEDgdltvigdRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDA--------EVGK 571
Cdd:PRK11000 107 keEINQRVNQVAEVLQLAHLLDR--------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvqmriEISR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958679184 572 hlfqlcicqtLHEKI---TILVTH-QLQYLKAASHILILKDGEMVQKG 615
Cdd:PRK11000 179 ----------LHKRLgrtMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
428-615 |
3.88e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLgELPPTSG----------------LVSVHGRIAYVSQQPWVfSGTVRS 491
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGeiwfdgqplhnlnrrqLLPVRHRIQVVFQDPNS-SLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILF----G-RKYEK-----ERYEKVIKAcalkkdlqLLEDG-DLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK15134 380 NVLQiieeGlRVHQPtlsaaQREQQVIAV--------MEEVGlDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 561 PLSAVDAEVGKHLFQLC-ICQTLHEKITILVTHQLQYLKAASH-ILILKDGEMVQKG 615
Cdd:PRK15134 452 PTSSLDKTVQAQILALLkSLQQKHQLAYLFISHDLHVVRALCHqVIVLRQGEVVEQG 508
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
97-386 |
3.96e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 62.58 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 97 IFTLIEETTRVVQPIFLGKIIDYFekYDSDDSAALHTAygyAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCHMIYR 176
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTI--IKGGDLDVLNEL---ALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 177 KALRLSNSAMGKTTTGQIVNLLSNDVNKF-DQVTIFLHFLWAGPLQAIGVTILLWVeigISCLAGLAILVIlLPLQSCIG 255
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLqSAVTDNLSQLLRNILQVIGGLIILFI---LSWKLTLVLLLV-IPLLLIAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 256 KLFSS-LRSKTAAFTDARIRTM---NEVITGMRIIKMYAWE----KSFADLITNLRKKEISKILGSSYLRGMNMASFFIA 327
Cdd:cd18557 154 KIYGRyIRKLSKEVQDALAKAGqvaEESLSNIRTVRSFSAEekeiRRYSEALDRSYRLARKKALANALFQGITSLLIYLS 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 328 NKVILFvtFTTYVLLGNKITA----SHVFVAMTLYGAVRlTVTLFFPSAIervsEAVVSVRRI 386
Cdd:cd18557 234 LLLVLW--YGGYLVLSGQLTVgeltSFILYTIMVASSVG-GLSSLLADIM----KALGASERV 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
761-1070 |
3.97e-10 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 62.57 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 761 LSWYLGIYTGLTAVTVLFGIARSLLVFYVLVNASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhls 840
Cdd:cd07346 38 LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRT---------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 841 hphpwpqngslqasvtsvtgsdvirfpevlllalpGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIP- 919
Cdd:cd07346 96 -----------------------------------GDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWk 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 920 ---WILIPLVPLSIIFVVLRRYFLETSRDVKRLESTtrspVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWF 996
Cdd:cd07346 141 ltlVALLLLPLYVLILRYFRRRIRKASREVRESLAE----LSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 997 LFLTTSRWFAVRLDAICAV-FVIVVAFG-SLVLAKTLDAGQVGLALSYsltlMGMFQWSVRQSAEVENM----MISVERV 1070
Cdd:cd07346 217 RAARLSALFSPLIGLLTALgTALVLLYGgYLVLQGSLTIGELVAFLAY----LGMLFGPIQRLANLYNQlqqaLASLERI 292
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-616 |
4.32e-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: 63.94 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 391 LLDELPER-KAQEPSDGKAIVHVQDF-------------TAFWDKALDtptlqGLSFTARPGELLAVVGPVGAGKSSLLS 456
Cdd:COG4172 256 LLAAEPRGdPRPVPPDAPPLLEARDLkvwfpikrglfrrTVGHVKAVD-----GVSLTLRRGETLGLVGESGSGKSTLGL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 457 AVLGeLPPTSGLVSVHG----------------RIAYVSQQPwvFSG-----TVRS------NILFGRKYEKERYEKVIk 509
Cdd:COG4172 331 ALLR-LIPSEGEIRFDGqdldglsrralrplrrRMQVVFQDP--FGSlsprmTVGQiiaeglRVHGPGLSAAERRARVA- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 510 acalkkdlQLLEDGDLtvigDRGAT------LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLciCQTLH 583
Cdd:COG4172 407 --------EALEEVGL----DPAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDL--LRDLQ 472
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958679184 584 EK--IT-ILVTHQLQYLKAASH-ILILKDGEMVQKGT 616
Cdd:COG4172 473 REhgLAyLFISHDLAVVRALAHrVMVMKDGKVVEQGP 509
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1130-1292 |
5.05e-10 |
|
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: 61.89 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1130 IVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDL----RKKMSII--------------------------P 1178
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPtSGKVLIDGQDIAAMSRKELrelrRKKISMVfqsfallphrtvlenvafglevqgvpR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1179 QVQLKEAIE-----DLPG---KMDTELaeSGsnfsvGQRQLVCLARAILKKNRILIIDEATANVDP--RT---DELIQ-Q 1244
Cdd:cd03294 135 AEREERAAEalelvGLEGwehKYPDEL--SG-----GMQQRVGLARALAVDPDILLMDEAFSALDPliRRemqDELLRlQ 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958679184 1245 KIREKfaqcTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNP 1292
Cdd:cd03294 208 AELQK----TIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1104-1285 |
5.08e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.67 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLS--EP-EGKI-----------WID----------- 1158
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPtSGRIiyhvalcekcgYVErpskvgepcpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1159 ---KILTTEIGL--------HDLRKKMSIIPQ------------VQLKEAIEDL--PGK----MDTELAES--------- 1200
Cdd:TIGR03269 85 cggTLEPEEVDFwnlsdklrRRIRKRIAIMLQrtfalygddtvlDNVLEALEEIgyEGKeavgRAVDLIEMvqlshrith 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1201 -GSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIID-SDKIMVLDS 1276
Cdd:TIGR03269 165 iARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDlSDKAIWLEN 244
|
....*....
gi 1958679184 1277 GRLREYDEP 1285
Cdd:TIGR03269 245 GEIKEEGTP 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1096-1279 |
5.25e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID----KILTTeigLHDL 1170
Cdd:COG1129 16 GVKALDGVSLE---------------LRPGEVHALLGENGAGKSTLMKILSGVYQPdSGEILLDgepvRFRSP---RDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSIIPQ-VQLkeaIEDL--------------PGKMDTE---------LAESG---------SNFSVGQRQLVCLARA 1217
Cdd:COG1129 78 AAGIAIIHQeLNL---VPNLsvaeniflgreprrGGLIDWRamrrrarelLARLGldidpdtpvGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1218 ILKKNRILIIDEATANVDPR-TDELIQQkIREKFAQ-CTVLTIAHRLNTIID-SDKIMVLDSGRL 1279
Cdd:COG1129 155 LSRDARVLILDEPTASLTEReVERLFRI-IRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
428-613 |
5.71e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQ-PWVFSGTVRSN 492
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaalaagVAIIYQElHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGR--------KYEKERYEKVIKACALKKDLqlleDGDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK11288 100 LYLGQlphkggivNRRLLNYEAREQLEHLGVDI----DPDTPL-----KYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 565 VDAEVGKHLFQLcICQTLHE-KITILVTHQLQYLKAASH-ILILKDGEMVQ 613
Cdd:PRK11288 171 LSAREIEQLFRV-IRELRAEgRVILYVSHRMEEIFALCDaITVFKDGRYVA 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1090-1278 |
5.93e-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: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1090 PGWPHEgVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWID-KILTTE- 1164
Cdd:COG1101 13 PGTVNE-KRALDGLNLT---------------IEEGDFVTVIGSNGAGKSTLlnaIAGSLPPDS--GSILIDgKDVTKLp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1165 -------IG---------------------LHDLR-KKMSIIPQV------QLKEAIED----LPGKMDTELaesgSNFS 1205
Cdd:COG1101 75 eykrakyIGrvfqdpmmgtapsmtieenlaLAYRRgKRRGLRRGLtkkrreLFRELLATlglgLENRLDTKV----GLLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 1206 VGQRQLVCLARAILKKNRILIIDEATANVDPRTDELI----QQKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGR 1278
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEEN--NLTTLMVTHNMEQALDyGNRLIMMHEGR 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
93-386 |
6.35e-10 |
|
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: 62.02 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGI-FTLIEETTRVVQPIFLGKIIDYFEKYDSDDSAALhtaYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMC 171
Cdd:cd18544 1 FILALlLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGL---LLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ--VTIFLHFLWAGpLQAIGVTILLW---VEIGISCLAGL-AILV 245
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNElfTSGLVTLIGDL-LLLIGILIAMFllnWRLALISLLVLpLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 246 ILLPLQSCIGKLFSSLRSKTA---AFtdarirtMNEVITGMRIIKMYAWEKSFADlitnlRKKEISKILGSSYLRGMNMA 322
Cdd:cd18544 157 ATYLFRKKSRKAYREVREKLSrlnAF-------LQESISGMSVIQLFNREKREFE-----EFDEINQEYRKANLKSIKLF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 323 SFF---------IAnkVILFVTFTTYVLLGNKITAShVFVAMTLYgavrltVTLFF-PsaIERVSE-------AVVSVRR 385
Cdd:cd18544 225 ALFrplvellssLA--LALVLWYGGGQVLSGAVTLG-VLYAFIQY------IQRFFrP--IRDLAEkfnilqsAMASAER 293
|
.
gi 1958679184 386 I 386
Cdd:cd18544 294 I 294
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1104-1286 |
6.40e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.55 E-value: 6.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTteIGL----HDLRKKMSII- 1177
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSIPKGLR--IGYlpqePPLDDDLTVLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1178 -------PQVQLKEAIEDLPGKMD-------------TELAESG--------------------------SNFSVGQRQL 1211
Cdd:COG0488 81 tvldgdaELRALEAELEELEAKLAepdedlerlaelqEEFEALGgweaearaeeilsglgfpeedldrpvSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1212 VCLARAILKKNRILIIDEATANVDPRT-----DELIQQKirekfaqCTVLTIAH-R--LNTIidSDKIMVLDSGRLREYD 1283
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNYP-------GTVLVVSHdRyfLDRV--ATRILELDRGKLTLYP 231
|
...
gi 1958679184 1284 EPY 1286
Cdd:COG0488 232 GNY 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1104-1296 |
6.89e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.43 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTE--IGLHD---------LR 1171
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPtEGQIFIDGEDVTHrsIQQRDicmvfqsyaLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1172 KKMSIIPQV----------------QLKEAIE--DLPGKMDTELAEsgsnFSVGQRQLVCLARAILKKNRILIIDEATAN 1233
Cdd:PRK11432 91 PHMSLGENVgyglkmlgvpkeerkqRVKEALElvDLAGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1234 VDPRTDELIQQKIREKFAQ--CTVLTIAH-RLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLF 1296
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQfnITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1104-1248 |
7.00e-10 |
|
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: 60.19 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGlHDLRKKMSII----- 1177
Cdd:COG4133 7 NLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPsAGEVLWNGEPIRDAR-EDYRRRLAYLghadg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1178 ----------------------PQVQLKEAIE--DLPGKMDTELaesgSNFSVGQRQLVCLARAILKKNRILIIDEATAN 1233
Cdd:COG4133 86 lkpeltvrenlrfwaalyglraDREAIDEALEavGLAGLADLPV----RQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170
....*....|....*
gi 1958679184 1234 VDPRTDELIQQKIRE 1248
Cdd:COG4133 162 LDAAGVALLAELIAA 176
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
426-622 |
7.43e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.74 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTS---GLVSVHG-------------RIAYVSQQP-WVFSG- 487
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGitltaktvwdireKVGIVFQNPdNQFVGa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 TVRSNILFG---RKYEKERYEKVIKacalkkdlQLLED-GDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:PRK13640 101 TVGDDVAFGlenRAVPRPEMIKIVR--------DVLADvGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 564 AVDAEVGKHLFQLCICQTLHEKITIL-VTHQLQYLKAASHILILKDGEMVQKGTYTEFLK 622
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVIsITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1097-1278 |
8.34e-10 |
|
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: 60.87 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP--EGKIwidKILTTEIG---LHDLR 1171
Cdd:COG1119 3 LLELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtyGNDV---RLFGERRGgedVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1172 KKMSII-PQVQLK----EAIEDL--------------PGKMDTELAE-----------SGSNF---SVGQRQLVCLARAI 1218
Cdd:COG1119 78 KRIGLVsPALQLRfprdETVLDVvlsgffdsiglyrePTDEQRERARellellglahlADRPFgtlSQGEQRRVLIARAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1219 LKKNRILIIDEATANVDPRTDELIQQKIReKFAQ---CTVLTIAHRLNTIIDS-DKIMVLDSGR 1278
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLD-KLAAegaPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
426-655 |
8.60e-10 |
|
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: 63.88 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR------------IAYVSQQPWVFSG-TVRSN 492
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILF-----GRKYEKERYEkvIKAcalkkdlqLLEDGDLTVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:TIGR01257 1024 ILFyaqlkGRSWEEAQLE--MEA--------MLEDTGLHHKRNEEAQdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 567 AEVGKHLFQLcICQTLHEKITILVTHQLQYLKA-ASHILILKDGEMVQKGTyTEFLKSGVDFGSLL----KKENEEAEPS 641
Cdd:TIGR01257 1094 PYSRRSIWDL-LLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT-PLFLKNCFGTGFYLtlvrKMKNIQSQRG 1171
|
250
....*....|....
gi 1958679184 642 PVPGTPTLRNRTFS 655
Cdd:TIGR01257 1172 GCEGTCSCTSKGFS 1185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1096-1285 |
8.97e-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: 62.90 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVI-VFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWI----DKILTTEIGLhD 1169
Cdd:TIGR03269 295 GVVkAVDNVSLE---------------VKEGEIFGIVGTSGAGKTTLSKIIAGVLEPtSGEVNVrvgdEWVDMTKPGP-D 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 LR----KKMSIIPQV-----------QLKEAIE-DLP---GKM-----------DTELAES-----GSNFSVGQRQLVCL 1214
Cdd:TIGR03269 359 GRgrakRYIGILHQEydlyphrtvldNLTEAIGlELPdelARMkavitlkmvgfDEEKAEEildkyPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1215 ARAILKKNRILIIDEATANVDPRTDELIQQKI---REKFAQcTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEP 1285
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDP 512
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1129-1280 |
1.02e-09 |
|
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: 59.90 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1129 GIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGlHDLRKKMSIIPQ-------------------------VQL 1182
Cdd:cd03264 29 GLLGPNGAGKTTLMRILATLTPPsSGTIRIDGQDVLKQP-QKLRRRIGYLPQefgvypnftvrefldyiawlkgipsKEV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1183 KEAIEDLPGKMDteLAESG----SNFSVGQRQLVCLARAILKKNRILIIDEATANVDP----RTDELIQQKIREKfaqcT 1254
Cdd:cd03264 108 KARVDEVLELVN--LGDRAkkkiGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeeriRFRNLLSELGEDR----I 181
|
170 180
....*....|....*....|....*..
