|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-914 |
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: 833.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 8 STFWNSSF-LDSPEADLPLCFEQTVLVWIPLGYLWLLAPWQLLhvYKSRTKRSSTTKLYLAK-QVFVGFLL-ILAAIELA 84
Cdd:TIGR00957 7 DPLWDWNVtWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFL--YLSRHDRGYIQMTHLNKtKTALGFLLwIVCWADLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 85 LVLTEDS-GQATVPaVRYTNPSLYLGTWLL-VLLIQYSRQWCVQkNSWFLSLFWILSILCGTFQFQTLIRTLL-QGDNSN 161
Cdd:TIGR00957 85 YSFWERShGRAPAP-VFLVSPTLLGITMLLaTFLIQLERRKGVQ-SSGIMLTFWLVALVCALAILRSKILLALkEDAIVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 162 LAYSCLFFISYGFQILILIFSAFSENNESSNNPS--------SIASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEM 233
Cdd:TIGR00957 163 PFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNhdpnpcpeSSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKED 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 234 KTKTLVSKFETHMKRELQKARRalqrrqeKSSQQNSGARLPGLNKNQSQSQdalVLEDVEKKKKKSGTKKDVPKswLMKA 313
Cdd:TIGR00957 243 TSEMVVPVLVENWKKECKKTRK-------QPVSAVYGKKDPSKPKGSSQLD---ANEEVEALIVKSPHKPRKPS--LFKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 314 LFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVR 393
Cdd:TIGR00957 311 LYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 394 TAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLV 473
Cdd:TIGR00957 391 TAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLM 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 474 IPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLT 553
Cdd:TIGR00957 471 VPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 554 PVLVSVVTFSVYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAIRHDCNF 633
Cdd:TIGR00957 551 PFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIK 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 634 D---KAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI 710
Cdd:TIGR00957 631 PgegNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWI 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 711 QNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:TIGR00957 711 QNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 791 VDAHVGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKnlktFLRHTGPEE 870
Cdd:TIGR00957 791 VDAHVGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE----FLRTYAPDE 866
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 767961632 871 EatvhDGSEEEDDDYGLISSVEE--IPEDAASITMRRENSFRRTLS 914
Cdd:TIGR00957 867 Q----QGHLEDSWTALVSGEGKEakLIENGMLVTDVVGKQLQRQLS 908
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
198-884 |
1.34e-162 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 516.60 E-value: 1.34e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 198 ASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKTLVSKFETHMKRELQKarralqrrqekssqqnsgarlpgln 277
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKK------------------------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 278 knqsqsqdalvledvekkkkksgtkkdvPKSWLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTyL 357
Cdd:PLN03130 287 ----------------------------PKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEP-A 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 358 WIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNF 437
Cdd:PLN03130 338 WIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 438 MHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAW 517
Cdd:PLN03130 418 LHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAW 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 518 EPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYVLVDSNniLDAQKAFTSITLFNILRFPLSMLP 597
Cdd:PLN03130 498 ENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGD--LTPARAFTSLSLFAVLRFPLFMLP 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 598 MMISSMLQASVSTERLEKYLGGDD---LDTSAIRHDCnfdKAMQFSEASFTWEHDSE-ATVRDVNLDIMAGQLVAVIGPV 673
Cdd:PLN03130 576 NLITQAVNANVSLKRLEELLLAEErvlLPNPPLEPGL---PAISIKNGYFSWDSKAErPTLSNINLDVPVGSLVAIVGST 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 674 GSGKSSLISAMLGEMENV-HGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLA 752
Cdd:PLN03130 653 GEGKTSLISAMLGELPPRsDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLT 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 753 EIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIV 832
Cdd:PLN03130 733 EIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRII 810
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 767961632 833 VLGNGTIVEKGSYSALLAKKGEFAKnlktFLRHTGPEEEaTVHDGSEEEDDD 884
Cdd:PLN03130 811 LVHEGMIKEEGTYEELSNNGPLFQK----LMENAGKMEE-YVEENGEEEDDQ 857
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
324-613 |
9.09e-154 |
|
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: 453.85 E-value: 9.09e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 324 KSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKK 403
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 404 ALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTK 483
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 484 SKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFS 563
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767961632 564 VYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18595 241 TYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-906 |
4.65e-147 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 472.54 E-value: 4.65e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 23 LPLCFEQTVLVWIPLGYLWLLAPWQLLHVYKSRTKRSSTTKLYLAKQVFVGFLLILAaieLALVLTEDSGQATVPAVRYT 102
Cdd:PLN03232 37 LVMIVSHSVLLGLCFYRIWIILDNAKAQIYVLRKKYYNCVLGILACYCVVEPVLRLV---MGISLFDMDEETDLPPFEVA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 103 NPSLYLGTW--LLVLLIQYSRQWcVQKNSWFLSlFWILSILCGTFQFQTLIRTLLQGDNSNLAYSCLFF----ISYGFQI 176
Cdd:PLN03232 114 SLMVEAFAWfsMLVLIGLETKQY-VKEFRWYVR-FGVVYVLVADAVLLDLVLPLKNSINRTALYLCISSrccqALFGILL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 177 LILI-----FSAFSENNESSNNPSSI--------------ASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKT 237
Cdd:PLN03232 192 LVYIpeldpYPGYHILNNESLDNVEYdalrggenicperyASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTET 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 238 LVSKFETHMKRELQKarralqrrqekssqqnsgarlpglnknqsqsqdalvledvekkkkksgtkkdvPKSWLMKALFKT 317
Cdd:PLN03232 272 LIKRFQRCWTEESRR-----------------------------------------------------PKPWLLRALNNS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 318 FYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTyLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIM 397
Cdd:PLN03232 299 LGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDP-AWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 398 ASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPIN 477
Cdd:PLN03232 378 AAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQ 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 478 AILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLV 557
Cdd:PLN03232 458 TLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 558 SVVTFSVYVLVDSNniLDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDD--------LDTSAirh 629
Cdd:PLN03232 538 TLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEErilaqnppLQPGA--- 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 630 dcnfdKAMQFSEASFTWEHDSE-ATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVH-GHITIKGTTAYVPQQ 707
Cdd:PLN03232 613 -----PAISIKNGYFSWDSKTSkPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQV 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 708 SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PLN03232 688 SWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 788 LSAVDAHVGKHIFNKVLGPNglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYsALLAKKGEFAKNLktfLRHTG 867
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTF-AELSKSGSLFKKL---MENAG 841
|
890 900 910
....*....|....*....|....*....|....*....
gi 767961632 868 PEEEATVHDGSEEEDDDYGLISSVEEIPEDAASITMRRE 906
Cdd:PLN03232 842 KMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKR 880
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
637-838 |
2.77e-118 |
|
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: 358.32 E-value: 2.77e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTW---EHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNG 713
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 TIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767961632 794 HVGKHIFNKVLGPNgLLKGKTRLLVTHSMHFLPQVDEIVVLGNGT 838
Cdd:cd03250 161 HVGRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
325-613 |
5.22e-118 |
|
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: 361.03 E-value: 5.22e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 325 SFLLKLVNDIFTFVSPQLLKLLISFASDRDTY-LWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKK 403
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEpLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 404 ALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTK 483
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 484 SKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFS 563
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767961632 564 VYVLVDsnNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
310-850 |
7.60e-118 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 393.38 E-value: 7.60e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 310 LMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLG 389
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 390 VKVRTAIMASVYKKALTLSN--LARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGV 467
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSksLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 468 GVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVI 547
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 548 FVFQLTPVLVSVVTFSVYVLvdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAI 627
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYL--LGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATCSTV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 628 R-----------HDCNFDKAMQFSEASFT--------------------------------------------------- 645
Cdd:PTZ00243 552 QdmeeywreqreHSTACQLAAVLENVDVTafvpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedtdygsp 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 646 ------------------------------------WEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEME 689
Cdd:PTZ00243 632 ssasrhiveggtgggheatptsersaktpkmktddfFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 690 NVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRI 769
Cdd:PTZ00243 712 ISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARV 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 770 SLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALL 849
Cdd:PTZ00243 792 SLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM 869
|
.
gi 767961632 850 A 850
Cdd:PTZ00243 870 R 870
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
325-613 |
5.30e-85 |
|
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: 274.33 E-value: 5.30e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 325 SFLLKLVNDIFTFVSPQLLKLLISFASDR-----DTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMAS 399
Cdd:cd18597 2 AGLLKLLADVLQVLSPLLLKYLINFVEDAylggpPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 400 VYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAI 479
Cdd:cd18597 82 IYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 480 LSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSV 559
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767961632 560 VTFSVYVLVdsNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18597 242 LSFITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
326-613 |
1.63e-84 |
|
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: 273.60 E-value: 1.63e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 326 FLLKLVNDIFTFVSPQLLK-LLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKA 404
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNrLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 405 LTLSNLA-------------------RKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLA 465
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 466 GVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCV 545
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 546 VIFVFQLTPVLVSVVTFSVYVLVdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
309-857 |
2.61e-78 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 265.87 E-value: 2.61e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 309 WLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFtAALIQSFCLQCYFQLCFKL 388
Cdd:COG1132 10 RRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLG-LALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 389 GVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSI---FFLWRELGPSVL 464
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALvvlFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 465 AGVGVMVLVIpinAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFS 540
Cdd:COG1132 169 LVLPLLLLVL---RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 541 QLQCVVIFVFQLTPVLVsvVTFSVYvLVdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYL--G 618
Cdd:COG1132 246 LFFPLMELLGNLGLALV--LLVGGL-LV-LSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLdeP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 619 GDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIK 698
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPV-LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 699 GT-------------TAYVPQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGG 764
Cdd:COG1132 401 GVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 765 QKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570
....*....|...
gi 767961632 845 YSALLAKKGEFAK 857
Cdd:COG1132 558 HEELLARGGLYAR 570
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
325-613 |
4.56e-77 |
|
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: 252.91 E-value: 4.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 325 SFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKA 404
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 405 LTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKS 484
Cdd:cd18559 82 LRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 485 KTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSV 564
Cdd:cd18559 162 RQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767961632 565 YVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18559 242 YVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
327-613 |
5.95e-77 |
|
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: 252.47 E-value: 5.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 327 LLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFC-LQCYFQLCfKLGVKVRTAIMASVYKKAL 405
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLsSHYNFQMN-KVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 406 TLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSK 485
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 486 TIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVY 565
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767961632 566 VLVdsNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18598 243 VLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
198-859 |
6.31e-75 |
|
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: 269.09 E-value: 6.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 198 ASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKTLVSKFETHMKRELQKARralqrrqekssqqnsgarlpgln 277
Cdd:TIGR01271 9 ANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAK----------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 278 KNqsqsqdalvledvekkkkksgtkkdvPKswLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLI-SFASDRDTY 356
Cdd:TIGR01271 66 KN--------------------------PK--LLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIaSYDPFNAPE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 357 LWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTN 436
Cdd:TIGR01271 118 REIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 437 FMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFA 516
Cdd:TIGR01271 198 LAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYC 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 517 WEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYVLVDSnniLDAQKAFTSITLFNILRFPLS-M 595
Cdd:TIGR01271 278 WEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALIKG---IILRRIFTTISYCIVLRMTVTrQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 596 LPMMISSMLQASVSTERLEKYLGGDD-------LDTSAI--------------------------RHDCNFDKAMQFSEA 642
Cdd:TIGR01271 355 FPGAIQTWYDSLGAITKIQDFLCKEEyktleynLTTTEVemvnvtaswdegigelfekikqnnkaRKQPNGDDGLFFSNF 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTwehdSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFG 722
Cdd:TIGR01271 435 SLY----VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFG 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 723 TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNK 802
Cdd:TIGR01271 511 LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 803 VLGPngLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNL 859
Cdd:TIGR01271 591 CLCK--LMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
306-857 |
6.82e-72 |
|
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: 251.68 E-value: 6.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 306 PKSWLMKALF---KTFYMVLLKSFLLKLvndiFTFVSPQLLKLLISF---ASDRDTyLWIgylCAILLFTAALIQSF--C 377
Cdd:COG2274 143 GLRWFLRLLRryrRLLLQVLLASLLINL----LALATPLFTQVVIDRvlpNQDLST-LWV---LAIGLLLALLFEGLlrL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 378 LQCYFQLcfKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSvDAQKLMD-VTNFMHMLWSSVLQIVLSIFFLW 456
Cdd:COG2274 215 LRSYLLL--RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREfLTGSLLTALLDLLFVLIFLIVLF 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 457 RELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKK----- 531
Cdd:COG2274 292 FYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKylnar 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 532 -ELKNLLAFSQLqcVVIFVFQLTPVLVsvVTFSVYvLVDSNNIldaqkaftsiTL-----FNIL--RF--PLSMLPMMIS 601
Cdd:COG2274 372 fKLRRLSNLLST--LSGLLQQLATVAL--LWLGAY-LVIDGQL----------TLgqliaFNILsgRFlaPVAQLIGLLQ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 602 SMLQASVSTERLEKYLGGD---DLDTSAIRHDcNFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKS 678
Cdd:COG2274 437 RFQDAKIALERLDDILDLPperEEGRSKLSLP-RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 679 SLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLE 744
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIdlrqidpaslrrqIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 745 MLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHF 824
Cdd:COG2274 596 ALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAHRLST 672
|
570 580 590
....*....|....*....|....*....|...