gi 1958679184 1255 VLTIAHRLNTIIDS-DKIMVLDSGRLR 1280
Cdd:cd03264 182 VILSTHIVEDVESLcNQVAVLNKGKLV 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1099-1260 |
1.03e-09 |
|
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: 60.14 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1099 VFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI-----LTT--EIGLHDL 1170
Cdd:COG4778 26 VLDGVSFS---------------VAAGECVALTGPSGAGKSTLLKCIYGNYLPdSGSILVRHDggwvdLAQasPREILAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKK--------MSIIPQVQLKEAIED--LPGKMDTELAE-------------------SGSNFSVGQRQLVCLARAILKK 1221
Cdd:COG4778 91 RRRtigyvsqfLRVIPRVSALDVVAEplLERGVDREEARararellarlnlperlwdlPPATFSGGEQQRVNIARGFIAD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958679184 1222 NRILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLTIAH 1260
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFH 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
428-593 |
1.21e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELP--PTSGLVSVhgriayvsqqPWVFSGTVRSNI-LFGRKYEKERY 504
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV----------PDNQFGREASLIdAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 505 EKVIKACALkkdlqlledGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD---AEVGKHLFQLcICQT 581
Cdd:COG2401 116 VELLNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQK-LARR 185
|
170
....*....|...
gi 1958679184 582 LheKIT-ILVTHQ 593
Cdd:COG2401 186 A--GITlVVATHH 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
424-623 |
1.23e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLV--SVHGRIAYVSQQPwvfsgtvrsnilfgrkyek 501
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQDH------------------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 502 eryekvikACALKKDLQLLE---------DGDLTVIGDRG-------------ATLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK15064 392 --------AYDFENDLTLFDwmsqwrqegDDEQAVRGTLGrllfsqddikksvKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 560 DPLSAVDAEVGKHLfqlcicQTLHEKIT---ILVTHQLQYLKA-ASHILILKDGEMVQ-KGTYTEFLKS 623
Cdd:PRK15064 464 EPTNHMDMESIESL------NMALEKYEgtlIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYLRS 526
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
416-616 |
1.28e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 416 TAFWDKALDTPTLqglsfTARPGELLAVVGPVGAGKSSLLS------------AVLGELPPTSGLVSV------HGRIAY 477
Cdd:PRK13645 20 TPFEFKALNNTSL-----TFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIkevkrlRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 478 VSQQP--WVFSGTVRSNILFGRKYEKERYEKVIKACA-LKKDLQLLEDgdltVIGDRGATLSGGQKARVNLARAVYQDAD 554
Cdd:PRK13645 95 VFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPeLLKLVQLPED----YVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 555 IYLLDDPLSAVDAEVGKHLFQLCI-CQTLHEKITILVTHQL-QYLKAASHILILKDGEMVQKGT 616
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFErLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
436-604 |
1.40e-09 |
|
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: 60.46 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 436 RPGELLAVVGPVGAGKSSLLSAVLGELPPTSGL------------------------------VSVHGRIAYVSQQPWVF 485
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkllegdVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 486 SGTVRSniLFGRKYEKERYEKVIKACALKKDLqlledgdltvigDRG-ATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:cd03236 104 KGKVGE--LLKKKDERGKLDELVDQLELRHVL------------DRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958679184 565 VDaeVGKHLFQLCICQTL--HEKITILVTHQ---LQYLKAASHIL 604
Cdd:cd03236 170 LD--IKQRLNAARLIRELaeDDNYVLVVEHDlavLDYLSDYIHCL 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1114-1260 |
1.66e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.93 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE--PE----GKIWIDKILTTEIGLHDLRKKMSIIPQV------- 1180
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvsGEVYLDGQDIFKMDVIELRRRVQMVFQIpnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1181 ------------------------QLKEAIE--DLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANV 1234
Cdd:PRK14247 98 sifenvalglklnrlvkskkelqeRVRWALEkaQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180
....*....|....*....|....*.
gi 1958679184 1235 DPRTDELIQQKIREKFAQCTVLTIAH 1260
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
431-627 |
1.84e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVS-----------------VHGRIAYVSQQP--WVFSGTVRS 491
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstskqkeikpVRKKVGVVFQFPesQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFGRK---YEKERYEKV----IKACALKKdlQLLEDGDLtvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13643 105 DVAFGPQnfgIPKEKAEKIaaekLEMVGLAD--EFWEKSPF--------ELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 565 VDAEVGKHLFQLciCQTLHE--KITILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSgVDF 627
Cdd:PRK13643 175 LDPKARIEMMQL--FESIHQsgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE-VDF 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1096-1279 |
1.99e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.58 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID----KI---------- 1160
Cdd:COG3845 17 GVVANDDVSLT---------------VRPGEIHALLGENGAGKSTLMKILYGLYQPdSGEILIDgkpvRIrsprdaialg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1161 -------------LT-TE---IGLHDLRKkmsiiPQVQLKEAIEDLpgkmdTELAES-G---------SNFSVGQRQLVC 1213
Cdd:COG3845 82 igmvhqhfmlvpnLTvAEnivLGLEPTKG-----GRLDRKAARARI-----RELSERyGldvdpdakvEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1214 LARAILKKNRILIIDEATANVDPR-TDELIqqKIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRL 1279
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQeADELF--EILRRLAAegKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
440-615 |
2.32e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.47 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 440 LLAVVGPVGAGKSSLLSAV-----LGELPPTSGLVSVHGRIAY---------------VSQQPWVFSG-TVRSNILFGRK 498
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpievrrevgmVFQYPNPFPHlTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 499 YEK---------ERYEKVIKACALKKDLQlledgdlTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeV 569
Cdd:PRK14267 112 LNGlvkskkeldERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-V 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958679184 570 GKHLFQLCICQTLHEKITILVTHQ-LQYLKAASHILILKDGEMVQKG 615
Cdd:PRK14267 184 GTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1114-1293 |
3.55e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE------PEGKIWI--DKILTTEIGLHDLRKKMSII-------- 1177
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLfgRNIYSPDVDPIEVRREVGMVfqypnpfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1178 -------------------PQVQLKEAIE------DLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATA 1232
Cdd:PRK14267 99 hltiydnvaigvklnglvkSKKELDERVEwalkkaALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 1233 NVDPRTDELIQQKIREKFAQCTVLTIAHR-LNTIIDSDKIMVLDSGRLREYDEPYVLLQNPE 1293
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1096-1278 |
4.33e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSL---ISALFRLSEPEGKIWID-------KILTTEi 1165
Cdd:PRK13549 17 GVKALDNVSLK---------------VRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTYEGEIIFEgeelqasNIRDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1166 glhdlRKKMSII-------PQVQLKEAI----EDLPG-------------------KMDTELAESGSNFSVGQRQLVCLA 1215
Cdd:PRK13549 81 -----RAGIAIIhqelalvKELSVLENIflgnEITPGgimdydamylraqkllaqlKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1216 RAILKKNRILIIDEATANV-DPRTDEL--IQQKIREKFAQCtvLTIAHRLNTIID-SDKIMVLDSGR 1278
Cdd:PRK13549 156 KALNKQARLLILDEPTASLtESETAVLldIIRDLKAHGIAC--IYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
406-620 |
5.21e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.33 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 406 GKAIVHVQDFT-AFWDKALdtptLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVhG---RIAYVSQQ 481
Cdd:TIGR03719 319 GDKVIEAENLTkAFGDKLL----IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GetvKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 482 pwvfsgtvRSNIlfgrKYEKERYEKVikacalkkdlqllEDG-DLTVIGDR--------------GA-------TLSGGQ 539
Cdd:TIGR03719 394 --------RDAL----DPNKTVWEEI-------------SGGlDIIKLGKReipsrayvgrfnfkGSdqqkkvgQLSGGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 540 KARVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfqlciCQTLHEKI------TILVTHQLQYL-KAASHILILK-DGEM 611
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVET---------LRALEEALlnfagcAVVISHDRWFLdRIATHILAFEgDSHV 519
|
250
....*....|
gi 1958679184 612 VQ-KGTYTEF 620
Cdd:TIGR03719 520 EWfEGNFSEY 529
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1098-1281 |
5.51e-09 |
|
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: 57.87 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGP--LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILT----------- 1162
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVLVDgEPVTgpgpdrgyvfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1163 -------------TEIGL--HDLRKK------MSIIPQVQLKEAIEDLPGkmdtELaeSGsnfsvGQRQLVCLARAILKK 1221
Cdd:cd03293 81 qdallpwltvldnVALGLelQGVPKAeareraEELLELVGLSGFENAYPH----QL--SG-----GMRQRVALARALAVD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1222 NRILIIDEATANVDPRTDELIQQ---KIREKFAQcTVLTIAHRlntiID-----SDKIMVLDS--GRLRE 1281
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEellDIWRETGK-TVLLVTHD----IDeavflADRVVVLSArpGRIVA 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
438-610 |
5.86e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.54 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 438 GELLAVVGPVGAGKSSLLSAVLGELPPTSG--------LVSVHGRIAYVSQQ----PWvfsGTVRSNILFGRKYE-KERY 504
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtapLAEAREDTRLMFQDarllPW---KKVIDNVGLGLKGQwRDAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 505 EKVIKACALkkdlqlledgdltviGDRG----ATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQ 580
Cdd:PRK11247 115 LQALAAVGL---------------ADRAnewpAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESL 179
|
170 180 190
....*....|....*....|....*....|..
gi 1958679184 581 TLHEKITI-LVTHQLQYLKA-ASHILILKDGE 610
Cdd:PRK11247 180 WQQHGFTVlLVTHDVSEAVAmADRVLLIEEGK 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
428-616 |
6.86e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.97 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQPWVFSG-TVRSN 492
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqtakimreaVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGRKY-EKERYEKVIKACAlkkDL--QLLEDGdltviGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:PRK11614 101 LAMGGFFaERDQFQERIKWVY---ELfpRLHERR-----IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958679184 570 GKHLFQLcICQTLHEKITILVTHQ--LQYLKAASHILILKDGEMVQKGT 616
Cdd:PRK11614 173 IQQIFDT-IEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
418-619 |
7.17e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 418 FWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-IAYVSQQPWVfsgTVRSNI--- 493
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWR---AVRSDIqmi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 -----------------------LFGRKYEKERYEKVIKACALKkdLQLLEDgdltVIGDRGATLSGGQKARVNLARAVY 550
Cdd:PRK15079 104 fqdplaslnprmtigeiiaeplrTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 551 QDADIYLLDDPLSAVDAEVGKHLFQLciCQTLHEKI---TILVTHQLQYLKAAS-HILILKDGEMVQKGTYTE 619
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNL--LQQLQREMglsLIFIAHDLAVVKHISdRVLVMYLGHAVELGTYDE 248
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1113-1292 |
7.38e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1113 LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLR----KKMSI----------- 1176
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPtRGQVLIDGVDIAKISDAELRevrrKKIAMvfqsfalmphm 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 --------------IPQVQLKEAIEDLPGKMDTELAESG--SNFSVGQRQLVCLARAILKKNRILIIDEATANVDP--RT 1238
Cdd:PRK10070 122 tvldntafgmelagINAEERREKALDALRQVGLENYAHSypDELSGGMRQRVGLARALAINPDILLMDEAFSALDPliRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 1239 ---DELIQQKIREkfaQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNP 1292
Cdd:PRK10070 202 emqDELVKLQAKH---QRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
431-622 |
8.17e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.02 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTARPGELLAVVGPVGAGKSSLLSAVLGeLPPTSGLVSVHGRI-------------AYVSQQ-PWVFSGTVrsnilFg 496
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelarhrAYLSQQqTPPFAMPV-----F- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 497 rKY-EKERYEKVIKAC---ALKKDLQLLEDGDLtvIGDRGATLSGGQKARVNLARAVYQ-------DADIYLLDDPLSAV 565
Cdd:PRK03695 88 -QYlTLHQPDKTRTEAvasALNEVAEALGLDDK--LGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 566 DAEVGKHLFQLC--ICQtlhEKITILVT-HQLQY-LKAASHILILKDGEMVQKGTYTEFLK 622
Cdd:PRK03695 165 DVAQQAALDRLLseLCQ---QGIAVVMSsHDLNHtLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
424-566 |
8.84e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------RIAYvsQQPWVFSG---------T 488
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTY--QKQLCFVGhrsginpylT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 489 VRSNILFGRKYEKERYEkVIKACALKKDLQLLedgDLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD 566
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-ITELCRLFSLEHLI---DYPC-----GLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1096-1279 |
1.34e-08 |
|
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: 57.06 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID----------KI---- 1160
Cdd:cd03219 12 GLVALDDVSFS---------------VRPGEIHGLIGPNGAGKTTLFNLISGFLRPtSGSVLFDgeditglpphEIarlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1161 -------------LTT----EIGLHDLRKKMSIIPQV-----QLKEAIED------LPGKMDtELAesgSNFSVGQRQLV 1212
Cdd:cd03219 77 igrtfqiprlfpeLTVlenvMVAAQARTGSGLLLARArreerEARERAEEllervgLADLAD-RPA---GELSYGQQRRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 1213 CLARAILKKNRILIIDEATANVDPR-TDELIQ--QKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGRL 1279
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEeTEELAEliRELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1098-1296 |
1.40e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 58.19 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSL---ISALFRLSEpeGKIWID-KILTT------EIGL 1167
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLlrmIAGFETPDS--GRILLDgRDVTGlppekrNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1168 ---------H----D-----LR-KKMS---IIPQVQlkEAIE--DLPGKMD---TELaeSGsnfsvGQRQLVCLARAILK 1220
Cdd:COG3842 82 vfqdyalfpHltvaEnvafgLRmRGVPkaeIRARVA--ELLElvGLEGLADrypHQL--SG-----GQQQRVALARALAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1221 KNRILIIDEATANVDPRTDELIQQKIREkfaqctvltIAHRLN-TII----D-------SDKIMVLDSGRLREYDEPYVL 1288
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRR---------LQRELGiTFIyvthDqeealalADRIAVMNDGRIEQVGTPEEI 223
|
....*...
gi 1958679184 1289 LQNPESLF 1296
Cdd:COG3842 224 YERPATRF 231
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
437-618 |
1.54e-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: 55.44 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 437 PGELLAVVGPVGAGKSSLLSAVLgelpptsglvsvhgriayvsqqpWVFSGtvRSNILFGRKYEKERYekvIKACAlkkD 516
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG-----------------------LALGG--AQSATRRRSGVKAGC---IVAAV---S 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 517 LQLLedgdLTVIGdrgatLSGGQKARVNLARAV----YQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTH 592
Cdd:cd03227 69 AELI----FTRLQ-----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
170 180
....*....|....*....|....*.
gi 1958679184 593 QLQYLKAASHILILKdgeMVQKGTYT 618
Cdd:cd03227 140 LPELAELADKLIHIK---KVITGVYK 162
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
424-619 |
1.59e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.47 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSG----------------LVSVHGRIAYVSQQPWVFSG 487
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGeilfdgenipamsrsrLYTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -TVRSNILFGRKYEKERYEKVIKACALKKdlqlledgdLTVIGDRGAT------LSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK11831 99 mNVFDNVAYPLREHTQLPAPLLHSTVMMK---------LEAVGLRGAAklmpseLSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 561 PLSAVDAEVGKHLFQLcICQTLHE-KIT-ILVTHQL-QYLKAASHILILKDGEMVQKGTYTE 619
Cdd:PRK11831 170 PFVGQDPITMGVLVKL-ISELNSAlGVTcVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQA 230
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
93-342 |
1.93e-08 |
|
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: 57.42 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIFTLIeeTTRVVQ---PIFLGKIIDYFEKYDSDDSAALHtaygYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVA 169
Cdd:cd18541 1 YLLGILFLI--LVDLLQlliPRIIGRAIDALTAGTLTASQLLR----YALLILLLALLIGIFRFLWRYLIFGASRRIEYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 170 MCHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVtiflhflwAGP--LQAIGVTIL----LWVEIGISclAGLAI 243
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMA--------LGPgiLYLVDALFLgvlvLVMMFTIS--PKLTL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 244 LVIL-LPLQSCIGKLFSSL---RSKTA--AFTDarirtMN----EVITGMRIIKMYAWE----KSFADLITNLRKKEIS- 308
Cdd:cd18541 145 IALLpLPLLALLVYRLGKKihkRFRKVqeAFSD-----LSdrvqESFSGIRVIKAFVQEeaeiERFDKLNEEYVEKNLRl 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1958679184 309 -K-----------ILGSSYLRGMNMASFFIANKVIL---FVTFTTYVLL 342
Cdd:cd18541 220 aRvdalffpliglLIGLSFLIVLWYGGRLVIRGTITlgdLVAFNSYLGM 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1114-1246 |
2.24e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDkilttEIGLHDL-RKKM----------------SI 1176
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFD-----GQPLHNLnRRQLlpvrhriqvvfqdpnsSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1177 IPQVQLKEAIED--------LPGKMDTE-----LAESG----------SNFSVGQRQLVCLARAILKKNRILIIDEATAN 1233
Cdd:PRK15134 376 NPRLNVLQIIEEglrvhqptLSAAQREQqviavMEEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170
....*....|...