gi 767961632 825 LPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:COG2274 673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAE 705
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
327-613 |
6.14e-69 |
|
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: 231.74 E-value: 6.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 327 LLKLVNDIFTFVSPQLLKLLISFASDR------------------DTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKL 388
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENtysssnstdklsvsyvtvEEFFSNGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 389 GVKVRTAIMASVYKKALTLS--NLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAG 466
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 467 VGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVV 546
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 547 IFVFQLTPVLVSVVTFSVYVLVDSNNiLDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
327-614 |
1.17e-60 |
|
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: 208.26 E-value: 1.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 327 LLKLVNDIFTFVSPQLLKLLI-SFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKAL 405
Cdd:cd18594 4 ILLFLEESLKIVQPLLLGRLVaYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 406 TLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSK 485
Cdd:cd18594 84 KLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 486 TIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVY 565
Cdd:cd18594 164 KYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767961632 566 VLvdSNNILDAQKAFTSITLFNILRFPLSM-LPMMISSMLQASVSTERLE 614
Cdd:cd18594 244 VL--TGNTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKRIQ 291
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
637-838 |
5.69e-60 |
|
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: 203.72 E-value: 5.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSeATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI-----------------TIKG 699
Cdd:cd03290 1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 700 TTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNL 779
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 780 DIYLLDDPLSAVDAHVGKHIFNKvlgpnGLLK-----GKTRLLVTHSMHFLPQVDEIVVLGNGT 838
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE-----GILKflqddKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
325-613 |
1.23e-56 |
|
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: 197.01 E-value: 1.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 325 SFLLKLVNDIFTFVSPQ-LLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKK 403
Cdd:cd18592 2 SILLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 404 ALTLSNLarKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTK 483
Cdd:cd18592 82 ILRLRSL--GDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 484 SKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFS 563
Cdd:cd18592 160 TGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767961632 564 VYVLvdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18592 240 AHVA--LGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
334-613 |
9.61e-54 |
|
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: 188.97 E-value: 9.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 334 IFTF-------VSPQLLKLLIS-FASDRDTY-LWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKA 404
Cdd:cd18593 4 IFLFleeairvVQPIFLGKLIRyFEGNGSSIsLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 405 LTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKS 484
Cdd:cd18593 84 LRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 485 KTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSV 564
Cdd:cd18593 164 SKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767961632 565 YVLVDsnNILDAQKAFTSITLFNILRFPLSM-LPMMISSMLQASVSTERL 613
Cdd:cd18593 244 YILLG--NILTAERVFVTMALYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
636-853 |
1.06e-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: 196.52 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 636 AMQFSEASFTWEhDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TA 702
Cdd:COG4988 336 SIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 703 YVPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:COG4988 415 WVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 782 YLLDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKG 853
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALR---RLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
654-862 |
1.91e-52 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 185.06 E-value: 1.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQV 733
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 734 LEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPngLLKGK 813
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMANK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767961632 814 TRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLKTF 862
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGY 259
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
441-857 |
3.52e-52 |
|
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: 192.29 E-value: 3.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 441 LWSSVLQIVLSIFFLWR---ELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNkDKRLKIMnEILSGIKILKYFAW 517
Cdd:COG4987 136 LLVALLVILAAVAFLAFfspALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYGA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 518 EPSFRDQVQNL------RKKELKNLLAFSQLqcVVIFVFQLTpvLVSVVTFSVYvLVDSNNILDAQKA---FTSITLFNI 588
Cdd:COG4987 214 LDRALARLDAAearlaaAQRRLARLSALAQA--LLQLAAGLA--VVAVLWLAAP-LVAAGALSGPLLAllvLAALALFEA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 589 LrfplSMLPMMISSMLQASVSTERLEKyLGGDDLDTSAIRHDCNFDK--AMQFSEASFTWEHDSEATVRDVNLDIMAGQL 666
Cdd:COG4987 289 L----APLPAAAQHLGRVRAAARRLNE-LLDAPPAVTEPAEPAPAPGgpSLELEDVSFRYPGAGRPVLDGLSLTLPPGER 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 667 VAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQNGTIKDNILFGT-EFNEKRYQQ 732
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLRLARpDATDEELWA 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 733 VLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpnGLLKG 812
Cdd:COG4987 444 ALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAG 520
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 767961632 813 KTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:COG4987 521 RTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQ 565
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
639-857 |
1.35e-42 |
|
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: 155.08 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 639 FSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVP 705
Cdd:cd03251 3 FKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 706 QQSWIQNGTIKDNILFGTEfNEKRyQQVLEAC--ALLPDLEM-LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIY 782
Cdd:cd03251 83 QDVFLFNDTVAENIAYGRP-GATR-EEVEEAAraANAHEFIMeLPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 783 LLDDPLSAVDAhVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:cd03251 161 ILDEATSALDT-ESERLVQAAL--ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
638-853 |
2.84e-42 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 153.92 E-value: 2.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 638 QFSEASFTWEHDsEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYV 704
Cdd:cd03254 4 EFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisrkslrsmiGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 705 PQQSWIQNGTIKDNILFGTEFNEKryQQVLEACALL---PDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKEAgahDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 782 YLLDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKG 853
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALE---KLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
637-837 |
3.78e-41 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 148.69 E-value: 3.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAY 703
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 704 VPQQSWIQNGTIKDNILfgtefnekryqqvleacallpdlemlpggdlaeigekginlSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767961632 784 LDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNG 837
Cdd:cd03228 120 LDEATSALDPETEALILEALR---ALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
638-857 |
7.48e-41 |
|
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: 150.46 E-value: 7.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 638 QFSEASFTWeHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYV 704
Cdd:cd03253 2 EFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 705 PQQSWIQNGTIKDNILFG----TEfnekryQQVLEAC--ALLPDLEM-LPGGDLAEIGEKGINLSGGQKQRISLARATYQ 777
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGrpdaTD------EEVIEAAkaAQIHDKIMrFPDGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 778 NLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
638-843 |
1.60e-40 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 148.89 E-value: 1.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 638 QFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-------------YV 704
Cdd:cd03245 4 EFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldpadlrrnigYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 705 PQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03245 84 PQDVTLFYGTLRDNITLGaPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 784 LDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG 843
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
657-869 |
1.71e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 152.31 E-value: 1.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMeNVHGHITIKGT-------TAYVPQQSWI-QN-----GTIKDNILFG- 722
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelreldpESWRKHLSWVgQNpqlphGTLRDNVLLGn 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 723 TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNK 802
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 803 VlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAknlkTFLRHTGPE 869
Cdd:PRK11174 528 L---NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA----TLLAHRQEE 587
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
655-860 |
2.45e-37 |
|
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: 140.37 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNILF 721
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsqiGLVSQEPVLFDGTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 GTefNEKRYQQVLEAC--ALLPD-LEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 798
Cdd:cd03249 100 GK--PDATDEEVEEAAkkANIHDfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 799 IFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLK 860
Cdd:cd03249 178 VQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
636-834 |
3.96e-37 |
|
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: 147.05 E-value: 3.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 636 AMQFSEASFTWEhDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------A 702
Cdd:TIGR02857 321 SLEFSGVSVAYP-GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdqiA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 703 YVPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767961632 782 YLLDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVL 834
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALR---ALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
634-844 |
6.26e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 6.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 634 DKAMQFSEASFTWehDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVP 705
Cdd:COG1121 4 MPAIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrriGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 706 QQSWIQNG---TIKDNILFGT--------EFNEKRYQQVLEAcallpdLEMLPGGDLAE--IGEkginLSGGQKQRISLA 772
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVLMGRygrrglfrRPSRADREAVDEA------LERVGLEDLADrpIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 773 RATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQ-VDEIVVLgNGTIVEKGS 844
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGP 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
504-857 |
4.19e-33 |
|
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: 137.18 E-value: 4.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 504 EILSGIKILKYFAWEPSFRDQVQ----NLRKKELKNLLAfSQLQCVVIFVFQLTpvLVSVVTFSVYVLVDSNNILDAQka 579
Cdd:TIGR01193 339 EDLNGIETIKSLTSEAERYSKIDsefgDYLNKSFKYQKA-DQGQQAIKAVTKLI--LNVVILWTGAYLVMRGKLTLGQ-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 580 ftSITLFNILRFPLSMLPMMIS---SMLQASVSTERL-EKYL-GGDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEAtV 654
Cdd:TIGR01193 414 --LITFNALLSYFLTPLENIINlqpKLQAARVANNRLnEVYLvDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNI-L 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNILF 721
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqfiNYLPQEPYIFSGSILENLLL 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 GTEFNEKRyQQVLEACALLP---DLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 798
Cdd:TIGR01193 571 GAKENVSQ-DEIWAACEIAEikdDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 799 IFNKVLGpnglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:TIGR01193 650 IVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
636-857 |
1.48e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 134.18 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 636 AMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAY---------- 703
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiADYseaalrqais 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 704 -VPQQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDlAEIGEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:PRK11160 418 vVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLEDDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 782 YLLDDPLSAVDAHVGKHIFNkvlgpngLL----KGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
322-593 |
3.14e-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: 126.60 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 322 LLKSFLLKLVNDIFTFVSPQLLKLLI-SFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASV 400
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 401 YKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSV-LAGVGVMVLVIPINAI 479
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 480 LSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSV 559
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 767961632 560 VTFSVYVLVDSNNILDAQKAFTSITLFNILRFPL 593
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
654-857 |
1.81e-31 |
|
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: 130.59 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNIL 720
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDlrqldpaelrarmALVPQDPVLFAASVMENIR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 FGTEfnEKRYQQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHvGK 797
Cdd:TIGR02204 436 YGRP--DATDEEVEAAARAAHAHEFisaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAE-SE 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 798 HIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:TIGR02204 513 QLVQQAL--ETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYAR 570
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
637-844 |
4.70e-31 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 121.45 E-value: 4.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---TT----------AY 703
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKiglhdlrsriSI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 704 VPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767961632 784 LDDPLSAVDAHVGKHIfNKVLGPNglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:cd03244 163 LDEATASVDPETDALI-QKTIREA--FKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
417-857 |
1.11e-30 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 129.48 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 417 VGETVNLMsvdaQKLMDVTNFmhmLWSSVLQIVLSIFFLWRELG------PSVlagVGVMVLVIPINAILSTKSKTIQVK 490
Cdd:TIGR01846 235 VGDTVARV----RELEQIRNF---LTGSALTVVLDLLFVVVFLAvmffysPTL---TGVVIGSLVCYALLSVFVGPILRK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 491 NMKNKDKR----LKIMNEILSGIKILKYFAWEPsfrdQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYV 566
Cdd:TIGR01846 305 RVEDKFERsaaaTSFLVESVTGIETIKATATEP----QFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 567 LVDSNNILDAQKAFTSITLFNIL----RFPLSMLPMMISSMLQASVSTERLekylgGDDLDT-SAIRHD-----CNFDKA 636
Cdd:TIGR01846 381 WFGAHLVIGGALSPGQLVAFNMLagrvTQPVLRLAQLWQDFQQTGIALERL-----GDILNSpTEPRSAglaalPELRGA 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAY 703
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGvdlaiadpawlrrQMGV 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 704 VPQQSWIQNGTIKDNILFGTEfnEKRYQQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD 780
Cdd:TIGR01846 536 VLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPR 613
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 781 IYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNM---REICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
654-840 |
2.39e-30 |
|
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: 119.18 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS---WIQNGTIKDNIL-- 720
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkriGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 ------FGTEFNEKRYQQVLEAcallpdLEMLPGGDLAE--IGEkginLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVDEA------LERVGLSELADrqIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767961632 793 AHvGKHIFNKVLgpNGL-LKGKTRLLVTHSMH-FLPQVDEIVVLgNGTIV 840
Cdd:cd03235 165 PK-TQEDIYELL--RELrREGMTILVVTHDLGlVLEYFDRVLLL-NRTVV 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
643-839 |
6.04e-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: 116.55 E-value: 6.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSW 709
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwdpnelgdhvGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 710 IQNGTIKDNILfgtefnekryqqvleacallpdlemlpggdlaeigekginlSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:cd03246 87 LFSGSIAENIL-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767961632 790 AVDaHVGKHIFNKVLGpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTI 839
Cdd:cd03246 126 HLD-VEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
639-856 |
8.71e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 118.36 E-value: 8.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 639 FSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVP 705
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 706 QQSWIQNGTIKDNILFGTEFNEKRyqQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIY 782
Cdd:cd03252 83 QENVLFNRSIRDNIALADPGMSME--RVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 783 LLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFA 856
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
652-840 |
5.69e-29 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 122.93 E-value: 5.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 652 ATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-------------YVPQQSWIQNGTIKDN 718
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdreelgrhigYLPQDVELFDGTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 719 IlfgTEFNEKRYQQVLEAcALLPDL-EM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAh 794
Cdd:COG4618 426 I---ARFGDADPEKVVAA-AKLAGVhEMilrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD- 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767961632 795 VGKHIFNKVLgpnGLLK--GKTRLLVTHSMHFLPQVDEIVVLGNGTIV 840
Cdd:COG4618 501 EGEAALAAAI---RALKarGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
622-878 |
9.42e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 122.38 E-value: 9.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 622 LDTSAIRHD-------CNFDKAMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGH 694
Cdd:PRK13657 313 EDAVPDVRDppgaidlGRVKGAVEFDDVSFSYDNSRQG-VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 695 ITIKGTT-------------AYVPQQSWIQNGTIKDNILFGTE-FNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGIN 760
Cdd:PRK13657 392 ILIDGTDirtvtraslrrniAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 761 LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIfNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIV 840
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAAL--DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
250 260 270
....*....|....*....|....*....|....*....
gi 767961632 841 EKGSYSALLAKKGEFAKNLKT-FLRHTGPEEEATVHDGS 878
Cdd:PRK13657 549 ESGSFDELVARGGRFAALLRAqGMLQEDERRKQPAAEGA 587
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
653-851 |
1.32e-28 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 121.69 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 653 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQSWIQNGTIKDNI 719
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 720 L-FGTEFNEkryQQVLEACALLPDLEM---LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAhV 795
Cdd:TIGR01842 413 ArFGENADP---EKIIEAAKLAGVHELilrLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-E 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 796 GKHIFNKVLGpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAK 851
Cdd:TIGR01842 489 GEQALANAIK-ALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
637-857 |
1.48e-28 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 121.66 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSlISAMLGEMENV-HGHITIKGTT-------------A 702
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKST-IANLLTRFYDIdEGEILLDGHDlrdytlaslrnqvA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 703 YVPQQSWIQNGTIKDNILFGTEFNEKRYQqvLEACALLPD----LEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQN 778
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTEQYSREQ--IEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 779 LDIYLLDDPLSAVDAHvGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:PRK11176 499 SPILILDEATSALDTE-SERAIQAAL--DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
639-821 |
4.39e-28 |
|
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: 119.77 E-value: 4.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 639 FSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVP 705
Cdd:TIGR02868 337 LRDLSAGYPGAPPV-LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 706 QQSWIQNGTIKDNILFGT-EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLL 784
Cdd:TIGR02868 416 QDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 767961632 785 DDPLSAVDAHVGKHIFNKVLGPnglLKGKTRLLVTHS 821
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAA---LSGRTVVLITHH 529
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
637-841 |
4.71e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 112.95 E-value: 4.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEAT--VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------TAYVPQ 706
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 707 QS----WIqngTIKDNILFGTEFN----EKRYQQVLEAcallpdlemlpggdLAEIGEKGI------NLSGGQKQRISLA 772
Cdd:cd03293 81 QDallpWL---TVLDNVALGLELQgvpkAEARERAEEL--------------LELVGLSGFenayphQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 773 RATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpnGLLK--GKTRLLVTHSMH---FLPqvDEIVVLGN--GTIVE 841
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELL---DIWRetGKTVLLVTHDIDeavFLA--DRVVVLSArpGRIVA 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
643-853 |
5.63e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 119.82 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI-------------KGTTAYVPQQSW 709
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFhdipltklqldswRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 710 IQNGTIKDNILFGtefNEKRYQQVLEACALLP----DLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:PRK10789 400 LFSDTVANNIALG---RPDATQQEIEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 786 DPLSAVDAHVGKHIFNKvLGPNGllKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKG 853
Cdd:PRK10789 477 DALSAVDGRTEHQILHN-LRQWG--EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
417-856 |
2.48e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 119.06 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 417 VGETVNLMSVDAQKLMDV--TNFMHMLWSSVLQIVLSIFFLWreLGPSvLAGVGV--MVLVIPINAILSTKSKTIQVKNM 492
Cdd:TIGR00958 257 TGELTSRLSSDTQTMSRSlsLNVNVLLRNLVMLLGLLGFMLW--LSPR-LTMVTLinLPLVFLAEKVFGKRYQLLSEELQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 493 KNKDKRLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFSqLQCVVIFVFQLTpVLVSVVTFSVYVLV 568
Cdd:TIGR00958 334 EAVAKANQVAEEALSGMRTVRSFAAEEGeasrFKEALEETLQLNKRKALAYA-GYLWTTSVLGML-IQVLVLYYGGQLVL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 569 DSnnildaqkAFTSITLFNILRFPLSM------LPMMISSMLQASVSTERLEKYLGGD-DLDTSAIRHDCNFDKAMQFSE 641
Cdd:TIGR00958 412 TG--------KVSSGNLVSFLLYQEQLgeavrvLSYVYSGMMQAVGASEKVFEYLDRKpNIPLTGTLAPLNLEGLIEFQD 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 642 ASFTWEHDSEATV-RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVPQQ 707
Cdd:TIGR00958 484 VSFSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 708 SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEM-LPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:TIGR00958 564 PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMeFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 787 PLSAVDAHVgkhifNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFA 856
Cdd:TIGR00958 644 ATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
654-841 |
2.55e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 109.02 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS----WIqngTIKDNILF 721
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtgpgpdrGVVFQEPallpWL---TVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 GTEFN----EKRYQQVLEAcallpdlemlpggdLAEIGEKGI------NLSGGQKQRISLARATYQNLDIYLLDDPLSAV 791
Cdd:COG1116 104 GLELRgvpkAERRERAREL--------------LELVGLAGFedayphQLSGGMRQRVAIARALANDPEVLLMDEPFGAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 792 DAHVGKHIfnkvlgpNGLL------KGKTRLLVTHSmhflpqVDE-------IVVLGN--GTIVE 841
Cdd:COG1116 170 DALTRERL-------QDELlrlwqeTGKTVLFVTHD------VDEavfladrVVVLSArpGRIVE 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
655-839 |
4.51e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.82 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQNGTIKDNILF 721
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEPALWGGTVRDNLPF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 GTEFNEKRYQQVlEACALLPDLEmLPGGDLaeigEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHvGKHIF 800
Cdd:COG4619 97 PFQLRERKFDRE-RALELLERLG-LPPDIL----DKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-NTRRV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767961632 801 NKVLGPNGLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTI 839
Cdd:COG4619 170 EELLREYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
503-855 |
5.44e-26 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 114.04 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 503 NEILSGIKILKYFAWEPSF--------------RDQVQNLRKKELKNLLA-FSQL-QCVVIFVFQLTPVlvsvVTFSVYV 566
Cdd:PRK10790 208 NEVINGMSVIQQFRQQARFgermgeasrshymaRMQTLRLDGFLLRPLLSlFSALiLCGLLMLFGFSAS----GTIEVGV 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 567 LVdsnnildaqkAFtsITLFNILRFPLSMLPMMISSMLQASVSTERL--------EKYlGGDDLDTSAIRHDCNfdkamq 638
Cdd:PRK10790 284 LY----------AF--ISYLGRLNEPLIELTTQQSMLQQAVVAGERVfelmdgprQQY-GNDDRPLQSGRIDID------ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 639 fsEASFTWEHDsEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVP 705
Cdd:PRK10790 345 --NVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 706 QQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:PRK10790 422 QDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767961632 786 DPLSAVDAHVGKHIfNKVLgpnGLLKGKTRLLV-THSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEF 855
Cdd:PRK10790 502 EATANIDSGTEQAI-QQAL---AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
638-838 |
7.32e-26 |
|
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: 106.40 E-value: 7.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 638 QFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYV 704
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 705 PQ--QSWIQNGTIKDNILFGTEF----NEKRYQQVLEACALLpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQ 777
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENlglpEEEIEERVEEALELV---------GLEGLRDRSPfTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 778 NLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGT 838
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKA--EGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
638-857 |
1.27e-25 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 106.26 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 638 QFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYV 704
Cdd:COG1122 2 ELENLSFSYPGGTPA-LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknlrelrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 705 PQQSWIQ--NGTIKDNILFGTEfN-----EKRYQQVLEAcallpdLEMLpggDLAEIGEKGI-NLSGGQKQRISLARATY 776
Cdd:COG1122 81 FQNPDDQlfAPTVEEDVAFGPE-NlglprEEIRERVEEA------LELV---GLEHLADRPPhELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 777 QNLDIYLLDDPLSAVDAHvGKHIFNKVLgpNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGE 854
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPR-GRRELLELL--KRLNKeGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDYEL 227
|
...