gi 1958679184 1234 VDpRTdelIQQKI 1246
Cdd:PRK15134 456 LD-KT---VQAQI 464
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1104-1285 |
2.30e-08 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 56.22 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKI-LTTEIGlhDLRKKMSIIPQVQ 1181
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTsGRATVAGHdVVREPR--EVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1182 -------------------------LKEAIEDLPGKMdtELAESG----SNFSVGQRQLVCLARAILKKNRILIIDEATA 1232
Cdd:cd03265 83 svddeltgwenlyiharlygvpgaeRRERIDELLDFV--GLLEAAdrlvKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1233 NVDPRTDELIQ---QKIREKFAQcTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEP 1285
Cdd:cd03265 161 GLDPQTRAHVWeyiEKLKEEFGM-TILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTP 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
428-612 |
2.33e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-IAYVSQQPWVFsgtVRSNI--LFGRKY---EK 501
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITRLKNREVPF---LRRQIgmIFQDHHllmDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 502 ERYEKV----IKACALKKDLQLLEDGDLTVIG--DRGAT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGK 571
Cdd:PRK10908 95 TVYDNVaiplIIAGASGDDIRRRVSAALDKVGllDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958679184 572 HLFQLcICQTLHEKITILV-THQLQYLKAASH-ILILKDGEMV 612
Cdd:PRK10908 175 GILRL-FEEFNRVGVTVLMaTHDIGLISRRSYrMLTLSDGHLH 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
394-561 |
2.78e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 394 ELPERKAqEPSDGKAIVHVQDFTAFWDKALdtPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG 473
Cdd:COG3845 243 LLRVEKA-PAEPGEVVLEVENLSVRDDRGV--PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 474 R--------------IAYVSQQPW----VFSGTVRSNILFGRkYEKERYEK--VIKACALKKD-LQLLEDGD--LTVIGD 530
Cdd:COG3845 320 EditglsprerrrlgVAYIPEDRLgrglVPDMSVAENLILGR-YRRPPFSRggFLDRKAIRAFaEELIEEFDvrTPGPDT 398
|
170 180 190
....*....|....*....|....*....|...
gi 1958679184 531 RGATLSGG--QKarVNLARAVYQDADIYLLDDP 561
Cdd:COG3845 399 PARSLSGGnqQK--VILARELSRDPKLLIAAQP 429
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1098-1281 |
2.79e-08 |
|
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: 55.72 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHD------- 1169
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGGRDVTDLPPKDrdiamvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 --------------------LRK--KMSIIPQVqlKEAIEDLpgKMDTELAESGSNFSVGQRQLVCLARAILKKNRILII 1227
Cdd:cd03301 79 qnyalyphmtvydniafglkLRKvpKDEIDERV--REVAELL--QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1228 DEATANVDPRTDELIQQKIRE--KFAQCTVLTIAH-RLNTIIDSDKIMVLDSGRLRE 1281
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQ 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
431-623 |
2.80e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.64 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTARPgeLLAVVGPVGAGKSSLLSAVLGELPPTSG-------------------LVSVHGRIAYVSQQPWVFSGTVRS 491
Cdd:PRK14271 42 MGFPARA--VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsifnyrdVLEFRRRVGMLFQRPNPFPMSIMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFGRKYEKERYEKVIKACALKKdlqLLEDGDLTVIGDRGAT----LSGGQKARVNLARAVYQDADIYLLDDPLSAVDA 567
Cdd:PRK14271 120 NVLAGVRAHKLVPRKEFRGVAQAR---LTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDP 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 568 EVGKHLFQLciCQTLHEKIT-ILVTHQL-QYLKAASHILILKDGEMVQKGTYTEFLKS 623
Cdd:PRK14271 197 TTTEKIEEF--IRSLADRLTvIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1099-1294 |
3.04e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.21 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1099 VFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KIL-----TTEIGLHDLR 1171
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDgKVLyfgkdIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1172 KKMSIIPQV--------------------------QLKEAIED------LPGKMDTELAESGSNFSVGQRQLVCLARAIL 1219
Cdd:PRK14246 90 KEVGMVFQQpnpfphlsiydniayplkshgikekrEIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1220 KKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPES 1294
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
424-612 |
3.04e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.91 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTS-----------------------GLVSVHGRIAYVSQ 480
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdgeiywsgsplkasnirdteraGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 481 QpwvfsgTVRSNILFGR----KYEKERYEKVIKAC-ALKKDLQLLEDGDLTVIGDRGatlsGGQKARVNLARAVYQDADI 555
Cdd:TIGR02633 93 L------SVAENIFLGNeitlPGGRMAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 556 YLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQLQYLKAASH-ILILKDGEMV 612
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDtICVIRDGQHV 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
424-619 |
3.14e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.07 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAV--LGELPP---TSGLVSVHG-------------RIAYVSQQP-WV 484
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPearVSGEVYLDGqdifkmdvielrrRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 485 FSGTVRSNILFGRKY------EKERYEKVIKAcaLKKdLQLLEDgdltvIGDR----GATLSGGQKARVNLARAVYQDAD 554
Cdd:PRK14247 95 PNLSIFENVALGLKLnrlvksKKELQERVRWA--LEK-AQLWDE-----VKDRldapAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 555 IYLLDDPLSAVDAEVGKHLFQLCIcqTLHEKITI-LVTH-QLQYLKAASHILILKDGEMVQKGTYTE 619
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFL--ELKKDMTIvLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
437-612 |
3.21e-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: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 437 PGELLAVVGPVGAGKSSLLSAVLGELPPTSGlvsvhgriayvsqqpwvfsgtvrsnilfgrkyekeryeKVIKACALKKD 516
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--------------------------------------GVIYIDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 517 LQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTL-----HEKITILVT 591
Cdd:smart00382 43 EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLlllksEKNLTVILT 122
|
170 180
....*....|....*....|.
gi 1958679184 592 HQLQYLKAASHILILKDGEMV 612
Cdd:smart00382 123 TNDEKDLGPALLRRRFDRRIV 143
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
424-566 |
3.30e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPT-SGLVSVHGR--------------IAYVSQQ---PWVF 485
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRrrgsgetiwdikkhIGYVSSSlhlDYRV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 486 SGTVRSNILFGRKYEKERYEKVIKAcalkkdLQLLEDGDLTVIGDRGAT-------LSGGQKARVNLARAVYQDADIYLL 558
Cdd:PRK10938 352 STSVRNVILSGFFDSIGIYQAVSDR------QQKLAQQWLDILGIDKRTadapfhsLSWGQQRLALIVRALVKHPTLLIL 425
|
....*...
gi 1958679184 559 DDPLSAVD 566
Cdd:PRK10938 426 DEPLQGLD 433
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1097-1279 |
3.64e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.65 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYsLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIW-----IDKILTTEIGLhdL 1170
Cdd:PRK10908 1 MIRFEHVSKAY-LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSaGKIWfsghdITRLKNREVPF--L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSII------------------PQVQLKEAIEDLPGKMDTELAESG-----SNFSV----GQRQLVCLARAILKKNR 1223
Cdd:PRK10908 78 RRQIGMIfqdhhllmdrtvydnvaiPLIIAGASGDDIRRRVSAALDKVGlldkaKNFPIqlsgGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1224 ILIIDEATANVDPRTDELIqQKIREKFAQ--CTVLTIAHRLNTIIDSD-KIMVLDSGRL 1279
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGI-LRLFEEFNRvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
425-619 |
3.78e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.39 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 425 TPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR---------------IAYVSQQP--WVFSG 487
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklresVGMVFQDPdnQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 TVRSNILFG----RKYEKERYEKVIKACAlKKDLQLLEDGDLtvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:PRK13636 99 SVYQDVSFGavnlKLPEDEVRKRVDNALK-RTGIEHLKDKPT-------HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 564 AVDAEVGKHLFQLCICQTLHEKITILV-THQLQYLKA-ASHILILKDGEMVQKGTYTE 619
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKELGLTIIIaTHDIDIVPLyCDNVFVMKEGRVILQGNPKE 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1097-1281 |
4.09e-08 |
|
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: 55.52 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSL-DGPL-VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-KILTT--EIGLHDL 1170
Cdd:COG4181 8 IIELRGLTKTVGTgAGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAgQDLFAldEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 R-KKMSIIPQ-VQL---KEAIED--LP----GKMD------TELAESG---------SNFSVGQRQLVCLARAILKKNRI 1224
Cdd:COG4181 88 RaRHVGFVFQsFQLlptLTALENvmLPlelaGRRDarararALLERVGlghrldhypAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1225 LIIDEATANVDPRTDELIQQKIREKFAQ--CTVLTIAHRLNTIIDSDKIMVLDSGRLRE 1281
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1097-1298 |
4.37e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.39 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1097 VIVFDNVNFTYSlDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDK--ILTTEIGLHDLRKK 1173
Cdd:PRK13636 5 ILKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPsSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1174 MSII---PQVQLKEA--IED---------LPGK-----MDTELAESGSN---------FSVGQRQLVCLARAILKKNRIL 1225
Cdd:PRK13636 84 VGMVfqdPDNQLFSAsvYQDvsfgavnlkLPEDevrkrVDNALKRTGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1226 IIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTI-IDSDKIMVLDSGRLreydepyVLLQNPESLFYK 1298
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVpLYCDNVFVMKEGRV-------ILQGNPKEVFAE 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
191-612 |
5.54e-08 |
|
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: 57.12 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 191 TGQIVNLLSNDVnkfDQVTIFLHFLwagPLQAIGVTILL-------WVEIGISCLAGLAILVILLPLQSCIGKLFSSLRs 263
Cdd:COG4615 104 AARLLAALTEDV---RTISQAFVRL---PELLQSVALVLgclaylaWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLR- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 264 KTAAFTDARIRTMNEVITGMRIIKMYAwEKSFA----DLITNLRKKEISKILG-SSYLRGMNMAS--FFIANKVILFVtF 336
Cdd:COG4615 177 RAREAEDRLFKHFRALLEGFKELKLNR-RRRRAffdeDLQPTAERYRDLRIRAdTIFALANNWGNllFFALIGLILFL-L 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 337 TTYVLLGNKITASHVFVAMTLYGAVRLTVtlffpSAIERVSEAVVSVRRIKNfllLDELPERKAQEPSDGKAIVHVQDFT 416
Cdd:COG4615 255 PALGWADPAVLSGFVLVLLFLRGPLSQLV-----GALPTLSRANVALRKIEE---LELALAAAEPAAADAAAPPAPADFQ 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 417 ---------AFWDKALDTP-TLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-------RIAYVS 479
Cdd:COG4615 327 tlelrgvtyRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpvtadnREAYRQ 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 480 QqpwvFSgTVRSNI-LFGRKYEKERYEKVIKACALKKDLQLleDGDLTVIGDRGAT--LSGGQKARVNLARAVYQDADIY 556
Cdd:COG4615 407 L----FS-AVFSDFhLFDRLLGLDGEADPARARELLERLEL--DHKVSVEDGRFSTtdLSQGQRKRLALLVALLEDRPIL 479
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 557 LLD------DPlsavdaeVGKHLF--QLcicqtLHE-----KITILVTHQLQYLKAASHILILKDGEMV 612
Cdd:COG4615 480 VFDewaadqDP-------EFRRVFytEL-----LPElkargKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
93-334 |
6.97e-08 |
|
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: 55.48 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILG-IFTLIEETTRVVQPIFLGKIIDYFEKyDSDDSAALHTAyGYAAVLSLCTLILAILHHLYFYHV-QCAGMRIRvam 170
Cdd:cd18548 1 AILApLFKLLEVLLELLLPTLMADIIDEGIA-NGDLSYILRTG-LLMLLLALLGLIAGILAGYFAAKAsQGFGRDLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 171 cHMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIGVTILLwveIGISclAGLA-ILVILL 248
Cdd:cd18548 76 -KDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNfVMMLLRMLVRAPIMLIGAIIMA---FRIN--PKLAlILLVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 249 PLQSCI--------GKLFSSLRSKtaafTDARIRTMNEVITGMRIIKMYAWE----KSFADLITNLRKKEIS--KILGSs 314
Cdd:cd18548 150 PILALVvflimkkaIPLFKKVQKK----LDRLNRVVRENLTGIRVIRAFNREdyeeERFDKANDDLTDTSLKagRLMAL- 224
|
250 260
....*....|....*....|
gi 1958679184 315 ylrgMNMASFFIANKVILFV 334
Cdd:cd18548 225 ----LNPLMMLIMNLAIVAI 240
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
761-1070 |
7.01e-08 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 55.47 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 761 LSWYLGIYTGLTAVTVLFGIARSLLVFYVLVNASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvdgaldshrhls 840
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPV---------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 841 hphpwpqnGSLqasVTSVTgSDV--IR--FPEVLLLALpgrilnrfskdighmDDLLPLT-------FLDFIQTLLLvvs 909
Cdd:cd18544 98 --------GRL---VTRVT-NDTeaLNelFTSGLVTLI---------------GDLLLLIgiliamfLLNWRLALIS--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 910 viavaaavipwiLIPLVPLSIIFVVLRRYfletSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQD 989
Cdd:cd18544 148 ------------LLVLPLLLLATYLFRKK----SRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 990 LHSEAWFLFLTTSRWF--AVRLDAICAVFVIVVAFGSLVLAKTLDAGQVGLALSYsltlMGMF---------QWSVRQSA 1058
Cdd:cd18544 212 EYRKANLKSIKLFALFrpLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQY----IQRFfrpirdlaeKFNILQSA 287
|
330
....*....|..
gi 1958679184 1059 evenmMISVERV 1070
Cdd:cd18544 288 -----MASAERI 294
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1105-1285 |
7.26e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.40 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1105 FTYSlDGPlVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE--GKIWIDKILT-TEIGLHDLRKKMSII---P 1178
Cdd:PRK13638 9 FRYQ-DEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkgAVLWQGKPLDySKRGLLALRQQVATVfqdP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1179 QVQ----------------LKEAIEDLPGKMDTELAESGSN---------FSVGQRQLVCLARAILKKNRILIIDEATAN 1233
Cdd:PRK13638 87 EQQifytdidsdiafslrnLGVPEAEITRRVDEALTLVDAQhfrhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1234 VDPRTDELIQQKIREKFAQCTVLTI-AHRLNTIID-SDKIMVLDSGRLREYDEP 1285
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1124-1267 |
7.41e-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: 53.15 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1124 SREKVGIVGRTGAGKSSLISALFRLSEPEGKiwIDKILTTEIGLHDLRKKMSIIPQVqlkeaiedlpgkmdtelaESGSN 1203
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--GVIYIDGEDILEEVLDQLLLIIVG------------------GKKAS 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 1204 FSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQ-------KIREKFAQCTVLTIAHRLNTIID 1267
Cdd:smart00382 61 GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrllLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
406-561 |
7.58e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 406 GKAIVHVQDFT-AFWDKALdtptLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVhG---RIAYVSQQ 481
Cdd:PRK11819 321 GDKVIEAENLSkSFGDRLL----IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GetvKLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 482 pwvfsgtvRSNIlfgrKYEKERYEKVikacalkkdlqllEDG-DLTVIGDR--------------GA-------TLSGGQ 539
Cdd:PRK11819 396 --------RDAL----DPNKTVWEEI-------------SGGlDIIKVGNReipsrayvgrfnfkGGdqqkkvgVLSGGE 450
|
170 180
....*....|....*....|..