gi 767961632 855 FAK 857
Cdd:COG1122 228 LEE 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
654-789 |
1.37e-25 |
|
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: 103.50 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNG-TIKDNI 719
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkeiGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 720 LFGTEF----NEKRYQQVLEAcallpdLEMLPGGDLAE--IGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:pfam00005 81 RLGLLLkglsKREKDARAEEA------LEKLGLGDLADrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
637-843 |
1.95e-25 |
|
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: 103.93 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYV 704
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 705 PQQSWIQNGTIKDNIlfgtefnekryqqvleacallpdlemlpggdlaeigekGINLSGGQKQRISLARATYQNLDIYLL 784
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 785 DDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG 843
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
649-863 |
2.51e-25 |
|
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: 105.71 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA------------YVPQQSWI-QNGTI 715
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVrkeprearrqigVLPDERGLyDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNILFGTEFNEKRYQQVLEACALLpdLEMLpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAh 794
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEEL--IELL---GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 795 VGKHIFNKVLgpnGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGEfaKNLKTFL 863
Cdd:COG4555 166 MARRLLREIL---RALKkeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIGE--ENLEDAF 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
654-843 |
4.50e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 102.90 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQqswiqngtikdnil 720
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkelarkiAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 fgtefnekryqqVLEACallpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:cd03214 81 ------------ALELL------------GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767961632 800 FNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03214 137 LE-------LLRrlarerGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
636-856 |
5.07e-25 |
|
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: 111.07 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 636 AMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------TTAY------ 703
Cdd:COG5265 357 EVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvTQASlraaig 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 704 -VPQQSWIQNGTIKDNILFG-TEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:COG5265 436 iVPQDTVLFNDTIAYNIAYGrPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 782 YLLDDPLSAVDAHVGKHIfNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFA 856
Cdd:COG5265 516 LIFDEATSALDSRTERAI-QAAL--REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
645-844 |
1.45e-24 |
|
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: 103.58 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQ 711
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarriAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 712 NG-TIKDNILFG--------TEFNEKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDI 781
Cdd:COG1120 88 FGlTVRELVALGryphlglfGRPSAEDREAVEEA------LERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961632 782 YLLDDPLSAVDAHvgkHIFnKVLgpnGLLK------GKTRLLVThsmHFLPQV----DEIVVLGNGTIVEKGS 844
Cdd:COG1120 159 LLLDEPTSHLDLA---HQL-EVL---ELLRrlarerGRTVVMVL---HDLNLAaryaDRLVLLKDGRIVAQGP 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
654-871 |
1.87e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 102.83 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYVPQQSWIQNG-TIKDNIL 720
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 F-------GTEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 794 hVGKHIFNKVLgpNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGEFAknlktFLRHTGPEEE 871
Cdd:COG1131 165 -EARRELWELL--RELAAeGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARLLEDV-----FLELTGEEAR 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
643-850 |
6.30e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.91 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMEN---VHGHITIKGTT-------------AYVPQ 706
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDllelsealrgrriGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 707 QSWIQ-NG-TIKDNILFGTEFN----EKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNL 779
Cdd:COG1123 91 DPMTQlNPvTVGDQIAEALENLglsrAEARARVLEL------LEAV---GLERRLDRYPHqLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 780 DIYLLDDPLSAVDAHVGKHIFnkvlgpnGLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEIL-------DLLRelqrerGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
654-850 |
7.47e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 106.53 E-value: 7.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT----------------AYVPQ---QSWIQNGT 714
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrslrelrrrvQMVFQdpySSLNPRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFGTEFN--------EKRYQQVLEACALLPD-LEMLPGGdlaeigekginLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:COG1123 361 VGDIIAEPLRLHgllsraerRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 786 DPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG1123 430 EPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
649-843 |
9.02e-24 |
|
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: 100.29 E-value: 9.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-----------TAYVPQQ-SWIQNGTIK 716
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQDyALFPHLTVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 717 DNILFGTEFNEKRYQQVLEACALLpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:cd03259 91 ENIAFGLKLRGVPKAEIRARVREL--LELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767961632 796 GKHIFNKVLgpnGLLK--GKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKG 843
Cdd:cd03259 166 REELREELK---ELQRelGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
642-850 |
2.99e-23 |
|
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: 99.88 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 642 ASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSW----IQ------ 711
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrVQmvfqdp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 712 ------NGTIKDNI-----LFGTEFNEKRYQQVLEACALLPD-LEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNL 779
Cdd:COG1124 89 yaslhpRHTVDRILaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPH-----------QLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 780 DIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSM----HFlpqVDEIVVLGNGTIVEKGSYSALL 849
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHDLavvaHL---CDRVAVMQNGRIVEELTVADLL 227
|
.
gi 767961632 850 A 850
Cdd:COG1124 228 A 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
654-843 |
3.64e-23 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 99.12 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------------TAYVPQQSwiqNG---- 713
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQMVFQDP---MSslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 --TIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:cd03257 98 rmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVG--LPEEVLNRYPHeLSGGQRQRVAIARALALNPKLLIADEPTSA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 791 VDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03257 176 LDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
643-839 |
9.60e-23 |
|
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: 97.56 E-value: 9.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEAT--VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENV-HGHITIKGTTA----------------- 702
Cdd:cd03255 7 SKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGTDIsklsekelaafrrrhig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 703 YVPQQ-SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLD 780
Cdd:cd03255 86 FVFQSfNLLPDLTALENVELPLLLAGVPKKERRERAEEL--LERV---GLGDRLNHYPSeLSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 781 IYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQVDEIVVLGNGTI 839
Cdd:cd03255 161 IILADEPTGNLDSETGKEVME-------LLRelnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
638-838 |
1.32e-22 |
|
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: 95.00 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 638 QFSEASFTweHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkgttayvpqqswiqngtikd 717
Cdd:cd00267 1 EIENLSFR--YGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 nilFGTEFNEKRYQQVLEACALLPDLemlpggdlaeigekginlSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 797
Cdd:cd00267 59 ---DGKDIAKLPLEELRRRIGYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767961632 798 HIFNKVLGPNglLKGKTRLLVTHSMHFLPQV-DEIVVLGNGT 838
Cdd:cd00267 118 RLLELLRELA--EEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
322-613 |
1.39e-22 |
|
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: 99.16 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 322 LLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFtAALIQSFCLQCYFQLCFKLGVKVRTAIMASVY 401
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLL-LALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 402 KKALTLSNLARKEYTVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSIFFL----WRelgpSVLAGVGVMVLVIPI 476
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNlVSSGLLQLLSDVLTLIGALVILfylnWK----LTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 477 NAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFSQLQCVVIFVFQL 552
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEReierFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767961632 553 TPVLVSVvtFSVYvLVdSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd07346 236 GTALVLL--YGGY-LV-LQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
655-850 |
1.09e-21 |
|
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: 94.88 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------------TAYVPQQSWIQNG-TIKD 717
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSlTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 NILFG----TEFNEKRYQQV----LEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:cd03261 97 NVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961632 790 AVDAhVGKHIFNK-VLGPNGLLkGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:cd03261 166 GLDP-IASGVIDDlIRSLKKEL-GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
654-839 |
2.39e-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: 92.08 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkgttayvpqqswiqngtikdnilFGTEFNEKRYQqV 733
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKEPEE-V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 734 LEACALLPDLEMLPGgDLaeIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAhVGKHIFNKVLgpNGLLK-G 812
Cdd:cd03230 72 KRRIGYLPEEPSLYE-NL--TVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELL--RELKKeG 145
|
170 180
....*....|....*....|....*...
gi 767961632 813 KTRLLVTHSMHFLPQV-DEIVVLGNGTI 839
Cdd:cd03230 146 KTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
654-844 |
3.69e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.98 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG-EMENvHGHITIKGTTAYV---PQQSWI----QNG------TIKDNI 719
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlETPD-SGRIVLNGRDLFTnlpPRERRVgfvfQHYalfphmTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 720 LFG----TEFNEKRYQQVLEacalLpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 794
Cdd:COG1118 97 AFGlrvrPPSKAEIRARVEE----L--LELV---QLEGLADRYPSqLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 795 VGKHIfNKVLGpnGLLK--GKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKGS 844
Cdd:COG1118 168 VRKEL-RRWLR--RLHDelGGTTVFVTHD-----QEealelaDRVVVMNQGRIEQVGT 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
643-844 |
4.59e-21 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 93.01 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAYVPQQSWIQ------ 711
Cdd:cd03260 5 DLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVLElrrrvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 712 ---------NGTIKDNILFG--------TEFNEKRYQQVLEACALLPDLemlpgGDLAeigeKGINLSGGQKQRISLARA 774
Cdd:cd03260 85 mvfqkpnpfPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAALWDEV-----KDRL----HALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 775 TYQNLDIYLLDDPLSAVDAhVGKHIFNKVLGpnGLLKGKTRLLVTHSMHflpQV----DEIVVLGNGTIVEKGS 844
Cdd:cd03260 156 LANEPEVLLLDEPTSALDP-ISTAKIEELIA--ELKKEYTIVIVTHNMQ---QAarvaDRTAFLLNGRLVEFGP 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
654-841 |
4.94e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.80 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENV-HGHITIKGTTA-----------------YVPQQS-WIQNGT 714
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGQDIsslserelarlrrrhigFVFQFFnLLPELT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFGTEFN----EKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:COG1136 103 ALENVALPLLLAgvsrKERRERAREL------LERV---GLGDRLDHRPSqLSGGQQQRVAIARALVNRPKLILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 790 AVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 841
Cdd:COG1136 174 NLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
654-838 |
5.47e-21 |
|
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: 91.09 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT---------------AYVPQQ-SWIQNGTIKD 717
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelpplrrriGMVFQDfALFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 NILFGtefnekryqqvleacallpdlemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 797
Cdd:cd03229 96 NIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767961632 798 HIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGT 838
Cdd:cd03229 138 EVRA-------LLKslqaqlGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
638-839 |
1.25e-20 |
|
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: 91.76 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 638 QFSEASFTWEHDSEATV-RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAY----------- 703
Cdd:cd03248 13 KFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpiSQYehkylhskvsl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 704 VPQQSWIQNGTIKDNILFG---TEFNE-KRYQQVLEACALLPDLEMlpgGDLAEIGEKGINLSGGQKQRISLARATYQNL 779
Cdd:cd03248 93 VGQEPVLFARSLQDNIAYGlqsCSFECvKEAAQKAHAHSFISELAS---GYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 780 DIYLLDDPLSAVDAHVGKHIFNKVLGPNgllKGKTRLLVTHSMHFLPQVDEIVVLGNGTI 839
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWP---ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
639-850 |
1.61e-20 |
|
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: 91.59 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 639 FSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEM-ENVHGHITIKG-------------TTAYV 704
Cdd:cd03295 3 FENVTKRYGGGKKA-VNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLiEPTSGEIFIDGedireqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 705 PQQ-SWIQNGTIKDNI-----LFGTEfNEKRYQQVLEACALLPdlemLPGGDLAE--IGEkginLSGGQKQRISLARATY 776
Cdd:cd03295 81 IQQiGLFPHMTVEENIalvpkLLKWP-KEKIRERADELLALVG----LDPAEFADryPHE----LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 777 QNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLkGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKGSYSALLA 850
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
654-844 |
2.05e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 94.01 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENV-HGHITIKGT-----------TAYVPQqswiqNG------TI 715
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-FETPdSGRILLDGRdvtglppekrnVGMVFQ-----DYalfphlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNILFGTEF----NEKRYQQVLEAcallpdLEMLpggDLAEIGEKGIN-LSGGQKQRISLARAtyqnL----DIYLLDD 786
Cdd:COG3842 95 AENVAFGLRMrgvpKAEIRARVAEL------LELV---GLEGLADRYPHqLSGGQQQRVALARA----LapepRVLLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 787 PLSAVDAHVGKH----IFNkvlgpngLLK--GKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKGS 844
Cdd:COG3842 162 PLSALDAKLREEmreeLRR-------LQRelGITFIYVTHD-----QEealalaDRIAVMNDGRIEQVGT 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
654-844 |
3.87e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.83 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENV-HGHITIKGT-----------TAYVPQqSWI--QNGTIKDNI 719
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-LEDPtSGEILIGGRdvtdlppkdrnIAMVFQ-SYAlyPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 720 LFGTEFN----EKRYQQVLEACALLpDLEML----PGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAV 791
Cdd:COG3839 97 AFPLKLRkvpkAEIDRRVREAAELL-GLEDLldrkPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSNL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961632 792 DAHvgkhifnkvlgpnglLKGKTR--------------LLVTHSmhflpQV------DEIVVLGNGTIVEKGS 844
Cdd:COG3839 165 DAK---------------LRVEMRaeikrlhrrlgtttIYVTHD-----QVeamtlaDRIAVMNDGRIQQVGT 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
655-840 |
5.83e-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: 5.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS----WIqngTIKDNILFG 722
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKDallpWL---NVLDNVAFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 723 TEFN----EKRYQQVLEACALLpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 797
Cdd:COG4525 101 LRLRgvpkAERRARAEELLALV---------GLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767961632 798 HIfnKVLgpngLLK-----GKTRLLVTHSmhflpqVDEIVVLGNGTIV 840
Cdd:COG4525 172 QM--QEL----LLDvwqrtGKGVFLITHS------VEEALFLATRLVV 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
648-834 |
1.42e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 648 HDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--AYVPQQSWIQNG---TIKDNILFG 722
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvAYVPQRSEVPDSlplTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 723 TeFNE--------KRYQQVLEACallpdLEMLPGGDLAE--IGEkginLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:NF040873 82 R-WARrglwrrltRDDRAAVDDA-----LERVGLADLAGrqLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767961632 793 AHVGKHIfnkvlgpNGLLK-----GKTRLLVTHSMHFLPQVDEIVVL 834
Cdd:NF040873 152 AESRERI-------IALLAeeharGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
655-839 |
7.10e-19 |
|
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: 86.04 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQ----------------NGTIKDN 718
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 719 ILFG--TEFNEKRYQQVLEACALLPDLemlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVg 796
Cdd:cd03262 97 ITLApiKVKGMSKAEAEERALELLEKV-----GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767961632 797 khiFNKVLgpnGLLK-----GKTRLLVTHSMHFLPQV-DEIVVLGNGTI 839
Cdd:cd03262 171 ---VGEVL---DVMKdlaeeGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
654-851 |
7.42e-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: 86.48 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMEN-VHGHITIKGT----------------TAYVPQQ-SWIQNGTI 715
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGTdltllsgkelrkarrrIGMIFQHfNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNILFGTEF----NEKRYQQVLEACALLpDLEmlpggDLAEIGEKgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAV 791
Cdd:cd03258 100 FENVALPLEIagvpKAEIEERVLELLELV-GLE-----DKADAYPA--QLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767961632 792 DAHVGKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAK 851
Cdd:cd03258 172 DPETTQSILALLRDINREL-GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
656-844 |
8.25e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 8.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-----------TAYVPQQ-SWIQNGTIKDNILFGT 723
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 EFNEKRY--------QQVLEAcallpdLEMLPGGDLAEigEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:PRK10851 100 TVLPRRErpnaaaikAKVTQL------LEMVQLAHLAD--RYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767961632 796 GKHIFNKVLGPNGLLKgKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK10851 172 RKELRRWLRQLHEELK-FTSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGT 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
643-840 |
8.34e-19 |
|
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: 85.77 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEaTVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG----------TTAYVPQQSWIQN 712
Cdd:cd03226 6 SFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 G--TIKDNILFGTEFNEKRYQQVLEacaLLPDLemlpggDLAEIGEKG-INLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:cd03226 85 FtdSVREELLLGLKELDAGNEQAET---VLKDL------DLYALKERHpLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 790 AVDAH----VGKhIFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIV 840
Cdd:cd03226 156 GLDYKnmerVGE-LIRELAA-----QGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
650-843 |
1.64e-18 |
|
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: 85.85 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 650 SEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-----------TAYVPQQ-SWIQNGTIKD 717
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 NILFG----TEFNEKRYQQVLEACALLPDLEMLpggdlaeiGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:cd03299 91 NIAYGlkkrKVDKKEIERKVLEIAEMLGIDHLL--------NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767961632 794 HVGKHIFN--KVLGPNgllKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKG 843
Cdd:cd03299 163 RTKEKLREelKKIRKE---FGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVG 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
647-842 |
1.70e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 647 EHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------AYVPQQS----WiQNgt 714
Cdd:PRK11248 10 DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaerGVVFQNEgllpW-RN-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFGTEF-NEKRYQQVLEAcallpdLEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:PRK11248 87 VQDNVAFGLQLaGVEKMQRLEIA------HQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 793 AhvgkhiFNKVLGPNGLLK-----GKTRLLVTHSMH---FLpqVDEIVVL--GNGTIVEK 842
Cdd:PRK11248 161 A------FTREQMQTLLLKlwqetGKQVLLITHDIEeavFM--ATELVLLspGPGRVVER 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
654-850 |
2.57e-18 |
|
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: 84.79 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------------TAYVPQ-QSWIQNGTIKDN 718
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 719 ILFG--TEFNEKRYQQVLEACALLPDL-EMLpggdlaeiGEKGINLSGGQKQRISLARATYQNLDIYLLDDP---LSAVd 792
Cdd:cd03224 96 LLLGayARRRAKRKARLERVYELFPRLkERR--------KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 793 ahVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:cd03224 167 --IVEEIFEAIRELRD--EGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
655-850 |
3.79e-18 |
|
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: 84.65 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---TTAYVPQQSWI--------QNG------TIKD 717
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELYELrrrigmlfQGGalfdslTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 NILFG----TEFNEK-RYQQVLEAcallpdLEM--LPG-GDL--AEigekginLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:COG1127 102 NVAFPlrehTDLSEAeIRELVLEK------LELvgLPGaADKmpSE-------LSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 788 LSAVDAhVGKHIFNKvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG1127 169 TAGLDP-ITSAVIDE------LIRelrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
649-844 |
4.06e-18 |
|
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: 83.62 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQSWIQNGTI 715
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNIlfgTEFNEKRYQQVLEACallpdlemlpggdlaEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:cd03369 99 RSNL---DPFDEYSDEEIYGAL---------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767961632 796 gKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:cd03369 161 -DALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
657-850 |
5.65e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.42 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLISAM--LGEMENVH---GHITIKGTTAYVPQQSWI-----------QN------GT 714
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQPEAGTirvGDITIDTARSLSQQKGLIrqlrqhvgfvfQNfnlfphRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFGTEFNEKRYQQvlEACALLPDLemlpggdLAEIGEKGIN------LSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:PRK11264 102 VLENIIEGPVIVKGEPKE--EATARAREL-------LAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 789 SAVDAHVGKHIFNKVlgpNGLLKGK-TRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK11264 173 SALDPELVGEVLNTI---RQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFA 233
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
643-844 |
5.95e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 84.79 E-value: 5.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSW---------IQN- 712
Cdd:TIGR04520 7 SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvgmvFQNp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 ------GTIKDNILFGTEfN--------EKRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARATYQN 778
Cdd:TIGR04520 87 dnqfvgATVEDDVAFGLE-NlgvpreemRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961632 779 LDIYLLDDPLSAVDAhVGK-------HIFNKVlgpngllKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:TIGR04520 155 PDIIILDEATSMLDP-KGRkevletiRKLNKE-------EGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
658-863 |
6.40e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 83.65 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 658 NLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQ---SWI-QNG------TIKDNILFG--- 722
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdlTALPPAErpvSMLfQENnlfphlTVAQNIGLGlrp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 723 ----TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAvdahvgkh 798
Cdd:COG3840 99 glklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSA-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 799 ifnkvLGPN------GLLK------GKTRLLVTHSmhflPQ-----VDEIVVLGNGTIVEKGSYSALLAkkGEFAKNLKT 861
Cdd:COG3840 160 -----LDPAlrqemlDLVDelcrerGLTVLMVTHD----PEdaariADRVLLVADGRIAADGPTAALLD--GEPPPALAA 228
|
..
gi 767961632 862 FL 863
Cdd:COG3840 229 YL 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
653-843 |
9.18e-18 |
|
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: 83.07 E-value: 9.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 653 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-----------TTAYVPQQ-SWIQNGTIKDNIL 720
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 FGTEFNEKRY----QQVLEACALLpDLEMLpggdlaeIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVG 796
Cdd:cd03301 95 FGLKLRKVPKdeidERVREVAELL-QIEHL-------LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 797 KHIFNKVlgpNGLLK--GKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKG 843
Cdd:cd03301 167 VQMRAEL---KRLQQrlGTTTIYVTHD-----QVeamtmaDRIAVMNDGQIQQIG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
654-844 |
1.30e-17 |
|
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: 83.16 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--TTAYVPQQSWI----------QNGTIKDNILF 721
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedATDVPVQERNVgfvfqhyalfRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 GTEFnEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIf 800
Cdd:cd03296 98 GLRV-KPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767961632 801 nkvlgpNGLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:cd03296 176 ------RRWLRrlhdelHVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGT 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
418-876 |
2.48e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 87.72 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 418 GETVNLMSVDAQKL-MDVTNFMHMLWSSVLQIvLSIFFLWRELgpSVLAGVGVMVLVIPI-NAILSTKSKTIQVKNMKN- 494
Cdd:PLN03232 1007 GRVINRFSKDIGDIdRNVANLMNMFMNQLWQL-LSTFALIGTV--STISLWAIMPLLILFyAAYLYYQSTSREVRRLDSv 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 495 -KDKRLKIMNEILSGIK-ILKYFAWepsfrDQVQNLRKKELKNLLAFSQLQC-----VVIFVFQLTPVLVSVV-TFSVYV 566
Cdd:PLN03232 1084 tRSPIYAQFGEALNGLSsIRAYKAY-----DRMAKINGKSMDNNIRFTLANTssnrwLTIRLETLGGVMIWLTaTFAVLR 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 567 LVDSNNildaQKAFTSiTLFNILRFPLSMLPMMISSMLQASV------STERLEKYLggdDLDTSAIRHDCN-------- 632
Cdd:PLN03232 1159 NGNAEN----QAGFAS-TMGLLLSYTLNITTLLSGVLRQASKaenslnSVERVGNYI---DLPSEATAIIENnrpvsgwp 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 633 FDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------- 699
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrr 1310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 700 TTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNL 779
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 780 DIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGE-FAKn 858
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTI---REEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFR- 1466
|
490
....*....|....*...
gi 767961632 859 lktFLRHTGPEEEATVHD 876
Cdd:PLN03232 1467 ---MVHSTGPANAQYLSN 1481
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
635-836 |
2.98e-17 |
|
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: 82.69 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 635 KAMQFSEASFTWEHDSEAT-----VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------- 701
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTgqtvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrke 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 702 ----------------AYVPQQswiqngTIKDNILFGTEFN-------EKRYQQVLEACALLPDLEMLPGgdlaeigekg 758
Cdd:cd03294 96 lrelrrkkismvfqsfALLPHR------TVLENVAFGLEVQgvpraerEERAAEALELVGLEGWEHKYPD---------- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 759 iNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLKgKTRLLVTHSMhflpqvDEIVVLGN 836
Cdd:cd03294 160 -ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQ-KTIVFITHDL------DEALRLGD 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
559-855 |
3.05e-17 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 87.31 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 559 VVTFSVYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDD-----LDTSAIRHDCNF 633
Cdd:TIGR00957 1202 IVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKeapwqIQETAPPSGWPP 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 634 DKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------------ 701
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiglhdlrfk 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 702 -AYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD 780
Cdd:TIGR00957 1362 iTIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTK 1441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 781 IYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEF 855
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTI---RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
645-848 |
3.28e-17 |
|
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: 81.85 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 645 TWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------------TAYVPQQ- 707
Cdd:cd03256 9 TYPNGKKA-LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 708 SWIQNGTIKDNILFG---------TEFNEKRYQQVLEACALLPDLEMLpggDLAEIgeKGINLSGGQKQRISLARATYQN 778
Cdd:cd03256 88 NLIERLSVLENVLSGrlgrrstwrSLFGLFPKEEKQRALAALERVGLL---DKAYQ--RADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 779 LDIYLLDDPLSAVD---AHvgkhifnKVLgpnGLLK------GKTRLLVTHSMHF-LPQVDEIVVLGNGTIVEKGSYSAL 848
Cdd:cd03256 163 PKLILADEPVASLDpasSR-------QVM---DLLKrinreeGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
656-843 |
5.69e-17 |
|
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: 80.80 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDI---MAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQ-SWIQNGT 714
Cdd:cd03297 12 DFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQyALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFGTEFNEKRYQQVLEAcallpdlEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767961632 794 HVGKHIFNKVlgpNGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03297 165 ALRLQLLPEL---KQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
636-876 |
7.62e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 636 AMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----------TAYVP 705
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 706 QQS---WIQNGTIKDNILFGT--------EFNEKRYQQVLEACALLPDLEMlpggDLAEIGEkginLSGGQKQRISLARA 774
Cdd:PRK15056 85 QSEevdWSFPVLVEDVVMMGRyghmgwlrRAKKRDRQIVTAALARVDMVEF----RHRQIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 775 TYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG-SYSAL 848
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIIS-------LLRelrdeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGpTETTF 229
|
250 260 270
....*....|....*....|....*....|.
gi 767961632 849 LAKKGEFAknLKTFLRH---TGPEEEATVHD 876
Cdd:PRK15056 230 TAENLELA--FSGVLRHvalNGSEESIITDD 258
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
655-794 |
1.11e-16 |
|
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: 79.45 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYVPQQS-WIQNGTIKDNILF 721
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHADgLKPELTVRENLRF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 722 -----GTEFNEKRYQQVLEACALlPDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 794
Cdd:COG4133 99 waalyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
638-841 |
1.21e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.71 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 638 QFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------TTAYVPQ----- 706
Cdd:COG2884 3 RFENVSKRYPGGREA-LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlKRREIPYlrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 707 ----QSW--IQNGTIKDNILFG---TEFNEKRYQQ-VLEAcallpdLEMLpggdlaEIGEKG----INLSGGQKQRISLA 772
Cdd:COG2884 82 gvvfQDFrlLPDRTVYENVALPlrvTGKSRKEIRRrVREV------LDLV------GLSDKAkalpHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 773 RATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQVDE-IVVLGNGTIVE 841
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIME-------LLEeinrrGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
655-844 |
2.34e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 79.27 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENV-HGHITIKGTTAYVPQQSWIQ----------------NGTIKD 717
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINL-LEEPdSGTITVDGEDLTDSKKDINKlrrkvgmvfqqfnlfpHLTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 NILFGTEFNEKRYQQVLEACAllpdLEMLpggDLAEIGEKG----INLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:COG1126 97 NVTLAPIKVKKMSKAEAEERA----MELL---ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 794 H-VGkhifnKVLgpnGLLK-----GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:COG1126 170 ElVG-----EVL---DVMRdlakeGMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGP 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
654-840 |
6.22e-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: 76.31 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayvpqqswIQNGTIKDNILFGTEFnekRYQqv 733
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------VSFASPRDARRAGIAM---VYQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 734 leacallpdlemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpnGLLK-- 811
Cdd:cd03216 83 ---------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RRLRaq 131
|
170 180 190
....*....|....*....|....*....|
gi 767961632 812 GKTRLLVTHSMHFLPQV-DEIVVLGNGTIV 840
Cdd:cd03216 132 GVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
653-822 |
6.77e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.28 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 653 TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAmLGEMENVHGHITIKGTTAY---------------------VPQQSWIQ 711
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRS-INRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 712 NGTIKDNILFGTEFNEKRYQQVLEACALlpdlEMLPGGDLAE-----IGEKGINLSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDEAVE----KSLKGASIWDevkdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 767961632 787 PLSAVDAHVGKHIFNKVLGpnglLKGK-TRLLVTHSM 822
Cdd:PRK14239 175 PTSALDPISAGKIEETLLG----LKDDyTMLLVTRSM 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
656-887 |
7.27e-16 |
|
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: 80.14 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQSwiq-ngTIKD 717
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrriGYVFQEArlfphlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 NILFGTEFNEK--RYQQVLEACALL---PDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:COG4148 97 NLLYGRKRAPRaeRRISFDEVVELLgigHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 793 AHVGKHIfnkvlgpngL-----LKGKTR---LLVTHSMhflpqvDEI-------VVLGNGTIVEKGSYSALLAKKGefak 857
Cdd:COG4148 166 LARKAEI---------LpylerLRDELDipiLYVSHSL------DEVarladhvVLLEQGRVVASGPLAEVLSRPD---- 226
|
250 260 270
....*....|....*....|....*....|..
gi 767961632 858 nlktfLRHTGPEEEA-TVHDGS-EEEDDDYGL 887
Cdd:COG4148 227 -----LLPLAGGEEAgSVLEATvAAHDPDYGL 253
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
656-887 |
1.05e-15 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 79.77 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQ-SWIQNGTIKD 717
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrriGYVFQEaRLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 NILFGTEF-----NEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:TIGR02142 95 NLRYGMKRarpseRRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 793 AHVGKHIFnkvlgPngLLKGKTR------LLVTHSM-HFLPQVDEIVVLGNGTIVEKGSYSALLAKkgefaKNLKTFLRh 865
Cdd:TIGR02142 164 DPRKYEIL-----P--YLERLHAefgipiLYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWAS-----PDLPWLAR- 230
|
250 260
....*....|....*....|...
gi 767961632 866 tgpEEEATVHDGS-EEEDDDYGL 887
Cdd:TIGR02142 231 ---EDQGSLIEGVvAEHDQHYGL 250
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
654-843 |
1.06e-15 |
|
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: 77.19 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQ-QSWIQNG-TIKDNILF-GTEFN--EK 728
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNPElTGRENIYLnGRLLGlsRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 729 RYQQVLEACAllpdlemlpggDLAEIGE------KgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH----VGKH 798
Cdd:cd03220 118 EIDEKIDEII-----------EFSELGDfidlpvK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRR 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767961632 799 IFNKVlgpnglLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03220 185 LRELL------KQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
654-872 |
1.33e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.97 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLI---------SAmlgemenvhGHITIKGT--TAY--------------VPQQ- 707
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcinllerpTS---------GSVLVDGVdlTALserelraarrkigmIFQHf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 708 SWIQNGTIKDNILFGTEFN----EKRYQQVLEacaLLpdlemlpggDLAEIGEKG----INLSGGQKQRISLARATYQNL 779
Cdd:COG1135 92 NLLSSRTVAENVALPLEIAgvpkAEIRKRVAE---LL---------ELVGLSDKAdaypSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 780 DIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS-YSALLAK 851
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILD-------LLKdinrelGLTIVLITHEMDVVRRIcDRVAVLENGRIVEQGPvLDVFANP 232
|
250 260
....*....|....*....|..