gi 1958679184 540 KARVNLARAVYQDADIYLLDDP 561
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEP 472
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1104-1293 |
8.35e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.76 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE------GKIWID--KILTTEIGL-HDLRKKM 1174
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirvGDITIDtaRSLSQQKGLiRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SII-------------------PQVQLKEAIEDLPGKMDTELAESG---------SNFSVGQRQLVCLARAILKKNRILI 1226
Cdd:PRK11264 88 GFVfqnfnlfphrtvleniiegPVIVKGEPKEEATARARELLAKVGlagketsypRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1227 IDEATANVDPrtdEL-------IQQKIREKFaqcTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPE 1293
Cdd:PRK11264 168 FDEPTSALDP---ELvgevlntIRQLAQEKR---TMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1084-1278 |
8.60e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.99 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1084 CRKRPPPG--WPHEGV-------------IVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRL 1148
Cdd:PRK13536 11 PRRLELSPieRKHQGIseakasipgsmstVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1149 SEP-EGKIwidkiltTEIGL------HDLRKKMSIIPQV-------------------------QLKEAIEDL------P 1190
Cdd:PRK13536 91 TSPdAGKI-------TVLGVpvparaRLARARIGVVPQFdnldleftvrenllvfgryfgmstrEIEAVIPSLlefarlE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1191 GKMDTELAEsgsnFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQC-TVLTIAH------RLn 1263
Cdd:PRK13536 164 SKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTHfmeeaeRL- 238
|
250
....*....|....*
gi 1958679184 1264 tiidSDKIMVLDSGR 1278
Cdd:PRK13536 239 ----CDRLCVLEAGR 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1104-1279 |
9.92e-08 |
|
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: 53.68 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE---GKIWIDKILTTEIGLHDlRKKMSIIPQV 1180
Cdd:cd03217 5 DLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvteGEILFKGEDITDLPPEE-RARLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1181 QLKEAIedlPG-KMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE-KFAQCTVLTI 1258
Cdd:cd03217 84 QYPPEI---PGvKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLII 160
|
170 180
....*....|....*....|...
gi 1958679184 1259 AH--RLNTIIDSDKIMVLDSGRL 1279
Cdd:cd03217 161 THyqRLLDYIKPDRVHVLYDGRI 183
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1126-1294 |
1.01e-07 |
|
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: 56.23 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1126 EKVGIVGRTGAGKSSLISALFRLSEPEGKIWID--KILT-TEIGLHDLRKKMSIIPQ-----------VqlkEAI--EDL 1189
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDgqDLDGlSRRALRPLRRRMQVVFQdpfgslsprmtV---GQIiaEGL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1190 ----PGKMDTE--------LAESG----------SNFSVGQRQLVCLARAILKKNRILIIDEATANVDpRTdelIQQKIR 1247
Cdd:COG4172 390 rvhgPGLSAAErrarvaeaLEEVGldpaarhrypHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VS---VQAQIL 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1248 EKFA------QCTVLTIAHRLNTI--IdSDKIMVLDSGRLREYDEPYVLLQNPES 1294
Cdd:COG4172 466 DLLRdlqrehGLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDAPQH 519
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1098-1296 |
1.11e-07 |
|
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: 54.17 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEI----------- 1165
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPtSGEILLDGKDITNLpphkrpvntvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1166 -----------------GLHDLRKKMSIIPQvQLKEAI-----EDLPGKMDTELaeSGsnfsvGQRQLVCLARAILKKNR 1223
Cdd:cd03300 79 qnyalfphltvfeniafGLRLKKLPKAEIKE-RVAEALdlvqlEGYANRKPSQL--SG-----GQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1224 ILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAH-RLNTIIDSDKIMVLDSGRLREYDEPYVLLQNPESLF 1296
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1104-1295 |
1.16e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.39 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALF-RLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQ--- 1179
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQhss 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ----------VQLKEAIEDLPGKMDTELAE-----------SGSNF---SVGQRQLVCLARAIL------KKNRILIIDE 1229
Cdd:PRK13548 87 lsfpftveevVAMGRAPHGLSRAEDDALVAaalaqvdlahlAGRDYpqlSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1230 ATANVDPRTDELIQQKIREkFAQ---CTVLTIAHRLN-TIIDSDKIMVLDSGRLREYDEPYVLLQnPESL 1295
Cdd:PRK13548 167 PTSALDLAHQHHVLRLARQ-LAHergLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT-PETL 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1098-1295 |
1.24e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.79 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPL---VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKIL----TTEIGLHD 1169
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTtGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 LRKKMSII---PQVQLKE-----AIEDLPG--KMDTE-------------------LAESGSNFSVGQRQLVCLArAILK 1220
Cdd:PRK13646 83 VRKRIGMVfqfPESQLFEdtverEIIFGPKnfKMNLDevknyahrllmdlgfsrdvMSQSPFQMSGGQMRKIAIV-SILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1221 KN-RILIIDEATANVDPRTDELIQ---QKIREKFAQcTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPESL 1295
Cdd:PRK13646 162 MNpDIIVLDEPTAGLDPQSKRQVMrllKSLQTDENK-TIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
430-616 |
1.31e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.23 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 430 GLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-IAYVSQQPWVFSGTVR------------------ 490
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhIEGLPGHQIARMGVVRtfqhvrlfremtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 491 --------SNILFG-------RKYEKEryekvikacALKKDLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDAD 554
Cdd:PRK11300 103 vaqhqqlkTGLFSGllktpafRRAESE---------ALDRAATWLERVGLLEHANRQAgNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 555 IYLLDDPLSAVDAEVGKHLFQLcICQTLHE-KITI-LVTHQLQYLKAAS-HILILKDGEMVQKGT 616
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDEL-IAELRNEhNVTVlLIEHDMKLVMGISdRIYVVNQGTPLANGT 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1113-1293 |
1.41e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.40 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1113 LVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSE------PEGKI-WIDK-ILTTEIGLHDLRKKM---------- 1174
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfrVEGKVtFHGKnLYAPDVDPVEVRRRIgmvfqkpnpf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 --SIIPQVQLKEAIEDLPGKMDT-----------------ELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVD 1235
Cdd:PRK14243 104 pkSIYDNIAYGARINGYKGDMDElverslrqaalwdevkdKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALD 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 1236 PRTDELIQQKIREKFAQCTVLTIAHRL-------------NTIIDSDKIMVldsGRLREYDEPYVLLQNPE 1293
Cdd:PRK14243 184 PISTLRIEELMHELKEQYTIIIVTHNMqqaarvsdmtaffNVELTEGGGRY---GYLVEFDRTEKIFNSPQ 251
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1122-1278 |
2.01e-07 |
|
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: 53.21 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1122 IKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIW-----IDKILTTEIglhdLRKKMSIIPQ---------------- 1179
Cdd:cd03224 23 VPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRfdgrdITGLPPHER----ARAGIGYVPEgrrifpeltveenlll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ---VQLKEAIEDLPGKM-------DTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE- 1248
Cdd:cd03224 99 gayARRRAKRKARLERVyelfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREl 178
|
170 180 190
....*....|....*....|....*....|.
gi 1958679184 1249 KFAQCTVLTIAHRLNTIID-SDKIMVLDSGR 1278
Cdd:cd03224 179 RDEGVTILLVEQNARFALEiADRAYVLERGR 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
424-615 |
2.34e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.55 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPP----TSGLV----------SVHGR-IAYVSQQPWVFSGT 488
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVlldgkpvapcALRGRkIATIMQNPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 489 VRSNilfgRKYEKERYEKVIKACALKKDLQLLEDGDL----TVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK10418 95 LHTM----HTHARETCLALGKPADDATLTAALEAVGLenaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 565 VDAEVGKHLFQLC--ICQTlHEKITILVTHQLQYL-KAASHILILKDGEMVQKG 615
Cdd:PRK10418 171 LDVVAQARILDLLesIVQK-RALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1117-1279 |
2.81e-07 |
|
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: 52.88 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1117 HLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKI------------------------LTTE--IGLhd 1169
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGVdvtaappadrpvsmlfqennlfahLTVEqnVGL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 lrkkmSIIPQVQL----KEAIEDLPGKM--DTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDP-RTDELI 1242
Cdd:cd03298 94 -----GLSPGLKLtaedRQAIEVALARVglAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPaLRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958679184 1243 Q--QKIREKfAQCTVLTIAHRLNTIID-SDKIMVLDSGRL 1279
Cdd:cd03298 169 DlvLDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
428-632 |
2.82e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-IAYVSQQPW-VFSGTVRsnILF----GRKYEK 501
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEpLAKLNRAQRkAFRRDIQ--MVFqdsiSAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 502 ERYEKVI-----------KACALKKDLQLLE--DGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAe 568
Cdd:PRK10419 106 KTVREIIreplrhllsldKAERLARASEMLRavDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL- 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 569 vgkhLFQLCICQTL----HEKIT--ILVTHQLQYL-KAASHILILKDGEMVQKGTYTEFLKSGVDFGSLLK 632
Cdd:PRK10419 185 ----VLQAGVIRLLkklqQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVLQ 251
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
428-611 |
3.04e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.86 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG----------RIAYVSQQ-PWVFSG-------TV 489
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeeaRAKLRAKHvGFVFQSfmliptlNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 490 RSNI-----LFGrkyEKERYEKViKACALKKDLQLledgdltviGDR----GATLSGGQKARVNLARAVYQDADIYLLDD 560
Cdd:PRK10584 106 LENVelpalLRG---ESSRQSRN-GAKALLEQLGL---------GKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 561 PLSAVDAEVGKH----LFQLcicQTLHEKITILVTHQLQYLKAASHILILKDGEM 611
Cdd:PRK10584 173 PTGNLDRQTGDKiadlLFSL---NREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
363-566 |
3.28e-07 |
|
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: 54.81 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 363 LTVTLFFPSAIERVSEAVVSVRR------------IKNFLLLDELPErKAQEPSDGKAIVHVQDFTAFW-------DKAL 423
Cdd:TIGR03269 222 MVLTSHWPEVIEDLSDKAIWLENgeikeegtpdevVAVFMEGVSEVE-KECEVEVGEPIIKVRNVSKRYisvdrgvVKAV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DtptlqGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSV----------------HGR----IAYVSQQPW 483
Cdd:TIGR03269 301 D-----NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRakryIGILHQEYD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 484 VFS-GTVRSNILFGRKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPL 562
Cdd:TIGR03269 376 LYPhRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
....
gi 1958679184 563 SAVD 566
Cdd:TIGR03269 456 GTMD 459
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1116-1293 |
3.40e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1116 KHLTALIksrekvgivGRTGAGKSSLISALFRLSE--PE----GKIWID--KILTTEIGLHDLRKK------------MS 1175
Cdd:PRK14239 31 NEITALI---------GPSGSGKSTLLRSINRMNDlnPEvtitGSIVYNghNIYSPRTDTVDLRKEigmvfqqpnpfpMS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 IIPQV-------------QLKEAIED-LPG-----KMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDP 1236
Cdd:PRK14239 102 IYENVvyglrlkgikdkqVLDEAVEKsLKGasiwdEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 1237 RTDELIQQKIREKFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPE 1293
Cdd:PRK14239 182 ISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1071-1279 |
3.58e-07 |
|
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: 52.72 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1071 IEYTDLEKEAPwecRKRPPPGWP----------HEGVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSS 1140
Cdd:cd03267 1 IEVSNLSKSYR---VYSKEPGLIgslkslfkrkYREVEALKGISFT---------------IEKGEIVGFIGPNGAGKTT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1141 LISALFRLSEP-EGKI-------WIDKI-LTTEIGL-----------------HDLRKKMSIIPQVQLKEAIEDLPGKMD 1194
Cdd:cd03267 63 TLKILSGLLQPtSGEVrvaglvpWKRRKkFLRRIGVvfgqktqlwwdlpvidsFYLLAAIYDLPPARFKKRLDELSELLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1195 TE--LAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTVLTIAHRLNTIID-SD 1269
Cdd:cd03267 143 LEelLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlAR 222
|
250
....*....|
gi 1958679184 1270 KIMVLDSGRL 1279
Cdd:cd03267 223 RVLVIDKGRL 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
416-566 |
3.59e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 416 TAFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTS---------------GLVSVHGRIAYVSQ 480
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKgavlwqgkpldyskrGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 481 QP--WVFSGTVRSNILFGRK----YEKERYEKVIKACALkKDLQLLEDGDLTVigdrgatLSGGQKARVNLARAVYQDAD 554
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRnlgvPEAEITRRVDEALTL-VDAQHFRHQPIQC-------LSHGQKKRVAIAGALVLQAR 156
|
170
....*....|..
gi 1958679184 555 IYLLDDPLSAVD 566
Cdd:PRK13638 157 YLLLDEPTAGLD 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
436-566 |
3.87e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 436 RPGELLAVVGPVGAGKSSLLSAVLGELPPTSG-------------------------------LVSVHgRIAYVSQQPWV 484
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtelqnyfkklyngeIKVVH-KPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 485 FSGTVRSniLFGRKYEKERYEKVIKACALKKDLqlleDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK13409 176 FKGKVRE--LLKKVDERGKLDEVVERLGLENIL----DRDIS-------ELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
..
gi 1958679184 565 VD 566
Cdd:PRK13409 243 LD 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
436-566 |
4.12e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 436 RPGELLAVVGPVGAGKSSLLSAVLGEL---------PPT---------------------SGLVSVHGRIAYVSQQPWVF 485
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSwdevlkrfrgtelqdyfkklaNGEIKVAHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 486 SGTVRSniLFGRKYEKERYEKVIKACALKKDLqlleDGDLTvigdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:COG1245 177 KGTVRE--LLEKVDERGKLDELAEKLGLENIL----DRDIS-------ELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
.
gi 1958679184 566 D 566
Cdd:COG1245 244 D 244
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1114-1294 |
4.46e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWID--KILTTEIGLHDLRKKMSII-------PQVQLK 1183
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITsGDLIVDglKVNDPKVDERLIRQEAGMVfqqfylfPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1184 EAIEDLP------GKMDTE------LAESG---------SNFSVGQRQLVCLARAILKKNRILIIDEATANVDPrtdELI 1242
Cdd:PRK09493 96 ENVMFGPlrvrgaSKEEAEkqarelLAKVGlaerahhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP---ELR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 1243 QQ--KIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPES 1294
Cdd:PRK09493 173 HEvlKVMQDLAEegMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
393-593 |
4.84e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 393 DELPERKAQEPSDGKAIVHVQDFTafWD---KALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPP---TS 466
Cdd:TIGR00956 743 DDVNDEKDMEKESGEDIFHWRNLT--YEvkiKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTG 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 467 GLVSVHGR---------IAYVSQQPwVFSG--TVRSNILFG---------RKYEKERY-EKVIKacalkkdlqLLEDGDL 525
Cdd:TIGR00956 821 GDRLVNGRpldssfqrsIGYVQQQD-LHLPtsTVRESLRFSaylrqpksvSKSEKMEYvEEVIK---------LLEMESY 890
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 526 --TVIGDRGATLSGGQKARVNLA-RAVYQDADIYLLDDPLSAVDAEVGkhlfqLCICQTLHEKI----TILVT-HQ 593
Cdd:TIGR00956 891 adAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQTA-----WSICKLMRKLAdhgqAILCTiHQ 961
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
421-569 |
4.84e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.43 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 421 KALDtptlqGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG----------------RIAYVSQQPWV 484
Cdd:PRK11308 29 KALD-----GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdllkadpeaqkllrqKIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 485 fSGTVRSNIlfGRKYE-----------KERYEKVikacalkkdLQLLEDGDL-TVIGDRGATL-SGGQKARVNLARAVYQ 551
Cdd:PRK11308 104 -SLNPRKKV--GQILEepllintslsaAERREKA---------LAMMAKVGLrPEHYDRYPHMfSGGQRQRIAIARALML 171
|
170
....*....|....*...