gi 767961632 852 KGEFAKNL-KTFLRHTGPEEEA 872
Cdd:COG1135 233 QSELTRRFlPTVLNDELPEELL 254
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
632-852 |
1.41e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 77.72 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 632 NFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQ 711
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 712 N---------------GTIKDNILFGTE---FNEKRYQQVLEACALLPDLEMLpggdlaeIGEKGINLSGGQKQRISLAR 773
Cdd:PRK13632 83 KkigiifqnpdnqfigATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 774 ATYQNLDIYLLDDPLSAVDAHvGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKK 852
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
637-861 |
1.44e-15 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 77.64 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-TAYVPQQSWIQNGTI 715
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 --KDNILFG--TEFN--------EKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03288 100 ilQDPILFSgsIRFNldpeckctDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 784 LDDPLSAVDAHVgKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKK-GEFAKNLKT 861
Cdd:cd03288 180 MDEATASIDMAT-ENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRT 255
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
654-848 |
1.57e-15 |
|
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: 76.39 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT------------TAYVPQqswiqngtikDNILF 721
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarqsLGYCPQ----------FDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 gTEFNekryqqVLEACALLPDLEMLPGGDLAEIGEKGI--------------NLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:cd03263 88 -DELT------VREHLRFYARLKGLPKSEIKEEVELLLrvlgltdkankrarTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 788 LSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVTHSMH---FLpqVDEIVVLGNGTIVEKGSYSAL 848
Cdd:cd03263 161 TSGLDPASRRAIWDLIL---EVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
656-848 |
2.24e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayVPQQSwIQNG---------------TIKDNIL 720
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED--VTHRS-IQQRdicmvfqsyalfphmSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 FGTEF----NEKRYQQVLEACALLpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:PRK11432 101 YGLKMlgvpKEERKQRVKEALELV---------DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767961632 796 GKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSAL 848
Cdd:PRK11432 172 RRSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
655-794 |
3.27e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG----TTAYVPQQSWI--QNG-----TIKDNILFGT 723
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdidDPDVAEACHYLghRNAmkpalTVAENLEFWA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 724 EFNEKRYQQVLEA-CAL-LPDLEMLPGGdlaeigekgiNLSGGQKQRISLAR--ATYQNldIYLLDDPLSAVDAH 794
Cdd:PRK13539 99 AFLGGEELDIAAAlEAVgLAPLAHLPFG----------YLSAGQKRRVALARllVSNRP--IWILDEPTAALDAA 161
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
654-843 |
4.33e-15 |
|
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: 74.95 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTI------------KDNILF 721
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALieapgfypnltaRENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 ---GTEFNEKRYQQVLEAcallpdlemlpgGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGK 797
Cdd:cd03268 96 larLLGIRKKRIDEVLDV------------VGLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767961632 798 HIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03268 164 ELRELILSLRD--QGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
647-844 |
5.38e-15 |
|
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: 75.35 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 647 EHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--TTAYVPQQSWI----QNG------T 714
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkdITNLPPHKRPVntvfQNYalfphlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFGTEFNEKRYQQVLEACAllpdlEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:cd03300 89 VFENIAFGLRLKKLPKAEIKERVA-----EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961632 794 HVGKHI------FNKVLgpngllkGKTRLLVTH------SMHflpqvDEIVVLGNGTIVEKGS 844
Cdd:cd03300 164 KLRKDMqlelkrLQKEL-------GITFVFVTHdqeealTMS-----DRIAVMNKGKIQQIGT 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
634-844 |
6.94e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.99 E-value: 6.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 634 DKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSS---LISAMLGEMENVHGHITIKGTTaYVPQQSW- 709
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGIT-LTAKTVWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 710 --------IQN-------GTIKDNILFGTEFNEKRYQQVLEACA-LLPDLEMLPggdlaEIGEKGINLSGGQKQRISLAR 773
Cdd:PRK13640 82 irekvgivFQNpdnqfvgATVGDDVAFGLENRAVPRPEMIKIVRdVLADVGMLD-----YIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 774 ATYQNLDIYLLDDPLSAVDAHVGKHIFN---KVLGPNGLlkgkTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKlirKLKKKNNL----TVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
643-867 |
7.27e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 75.82 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTaYVPQQSW---------IQN- 712
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvgmvFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 ------GTIKDNILFGTEFNE-------KRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNL 779
Cdd:PRK13635 91 dnqfvgATVQDDVAFGLENIGvpreemvERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 780 DIYLLDDPLSAVDAhVGKHifnKVLGPNGLLKGKTRLLV---THSMHFLPQVDEIVVLGNGTIVEKG------SYSALLA 850
Cdd:PRK13635 160 DIIILDEATSMLDP-RGRR---EVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGtpeeifKSGHMLQ 235
|
250 260
....*....|....*....|
gi 767961632 851 KKG---EFAKNLKTFLRHTG 867
Cdd:PRK13635 236 EIGldvPFSVKLKELLKRNG 255
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
649-793 |
7.31e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.70 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI--KGTTAYVPQQSWIQNGTIKDNILF---GT 723
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAE 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 EFNEKRYQQVLEACAlLPDLEmlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:COG4178 454 AFSDAELREALEAVG-LGHLA----ERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
654-841 |
8.84e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.07 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISA---MLGEMENVH--GHITIKGTTAY---------------VPQQSwiqN- 712
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPGARveGEILLDGEDIYdpdvdvvelrrrvgmVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 --GTIKDNILFGtefnekryqqvleacalLPDLEMLPGGDLAEIGEK------------------GINLSGGQKQRISLA 772
Cdd:COG1117 104 fpKSIYDNVAYG-----------------LRLHGIKSKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 773 RATYQNLDIYLLDDPLSAVD----AHVGKHIFNkvlgpnglLKGK-TRLLVTHSMHflpQV----DEIVVLGNGTIVE 841
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDpistAKIEELILE--------LKKDyTIVIVTHNMQ---QAarvsDYTAFFYLGELVE 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
655-854 |
9.00e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI-KGTT-AYVPQ-QSWIQNGTIKDNILFGtefNEKRYQ 731
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRiGYLPQePPLDDDLTVLDTVLDG---DAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 732 QVLEACALLPDLEMlPGGDLAEIGEK-----------------------GI----------NLSGGQKQRISLARATYQN 778
Cdd:COG0488 92 LEAELEELEAKLAE-PDEDLERLAELqeefealggweaearaeeilsglGFpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 779 LDIYLLDDP-----LSAVD---AHVGKHifnkvlgPNGLlkgktrLLVTHSMHFLPQV-DEIVVLGNGTIVE-KGSYSAL 848
Cdd:COG0488 171 PDLLLLDEPtnhldLESIEwleEFLKNY-------PGTV------LVVSHDRYFLDRVaTRILELDRGKLTLyPGNYSAY 237
|
....*.
gi 767961632 849 LAKKGE 854
Cdd:COG0488 238 LEQRAE 243
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
656-794 |
9.83e-15 |
|
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: 74.23 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSL---ISAMLGEMENVHGHITIKG----------TTAYVPQQS-WIQNGTIKDNILF 721
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDDiLLPGLTVRETLTY 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 722 -----GTEFNEKRYQQVLEACALLPDLEMLP-GGDLAEigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 794
Cdd:cd03234 105 tailrLPRKSSDAIRKKRVEDVLLRDLALTRiGGNLVK------GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
656-843 |
1.21e-14 |
|
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: 73.68 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---TTAYV---PQQSWIQNG------TIKDNILFG- 722
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPadrPVSMLFQENnlfahlTVEQNVGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 723 ------TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVG 796
Cdd:cd03298 96 spglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767961632 797 KHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQVDE-IVVLGNGTIVEKG 843
Cdd:cd03298 165 AEMLDLVLDLHA-ETKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
643-850 |
2.22e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 74.10 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------------------- 700
Cdd:COG4167 19 GLFRRQQFEA-VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdykyrckhirmifqdpn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 701 TAYVPQQswiQNGTIKDNIL-FGTEFNEK-RYQQV---LEACALLPDLemlpggdlAEIGekgIN-LSGGQKQRISLARA 774
Cdd:COG4167 98 TSLNPRL---NIGQILEEPLrLNTDLTAEeREERIfatLRLVGLLPEH--------ANFY---PHmLSSGQKQRVALARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 775 TYQNLDIYLLDDPLSAVDAHVGKHIFNKvlgpngLLKGKTRL-----LVTHSM----HFlpqVDEIVVLGNGTIVEKGSY 845
Cdd:COG4167 164 LILQPKIIIADEALAALDMSVRSQIINL------MLELQEKLgisyiYVSQHLgivkHI---SDKVLVMHQGEVVEYGKT 234
|
....*
gi 767961632 846 SALLA 850
Cdd:COG4167 235 AEVFA 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
654-850 |
2.71e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 73.48 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVPQqswiqnG------ 713
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitglpphriarlgiGYVPE------Grrifps 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 -TIKDNILFG--TEFNEKRYQQVLE-ACALLPDL-EML--PGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:COG0410 93 lTVEENLLLGayARRDRAEVRADLErVYELFPRLkERRrqRAG----------TLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 787 P---LSAVdahVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG0410 163 PslgLAPL---IVEEIFEIIRRLNR--EGVTILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLA 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
658-850 |
2.85e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.08 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 658 NLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSWI-----QNG-----TIKDNILFG--- 722
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVsmlfqENNlfshlTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 723 ----TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 798
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 799 IFNkvlgpngLL------KGKTRLLVTHS----MHFLPQVdeiVVLGNGTIVEKGSYSALLA 850
Cdd:PRK10771 168 MLT-------LVsqvcqeRQLTLLMVSHSledaARIAPRS---LVVADGRIAWDGPTDELLS 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
654-873 |
3.25e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.66 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAYVPQQSWIQ---------------NG 713
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPDVDPVEvrrrigmvfqkpnpfPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 TIKDNILFGTEFN------EKRYQQVLEACALLPDLEmlpggdlAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PRK14243 106 SIYDNIAYGARINgykgdmDELVERSLRQAALWDEVK-------DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 788 LSAVDAHVGKHIFNKVlgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLakkGEFAKNLKTFlrhTG 867
Cdd:PRK14243 179 CSALDPISTLRIEELM---HELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYL---VEFDRTEKIF---NS 249
|
....*.
gi 767961632 868 PEEEAT 873
Cdd:PRK14243 250 PQQQAT 255
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
654-850 |
3.88e-14 |
|
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: 72.85 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSW-------------IQNGTIKDN 718
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdiTGLPPHEIArlgigrtfqiprlFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 719 ILFGTEFNEKRYQ-----------------QVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDI 781
Cdd:cd03219 96 VMVAAQARTGSGLllararreereareraeELLERVGLADLADRPAG-----------ELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961632 782 YLLDDP---LSAVDAHVGKHIFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:cd03219 165 LLLDEPaagLNPEETEELAELIRELRE-----RGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRN 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
649-844 |
4.79e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.98 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-TTAYVPQ---------QSW--IQNGTIK 716
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAenrhvntvfQSYalFPHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 717 DNILFGTEF----NEKRYQQVLEAcallpdLEMLPGGDLAEigEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:PRK09452 105 ENVAFGLRMqktpAAEITPRVMEA------LRMVQLEEFAQ--RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 793 AHVGKHIFNKvlgpnglLK------GKTRLLVTH------SMHflpqvDEIVVLGNGTIVEKGS 844
Cdd:PRK09452 177 YKLRKQMQNE-------LKalqrklGITFVFVTHdqeealTMS-----DRIVVMRDGRIEQDGT 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
656-865 |
5.49e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAM--LGEMEN----VHGhITIKGTTA----------YVPQQSWI-QNGTIKDN 718
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDG-LKVNDPKVderlirqeagMVFQQFYLfPHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 719 ILFGTEFNEKRYQQVLEACALlpdlEMLPGGDLAE-IGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVgK 797
Cdd:PRK09493 98 VMFGPLRVRGASKEEAEKQAR----ELLAKVGLAErAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL-R 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 798 HIFNKV---LGPNGLlkgkTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAKKGefAKNLKTFLRH 865
Cdd:PRK09493 173 HEVLKVmqdLAEEGM----TMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIKNPP--SQRLQEFLQH 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
654-844 |
5.66e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.88 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQS-----WiqngTI 715
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSslsfpF----TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNILFGTE---FNEKRYQQVLEACALLPDLEMLPGGDLAEigekginLSGGQKQRISLARA----TYQNLD--IYLLDD 786
Cdd:PRK13548 94 EEVVAMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqlWEPDGPprWLLLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 787 PLSAVD-AHvgKHIfnkVLgpnGLLKGKTR---LLVTHSMHFLPQV----DEIVVLGNGTIVEKGS 844
Cdd:PRK13548 167 PTSALDlAH--QHH---VL---RLARQLAHergLAVIVVLHDLNLAaryaDRIVLLHQGRLVADGT 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
632-843 |
6.15e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 632 NFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI-------------TIK 698
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 699 GTTAYVPQQSWIQ--NGTIKDNILFGTEFNEKRYQQVLEACA-LLPDLEMLPGGDlaeigEKGINLSGGQKQRISLARAT 775
Cdd:PRK13648 83 KHIGIVFQNPDNQfvGSIVKYDVAFGLENHAVPYDEMHRRVSeALKQVDMLERAD-----YEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 776 YQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKG 843
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKS-EHNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
637-865 |
6.99e-14 |
|
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: 72.96 E-value: 6.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLgEMENVHGHITIKGTT-------------AY 703
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwnsvplqkwrkafGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 704 VPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 784 LDDPLSAVDAhVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEF------AK 857
Cdd:cd03289 162 LDEPSAHLDP-ITYQVIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFkqaispSD 238
|
....*...
gi 767961632 858 NLKTFLRH 865
Cdd:cd03289 239 RLKLFPRR 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
654-852 |
7.16e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA--------YVPQQSwiqnGtiKDNILF---- 721
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPELT----G--RENIYLngrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 -GteFNEKRYQQVLEACAllpdlemlpggDLAEIGEKgINL-----SGGQKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:COG1134 116 lG--LSRKEIDEKFDEIV-----------EFAELGDF-IDQpvktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 796 GKHIFNKVlgpNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS-------YSALLAKK 852
Cdd:COG1134 182 QKKCLARI---RELREsGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDpeeviaaYEALLAGR 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
637-852 |
1.39e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.12 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWE----HDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT----------- 701
Cdd:PRK13646 3 IRFDNVSYTYQkgtpYEHQA-IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 702 ------AYVPQ--QSWIQNGTIKDNILFGTE-FNEKRYQQVLEACALLPDLemlpgGDLAEIGEKG-INLSGGQKQRISL 771
Cdd:PRK13646 82 pvrkriGMVFQfpESQLFEDTVEREIIFGPKnFKMNLDEVKNYAHRLLMDL-----GFSRDVMSQSpFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 772 ARATYQNLDIYLLDDPLSAVDAHvGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 767961632 851 KK 852
Cdd:PRK13646 236 DK 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
654-851 |
1.82e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkGTT---AYVPQQswiQ-----NGTIKDNIlfgTEF 725
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETvkiGYFDQH---QeeldpDKTVLDEL---RDG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 726 NEKRYQQvlEACALLPDLeMLPGGD-LAEIGekgiNLSGGQKQRISLARATYQNLDIYLLDDP-----LSAVDAhvgkhi 799
Cdd:COG0488 404 APGGTEQ--EVRGYLGRF-LFSGDDaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA------ 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 800 fnkvLgpNGLL---KGkTRLLVTHSMHFLPQV-DEIVVLGNGTIVEK-GSYSALLAK 851
Cdd:COG0488 471 ----L--EEALddfPG-TVLLVSHDRYFLDRVaTRILEFEDGGVREYpGGYDDYLEK 520
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
445-792 |
2.12e-13 |
|
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: 74.56 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 445 VLQIVLSIFFLWRELGPSV-LAGVGVMVLVIPINAILSTKSKtiQVKNMKNkDKRLKIMNEI---LSGIKILKYFAWEPS 520
Cdd:TIGR01271 1009 LTLIVLGAIFVVSVLQPYIfIAAIPVAVIFIMLRAYFLRTSQ--QLKQLES-EARSPIFSHLitsLKGLWTIRAFGRQSY 1085
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 521 FrdqvQNLRKKELK----------NLLAFSQLQCVVIFV-FQLTPVLVSVVTFSV------YVLVDSNNILDA-QKAF-T 581
Cdd:TIGR01271 1086 F----ETLFHKALNlhtanwflylSTLRWFQMRIDIIFVfFFIAVTFIAIGTNQDgegevgIILTLAMNILSTlQWAVnS 1161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 582 SITLFNILRfPLSMLPMMISSMLQASVSTERLEKYLGGDDL--DTSAIRHDCNFDKAMQFSEASFTWEHDSEATVRDVNL 659
Cdd:TIGR01271 1162 SIDVDGLMR-SVSRVFKFIDLPQEEPRPSGGGGKYQLSTVLviENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSF 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 660 DIMAGQLVAVIGPVGSGKSSLISAMLgEMENVHGHITIKGTT-------------AYVPQQSWIQNGTIKDNILFGTEFN 726
Cdd:TIGR01271 1241 SVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSwnsvtlqtwrkafGVIPQKVFIFSGTFRKNLDPYEQWS 1319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 727 EKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:TIGR01271 1320 DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
654-792 |
4.54e-13 |
|
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: 69.49 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------------TAYVPQQSWI-QNGTIKDN 718
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIfRKLTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 719 ILFGTEFNEKRYQQVLE-ACALLPDLemlpggDLAEI-GEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:cd03218 96 ILAVLEIRGLSKKEREEkLEELLEEF------HITHLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
649-792 |
5.36e-13 |
|
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: 67.95 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI--KGTTAYVPQQSWIQNGTIKDNILFgtefn 726
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGTLREQLIY----- 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 727 ekryqqvleacallpdlemlPGGDlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:cd03223 87 --------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
654-844 |
7.31e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.99 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQ---------------SWIQNGTIK 716
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdlTALSEKElrkarrqigmifqhfNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 717 DNILFGTEFN----EKRYQQVLEacaLLpdlemlpggDLAEIGEKG----INLSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:PRK11153 101 DNVALPLELAgtpkAEIKARVTE---LL---------ELVGLSDKAdrypAQLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961632 789 SAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK11153 169 SALDPATTRSILE-------LLKdinrelGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGT 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
637-820 |
7.48e-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: 68.59 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------TAYVPQQ 707
Cdd:cd03292 1 IEFINVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 708 --------SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGG--DLAEigekgiNLSGGQKQRISLARATYQ 777
Cdd:cd03292 80 igvvfqdfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKhrALPA------ELSGGEQQRVAIARAIVN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767961632 778 NLDIYLLDDPLSAVDAHVGKHIFNKVLGPNglLKGKTRLLVTH 820
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKIN--KAGTTVVVATH 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
654-844 |
9.63e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-------------AYVPQQSWIQNG-TIKDNI 719
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarrlALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 720 LFG-----------TEFNEKRYQQVLEACallpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PRK11231 98 AYGrspwlslwgrlSAEDNARVNQAMEQT------------RINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 788 LSAVDahvgkhiFNKVLGPNGLL-----KGKTRLLVTHSmhfLPQV----DEIVVLGNGTIVEKGS 844
Cdd:PRK11231 166 TTYLD-------INHQVELMRLMrelntQGKTVVTVLHD---LNQAsrycDHLVVLANGHVMAQGT 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
645-845 |
1.20e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.63 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-AYVPQ---------QSW--IQN 712
Cdd:PRK11607 26 TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlSHVPPyqrpinmmfQSYalFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 GTIKDNILFGTEFNEKRYQQVLEACAllpdlEMLPGGDLAEI-GEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAV 791
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 792 DAHVGKHIFNKVLgpnGLLK--GKTRLLVTHSmhflpQVDEIVVLGNGTIVEKGSY 845
Cdd:PRK11607 181 DKKLRDRMQLEVV---DILErvGVTCVMVTHD-----QEEAMTMAGRIAIMNRGKF 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
638-838 |
1.46e-12 |
|
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: 65.93 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 638 QFSEASFTWEhdSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--AYVPQqswiqngti 715
Cdd:cd03221 2 ELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVkiGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 kdnilfgtefnekryqqvleacallpdlemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDahv 795
Cdd:cd03221 71 ---------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD--- 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767961632 796 gkhIFNKVLGPNGLLK-GKTRLLVTHSMHFLPQV-DEIVVLGNGT 838
Cdd:cd03221 103 ---LESIEALEEALKEyPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
656-858 |
1.73e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.89 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayvpqqswIQNG---------------------- 713
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERV--------ITAGkknkklkplrkkvgivfqfpeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 -----TIKDNILFG-------TEFNEKRYQQVLEACALLPD-LEMLPggdlaeigekgINLSGGQKQRISLARATYQNLD 780
Cdd:PRK13634 97 qlfeeTVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEElLARSP-----------FELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 781 IYLLDDPLSAVDAHVGKHI---FNKVLGPNGLlkgkTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLAKKGEFA 856
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMmemFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELE 241
|
..
gi 767961632 857 KN 858
Cdd:PRK13634 242 AI 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
655-841 |
1.76e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKgttayVPQQSWIQNGTIKDNILFGTEFNEKRYqqVL 734
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDAVE--LL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 735 EACALlpdlemlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD---AHVGKHIFNKVLGPngllK 811
Cdd:COG2401 120 NAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARR----A 186
|
170 180 190
....*....|....*....|....*....|..
gi 767961632 812 GKTRLLVTHSMHFLP--QVDEIVVLGNGTIVE 841
Cdd:COG2401 187 GITLVVATHHYDVIDdlQPDLLIFVGYGGVPE 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
657-868 |
2.19e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.31 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQSWIQNGTIKDNILFGT 723
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfglmdlrkVLGIIPQAPVLFSGTVRFNLDPFN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 EFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAV----DAHVGKHI 799
Cdd:PLN03130 1338 EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVdvrtDALIQKTI 1417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 800 FNKvlgpnglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGE-FAKnlktFLRHTGP 868
Cdd:PLN03130 1418 REE-------FKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSaFSK----MVQSTGA 1476
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
655-793 |
2.28e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI--------TIKGTTAYVPQQS----WiqnGTIKDNILFG 722
Cdd:PRK11247 29 NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaEAREDTRLMFQDArllpW---KKVIDNVGLG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 723 TEFN-EKRYQQVLEACALlpdlemlpgGDLAeiGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:PRK11247 106 LKGQwRDAALQALAAVGL---------ADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-843 |
2.38e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAmLGEMENVHGHITIKGTTAYVPQQSWIQNGTI------- 715
Cdd:PRK14258 12 NLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 -----KDNIlfgteFNEKRYQQVLEACALL---PDLEM-------LPGGDL-----AEIGEKGINLSGGQKQRISLARAT 775
Cdd:PRK14258 91 smvhpKPNL-----FPMSVYDNVAYGVKIVgwrPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 776 YQNLDIYLLDDPLSAVDAHVGKHIfnKVLGPNGLLKGK-TRLLVTHSMHFLPQVDEIVVL--GN----GTIVEKG 843
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKV--ESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFfkGNenriGQLVEFG 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
655-841 |
2.44e-12 |
|
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: 67.46 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVpQQSW--IQNGTI 715
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlfaldedararlrarhvGFV-FQSFqlLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNI-----LFGTEFNEKRYQQVLEACALLPDLEMLPGGdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:COG4181 108 LENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 791 VDAHVGKHIFnkvlgpnGLL------KGKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 841
Cdd:COG4181 177 LDAATGEQII-------DLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
654-853 |
2.63e-12 |
|
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: 66.78 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEM--ENVHGHITIKGttayvpqqswiqngtikDNILFgTEFNEKryq 731
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-----------------EDITD-LPPEER--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 732 qvleacALL---------PDLEMLPGGD-LAEIGEkgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFN 801
Cdd:cd03217 75 ------ARLgiflafqypPEIPGVKNADfLRYVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 802 KVlgpNGLL-KGKTRLLVTHSMHFLPQV--DEIVVLGNGTIVEKGSYSAL--LAKKG 853
Cdd:cd03217 146 VI---NKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKELAleIEKKG 199
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
648-844 |
2.81e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.80 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 648 HDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG----TTAY--------VPQQSwiqNG-- 713
Cdd:COG4604 11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvaTTPSrelakrlaILRQE---NHin 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 ---TIKDNILFGtefnekRY------------QQVLEACALLpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQ 777
Cdd:COG4604 88 srlTVRELVAFG------RFpyskgrltaedrEIIDEAIAYL---------DLEDLADRYLDeLSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 778 NLDIYLLDDPLSAVDAHVGKHIFnkvlgpnGLLK------GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGS 844
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMM-------KLLRrladelGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGT 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
654-843 |
3.27e-12 |
|
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: 66.42 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVH--GHITIKGT----------TAYVPQqswiqngtikDNILF 721
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRpldkrsfrkiIGYVPQ----------DDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 GTefnekryQQVLEAcallpdLEMlpggdLAEIgeKGInlSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFn 801
Cdd:cd03213 95 PT-------LTVRET------LMF-----AAKL--RGL--SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767961632 802 kvlgpnGLLK-----GKTRLLVTH----SMHFLpqVDEIVVLGNGTIVEKG 843
Cdd:cd03213 152 ------SLLRrladtGRTIICSIHqpssEIFEL--FDKLLLLSQGRVIYFG 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
655-843 |
3.82e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-YVPQ---------QSWI--QNGTIKDNILFG 722
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMnDVPPaergvgmvfQSYAlyPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 723 TEFN-------EKRYQQVLEACALLPDLEMLPGGdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA-- 793
Cdd:PRK11000 100 LKLAgakkeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAal 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 794 HVGKHI----FNKVLgpngllkGKTRLLVTHSmhflpQV------DEIVVLGNGTIVEKG 843
Cdd:PRK11000 169 RVQMRIeisrLHKRL-------GRTMIYVTHD-----QVeamtlaDKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
656-844 |
4.08e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.77 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------------TAYVPQQSWIQ--NGTIKDN 718
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVditdkkvklsdirkkVGLVFQYPEYQlfEETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 719 ILFGT----EFNEKRYQQVLEACALLpdlemlpGGDLAEIGEKG-INLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA 793
Cdd:PRK13637 105 IAFGPinlgLSEEEIENRVKRAMNIV-------GLDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 794 HVGKHIFNKVlgpnGLLKGK---TRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGS 844
Cdd:PRK13637 178 KGRDEILNKI----KELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
654-843 |
5.21e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.79 E-value: 5.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAYVPQQSWIQ----------------N 712
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 GTIKDNILFGTEFN---------EKRYQQVLEACALLPDLEmlpggdlAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:PRK14267 100 LTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEVK-------DRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767961632 784 LDDPLSAVDAhVGKHIFNKVLGPngLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:PRK14267 173 MDEPTANIDP-VGTAKIEELLFE--LKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVG 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
656-834 |
5.26e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQSWIQ-----------NGTIKDNILFG 722
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdiSTLKPEIYRQQvsycaqtptlfGDTVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 723 TEFnekRYQQVLEAcALLPDLEM--LPggdlAEIGEKGIN-LSGGQKQRISLARatyqNLD----IYLLDDPLSAVDAHv 795
Cdd:PRK10247 105 WQI---RNQQPDPA-IFLDDLERfaLP----DTILTKNIAeLSGGEKQRISLIR----NLQfmpkVLLLDEITSALDES- 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 767961632 796 GKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVL 834
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
654-849 |
6.01e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.71 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-------------TAYVPQQSWIQ-NGTIKDNI 719
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLSfEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 720 LFGTEFNEKRYQQVLEACALLPDlEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHvgkH 798
Cdd:PRK09536 99 EMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN---H 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767961632 799 IFNKVLGPNGLLK-GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALL 849
Cdd:PRK09536 175 QVRTLELVRRLVDdGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
642-849 |
8.42e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.55 E-value: 8.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 642 ASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttAYVPQQSWI----------- 710
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLararigvvpqf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 711 ----QNGTIKDNIL-FGTEFNEKRYQqvLEAcaLLPDLEmlpggDLAEIGEKG----INLSGGQKQRISLARATYQNLDI 781
Cdd:PRK13536 123 dnldLEFTVRENLLvFGRYFGMSTRE--IEA--VIPSLL-----EFARLESKAdarvSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 782 YLLDDPLSAVDAHVGKHIFNKVLGPngLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALL 849
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSL--LARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
649-844 |
1.02e-11 |
|
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: 65.47 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEM-------ENVHGH------ITIKGTTAYVPQQSWIQNG-T 714
Cdd:cd03265 12 DFEA-VRGVSFRVRRGEIFGLLGPNGAGKTTTIK-MLTTLlkptsgrATVAGHdvvrepREVRRRIGIVFQDLSVDDElT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNI-----LFGTEfNEKRYQQVLEACALLpdlemlpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:cd03265 90 GWENLyiharLYGVP-GAERRERIDELLDFV---------GLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 789 SAVDAHVGKHIFNKVlgpNGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:cd03265 160 IGLDPQTRAHVWEYI---EKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGT 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
649-850 |
1.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTA-----------------YVPQQSWIQ 711
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqgirklvgivfQNPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 712 NgTIKDNILFGTEfnekryqqvlEACalLPDLEMLPGGD--LAEIG-EK-----GINLSGGQKQRISLARATYQNLDIYL 783
Cdd:PRK13644 93 R-TVEEDLAFGPE----------NLC--LPPIEIRKRVDraLAEIGlEKyrhrsPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 784 LDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
632-850 |
1.17e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 632 NFDKAMQFSEASFTWEHdSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------ 699
Cdd:PRK15112 9 NLSKTFRYRTGWFRRQT-VEA-VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 700 ----------TTAYVPQQ--SWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDlemlpggdlaEIGEKGINLSGGQKQ 767
Cdd:PRK15112 87 qrirmifqdpSTSLNPRQriSQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPD----------HASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 768 RISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYS 846
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQE-KQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTA 235
|
....
gi 767961632 847 ALLA 850
Cdd:PRK15112 236 DVLA 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
634-860 |
1.43e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.91 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 634 DKAMQFSEASFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQN- 712
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 --------------GTIKDNILFGTEFNEKRYQQVLEACAllpdlEMLPGGDLAEIGEKG-INLSGGQKQRISLARATYQ 777
Cdd:PRK13647 81 vglvfqdpddqvfsSTVWDDVAFGPVNMGLDKDEVERRVE-----EALKAVRMWDFRDKPpYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 778 NLDIYLLDDPLSAVDAHvGKHIFNKVLgpNGLLK-GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLAKKGEF 855
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPR-GQETLMEIL--DRLHNqGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
....*
gi 767961632 856 AKNLK 860
Cdd:PRK13647 233 QAGLR 237
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
704-860 |
1.72e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 704 VPQQSWIQNGTIKDNILFGTEfnEKRYQQVLEAC---ALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLD 780
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKE--DATREDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 781 IYLLDDPLSAVDAHVGKHIFNKVLGpnglLKGK---TRLLVTHSMHFLPQVDEIVVLGN----GTIVE-KGSYSALL-AK 851
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVD----IKDKadkTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLsVQ 1454
|
....*....
gi 767961632 852 KGEFAKNLK 860
Cdd:PTZ00265 1455 DGVYKKYVK 1463
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
643-844 |
1.94e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 65.48 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI----------QN 712
Cdd:PRK13639 8 KYSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevrktvgivfQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 G-------TIKDNILFG-------TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQN 778
Cdd:PRK13639 87 PddqlfapTVEEDVAFGplnlglsKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 779 LDIYLLDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSMHFLP-QVDEIVVLGNGTIVEKGS 844
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNK--EGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
654-801 |
2.75e-11 |
|
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: 67.47 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENVHG---HITIKGTTAYVPQQSWIQNGTIKDNILF---GTEFNE 727
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYpdsSEDMKR 546
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 728 KRY-QQVLEACALLPDLEML--PGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFN 801
Cdd:TIGR00954 547 RGLsDKDLEQILDNVQLTHIleREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
654-850 |
2.86e-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: 65.84 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG---EMENVHGHITIKGT-----------------TAYVPQQS----- 708
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdllklsekelrkirgreIQMIFQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 709 --WiqngTIKDNI-----LFGTEFNEKRYQQVLEAcallpdLEMLpggdlaeigekGIN------------LSGGQKQRI 769
Cdd:COG0444 101 pvM----TVGDQIaeplrIHGGLSKAEARERAIEL------LERV-----------GLPdperrldrypheLSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 770 SLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEK 842
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILN-------LLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEE 232
|
....*...
gi 767961632 843 GSYSALLA 850
Cdd:COG0444 233 GPVEELFE 240
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
657-844 |
2.89e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLI---SAMLGEMENVHGHITIKGTT------------------AYVPQQ-SWIQNGT 714
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTvqregrlardirksrantGYIFQQfNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFG------------TEFNEKRYQQVLEAcallpdlemLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDI 781
Cdd:PRK09984 103 VLENVLIGalgstpfwrtcfSWFTREQKQRALQA---------LTRVGMVHFAHQRVStLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 782 YLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHF-LPQVDEIVVLGNGTIVEKGS 844
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQ-NDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGS 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
632-864 |
3.28e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 66.21 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 632 NFDKAMQFSEASFTWEHDSEAT-----VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttayvpq 706
Cdd:PRK10070 17 HPQRAFKYIEQGLSKEQILEKTglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 707 qswIQNGTIKDNILfgTEFNEKRYQQVLEACALLPDLEMLP----GGDLAEIG-----EKGIN----------------- 760
Cdd:PRK10070 90 ---VDIAKISDAEL--REVRRKKIAMVFQSFALMPHMTVLDntafGMELAGINaeerrEKALDalrqvglenyahsypde 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 761 LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGpnglLKGKTRLLVTHSMHFLPQV----DEIVVLGN 836
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVK----LQAKHQRTIVFISHDLDEAmrigDRIAIMQN 240
|
250 260
....*....|....*....|....*...
gi 767961632 837 GTIVEKGSYSALLAKKGEfaKNLKTFLR 864
Cdd:PRK10070 241 GEVVQVGTPDEILNNPAN--DYVRTFFR 266
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
647-850 |
6.74e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.83 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 647 EHDseaTVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAY----------VPQQSWIQNGTIK 716
Cdd:PRK10619 17 EHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 717 DNILFgTEFNEKRYQQVLEACALLPdLEMLP-----------------GGDLAEIGEKGINLSGGQKQRISLARATYQNL 779
Cdd:PRK10619 94 LTMVF-QHFNLWSHMTVLENVMEAP-IQVLGlskqeareravkylakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 780 DIYLLDDPLSAVDAH-VGK--HIFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK10619 172 EVLLFDEPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
654-792 |
6.79e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.51 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TA------------YVPQQSWI-QNGTIKDN 718
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdiTHlpmhkrarlgigYLPQEASIfRKLTVEDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 719 I---LFGTEFNEKRYQQVLEAcaLLPDLemlpggDLAEIGE-KGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:COG1137 99 IlavLELRKLSKKEREERLEE--LLEEF------GITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
643-860 |
7.48e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 63.67 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT---------------------- 700
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyqldrkqrrafrrdvqlvfq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 701 ---TAYVPQQS--WIQNGTIKDNILFGTEFNEKRYQQVLEACALLPD-LEMLPGgdlaeigekgiNLSGGQKQRISLARA 774
Cdd:TIGR02769 96 dspSAVNPRMTvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEdADKLPR-----------QLSGGQLQRINIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 775 TYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSA 847
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILE-------LLRklqqafGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQ 237
|
250
....*....|...