gi 1958679184 552 DADIYLLDDPLSAVDAEV 569
Cdd:PRK11308 172 DPDVVVADEPVSALDVSV 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
426-616 |
4.85e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.82 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 426 PTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-----------------RIAYVSQQP--WVFS 486
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdikqirkKVGLVFQFPesQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 487 GTVRSNILFGRK---YEKERYEKVikacALKKdlqlledgdLTVIG------DRGA-TLSGGQKARVNLARAVYQDADIY 556
Cdd:PRK13649 101 ETVLKDVAFGPQnfgVSQEEAEAL----AREK---------LALVGiseslfEKNPfELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 557 LLDDPLSAVDAEVGKHLFQLciCQTLHEK-ITI-LVTHQLQYL-KAASHILILKDGEMVQKGT 616
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTL--FKKLHQSgMTIvLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
421-612 |
5.08e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 421 KALDTPTLqglsfTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQ-PWVF 485
Cdd:PRK10982 12 KALDNVNL-----KVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQElNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 486 SGTVRSNILFGRKYEKERYekVIKACALKKDLQLLEDGDLTV-IGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSA 564
Cdd:PRK10982 87 QRSVMDNMWLGRYPTKGMF--VDQDKMYRDTKAIFDELDIDIdPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 565 VDAEVGKHLFQlcICQTLHEK--ITILVTHQL-QYLKAASHILILKDGEMV 612
Cdd:PRK10982 165 LTEKEVNHLFT--IIRKLKERgcGIVYISHKMeEIFQLCDEITILRDGQWI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
352-623 |
6.10e-07 |
|
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: 54.25 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 352 FVAMTLYGAVRLTVTL-----FFPS--AIERVSEAVVSVRriknflllDELPERKAQEPSDGKA--IVHVQDFTAFWDKA 422
Cdd:TIGR01257 1879 LVAMAVEGVVYFLLTLliqhhFFLSrwIAEPAKEPIFDED--------DDVAEERQRIISGGNKtdILRLNELTKVYSGT 1950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 423 lDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR-----IAYVSQQ-PWVFSGTVRSNILFG 496
Cdd:TIGR01257 1951 -SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnISDVHQNmGYCPQFDAIDDLLTG 2029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 497 RK--YEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHL 573
Cdd:TIGR01257 2030 REhlYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAgTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 574 FQLCICQTLHEKITILVTHQLQYLKA-ASHILILKDGEMVQKGTyTEFLKS 623
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGT-IQHLKS 2159
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
428-615 |
7.81e-07 |
|
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: 50.99 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGElpptSGLVSVHGRIAYVSQqpwvfsgtvrsNILFGRKYEKER---- 503
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH----PKYEVTEGEILFKGE-----------DITDLPPEERARlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 504 ----YEKVIKACALKKDLQLLEDGdltvigdrgatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQlcIC 579
Cdd:cd03217 81 lafqYPPEIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE--VI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958679184 580 QTLHEKIT--ILVTHQ---LQYLKaASHILILKDGEMVQKG 615
Cdd:cd03217 148 NKLREEGKsvLIITHYqrlLDYIK-PDRVHVLYDGRIVKSG 187
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1124-1283 |
8.68e-07 |
|
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: 51.14 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1124 SREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILtteigLHDLRKKMSIIPQ----------------------- 1179
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDgGTIVLNGTV-----LFDSRKKINLPPQqrkiglvfqqyalfphlnvrenl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ---------VQLKEAIEDLPGKMD-TELAESGS-NFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE 1248
Cdd:cd03297 97 afglkrkrnREDRISVDELLDLLGlDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958679184 1249 --KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYD 1283
Cdd:cd03297 177 ikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
421-612 |
9.05e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 421 KALDTPTL-QGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-RIAYVSQQPWVFSG----------- 487
Cdd:PRK11288 261 DGLKGPGLrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkae 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 ------TVRSNI-------------LFGRKYEKERYEKVIKACALKKdlqllEDGDlTVIGdrgaTLSGGQKARVNLARA 548
Cdd:PRK11288 341 giipvhSVADNInisarrhhlragcLINNRWEAENADRFIRSLNIKT-----PSRE-QLIM----NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 549 VYQDADIYLLDDPLSAVDaeVG-KHLfqlcICQTLHE----KITIL-VTHQL-QYLKAASHILILKDGEMV 612
Cdd:PRK11288 411 LSEDMKVILLDEPTRGID--VGaKHE----IYNVIYElaaqGVAVLfVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
421-609 |
9.58e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 421 KALDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--------------IAYVSQQP---- 482
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISEDRkrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 483 WVFSGTVRSNILFG--RKYEKeryekviKACALKKDLQLLEDGDL------------TVIGdrgaTLSGGQKARVNLARA 548
Cdd:PRK10762 341 LVLGMSVKENMSLTalRYFSR-------AGGSLKHADEQQAVSDFirlfniktpsmeQAIG----LLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 549 VYQDADIYLLDDPLSAVDAEVGKHLFQLcICQTLHEKITI-LVTHQL-QYLKAASHILILKDG 609
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQL-INQFKAEGLSIiLVSSEMpEVLGMSDRILVMHEG 471
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
428-637 |
1.09e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGRIAYVSqqpwVFSG-----TVRSNILF------- 495
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIA----ISAGlsgqlTGIENIEFkmlcmgf 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 496 GRKYEKERYEKVIKACALkkdlqlledGDLtvIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSavdaeVGKHLF- 574
Cdd:PRK13546 116 KRKEIKAMTPKIIEFSEL---------GEF--IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS-----VGDQTFa 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 575 QLCIcQTLHE-----KITILVTHQL-QYLKAASHILILKDGEMVQKG-------TYTEFLKsgvDFGSLLKKENEE 637
Cdd:PRK13546 180 QKCL-DKIYEfkeqnKTIFFVSHNLgQVRQFCTKIAWIEGGKLKDYGelddvlpKYEAFLN---DFKKKSKAEQKE 251
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
428-622 |
1.80e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------RIAYVSQQPWVFsG---------TVR-S 491
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrRKEFARRIGVVF-GqrsqlwwdlPAIdS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 492 NILFGRKYE--KERYEKVIKACAlkkdlQLLEDGDLTVIGDRgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEV 569
Cdd:COG4586 117 FRLLKAIYRipDAEYKKRLDELV-----ELLDLGELLDTPVR--QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 570 gkhlfQLCICQTLHE-----KITILVT-HQLQYLKA-ASHILILKDGEMVQKGTYTEFLK 622
Cdd:COG4586 190 -----KEAIREFLKEynrerGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1087-1296 |
1.98e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.76 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1087 RPPPGWPHEGVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKI----- 1160
Cdd:PRK11607 7 RPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPtAGQIMLDGVdlshv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1161 -------------------LTTE----IGLhdlrkKMSIIPQVQLKEAIEDLPG--KMDTELAESGSNFSVGQRQLVCLA 1215
Cdd:PRK11607 87 ppyqrpinmmfqsyalfphMTVEqniaFGL-----KQDKLPKAEIASRVNEMLGlvHMQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1216 RAILKKNRILIIDEATANVDPRTDELIQQK---IREKFAQCTVLTIAHRLNTIIDSDKIMVLDSGRLREYDEPYVLLQNP 1292
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEvvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
....
gi 1958679184 1293 ESLF 1296
Cdd:PRK11607 242 TTRY 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1115-1296 |
2.04e-06 |
|
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: 50.42 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1115 LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID-------KILTTEIGL---------H--------- 1168
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGgedatdvPVQERNVGFvfqhyalfrHmtvfdnvaf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1169 --DLRKKMSIIPQVQLKEAIEDLPGKMDTE-LAES-GSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQ 1244
Cdd:cd03296 98 glRVKPRSERPPEAEIRAKVHELLKLVQLDwLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1245 KIREKFAQCTVLTI--AHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPESLF 1296
Cdd:cd03296 178 WLRRLHDELHVTTVfvTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1114-1281 |
2.25e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.84 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKI-WIDKILTT-------------------EIGLHDLRK 1172
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPsQGNVsWRGEPLAKlnraqrkafrrdiqmvfqdSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KM------------------------SIIPQVQLKEAIED-LPGKMdtelaeSGsnfsvGQRQLVCLARAILKKNRILII 1227
Cdd:PRK10419 107 TVreiireplrhllsldkaerlarasEMLRAVDLDDSVLDkRPPQL------SG-----GQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 1228 DEATANVDPRTD-ELIQQ--KIREKFAQCTVLtIAHRLNTIID-SDKIMVLDSGRLRE 1281
Cdd:PRK10419 176 DEAVSNLDLVLQaGVIRLlkKLQQQFGTACLF-ITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
391-611 |
2.84e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 391 LLDELPErKAQEPsdGKAIVHVQDFTAfwdkaLDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVS 470
Cdd:PRK10982 235 LTQRFPD-KENKP--GEVILEVRNLTS-----LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTIT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 471 VHGR--------------IAYVSQQ----------PWVFSGTVrSNIlfgRKYeKERYeKVIKACALKKDLQLLED---- 522
Cdd:PRK10982 307 LHGKkinnhnaneainhgFALVTEErrstgiyaylDIGFNSLI-SNI---RNY-KNKV-GLLDNSRMKSDTQWVIDsmrv 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 523 ---GDLTVIGdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQL-QYLK 598
Cdd:PRK10982 381 ktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLG 456
|
250
....*....|...
gi 1958679184 599 AASHILILKDGEM 611
Cdd:PRK10982 457 ITDRILVMSNGLV 469
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1104-1278 |
3.31e-06 |
|
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: 51.36 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSL---ISALFRLSEPEGKI-WIDKIL-------TTEIGLHDLRK 1172
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTWDGEIyWSGSPLkasnirdTERAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KMSIIPQVQLKEAI-----EDLPG-------------KMDTELAESGSN-------FSVGQRQLVCLARAILKKNRILII 1227
Cdd:TIGR02633 86 ELTLVPELSVAENIflgneITLPGgrmaynamylrakNLLRELQLDADNvtrpvgdYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 1228 DEATANVDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGR 1278
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
93-325 |
4.55e-06 |
|
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: 50.23 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIFTLIEET-TRVVQPIFLGKIIDYFEkydsDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMC 171
Cdd:cd18778 1 LILTLLCALLSTlLGLVPPWLIRELVDLVT----IGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVtiFLHflwAGP------LQAIGVTILLwveIGISCLagLAILV 245
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERL--IAD---GIPqgitnvLTLVGVAIIL---FSINPK--LALLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 246 IL-LPLQSCIGKLFsslrSKTA--AFTDARIRT--MNEV----ITGMRIIKMYAWE----KSFADLITNLRKkeiskilg 312
Cdd:cd18778 147 LIpIPFLALGAWLY----SKKVrpRYRKVREALgeLNALlqdnLSGIREIQAFGREeeeaKRFEALSRRYRK-------- 214
|
250
....*....|...
gi 1958679184 313 sSYLRGMNMASFF 325
Cdd:cd18778 215 -AQLRAMKLWAIF 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1096-1260 |
5.47e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILttEIGLHDlrkkm 1174
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADsGRIHCGTKL--EVAYFD----- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 siipqvQLKEAIEdlPGK--MDTeLAESGSNFSV------------------------------GQRQLVCLARAILKKN 1222
Cdd:PRK11147 389 ------QHRAELD--PEKtvMDN-LAEGKQEVMVngrprhvlgylqdflfhpkramtpvkalsgGERNRLLLARLFLKPS 459
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958679184 1223 RILIIDEATANVDPRTDELIQQKIREkfAQCTVLTIAH 1260
Cdd:PRK11147 460 NLLILDEPTNDLDVETLELLEELLDS--YQGTVLLVSH 495
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1114-1261 |
5.89e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.80 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRL-----SEPEGKIWIDKILTTEIGLHDLRKKMSIipqvqlKEAIEd 1188
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkgtpVAGCVDVPDNQFGREASLIDAIGRKGDF------KDAVE- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1189 lpgkmdtELAESG-----------SNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE--KFAQCTV 1255
Cdd:COG2401 118 -------LLNAVGlsdavlwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKlaRRAGITL 190
|
....*.
gi 1958679184 1256 LTIAHR 1261
Cdd:COG2401 191 VVATHH 196
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
438-622 |
6.02e-06 |
|
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: 48.34 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 438 GELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG-RIAYVSQQpwvfsgtvrsnilfgrkyekeryekvikacalkkd 516
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY----------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 517 lqlledgdltvigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKITILVT-HQLQ 595
Cdd:cd03222 70 ----------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVeHDLA 133
|
170 180
....*....|....*....|....*..
gi 1958679184 596 YLKAASHILILKDGEmvqKGTYTEFLK 622
Cdd:cd03222 134 VLDYLSDRIHVFEGE---PGVYGIASQ 157
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
93-369 |
6.02e-06 |
|
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: 49.77 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIFTLIEETTRVVQPIFLGKIIDYFEKydSDDSAALHTaygYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCH 172
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAIDEYIP--NGDLSGLLI---IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 173 MIYRKALRLSNSAMGKTTTGQIVNLLSNDVNK----FDQ--VTIFLHFlwagpLQAIGVT-ILLW--VEIGISCLAGLAI 243
Cdd:cd18545 78 DLFSHLQKLSFSFFDSRPVGKILSRVINDVNSlsdlLSNglINLIPDL-----LTLVGIViIMFSlnVRLALVTLAVLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 244 LVILL-PLQSCIGKLFSSLRSKTAAFTDArirtMNEVITGMRIIKMYAWEK----SFADLITNLRKkeiskilgsSYLRG 318
Cdd:cd18545 153 LVLVVfLLRRRARKAWQRVRKKISNLNAY----LHESISGIRVIQSFAREDeneeIFDELNRENRK---------ANMRA 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 319 MNMASFF---------IANKVILFvtFTTYVLLGNKITAShVFVAMTLYgavrltVTLFF 369
Cdd:cd18545 220 VRLNALFwplvelisaLGTALVYW--YGGKLVLGGAITVG-VLVAFIGY------VGRFW 270
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1130-1283 |
6.17e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1130 IVGRTGAGKSSLISALFRLSEP-EGKIWID---------KI-LTTE---IG------------------LHDLRKKMSii 1177
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPqKGRIVLNgrvlfdaekGIcLPPEkrrIGyvfqdarlfphykvrgnlRYGMAKSMV-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1178 PQ----VQLKeAIEDLpgkmdteLAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVD-PRTDELIQ--QKIREKF 1250
Cdd:PRK11144 107 AQfdkiVALL-GIEPL-------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPylERLAREI 178
|
170 180 190
....*....|....*....|....*....|....
gi 1958679184 1251 aQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYD 1283
Cdd:PRK11144 179 -NIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1098-1304 |
7.02e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.36 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPL---VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIG----LHD 1169
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPtQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1170 LRKKMSII---PQVQL-------------------KEAIEDLPGK------MDTELAE-SGSNFSVGQRQLVCLARAILK 1220
Cdd:PRK13649 83 IRKKVGLVfqfPESQLfeetvlkdvafgpqnfgvsQEEAEALAREklalvgISESLFEkNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1221 KNRILIIDEATANVDPR-TDELIQqkIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPESLF 1296
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKgRKELMT--LFKKLHQsgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQDVDFLE 240
|
....*...