gi 767961632 848 LLAKKGEFAKNLK 860
Cdd:TIGR02769 238 LLSFKHPAGRNLQ 250
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
656-865 |
7.85e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAM-LGEMENvHGHITIKGT-------------------TAYVPQQS--WiQNG 713
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQYnlW-PHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 TIKDNIL------FGTEFNE--KRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:PRK11124 98 TVQQNLIeapcrvLGLSKDQalARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 786 DPLSAVDAHVGKHIFN--KVLGPNGLlkgkTRLLVTHSMHFLPQVDEIVV-LGNGTIVEKGSYSALLAKKGEfakNLKTF 862
Cdd:PRK11124 167 EPTAALDPEITAQIVSiiRELAETGI----TQVIVTHEVEVARKTASRVVyMENGHIVEQGDASCFTQPQTE---AFKNY 239
|
...
gi 767961632 863 LRH 865
Cdd:PRK11124 240 LSH 242
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
655-823 |
8.79e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.57 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-AYVPQQ---SWI----QN---GT-----IKDN 718
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvTKLPEYkraKYIgrvfQDpmmGTapsmtIEEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 719 IL----------FGTEFNEKRYQQVLEACALLpdlemlpggDL-------AEIGekgiNLSGGQKQRISLARATYQNLDI 781
Cdd:COG1101 103 LAlayrrgkrrgLRRGLTKKRRELFRELLATL---------GLglenrldTKVG----LLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767961632 782 YLLDDPLSAVDAHVGKHIF---NKVLGPNGLlkgkTRLLVTHSMH 823
Cdd:COG1101 170 LLLDEHTAALDPKTAALVLeltEKIVEENNL----TTLMVTHNME 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
632-844 |
9.27e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.87 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 632 NFDKAMQFSEASFTWEHDSEATVRDVN---LDIMAGQLVAVIGPVGSGKSSLIS------------AMLGEMENVHGHIT 696
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 697 IK---------GTTAYVPQQSWIQNgTIKDNILFGT----EFNEKRYQQVLEacalLPDLEMLPGgDLAEigEKGINLSG 763
Cdd:PRK13645 82 IKevkrlrkeiGLVFQFPEYQLFQE-TIEKDIAFGPvnlgENKQEAYKKVPE----LLKLVQLPE-DYVK--RSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 764 GQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEK 842
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNK-EYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISI 232
|
..
gi 767961632 843 GS 844
Cdd:PRK13645 233 GS 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
654-843 |
9.56e-11 |
|
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: 62.21 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGqLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------TTAYVPQQ-SWIQNGTIKD--- 717
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfGVYPNFTVREfld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 --NILFGTEFNE--KRYQQVLEACallpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:cd03264 95 yiAWLKGIPSKEvkARVDEVLELV------------NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 793 AhVGKHIFNKVLGpnGLLKGKTRLLVTH-----SMHflpqVDEIVVLGNGTIVEKG 843
Cdd:cd03264 163 P-EERIRFRNLLS--ELGEDRIVILSTHivedvESL----CNQVAVLNKGKLVFEG 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
643-840 |
1.01e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMEN-VHGHITIKGTTA------------------- 702
Cdd:PRK10535 13 SYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQDVatldadalaqlrrehfgfi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 703 -----YVPQQSWIQNGTIKdNILFGTEFNEKRyqqvLEACALLPDLemlpggDLAE-IGEKGINLSGGQKQRISLARATY 776
Cdd:PRK10535 92 fqryhLLSHLTAAQNVEVP-AVYAGLERKQRL----LRAQELLQRL------GLEDrVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 777 QNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK-----GKTRLLVTHSMHFLPQVDEIVVLGNGTIV 840
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMA-------ILHqlrdrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
654-837 |
1.45e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 62.10 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVP---QQSWIQN------GTIKDNILFGT- 723
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNysllpwLTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 ----EFNEKRYQQVLEAcallpDLEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKH 798
Cdd:TIGR01184 81 rvlpDLSKSERRAIVEE-----HIALV---GLTEAADKRPGqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767961632 799 IFNKvlgpngLLK-----GKTRLLVTHSM-HFLPQVDEIVVLGNG 837
Cdd:TIGR01184 153 LQEE------LMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
654-843 |
1.74e-10 |
|
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: 61.53 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG---------TTAYVPQQSWI-QNGTIKDNILFgt 723
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLyPKMKVIDQLVY-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 eFNEKRYQQVLEACALLPD-LEMLpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVD---AHVGKH 798
Cdd:cd03269 94 -LAQLKGLKKEEARRRIDEwLERL---ELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767961632 799 IFNKVLGpngllKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03269 170 VIRELAR-----AGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
645-828 |
1.94e-10 |
|
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: 61.22 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT----TAYVPQQS--WI--QNG--- 713
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeQRDEPHENilYLghLPGlkp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 --TIKDNILFGTEFNEKRYQQVLEACAL--LPDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:TIGR01189 87 elSALENLHFWAAIHGGAQRTIEDALAAvgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 767961632 790 AVDAHvGKHIFNKVLGPNgLLKGKTRLLVTHsmHFLPQV 828
Cdd:TIGR01189 157 ALDKA-GVALLAGLLRAH-LARGGIVLLTTH--QDLGLV 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
654-850 |
2.13e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.90 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------------AYVPQ-QSWIQNGTIKDNIL 720
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvpsrarharqrvGVVPQfDNLDPDFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 -FGTEFNEKRyQQVLEACALLPDLEMLPGGDLAEIGEkginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:PRK13537 103 vFGRYFGLSA-AAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767961632 800 FNKVlgPNGLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK13537 178 WERL--RSLLARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
634-870 |
2.44e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 634 DKAMQFSEASFTWEHDSEAT-VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTaYVPQQSW--- 709
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVNqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL-LTAENVWnlr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 710 ------IQN-------GTIKDNILFGTEfNE--------KRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQR 768
Cdd:PRK13642 81 rkigmvFQNpdnqfvgATVEDDVAFGME-NQgipreemiKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 769 ISLARATYQNLDIYLLDDPLSAVDAhVGKHIFNKVLGPnglLKGK---TRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSY 845
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDP-TGRQEIMRVIHE---IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAP 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 767961632 846 SALLAKKGE---------FAKNLKTFLRHTG---PEE 870
Cdd:PRK13642 225 SELFATSEDmveigldvpFSSNLMKDLRKNGfdlPEK 261
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
656-848 |
2.68e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.41 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAM-----------------------LGEMENVHGHITIKGTT----------- 701
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdtgtiewifkdeknkkkTKEKEKVLEKLVIQKTRfkkikkikeir 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 702 ---AYVPQQSWIQ--NGTIKDNILFG-------TEFNEKRYQQVLEACALlpDLEMLPggdlaeigEKGINLSGGQKQRI 769
Cdd:PRK13651 105 rrvGVVFQFAEYQlfEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQ--------RSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 770 SLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvLGPNGLLKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKG-SYSA 847
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTYDI 252
|
.
gi 767961632 848 L 848
Cdd:PRK13651 253 L 253
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
654-849 |
3.09e-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: 61.64 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHG-HITIKGTT-------------AYV-P--QQSWIQNGTIK 716
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedvwelrkriGLVsPalQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 717 DNIL---FGT-----EFNEkryQQVLEACALLPDLEMlpgGDLAE--IGEkginLSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:COG1119 99 DVVLsgfFDSiglyrEPTD---EQRERARELLELLGL---AHLADrpFGT----LSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 787 PLSAVDAHvGKHIFNKVLgpNGLLK--GKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALL 849
Cdd:COG1119 169 PTAGLDLG-ARELLLALL--DKLAAegAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
652-839 |
3.42e-10 |
|
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: 60.14 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 652 ATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVP----QQSWIQNG 713
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvtrrsprdairagiAYVPedrkREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 TIKDNILfgtefnekryqqvleacalLPDLemlpggdlaeigekginLSGGQKQRISLARATYQNLDIYLLDDPLSAVDa 793
Cdd:cd03215 94 SVAENIA-------------------LSSL-----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767961632 794 hVG--KHIFNKVLgpngLL--KGKTRLLVTHSMHFLPQV-DEIVVLGNGTI 839
Cdd:cd03215 137 -VGakAEIYRLIR----ELadAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
622-841 |
4.51e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 622 LDTSAIRHdcnfdkamQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT- 700
Cdd:PRK10419 4 LNVSGLSH--------HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 701 ------------------------TAYVPQQS--WIqngtIKDNILFGTEFNEK----RYQQVLEACALLP-DLEMLPGg 749
Cdd:PRK10419 76 laklnraqrkafrrdiqmvfqdsiSAVNPRKTvrEI----IREPLRHLLSLDKAerlaRASEMLRAVDLDDsVLDKRPP- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 750 dlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSM- 822
Cdd:PRK10419 151 ----------QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR-------LLKklqqqfGTACLFITHDLr 213
|
250 260
....*....|....*....|..
gi 767961632 823 ---HFLPQVdeiVVLGNGTIVE 841
Cdd:PRK10419 214 lveRFCQRV---MVMDNGQIVE 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
657-850 |
7.62e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--------------TTAYVPQQSWI-QNGTIKDNILF 721
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEENLAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 GTEFNEK-RYQQVLEAC-ALLPDLemlpggdLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:PRK11614 104 GGFFAERdQFQERIKWVyELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767961632 800 FNKVLGPNGllKGKTRLLVTHSMH-FLPQVDEIVVLGNGTIVEKGSYSALLA 850
Cdd:PRK11614 177 FDTIEQLRE--QGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
654-843 |
7.83e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAM-----LGEMENVHGHITIKGTTAY----------------VPQQswIQN 712
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFkmdvielrrrvqmvfqIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 GTIKDNILFGTEFN---------EKRYQQVLEACALLPDLEmlpggdlAEIGEKGINLSGGQKQRISLARATYQNLDIYL 783
Cdd:PRK14247 97 LSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 784 LDDPLSAVDAHVGKHIFNKVLgpnGLLKGKTRLLVThsmHFLPQV----DEIVVLGNGTIVEKG 843
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFL---ELKKDMTIVLVT---HFPQQAarisDYVAFLYKGQIVEWG 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
643-844 |
9.30e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.49 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEAT----VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSW-IQNgtiKD 717
Cdd:PRK13633 11 SYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRN---KA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 NILFGTEFNEKRYQQVLEACALLPdlEMLpGGDLAEIGE------KGIN-----------LSGGQKQRISLARATYQNLD 780
Cdd:PRK13633 88 GMVFQNPDNQIVATIVEEDVAFGP--ENL-GIPPEEIRErvdeslKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 781 IYLLDDPLSAVDAHVGKHIFNKVLGPNGLlKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKK-YGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
655-841 |
1.01e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.96 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGemenVH----GHITIKGTT--------------AYVPQQ-SWIQNGTI 715
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSG----VYqpdsGEILLDGEPvrfrsprdaqaagiAIIHQElNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNILFGTE------FNEKR-YQQVLEACALLpDLEMLPGgdlAEIGEkginLSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:COG1129 97 AENIFLGREprrgglIDWRAmRRRARELLARL-GLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 789 SAVDAHVGKHIFNKVLGpnglLK--GKTRLLVThsmHFLPQV----DEIVVLGNGTIVE 841
Cdd:COG1129 169 ASLTEREVERLFRIIRR----LKaqGVAIIYIS---HRLDEVfeiaDRVTVLRDGRLVG 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
654-850 |
1.01e-09 |
|
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: 60.05 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQswI---------QNG------TIK 716
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRdiTGLPPHR--IarlgiartfQNPrlfpelTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 717 DNIL-----------FGTEFNEKRYQ-----------QVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARA 774
Cdd:COG0411 98 ENVLvaaharlgrglLAALLRLPRARreereareraeELLERVGLADRADEPAG-----------NLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 775 tyqnL----DIYLLDDP---LSAVDAHVGKHIFNKVLGPNGLlkgkTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYS 846
Cdd:COG0411 167 ----LatepKLLLLDEPaagLNPEETEELAELIRRLRDERGI----TILLIEHDMDLVMGLaDRIVVLDFGRVIAEGTPA 238
|
....
gi 767961632 847 ALLA 850
Cdd:COG0411 239 EVRA 242
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
654-823 |
1.10e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.83 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTayVPQQSWIQNGTIKDNIL-FGTEFNEkryqq 732
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP--MSKLSSAAKAELRNQKLgFIYQFHH----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 733 vleacaLLPD---LE-----MLPGGD------------LAEIG-EKGIN-----LSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:PRK11629 98 ------LLPDftaLEnvampLLIGKKkpaeinsralemLAAVGlEHRANhrpseLSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 767961632 787 PLSAVDAHVGKHIFNkVLGPNGLLKGKTRLLVTHSMH 823
Cdd:PRK11629 172 PTGNLDARNADSIFQ-LLGELNRLQGTAFLVVTHDLQ 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
655-852 |
1.21e-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: 61.87 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI-KGTTA-YVPQQSWI-QNGTIKDNILFG--------T 723
Cdd:TIGR03719 22 KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVgYLPQEPQLdPTKTVRENVEEGvaeikdalD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 EFNE-------------------KRYQQVLEACA---LLPDLEM------LPGGDlAEIGekgiNLSGGQKQRISLARAT 775
Cdd:TIGR03719 102 RFNEisakyaepdadfdklaaeqAELQEIIDAADawdLDSQLEIamdalrCPPWD-ADVT----KLSGGERRRVALCRLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 776 YQNLDIYLLDDPLSAVDAH----VGKHIFNkvlgpnglLKGkTRLLVTHSMHFLPQVDE-IVVLGNGT-IVEKGSYSALL 849
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAEsvawLERHLQE--------YPG-TVVAVTHDRYFLDNVAGwILELDRGRgIPWEGNYSSWL 247
|
...
gi 767961632 850 AKK 852
Cdd:TIGR03719 248 EQK 250
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
645-793 |
1.53e-09 |
|
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: 58.66 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI--------QNG--- 713
Cdd:cd03231 7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArgllylghAPGikt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 --TIKDNILFGTEFNEKryQQVLEAcallpdlemlpggdLAEIGEKGI------NLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:cd03231 87 tlSVLENLRFWHADHSD--EQVEEA--------------LARVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILD 150
|
....*...