gi 1958679184 1297 YKmvqQLG 1304
Cdd:PRK13649 241 EK---QLG 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1108-1283 |
7.31e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.43 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1108 SLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTT--------EIGLHDLRKKMSIIP 1178
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIGGNPCArltpakahQLGIYLVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1179 QVQLKEAIE-DLPGKMDTE------LAESGSNFS---------VGQRQLVCLARAILKKNRILIIDEATANVDPRTDELI 1242
Cdd:PRK15439 100 NLSVKENILfGLPKRQASMqkmkqlLAALGCQLDldssagsleVADRQIVEILRGLMRDSRILILDEPTASLTPAETERL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958679184 1243 QQKIREKFAQ-CTVLTIAHRLNTIID-SDKIMVLD------SGRLREYD 1283
Cdd:PRK15439 180 FSRIRELLAQgVGIVFISHKLPEIRQlADRISVMRdgtialSGKTADLS 228
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
93-389 |
8.00e-06 |
|
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: 49.42 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSDDSAalHTAYGYAAVLSLCTLILAILHHLYFYHvqcagMRIRVAmcH 172
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG--YYLGVYAALLVLASVLLVLLRWLLFVL-----AGLRAS--R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 173 MIYRKALR-LSNSAMG---KTTTGQIVNLLSNDVNKFDQV--TIFLHFLWAGpLQAIGVTILlwveIGISCLAGLAILVI 246
Cdd:cd18580 73 RLHDKLLRsVLRAPMSffdTTPSGRILNRFSKDIGLIDEElpLALLDFLQSL-FSVLGSLIV----IAIVSPYFLIVLPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 247 LLPLQSCIGKLFSS----LR-----SKTAAFTdarirTMNEVITGMRIIKMYAWEKSFADliTNLRKKEISkiLGSSYLr 317
Cdd:cd18580 148 LLVVYYLLQRYYLRtsrqLRrleseSRSPLYS-----HFSETLSGLSTIRAFGWQERFIE--ENLRLLDAS--QRAFYL- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 318 gMNMASF-------FIANKVILFVTFTTyVLLGNKITASHVFVAMTLygAVRLTVTLFFpsAIERVSE---AVVSVRRIK 387
Cdd:cd18580 218 -LLAVQRwlglrldLLGALLALVVALLA-VLLRSSISAGLVGLALTY--ALSLTGSLQW--LVRQWTEletSMVSVERIL 291
|
..
gi 1958679184 388 NF 389
Cdd:cd18580 292 EY 293
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1114-1306 |
9.20e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.81 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWID----KILTTEIG---------LHDLRKKMSIIPQ 1179
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPsEGSIVVNgqtiNLVRDKDGqlkvadknqLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ------------------VQL-----KEAIE------DLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEA 1230
Cdd:PRK10619 100 hfnlwshmtvlenvmeapIQVlglskQEAREravkylAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1231 TANVDPrtdELIQQ--KIREKFAQ--CTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPESlfyKMVQQLGK 1305
Cdd:PRK10619 180 TSALDP---ELVGEvlRIMQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQS---PRLQQFLK 253
|
.
gi 1958679184 1306 G 1306
Cdd:PRK10619 254 G 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
405-613 |
1.05e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.78 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 405 DGKAIVHVQDFTAFwdkalDTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR---------- 474
Cdd:PRK09700 261 AHETVFEVRNVTSR-----DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsplda 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 475 ----IAYVSQ---QPWVFSG-TVRSNILFGRKYEKERYEKVIKACALKKDLQLLED--GDLTV----IGDRGATLSGGQK 540
Cdd:PRK09700 336 vkkgMAYITEsrrDNGFFPNfSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENqrELLALkchsVNQNITELSGGNQ 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 541 ARVNLARAVYQDADIYLLDDPLSAVD----AEVGKHLFQLcicqTLHEKITILVTHQL-QYLKAASHILILKDGEMVQ 613
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQL----ADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
442-610 |
1.34e-05 |
|
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: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 442 AVVGPVGAGKSSLLSAVL----GELPPTSGLVSVHGRIAyvsqqpwvFSGTVRSNI------LFGRKYEKERYEKVIKAC 511
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDPKLI--------REGEVRAQVklafenANGKKYTITRSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 512 AlkkdlqLLEDGDLTVIGDRG-ATLSGGQKA------RVNLARAVYQDADIYLLDDPLSAVDAEVgkhlfqlcICQTLHE 584
Cdd:cd03240 98 I------FCHQGESNWPLLDMrGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN--------IEESLAE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958679184 585 KIT----------ILVTHQLQYLKAASHIL-ILKDGE 610
Cdd:cd03240 164 IIEerksqknfqlIVITHDEELVDAADHIYrVEKDGR 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1090-1280 |
1.56e-05 |
|
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: 49.05 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1090 PGWPHE-GVIVFDNVNFT-YSLDGPLV--LKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP--EGKIWID-KILT 1162
Cdd:TIGR02633 247 PHEPHEiGDVILEARNLTcWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGkfEGNVFINgKPVD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1163 TEIGLHDLRKKMSIIPQVQLKEAIEDLPG-----------------KMDTElAESGS--------------------NFS 1205
Cdd:TIGR02633 327 IRNPAQAIRAGIAMVPEDRKRHGIVPILGvgknitlsvlksfcfkmRIDAA-AELQIigsaiqrlkvktaspflpigRLS 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1206 VGQRQLVCLARAILKKNRILIIDEATANVDPRTD----ELIQQKIREKFAqctVLTIAHRLNTIID-SDKIMVLDSGRLR 1280
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKyeiyKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKLK 482
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
424-618 |
1.73e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLG--ELPPTSGLVSVHGR--------------IAYVSQQPWVFSG 487
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdllelspedragegIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 TvrSNILF-------GRKY-EKERYEKVIKACALKKDLQLLEDGDLTVIGDRGATLSGGQKARVNLARAVYQDADIYLLD 559
Cdd:PRK09580 93 V--SNQFFlqtalnaVRSYrGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 560 DPLSAVDAEVGKHLFQLCICQTLHEKITILVTHQ---LQYLKaASHILILKDGEMVQKGTYT 618
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDFT 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
394-576 |
1.81e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 394 ELPERKAQEPSDgKAIVHVQDFTA--FWDkaldtptlqgLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSV 471
Cdd:PRK15439 254 ELPGNRRQQAAG-APVLTVEDLTGegFRN----------ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIML 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 472 HGR--------------IAYVS---QQP---------WVFSGTVRSNILF--GRKYEKERYEKVIKACALKkdlqlLEDG 523
Cdd:PRK15439 323 NGKeinalstaqrlargLVYLPedrQSSglyldaplaWNVCALTHNRRGFwiKPARENAVLERYRRALNIK-----FNHA 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958679184 524 DLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQL 576
Cdd:PRK15439 398 EQAA-----RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQL 445
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
424-673 |
1.98e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSG-LVSVHGRIAYVS---QQPWV--------------- 484
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGeRQSQFSHITRLSfeqLQKLVsdewqrnntdmlspg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 485 ---FSGTVRSNILFGRKyEKERYEKVIKACALKKdlqLLEdgdltvigDRGATLSGGQKARVNLARAVYQDADIYLLDDP 561
Cdd:PRK10938 95 eddTGRTTAEIIQDEVK-DPARCEQLAQQFGITA---LLD--------RRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 562 LSAVDAEVGKHLFQLcICQTLHEKITI-LVTHQLQYLKA-ASHILILKDGEMVQKGTYTEFLKSGVdFGSLLKKENEEAE 639
Cdd:PRK10938 163 FDGLDVASRQQLAEL-LASLHQSGITLvLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQAL-VAQLAHSEQLEGV 240
|
250 260 270
....*....|....*....|....*....|....
gi 1958679184 640 PSPVPGTPTLRNRTFSEAsiwsqqsSRPSLKDGV 673
Cdd:PRK10938 241 QLPEPDEPSARHALPANE-------PRIVLNNGV 267
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1098-1248 |
2.08e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 47.70 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1098 IVFDNVNFTYSLDGPLVLKHLTAliKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWI-----DkiLTTEIG---LH 1168
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDC--PQGETLVLLGPSGAGKSSLLRVLNLLEMPRsGTLNIagnhfD--FSKTPSdkaIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1169 DLRKKMSIIPQ-----------------------VQLKEAIEDLPGKMDT-ELAESGSNF----SVGQRQLVCLARAILK 1220
Cdd:PRK11124 79 ELRRNVGMVFQqynlwphltvqqnlieapcrvlgLSKDQALARAEKLLERlRLKPYADRFplhlSGGQQQRVAIARALMM 158
|
170 180
....*....|....*....|....*...
gi 1958679184 1221 KNRILIIDEATANVDPRTDELIQQKIRE 1248
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRE 186
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
93-386 |
2.93e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 47.47 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILG-IFTLIEETTRVVQPIFLGKIIDYFEKY---DSDDSAALHTAYGYA---AVLSLCTLILAILHHLYFYHV---QCA 162
Cdd:cd18577 1 LIIGlLAAIAAGAALPLMTIVFGDLFDAFTDFgsgESSPDEFLDDVNKYAlyfVYLGIGSFVLSYIQTACWTITgerQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 163 gmRIRVAmchmIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKfdqvtiflhflwagpLQ-AIGVTILLWVEIGISCLAGL 241
Cdd:cd18577 81 --RIRKR----YLKALLRQDIAWFDKNGAGELTSRLTSDTNL---------------IQdGIGEKLGLLIQSLSTFIAGF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 242 AI---------LVIL--LPLQSCIGKLFSSLRSKTAaftdARIRTM--------NEVITGMRIIKMYAWE----KSFADL 298
Cdd:cd18577 140 IIafiyswkltLVLLatLPLIAIVGGIMGKLLSKYT----KKEQEAyakagsiaEEALSSIRTVKAFGGEekeiKRYSKA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 299 ITNLRKKEISKilgsSYLRGMNMASFFiankvilFVTFTTYVL---------LGNKITASHVFVAM--TLYGAvrLTVTL 367
Cdd:cd18577 216 LEKARKAGIKK----GLVSGLGLGLLF-------FIIFAMYALafwygsrlvRDGEISPGDVLTVFfaVLIGA--FSLGQ 282
|
330
....*....|....*....
gi 1958679184 368 FFPSaIERVSEAVVSVRRI 386
Cdd:cd18577 283 IAPN-LQAFAKARAAAAKI 300
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1195-1278 |
2.93e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.29 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1195 TELA-ESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPR-TDELIQ--QKIREKFaQCTVLTIAHRLNTIID-SD 1269
Cdd:PRK11300 144 LEHAnRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKeTKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSD 222
|
....*....
gi 1958679184 1270 KIMVLDSGR 1278
Cdd:PRK11300 223 RIYVVNQGT 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1114-1263 |
3.05e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.12 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDK--------------ILTTEIGL----HDLRKKMS 1175
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaeLRNQKLGFiyqfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 IIPQVQLKEAIEDLPGKMDTE-----LAESG---------SNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDEL 1241
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSralemLAAVGlehranhrpSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190
....*....|....*....|....*....|
gi 1958679184 1242 IQQKIRE-KFAQCTV-------LTIAHRLN 1263
Cdd:PRK11629 184 IFQLLGElNRLQGTAflvvthdLQLAKRMS 213
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
164-386 |
3.10e-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: 47.42 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 164 MRIRVAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ-VTIFLHFLWAGPLQAIG-VTILLWVEIGISCLAGL 241
Cdd:cd18552 72 RDLRNDL----FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGlLGVLFYLDWKLTLIALV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 242 AILVILLPLQScIGKLFSSLRSKTAAFTDARIRTMNEVITGMRIIKMYAWEKS----FADLITNLRKKEISKILGSSYLR 317
Cdd:cd18552 148 VLPLAALPIRR-IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSS 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 318 GMN--MASFFIAnkVILFvtFTTYVLLGNKITASHVFVAMTLYGAV-----RLTvtlffpSAIERVSEAVVSVRRI 386
Cdd:cd18552 227 PLMelLGAIAIA--LVLW--YGGYQVISGELTPGEFISFITALLLLyqpikRLS------NVNANLQRGLAAAERI 292
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
428-612 |
3.19e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 46.08 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSaVL---GELPPTSGLVSVHGR---------IAYVSQQPwVFSG--TVRSNI 493
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLD-VLagrKTAGVITGEILINGRpldknfqrsTGYVEQQD-VHSPnlTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 LFgrkyekeryekvikACALkkdlqlledgdltvigdRGatLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGkhl 573
Cdd:cd03232 101 RF--------------SALL-----------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA--- 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958679184 574 fqLCICQTLhEKI-----TILVT-HQ--LQYLKAASHILILK-DGEMV 612
Cdd:cd03232 145 --YNIVRFL-KKLadsgqAILCTiHQpsASIFEKFDRLLLLKrGGKTV 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1129-1279 |
3.61e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1129 GIVGRTGAGKSSLISALFRLSEP-EGKIWID----KILTT----EIGLHDLRKKMSIIPQVQLKEAI--EDLPGKMD--- 1194
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPdAGSILIDgqemRFASTtaalAAGVAIIYQELHLVPEMTVAENLylGQLPHKGGivn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1195 ---------TELAESGSNF---------SVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTV- 1255
Cdd:PRK11288 114 rrllnyearEQLEHLGVDIdpdtplkylSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVi 193
|
170 180
....*....|....*....|....*
gi 1958679184 1256 LTIAHRLNTIID-SDKIMVLDSGRL 1279
Cdd:PRK11288 194 LYVSHRMEEIFAlCDAITVFKDGRY 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1107-1281 |
4.49e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.25 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1107 YSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIDKILTTEIGLHDLRKKMS---------- 1175
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPtSGTLLFEGEDISTLKPEIYRQQVSycaqtptlfg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1176 -------IIP------QVQLKEAIEDLP--GKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDP---- 1236
Cdd:PRK10247 95 dtvydnlIFPwqirnqQPDPAIFLDDLErfALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDEsnkh 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958679184 1237 RTDELIQQKIREKfaQCTVLTIAHRLNTIIDSDKIMVLDS--GRLRE 1281
Cdd:PRK10247 175 NVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITLQPhaGEMQE 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1114-1304 |
5.14e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1114 VLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEG----------------KIWIDKILTTEIG----LHDLRKK 1173
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEgvikrngklrigyvpqKLYLDTTLPLTVNrflrLRPGTKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1174 MSIIPQVQLKEAIEDLPGKMdtelaesgSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTD----ELIQQKIREk 1249
Cdd:PRK09544 99 EDILPALKRVQAGHLIDAPM--------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQvalyDLIDQLRRE- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958679184 1250 fAQCTVLTIAHRLNTII-DSDKIMVLD-----SGrlreydEPYVLLQNPE--SLF-YKMVQQLG 1304
Cdd:PRK09544 170 -LDCAVLMVSHDLHLVMaKTDEVLCLNhhiccSG------TPEVVSLHPEfiSMFgPRGAEQLG 226
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
168-386 |
5.18e-05 |
|
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: 46.70 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 168 VAMCHMIYRKALRLSNSAMGK----------TT-TGQIVNLLSNDVNKFD-----QVTIFLHFLwagpLQAIGVTILL-- 229
Cdd:cd18606 57 LLLAYLGIRASKRLHNKALKRvlrapmsffdTTpLGRILNRFSKDTDVLDnelpdSLRMFLYTL----SSIIGTFILIii 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 230 ---WVEIGISCLAGLAILVILLPLQSC--IGKLFSSLRSKT-AAFtdarirtmNEVITGMRIIKMYAWEKSFadlitnLR 303
Cdd:cd18606 133 ylpWFAIALPPLLVLYYFIANYYRASSreLKRLESILRSFVyANF--------SESLSGLSTIRAYGAQDRF------IK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 304 KKEiskilgsSYLRGMNMASF--------------FIANKVILFVTFTTyVLLGNKITASHVFVAMTlYGavrLTVTLFF 369
Cdd:cd18606 199 KNE-------KLIDNMNRAYFltianqrwlairldLLGSLLVLIVALLC-VTRRFSISPSSTGLVLS-YV---LQITQVL 266
|
250 260
....*....|....*....|
gi 1958679184 370 PSAIERVSEA---VVSVRRI 386
Cdd:cd18606 267 SWLVRQFAEVennMNSVERL 286
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1122-1275 |
5.27e-05 |
|
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: 46.25 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1122 IKSREKVGIVGRTGAGKSSLISALFRLSEPEG---------------KIWIDKILTTEIGLHDLRKKMSIIPQVQLKEA- 1185
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEgdieieldtvsykpqYIKADYEGTVRDLLSSITKDFYTHPYFKTEIAk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1186 ---IEDLpgkMDTELAEsgsnFSVGQRQLVCLARAILKKNRILIIDEATANVDPRtDELIQQKIREKFA---QCTVLTIA 1259
Cdd:cd03237 102 plqIEQI---LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIRRFAennEKTAFVVE 173
|
170
....*....|....*...
gi 1958679184 1260 HRLnTIID--SDKIMVLD 1275
Cdd:cd03237 174 HDI-IMIDylADRLIVFE 190
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
93-322 |
5.65e-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: 46.66 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIF-TLIEETTRVVQPIFLGKIIDYFEKYDSDdsaalhtaYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMC 171
Cdd:cd18551 1 LILALLlSLLGTAASLAQPLLVKNLIDALSAGGSS--------GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 172 HMIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQV--TIFLHFLwAGPLQAIGVTILL----WVEIGISCLAGLAILV 245
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELitSGLPQLV-TGVLTVVGAVVLMflldWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 246 ILLPLQSCIGKLFSSLRSKTAAFTDArirtMNEVITGMRIIKMYAWEKSFAdlitnlrkKEISKILGSSYLRGMNMA 322
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAA----LERALSAIRTVKASNAEERET--------KRGGEAAERLYRAGLKAA 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1104-1292 |
5.72e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 47.14 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKILTTEIGLHDLRKKMSIIPQ--- 1179
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTaGTVLVAGDDVEALSARAASRRVASVPQdts 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ----VQLKEAIE----------DLPGKMDTELAESGSN--------------FSVGQRQLVCLARAILKKNRILIIDEAT 1231
Cdd:PRK09536 88 lsfeFDVRQVVEmgrtphrsrfDTWTETDRAAVERAMErtgvaqfadrpvtsLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 1232 ANVD----PRTDELIQQKIREKFaqcTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNP 1292
Cdd:PRK09536 168 ASLDinhqVRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1100-1291 |
6.57e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.03 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1100 FDNVNFTYsldGPLVLKHLTAL-IKSREKVGIVGRTGAGKSSLISALfrLSEP---EGKIWID-KILTTEIGLHDLRKKM 1174
Cdd:PRK11614 8 FDKVSAHY---GKIQALHEVSLhINQGEIVTLIGANGAGKTTLLGTL--CGDPratSGRIVFDgKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SIIPQ-----------------------VQLKEAIE---DLPGKMDTELAESGSNFSVGQRQLVCLARAILKKNRILIID 1228
Cdd:PRK11614 83 AIVPEgrrvfsrmtveenlamggffaerDQFQERIKwvyELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958679184 1229 EATANVDPrtdeLIQQKIREKFAQC-----TVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQN 1291
Cdd:PRK11614 163 EPSLGLAP----IIIQQIFDTIEQLreqgmTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLAN 227
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
93-386 |
8.07e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 46.35 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSDDsAALHTAYGYAAVLSLCTLILAILHHLYFYHVQCAGMRIRVAMCH 172
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPG-GNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 173 MIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQ--VTIFLHFLWAGpLQAIGV-TILLWVEigisclAGLAILVIL-L 248
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDflSDGLPDFLTNI-LMIIGIgVVLFSLN------WKLALLVLIpV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 249 PLQSCIGKLFS-SLRSKTAAFTDARIR---TMNEVITGMRIIKMYAWEKS----FADLITNLRkkEISKILGSSYLRGMN 320
Cdd:cd18563 154 PLVVWGSYFFWkKIRRLFHRQWRRWSRlnsVLNDTLPGIRVVKAFGQEKReikrFDEANQELL--DANIRAEKLWATFFP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958679184 321 MASFFIANKVILFVTFTTYVLLGNKITAShVFVAMT-----LYGAVRltvtlFFPSAIERVSEAVVSVRRI 386
Cdd:cd18563 232 LLTFLTSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLsylgmFYGPLQ-----WLSRLNNWITRALTSAERI 296
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1126-1282 |
1.25e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1126 EKVGIVGRTGAGKSSLISALFRLSEPEGKIW------IDKILT-TEIGLHDLR-KKMSIIPQ-------------VQLKE 1184
Cdd:PRK09473 43 ETLGIVGESGSGKSQTAFALMGLLAANGRIGgsatfnGREILNlPEKELNKLRaEQISMIFQdpmtslnpymrvgEQLME 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1185 AIEdLPGKMDTELAESGS---------------------NFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQ 1243
Cdd:PRK09473 123 VLM-LHKGMSKAEAFEESvrmldavkmpearkrmkmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM 201
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958679184 1244 QKIRE---KFaQCTVLTIAHRLNTIIDS-DKIMVLDSGRLREY 1282
Cdd:PRK09473 202 TLLNElkrEF-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEY 243
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
98-358 |
1.36e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 45.61 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 98 FTLIEETTRVVQPIFLGKIIDYFekYDSDDSAALHTAYGYAAVLSLCTLILAILHHLYFyhvQCAGMRIRVAMCHMIYRK 177
Cdd:cd18572 4 FLVVAALSELAIPHYTGAVIDAV--VADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCF---SYAGTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 178 ALRLSNSAMGKTTTGQIVNLLSNDVNKF-DQVTIFLH-FLWAGpLQAIGVTILLWV---EIGISCLAGLAILVIllplqs 252
Cdd:cd18572 79 LLRQDIAFFDATKTGELTSRLTSDCQKVsDPLSTNLNvFLRNL-VQLVGGLAFMFSlswRLTLLAFITVPVIAL------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 253 cIGKLFSSLRSKTAAFTDARI----RTMNEVITGMRIIKMYAWEKS----FADLITNLRKKEISKILGSSYLRGMNMASF 324
Cdd:cd18572 152 -ITKVYGRYYRKLSKEIQDALaeanQVAEEALSNIRTVRSFATEERearrYERALDKALKLSVRQALAYAGYVAVNTLLQ 230
|
250 260 270
....*....|....*....|....*....|....
gi 1958679184 325 FIANKVILFVTFttYVLLGNKITAsHVFVAMTLY 358
Cdd:cd18572 231 NGTQVLVLFYGG--HLVLSGRMSA-GQLVTFMLY 261
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
424-566 |
1.51e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 424 DTPTLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG--------------RIAYVSQqpwvfsG-- 487
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdmadarhrravcpRIAYMPQ------Glg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 488 -------TVRSNI-LFGRKY---EKERYEKVikacalkkdLQLLEDGDLTVIGDRGA-TLSGGQKARVNLARAVYQDADI 555
Cdd:NF033858 87 knlyptlSVFENLdFFGRLFgqdAAERRRRI---------DELLRATGLAPFADRPAgKLSGGMKQKLGLCCALIHDPDL 157
|
170
....*....|.
gi 1958679184 556 YLLDDPLSAVD 566
Cdd:NF033858 158 LILDEPTTGVD 168
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1096-1252 |
1.53e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.48 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWIDKiltTEIGLHDLRKKM 1174
Cdd:PRK13539 14 GRVLFSGLSFT---------------LAAGEALVLTGPNGSGKTTLLRLIAGLLPPAaGTIKLDG---GDIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1175 SII-------PQVQLKEAIE---DLPGKMDTELAES-------------GSNFSVGQRQLVCLARAILKKNRILIIDEAT 1231
Cdd:PRK13539 76 HYLghrnamkPALTVAENLEfwaAFLGGEELDIAAAleavglaplahlpFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|.
gi 1958679184 1232 ANVDPRTDELIQQKIREKFAQ 1252
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQ 176
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
761-1070 |
1.70e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 45.19 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 761 LSWYLGIYTGLTAVTVLFGIARSLLVFYVLVNASQTLHNRMFESILKAPVLFFDRNPieltqlevfrvvdgaldshrhls 840
Cdd:cd18563 42 LLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQ----------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 841 hphpwpqngslqasvtsvtgsdvirfpevlllalPGRILNRFSKDIGHMDDLLPLTFLDFIQTLLLVVSVIAVAAAVIPW 920
Cdd:cd18563 99 ----------------------------------TGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 921 ----ILIPLVPLSIIFVVLRRYFletsRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFD------AHQDL 990
Cdd:cd18563 145 lallVLIPVPLVVWGSYFFWKKI----RRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDeanqelLDANI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 991 HSEAWFLFLTTSRWFavrLDAICAVFVIVVAfGSLVLAKTLDAGQVGLALSYsltlMGMF----QWSVRQSAEVENMMIS 1066
Cdd:cd18563 221 RAEKLWATFFPLLTF---LTSLGTLIVWYFG-GRQVLSGTMTLGTLVAFLSY----LGMFygplQWLSRLNNWITRALTS 292
|
....
gi 1958679184 1067 VERV 1070
Cdd:cd18563 293 AERI 296
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
394-576 |
1.86e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 394 ELPERKAQEPSD-GKAIVHVQDFTAfWDKalDTPTLQ---GLSFTARPGELLAVVGPVGAGKSSLLSAVLGELP-PTSGL 468
Cdd:PRK13549 243 ELTALYPREPHTiGEVILEVRNLTA-WDP--VNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 469 VSVHGR--------------IAYVS----QQPWVFSGTVRSNIL---FGRKYEKERYEKVIKACALKKDLQLLE----DG 523
Cdd:PRK13549 320 IFIDGKpvkirnpqqaiaqgIAMVPedrkRDGIVPVMGVGKNITlaaLDRFTGGSRIDDAAELKTILESIQRLKvktaSP 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958679184 524 DLTVigdrgATLSGGQKARVNLARAVYQDADIYLLDDPLSAVD----AEVGKHLFQL 576
Cdd:PRK13549 400 ELAI-----ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYEIYKLINQL 451
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1104-1293 |
2.19e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.50 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1104 NFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRL-SEPEGKIWIDKILTTEIGLHD-LRKKMSIIPQ-- 1179
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvPRDAGNIIIDDEDISLLPLHArARRGIGYLPQea 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1180 ------------VQLKEAIEDLPGKMDTELAES--------------GSNFSVGQRQLVCLARAILKKNRILIIDEATAN 1233
Cdd:PRK10895 88 sifrrlsvydnlMAVLQIRDDLSAEQREDRANElmeefhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 1234 VDPRTDELIQQKIRE-KFAQCTVLTIAHRLNTIID-SDKIMVLDSGRLREYDEPYVLLQNPE 1293
Cdd:PRK10895 168 VDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
1129-1149 |
2.48e-04 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They 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. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 42.71 E-value: 2.48e-04
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1095-1278 |
2.73e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 44.80 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1095 EGVIVFDNVNFTYslDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPE-GKIWI-DKILTTEIglHDLRK 1172
Cdd:PRK13537 5 VAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLcGEPVPSRA--RHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1173 KMSIIPQ----------------------VQLKEAIEDLPGKMDTELAESGSNFSV-----GQRQLVCLARAILKKNRIL 1225
Cdd:PRK13537 81 RVGVVPQfdnldpdftvrenllvfgryfgLSAAAARALVPPLLEFAKLENKADAKVgelsgGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1226 IIDEATANVDPRTDELIQQKIREKFAQC-TVLTIAH------RLntiidSDKIMVLDSGR 1278
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGR 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
405-477 |
2.78e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 45.06 E-value: 2.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 405 DGKAIVHVQDFT-AFWDKALDTPTLQGLSFTARPGELLAVVGPVGAGKS-SLLSaVLGELPPtsGLVSVHGRIAY 477
Cdd:COG4172 2 MSMPLLSVEDLSvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRLLPD--PAAHPSGSILF 73
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
420-568 |
3.03e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 420 DKALdtptLQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHGR--IAYVSQ-----QPwvfSGTVRSN 492
Cdd:PRK11147 331 GKQL----VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKleVAYFDQhraelDP---EKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGRKyekeryekvikacalkkdlqlledgDLTVIG----------------DRGAT----LSGGQKARVNLARAVYQD 552
Cdd:PRK11147 404 LAEGKQ-------------------------EVMVNGrprhvlgylqdflfhpKRAMTpvkaLSGGERNRLLLARLFLKP 458
|
170
....*....|....*.
gi 1958679184 553 ADIYLLDDPLSAVDAE 568
Cdd:PRK11147 459 SNLLILDEPTNDLDVE 474
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1086-1316 |
3.27e-04 |
|
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: 45.39 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1086 KRPPPGWPhEGVIVfDNVNFTYSLDGPLVLKHLTALIKSREKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEI 1165
Cdd:TIGR01257 919 ERELPGLV-PGVCV-KNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1166 GLHDLRKKMSIIPQ-----------------VQLK-EAIEDLPGKMDTELAESG---------SNFSVGQRQLVCLARAI 1218
Cdd:TIGR01257 997 NLDAVRQSLGMCPQhnilfhhltvaehilfyAQLKgRSWEEAQLEMEAMLEDTGlhhkrneeaQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1219 LKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTI-IDSDKIMVLDSGRLREYDEPYVLLQNPESLFY 1297
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFY 1156
|
250 260
....*....|....*....|....*.
gi 1958679184 1298 -------KMVQQLGKGEAAALTETAK 1316
Cdd:TIGR01257 1157 ltlvrkmKNIQSQRGGCEGTCSCTSK 1182
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
435-472 |
3.60e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 42.87 E-value: 3.60e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1958679184 435 ARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVH 472
Cdd:COG3709 2 SGPGRLIYVVGPSGAGKDSLLAAARARLAADPRLVFAR 39
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
535-623 |
3.75e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.35 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 535 LSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQLCICQTLHEKIT-ILVTHQLQYL-KAASHILILKDGEMV 612
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlVLITHDLALVaEAAHKIIVMYAGQVV 233
|
90
....*....|.
gi 1958679184 613 QKGTYTEFLKS 623
Cdd:PRK11022 234 ETGKAHDIFRA 244
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1128-1147 |
4.03e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 43.99 E-value: 4.03e-04
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1096-1278 |
5.16e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1096 GVIVFDNVNFTysldgplvlkhltalIKSREKVGIVGRTGAGKSSLISALFRLSEP-EGKIWIdkiLTTEIGLHD----L 1170
Cdd:PRK10982 10 GVKALDNVNLK---------------VRPHSIHALMGENGAGKSTLLKCLFGIYQKdSGSILF---QGKEIDFKSskeaL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1171 RKKMSIIPQ----VQLKEAIEDL-------------PGKM-------------DTELAESGSNFSVGQRQLVCLARAILK 1220
Cdd:PRK10982 72 ENGISMVHQelnlVLQRSVMDNMwlgryptkgmfvdQDKMyrdtkaifdeldiDIDPRAKVATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958679184 1221 KNRILIIDEATANVDPRTDE---LIQQKIREKfaQCTVLTIAHRLNTIID-SDKIMVLDSGR 1278
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKEVNhlfTIIRKLKER--GCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
1127-1147 |
6.03e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 40.68 E-value: 6.03e-04
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
93-341 |
7.26e-04 |
|
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: 43.16 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIFTLIEETTRVVQPIFLGKIID-YFEKYDSDDSAALHTAYGYAAVLSLCTLILAILHHLYFY---HV-QCAGMRIR 167
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDlIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRlmaRVsQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 168 VAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQV--TIFLHFLwAGPLQAIGVTIL-LWVEIGISCLAGLAIL 244
Cdd:cd18547 82 KDL----FEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQAlsQSLTQLI-SSILTIVGTLIMmLYISPLLTLIVLVTVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 245 VILLplqscIGKLFSslrSKTAAFTDARIRT-------MNEVITGMRIIKMYAWE----KSFADLITNLRKkeiskilgS 313
Cdd:cd18547 157 LSLL-----VTKFIA---KRSQKYFRKQQKAlgelngyIEEMISGQKVVKAFNREeeaiEEFDEINEELYK--------A 220
|
250 260 270
....*....|....*....|....*....|
gi 1958679184 314 SYlrgmnMASFF--IANKVILFVTFTTYVL 341
Cdd:cd18547 221 SF-----KAQFYsgLLMPIMNFINNLGYVL 245
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
92-293 |
7.45e-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: 43.19 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 92 YLILGIFTLIEETTRVVQPIFLGKIIDYFekydsDDSAALHTAYGYAAVLSLCTLILAILHHLYFYHV----QCAGMRIR 167
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV-----IGGGLRELLWLLALLILGVALLRGVFRYLQGYLAekasQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 168 VAMchmiYRKALRLSNSAMGKTTTGQIVNLLSNDVnkfDQVTIFLHFlwagplQAIG-VTILLWVEIGISCLAGL----- 241
Cdd:cd18542 76 NDL----YDHLQRLSFSFHDKARTGDLMSRCTSDV---DTIRRFLAF------GLVElVRAVLLFIGALIIMFSInwklt 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 242 AILVILLPL--------QSCIGKLFSSLRSKTAAFTdariRTMNEVITGMRIIKMYAWEK 293
Cdd:cd18542 143 LISLAIIPFialfsyvfFKKVRPAFEEIREQEGELN----TVLQENLTGVRVVKAFARED 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1130-1272 |
8.15e-04 |
|
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: 41.58 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1130 IVGRTGAGKSSLISALfrlsepegkIWIDKILTTEIGLHDLRKKMSIIPQVQLkeaiedlpgkmdtELAESGSNFSVGQR 1209
Cdd:cd03227 26 ITGPNGSGKSTILDAI---------GLALGGAQSATRRRSGVKAGCIVAAVSA-------------ELIFTRLQLSGGEK 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 1210 QLV--CLARAILKKNR--ILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLTIAHRLNTIIDSDKIM 1272
Cdd:cd03227 84 ELSalALILALASLKPrpLYILDEIDRGLDPRDGQALAEAILEHLVKgAQVIVITHLPELAELADKLI 151
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1202-1248 |
8.74e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 42.69 E-value: 8.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958679184 1202 SNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIRE 1248
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRD 197
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
93-310 |
9.85e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 42.85 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGI-FTLIEETTRVVQPIFLGKIIDyfEKYDSDDSAALHTAYGYAAVLSLCTLILAILHHLYF----YHVQcAGMRIR 167
Cdd:cd18543 1 LILALlAALLATLAGLAIPLLTRRAID--GPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAgrlsLGVE-HDLRTD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 168 vamchmIYRKALRLSNSAMGKTTTGQIVNLLSNDVNKFDQVTIFLHFLWAGPLQAIGVTILLWVeigISCLAGLAILVIL 247
Cdd:cd18543 78 ------LFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLV---LSPPLALVALASL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958679184 248 LPLqscigkLFSSLRSKTAAFTDARI---------RTMNEVITGMRIIKMYAWEKS----FADLITNLRKKEISKI 310
Cdd:cd18543 149 PPL------VLVARRFRRRYFPASRRaqdqagdlaTVVEESVTGIRVVKAFGRERReldrFEAAARRLRATRLRAA 218
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1206-1278 |
1.08e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 1.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958679184 1206 VGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQ-CTVLTIAHRLNTIID-SDKIMVLDSGR 1278
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRvADSITVLRDGR 216
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
876-1024 |
1.16e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 42.79 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 876 GRILNRFSKDIGHMDDLLPLTF----LDFIqTLLLVVSVIAVAAAVIPWILIPLVPLSIIFVvlrRYFLETSRDVKRLES 951
Cdd:cd18554 103 GEIISRVINDVEQTKDFITTGLmniwLDMI-TIIIAICIMLVLNPKLTFVSLVIFPFYILAV---KYFFGRLRKLTKERS 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958679184 952 TTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFD-AHQDLHSEAwflfLTTSRWFAVRLDAICAVF----VIVVAFGS 1024
Cdd:cd18554 179 QALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDkRNGHFLTRA----LKHTRWNAKTFSAVNTITdlapLLVIGFAA 252
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
751-1070 |
1.19e-03 |
|
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: 42.45 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 751 ANGNVTGtldLSWYLGIYTGLTAVTVLFGIARSLLVFYVLVNASQTLHNRMFESILKAPVLFFDRNPIeltqlevfrvvd 830
Cdd:cd18545 32 PNGDLSG---LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPV------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 831 galdshrhlshphpwpqngslqasvtsvtgsdvirfpevlllalpGRILNRFSKDIGHMDDLLPLTFLDFI-QTLLLVvs 909
Cdd:cd18545 97 ---------------------------------------------GKILSRVINDVNSLSDLLSNGLINLIpDLLTLV-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 910 viavaaavipWILI---------PLVPLSI--IFVVLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEE 978
Cdd:cd18545 130 ----------GIVIimfslnvrlALVTLAVlpLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARED 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 979 RCQELFDAHQDLHSEAWflfLTTSR-----WFAVRLDAICAVFVIVVAFGSLVLAKTLDAGQVGLALSYsltlMGMFQWS 1053
Cdd:cd18545 200 ENEEIFDELNRENRKAN---MRAVRlnalfWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGY----VGRFWQP 272
|
330 340
....*....|....*....|.
gi 1958679184 1054 VRQSAEVENMMISV----ERV 1070
Cdd:cd18545 273 IRNLSNFYNQLQSAmasaERI 293
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
431-611 |
1.39e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 431 LSFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSG-------LVSVHGRIAYVSQQPWVFSGTVrsniLF-------G 496
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGeilldgkPVTAEQPEDYRKLFSAVFTDFH----LFdqllgpeG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 497 RKYEKERYEKVIKACALKKDLQLlEDGDLTVIgdrgaTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVGKHLFQL 576
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKLEL-EDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 1958679184 577 CICQTLHEKITIL-VTHQLQYLKAASHILILKDGEM 611
Cdd:PRK10522 492 LLPLLQEMGKTIFaISHDDHYFIHADRLLEMRNGQL 527
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1075-1285 |
1.49e-03 |
|
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: 42.86 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1075 DLEKEAPWECRKRPPPGWPHEGVIVFDNVNFTYSLD--------GPLvlkHLTalIKSREKVGIVGRTGAGKSSLISALF 1146
Cdd:COG4615 305 ALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEdgdegftlGPI---DLT--IRRGELVFIVGGNGSGKSTLAKLLT 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1147 RLSEPE-GKIWIDKILTTEIGLHDLRKKMSII-------------PQVQLKEAIEDLPGKMdtELAE---------SGSN 1203
Cdd:COG4615 380 GLYRPEsGEILLDGQPVTADNREAYRQLFSAVfsdfhlfdrllglDGEADPARARELLERL--ELDHkvsvedgrfSTTD 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1204 FSVGQRQLVCLARAILKKNRILIIDEATANVDPR-----TDELIQQ-KIREKfaqcTVLTIAHrlntiiD------SDKI 1271
Cdd:COG4615 458 LSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTELLPElKARGK----TVIAISH------DdryfdlADRV 527
|
250
....*....|....
gi 1958679184 1272 MVLDSGRLREYDEP 1285
Cdd:COG4615 528 LKMDYGKLVELTGP 541
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1129-1277 |
1.55e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1129 GIVGRTGAGKSSLISALFRL-SEPEGKI-WIDKILT-------TEIGLHDLRKKMSIIPQVQLKEAI------------- 1186
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIyTRDAGSIlYLGKEVTfngpkssQEAGIGIIHQELNLIPQLTIAENIflgrefvnrfgri 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1187 --EDLPGKMDTELAESGSNF---------SVGQRQLVCLARAILKKNRILIIDEAT-ANVDPRTDELIQQkIREKFAQ-C 1253
Cdd:PRK10762 114 dwKKMYAEADKLLARLNLRFssdklvgelSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLFRV-IRELKSQgR 192
|
170 180
....*....|....*....|....*
gi 1958679184 1254 TVLTIAHRLNTIID-SDKIMVLDSG 1277
Cdd:PRK10762 193 GIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1130-1236 |
1.57e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1130 IVGRTGAGKSSLIS----ALFRLSEPEGK--IWIDKILT-----TEIGL---HDLRKKMSIIPQV-QLKEAIEDLPGKMD 1194
Cdd:cd03240 27 IVGQNGAGKTTIIEalkyALTGELPPNSKggAHDPKLIRegevrAQVKLafeNANGKKYTITRSLaILENVIFCHQGESN 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958679184 1195 TELAESGSNFSVGQRQLVC------LARAILKKNRILIIDEATANVDP 1236
Cdd:cd03240 107 WPLLDMRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLDE 154
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1205-1296 |
2.54e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.94 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1205 SVGQRQLVCLARAILKKNRILIIDEATANVDP--RTDELIQQKIREKFAQCTVLTIAH-RLNTIIDSDKIMVLDSGRLRE 1281
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQ 214
|
90
....*....|....*
gi 1958679184 1282 YDEPYVLLQNPESLF 1296
Cdd:PRK11000 215 VGKPLELYHYPANRF 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
432-592 |
3.20e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 432 SFTARPGELLAVVGPVGAGKSSLLSAVLGELPPTSGLVSVHG------------RIAYVSQQpwvFS--G--TVRSNI-- 493
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdagdiatrrRVGYMSQA---FSlyGelTVRQNLel 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 494 ---LFGrkYEKERYEKVIKacalkkdlQLLEDGDLT-VIGDRGATLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAeV 569
Cdd:NF033858 363 harLFH--LPAAEIAARVA--------EMLERFDLAdVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP-V 431
|
170 180
....*....|....*....|....*
gi 1958679184 570 GKHLF-QLCICQTLHEKITILV-TH 592
Cdd:NF033858 432 ARDMFwRLLIELSREDGVTIFIsTH 456
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
428-567 |
3.45e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 428 LQGLSFTARPGELLAVVGPVGAGKSSLLSAVLGElpPTSGLVSVHGRIAYVSQQPWVF---SG------------TVRSN 492
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYIEGDIRISGFPKKQETFariSGyceqndihspqvTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 493 ILFGR--KYEKE--RYEKVIkacALKKDLQLLEDGDL--TVIGDRGAT-LSGGQKARVNLARAVYQDADIYLLDDPLSAV 565
Cdd:PLN03140 974 LIYSAflRLPKEvsKEEKMM---FVDEVMELVELDNLkdAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
..
gi 1958679184 566 DA 567
Cdd:PLN03140 1051 DA 1052
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
922-1070 |
5.17e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 40.63 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 922 LIPLVPLSIIFVVLRRYfletSRDVKRLESTTRSPV---FSHLSSSLQGLWTIRAYKAE--ERcQELFDAHQDLHSEAWF 996
Cdd:cd18565 158 LVALLPVPLIIAGTYWF----QRRIEPRYRAVREAVgdlNARLENNLSGIAVIKAFTAEdfER-ERVADASEEYRDANWR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 997 LFLTTSRWFAVRLDAICAVFVIVVAFGSLV-------LAKTLDAGqvglALSYSLTLMGMFQWSVRQSAEV----ENMMI 1065
Cdd:cd18565 233 AIRLRAAFFPVIRLVAGAGFVATFVVGGYWvldgpplFTGTLTVG----TLVTFLFYTQRLLWPLTRLGDLidqyQRAMA 308
|
....*
gi 1958679184 1066 SVERV 1070
Cdd:cd18565 309 SAKRV 313
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
922-1070 |
6.36e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 40.11 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 922 LIPLVPLSIIFVVLRRYFletsrdvKRLEsttrsPVFSH-------LSSSLQ----GLWTIRAYKAEERCQELFDAHQDL 990
Cdd:cd18542 143 LISLAIIPFIALFSYVFF-------KKVR-----PAFEEireqegeLNTVLQenltGVRVVKAFAREDYEIEKFDKENEE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 991 HSEAWFLFLTTSRWFAVRLDAIC-AVFVIVVAFGS-LVLAKTLDAGQVGLALSYsltlMGMFQWSVRQSAEVENMM---- 1064
Cdd:cd18542 211 YRDLNIKLAKLLAKYWPLMDFLSgLQIVLVLWVGGyLVINGEITLGELVAFISY----LWMLIWPVRQLGRLINDMsras 286
|
....*.
gi 1958679184 1065 ISVERV 1070
Cdd:cd18542 287 ASAERI 292
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1130-1275 |
7.68e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1130 IVGRTGAGKSSLISALFRLSEPE-GKIW--------IDKILTTEIGlHDLRKKMSIIPQVQLK------EAIEDLPG--- 1191
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSsGNIYykncninnIAKPYCTYIG-HNLGLKLEMTVFENLKfwseiyNSAETLYAaih 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 1192 --KMDTELAESGSNFSVGQRQLVCLARAILKKNRILIIDEATANVDPRTDELIQQKIREKFAQCTVLTIAHRLNTIIDSD 1269
Cdd:PRK13541 110 yfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKSA 189
|
....*.
gi 1958679184 1270 KIMVLD 1275
Cdd:PRK13541 190 QILQLD 195
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
93-250 |
8.51e-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: 39.76 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 93 LILGIFTLIEETTRVVQPIFLGKIIDYFEKYDSDDSAALHTAY---GYAAvLSLCTLILAILHHLYFYHvqcAGMRirva 169
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYylgIYAL-ISLLSVLLGTLRYLLFFF---GSLR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 170 MCHMIYRkalRLSNSAMG-------KTTTGQIVNLLSNDVNKFDqvtiflhflwagplQAIGVTILLWVEIGISCLAGLA 242
Cdd:cd18604 74 ASRKLHE---RLLHSVLRaplrwldTTPVGRILNRFSKDIETID--------------SELADSLSSLLESTLSLLVILI 136
|
....*...
gi 1958679184 243 ILVILLPL 250
Cdd:cd18604 137 AIVVVSPA 144
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
435-567 |
9.04e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.48 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 435 ARPGELLAVVGPVGAGKSSLLSAVLGElppTSG-LVSVHGRIAYVSQQP----------WVFSG---------TVRSNIL 494
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASN---TDGfHIGVEGVITYDGITPeeikkhyrgdVVYNAetdvhfphlTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958679184 495 FGRKYE--KERYEKVIKACALKK--DLQL----LEDGDLTVIGD---RGatLSGGQKARVNLARAVYQDADIYLLDDPLS 563
Cdd:TIGR00956 161 FAARCKtpQNRPDGVSREEYAKHiaDVYMatygLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
....
gi 1958679184 564 AVDA 567
Cdd:TIGR00956 239 GLDS 242
|
|
| |