gi 767961632 786 DPLSAVDA 793
Cdd:cd03231 151 EPTTALDK 158
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
654-850 |
1.65e-09 |
|
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: 61.24 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENVHGHITIKGT-------TAYVPQQSWIQ------NG------T 714
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdldglsrRALRPLRRRMQvvfqdpFGslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNI-----LFGTEFNEK-RYQQVLEAcallpdlemlpggdLAEIG-----------EkginLSGGQKQRISLARATYQ 777
Cdd:COG4172 381 VGQIIaeglrVHGPGLSAAeRRARVAEA--------------LEEVGldpaarhryphE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 778 NLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA 850
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILD-------LLRdlqrehGLAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
644-843 |
2.74e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.50 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 644 FTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttaYVPqqsWIQNGTIKDNI--LF 721
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVP---WKRRKKFLRRIgvVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 722 GT---------------------EFNEKRYQQVLEACAllpdlEMLpggDLAEIGEKGI-NLSGGQKQRISLARATYQNL 779
Cdd:cd03267 101 GQktqlwwdlpvidsfyllaaiyDLPPARFKKRLDELS-----ELL---DLEELLDTPVrQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 780 DIYLLDDPLSAVDAHVGKHIFNKVLGPNGlLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNR-ERGTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
654-843 |
4.68e-09 |
|
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: 57.38 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-TTAYVPQQSWIQNG------------TIKDNIL 720
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLGfvsdstglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 -FGTEFNEKRYQQVLEACALLPDLEMlpgGDLAEIGEKGinLSGGQKQRISLARATYQNLDIYLLDDPLSAVDahvgkhi 799
Cdd:cd03266 101 yFAGLYGLKGDELTARLEELADRLGM---EELLDRRVGG--FSTGMRQKVAIARALVHDPPVLLLDEPTTGLD------- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767961632 800 fnkVLGPNGLLK--------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKG 843
Cdd:cd03266 169 ---VMATRALREfirqlralGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
654-840 |
5.05e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVP----QQSWIQNGTI 715
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPvrirsprdairagiAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNIL---------FGTEFNEKRYQQVLEACALL----PDLEmlpggdlAEIGekgiNLSGGQKQRISLARATYQNLDIY 782
Cdd:COG1129 348 RENITlasldrlsrGGLLDRRRERALAEEYIKRLriktPSPE-------QPVG----NLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 783 LLDDPLSAVDahVG-KH-IFNKVlgpNGLLK-GKTRLLVTHSmhfLPQV----DEIVVLGNGTIV 840
Cdd:COG1129 417 ILDEPTRGID--VGaKAeIYRLI---RELAAeGKAVIVISSE---LPELlglsDRILVMREGRIV 473
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
637-846 |
5.43e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEHDSEATVR---DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-TTAYVPQQSWIQN 712
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 GTIKDNILFgtEFNEKRY--QQVLEACALLPD----------------LEMLpgGDLAEIGEKG-INLSGGQKQRISLAR 773
Cdd:PRK13643 82 VRKKVGVVF--QFPESQLfeETVLKDVAFGPQnfgipkekaekiaaekLEMV--GLADEFWEKSpFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 774 ATYQNLDIYLLDDPLSAVDAHVGKHIFNkvLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYS 846
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
654-792 |
5.44e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.60 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITI--------------KGTTAYVPQQSWI-QNGTIKDN 718
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 719 ILFGTEFNE--KRYQQVLEACALLPDLEMLPGGDlaeigEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:PRK10895 99 LMAVLQIRDdlSAEQREDRANELMEEFHIEHLRD-----SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
654-844 |
8.24e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--TTAY-----------VPQQSWIQNGTIKDNIl 720
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGreIGAYglrelrrqfsmIPQDPVLFDGTVRQNV- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 fgTEFNEKRYQQV---LEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSA-VDAHVG 796
Cdd:PTZ00243 1405 --DPFLEASSAEVwaaLELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEATAnIDPALD 1482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767961632 797 KHIFNKVLGPnglLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:PTZ00243 1483 RQIQATVMSA---FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
649-844 |
1.22e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYV--------------------PQQS 708
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFgkdifqidaiklrkevgmvfQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 709 WIQNGTIKDNILFGTE---FNEKR-YQQVLEACallpdleMLPGGDLAEIGEK----GINLSGGQKQRISLARATYQNLD 780
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKshgIKEKReIKKIVEEC-------LRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 781 IYLLDDPLSAVDAhVGKHIFNKVLgpNGLLKGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK14246 174 VLLMDEPTSMIDI-VNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGS 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
575-841 |
1.71e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 575 DAQKAFT-SITLFnILRFPL-SM---LPMMISsmlqASVSTERLEKY-LGGD--DLDTSAIRHDCnfdKAMQFSEASFTW 646
Cdd:PRK10522 261 DTNVAATySLTLL-FLRTPLlSAvgaLPTLLS----AQVAFNKLNKLaLAPYkaEFPRPQAFPDW---QTLELRNVTFAY 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 647 eHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLisAML--GEMENVHGHITIKGTT-------AYVPQQSWIqngtIKD 717
Cdd:PRK10522 333 -QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTL--AMLltGLYQPQSGEILLDGKPvtaeqpeDYRKLFSAV----FTD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 718 NILF-------GTEFNEKRYQQVLEACALLPDLEmLPGGDLAEIgekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:PRK10522 406 FHLFdqllgpeGKPANPALVEKWLERLKMAHKLE-LEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767961632 791 VDAHVgKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 841
Cdd:PRK10522 480 QDPHF-RREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
654-836 |
2.04e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.49 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------------TTAYVPQQSWI-QNGTIKDNIL 720
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 FGTEFNEKRYQQV-LEACALLPDLemlpgGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:TIGR01257 1026 FYAQLKGRSWEEAqLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|....*..
gi 767961632 800 FNKVLgpnGLLKGKTRLLVTHSMhflpqvDEIVVLGN 836
Cdd:TIGR01257 1101 WDLLL---KYRSGRTIIMSTHHM------DEADLLGD 1128
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
643-889 |
2.54e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEA-TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTtAYVPQQSW---------IQN 712
Cdd:PRK13650 11 TFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 -------GTIKDNILFGTEFNEKRYQQ----VLEAcallpdLEMLPGGDLAEigEKGINLSGGQKQRISLARATYQNLDI 781
Cdd:PRK13650 90 pdnqfvgATVEDDVAFGLENKGIPHEEmkerVNEA------LELVGMQDFKE--REPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 782 YLLDDPLSAVDahvgkhifnkvlgPNGLLK------------GKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALL 849
Cdd:PRK13650 162 IILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767961632 850 AKKGE---------FAKNLKTFLRHTGPEEEATVHDGSEEEDDDYGLIS 889
Cdd:PRK13650 229 SRGNDllqlgldipFTTSLVQSLRQNGYDLPEGYLTEKELEEQLWELIS 277
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
664-844 |
3.35e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.36 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 664 GQLVAVIGPVGSGKSSLISAMLGEMEN---VHGHITIKGT----------TAYVPQQS-WIQNGTIKDNILFGTEFNEKR 729
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMpidakemraiSAYVQQDDlFIPTLTVREHLMFQAHLRMPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 730 Y----QQVLEACALLPDLEMLPGGDLAeIGEKGI--NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFnKV 803
Cdd:TIGR00955 131 RvtkkEKRERVDEVLQALGLRKCANTR-IGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV-QV 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767961632 804 LgpNGL-LKGKTRLLVTH--SMHFLPQVDEIVVLGNGTIVEKGS 844
Cdd:TIGR00955 209 L--KGLaQKGKTIICTIHqpSSELFELFDKIILMAEGRVAYLGS 250
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
660-864 |
7.47e-08 |
|
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: 54.34 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 660 DIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-AYVPQQ-SWIQNGTIKDnILFGT--EFNEKRYQQVle 735
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvSYKPQYiKADYEGTVRD-LLSSItkDFYTHPYFKT-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 736 acallpdlEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVDA----HVGKHIFNKVLGPNgll 810
Cdd:cd03237 98 --------EIAKPLQIEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAENNE--- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 811 kgKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYS---ALLAKKGEFAKNLK-TFLR 864
Cdd:cd03237 167 --KTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANppqSLRSGMNRFLKNLDiTFRR 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
661-790 |
9.23e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 661 IMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQqsWI---QNGTIKDNILF-GTEFNEKRYQQvlea 736
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLLRSiTDDLGSSYYKS---- 435
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 737 callpdlEMLPGGDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPlSA 790
Cdd:PRK13409 436 -------EIIKPLQLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
656-792 |
9.59e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.27 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-----------------AYVPQQSWI-QNGTIKD 717
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVRG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 718 NILFG-TEFNEKRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARATYQNLDIYLLDDPLSAVD 792
Cdd:PRK11144 96 NLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
645-862 |
1.11e-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: 55.58 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG--EMENVHG----HITIKGTTAYVPQQS---------- 708
Cdd:TIGR03269 7 TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGriiyHVALCEKCGYVERPSkvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 709 ----------WIQNGTIKDN------ILFGTEF----NEKRYQQVLEAcalLPDLE------MLPGGDLAE-------IG 755
Cdd:TIGR03269 87 gtlepeevdfWNLSDKLRRRirkriaIMLQRTFalygDDTVLDNVLEA---LEEIGyegkeaVGRAVDLIEmvqlshrIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 756 EKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLgpNGLLKGKTRLLVTHsmHFlPQV-----DE 830
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASGISMVLTS--HW-PEViedlsDK 238
|
250 260 270
....*....|....*....|....*....|..
gi 767961632 831 IVVLGNGTIVEKGSYSALLAKKGEFAKNLKTF 862
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVFMEGVSEVEKE 270
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
657-844 |
1.22e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLISAML-------GEMEnVHGHITIKGTTA-------Y-VPQQSWI-QNGTIKDNIL 720
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAgivppdsGTLE-IGGNPCARLTPAkahqlgiYlVPQEPLLfPNLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 721 FG---TEFNEKRYQQVLEA--CALlpDLEMLPGgdLAEIGEkginlsggqKQRISLARATYQNLDIYLLDDPLSAVDAHV 795
Cdd:PRK15439 109 FGlpkRQASMQKMKQLLAAlgCQL--DLDSSAG--SLEVAD---------RQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767961632 796 GKHIFNKVlgpNGLL-KGKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK15439 176 TERLFSRI---RELLaQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGK 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
643-844 |
1.44e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG--TTAYVPQQS------WIQNGT 714
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehIQHYASKEVarriglLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFGTEFNEKRY-QQVLEACALLPDLEMLPGG----DLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPL 788
Cdd:PRK10253 92 TPGDITVQELVARGRYpHQPLFTRWRKEDEEAVTKAmqatGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 789 SAVDahVGKHI-FNKVLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGS 844
Cdd:PRK10253 172 TWLD--ISHQIdLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGA 227
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
654-844 |
1.47e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.77 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAML---------GEMENVHGHITIKGTTAY----VPQQSWIQNGT------ 714
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhLKKEQPGNHDRIEGLEHIdkviVIDQSPIGRTPrsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 ---IKDNI--LF-----GTEFN----EKRYQ-----QVL-----EACALLPD-------LEMLP--GGDLAEIGEKGINL 761
Cdd:cd03271 91 ytgVFDEIreLFcevckGKRYNretlEVRYKgksiaDVLdmtveEALEFFENipkiarkLQTLCdvGLGYIKLGQPATTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 762 SGGQKQRISLA-----RATYQNLdiYLLDDPLSAVDAHVGKHIFNkVLgpNGLL-KGKTRLLVTHSMHFLPQVDEIVVLG 835
Cdd:cd03271 171 SGGEAQRIKLAkelskRSTGKTL--YILDEPTTGLHFHDVKKLLE-VL--QRLVdKGNTVVVIEHNLDVIKCADWIIDLG 245
|
250
....*....|....*
gi 767961632 836 ------NGTIVEKGS 844
Cdd:cd03271 246 peggdgGGQVVASGT 260
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
655-794 |
1.59e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------AYVPQQSWI--QNGtIKD------NIL 720
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdEYHQDLLYLghQPG-IKTeltaleNLR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 721 F----GTEFNEKRYQQVLEACALLpDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAH 794
Cdd:PRK13538 97 FyqrlHGPGDDEALWEALAQVGLA-GFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
656-852 |
1.60e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.06 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAyVPQQSwiqNGTIKD-----NILFgtEFNEkry 730
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETG---NKNLKKlrkkvSLVF--QFPE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 731 QQVLEAcALLPDLEMLP---GGDLAEIGEKGI------------------NLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:PRK13641 96 AQLFEN-TVLKDVEFGPknfGFSEDEAKEKALkwlkkvglsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 790 AVDAHVGKHIFNkvLGPNGLLKGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALLAKK 852
Cdd:PRK13641 175 GLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
655-792 |
2.32e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--------------TAYVPQqswiqnG------- 713
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmadarhrravcprIAYMPQ------Glgknlyp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 --TIKDNI-----LFG---TEfNEKRYQQVLEACALLPDLEMlPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYL 783
Cdd:NF033858 92 tlSVFENLdffgrLFGqdaAE-RRRRIDELLRATGLAPFADR-PAG----------KLSGGMKQKLGLCCALIHDPDLLI 159
|
....*....
gi 767961632 784 LDDPLSAVD 792
Cdd:NF033858 160 LDEPTTGVD 168
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
645-793 |
2.70e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.69 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 645 TWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISaMLGEMENV-HGHITIKGTT-----------AYV-------P 705
Cdd:PRK11650 12 SYDGKTQV-IKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERItSGEIWIGGRVvnelepadrdiAMVfqnyalyP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 706 QQSWIQN--------GTIKDNIlfgtefnEKRyqqVLEACALLpdlemlpggdlaEIGE----KGINLSGGQKQRISLAR 773
Cdd:PRK11650 90 HMSVRENmayglkirGMPKAEI-------EER---VAEAARIL------------ELEPlldrKPRELSGGQRQRVAMGR 147
|
170 180
....*....|....*....|
gi 767961632 774 ATYQNLDIYLLDDPLSAVDA 793
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDA 167
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
651-851 |
3.57e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.04 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 651 EATVR---DVNLDIMAGQLVAVIGPVGSGKSSLiSAMLGEMEN-VHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFN 726
Cdd:PRK11308 25 ERLVKaldGVSFTLERGKTLAVVGESGCGKSTL-ARLLTMIETpTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 727 ----EKRYQQVLEAcALLPD------------LEMLpggdlAEIGEKGIN-------LSGGQKQRISLARATYQNLDIYL 783
Cdd:PRK11308 104 slnpRKKVGQILEE-PLLINtslsaaerrekaLAMM-----AKVGLRPEHydryphmFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 784 LDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAK 851
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLN-------LMMdlqqelGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
654-848 |
3.82e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------TTAYVPQQSWIQ------------NGT 714
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlsPGKLQALRRDIQfifqdpyasldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNI--------LFGTEFNEKRYQQVLEACALLPDLEM-LPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:PRK10261 420 VGDSImeplrvhgLLPGKAAAARVAWLLERVGLLPEHAWrYPH-----------EFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961632 786 DPLSAVDAHVGKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQVD-EIVVLGNGTIVEKGSYSAL 848
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAV 551
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
645-828 |
4.46e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 645 TWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWI-----------QNG 713
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFmaylghlpglkADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 TIKDNILFGTEFNEKRYQQvleacallpdlemLPGGDLAEIGEKGI------NLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQ-------------MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767961632 788 LSAVDAHvGKHIFNKVLGPNgLLKGKTRLLVTHSMHFLPQV 828
Cdd:PRK13543 165 YANLDLE-GITLVNRMISAH-LRGGGAALVTTHGAYAAPPV 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
656-844 |
4.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.93 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIK----------GTTAYVPQQSWIQN------------- 712
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKIKNfkelrrrvsmvfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 --------GTIKDNILFG-------TEFNEKRYQQVLEACALLPD-LEMLPGGdlaeigekginLSGGQKQRISLARATY 776
Cdd:PRK13631 124 fpeyqlfkDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 777 QNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGllKGKTRLLVTHSM-HFLPQVDEIVVLGNGTIVEKGS 844
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
663-849 |
6.85e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.71 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 663 AGQLVAVIGPVGSGKSSLISaMLGEMEN-VHGHITIKGTT-------------AYVPQQSWIQNG-TIKDNILFGT---- 723
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLK-MLGRHQPpSEGEILLDAQPleswsskafarkvAYLPQQLPAAEGmTVRELVAIGRypwh 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 ----EFNEKRYQQVLEACALLpdlemlpggDLAEIGEKGIN-LSGGQKQRISLARATYQNLDIYLLDDPLSAVD-AHVgk 797
Cdd:PRK10575 115 galgRFGAADREKVEEAISLV---------GLKPLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQ-- 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 798 hifNKVLGPNGLL---KGKTRLLVTHSMHFLPQ-VDEIVVLGNGTIVEKGSYSALL 849
Cdd:PRK10575 184 ---VDVLALVHRLsqeRGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
325-612 |
8.37e-07 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 51.63 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 325 SFLLKLVNDIFTFVSPQLLKLLISF---ASDRDTYLWIGYL---CAILLFTAALIQSFClqcyfqlCFKLGVKVRTAIMA 398
Cdd:cd18548 4 APLFKLLEVLLELLLPTLMADIIDEgiaNGDLSYILRTGLLmllLALLGLIAGILAGYF-------AAKASQGFGRDLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 399 SVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTN-FMHMLWSSVLQIVLSIFFLWR---ELGPSVLAGVGVMVLVI 474
Cdd:cd18548 77 DLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMmLLRMLVRAPIMLIGAIIMAFRinpKLALILLVAIPILALVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 475 pinAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEP----SFRDQVQNLRKKELKNLLAFSQLQCVVIFVF 550
Cdd:cd18548 157 ---FLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDyeeeRFDKANDDLTDTSLKAGRLMALLNPLMMLIM 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961632 551 QLTpvLVSVVTFSVYvLVDSNNILDAQ-KAFTSItLFNILrFPLSMLPMMISSMLQASVSTER 612
Cdd:cd18548 234 NLA--IVAILWFGGH-LINAGSLQVGDlVAFINY-LMQIL-MSLMMLSMVFVMLPRASASAKR 291
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
649-854 |
1.29e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLG--EMENVHGHITIKGT--TAYVPQ-----------QSWIQNG 713
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKdlLELSPEdragegifmafQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 TIKDNILFGTEFNEKRYQQvleacallpDLEMLPGGDLAEIGEKGINL----------------SGGQKQRISLARATYQ 777
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSYR---------GQEPLDRFDFQDLMEEKIALlkmpedlltrsvnvgfSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 778 NLDIYLLDDPLSAVDAHVGKHIFNkvlGPNGLLKGK-TRLLVTHSMHFLPQV--DEIVVLGNGTIVEKGSYSalLAKKGE 854
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVAD---GVNSLRDGKrSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSGDFT--LVKQLE 237
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
657-792 |
1.37e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 50.61 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGeMENVHGHITIKGTT-------------AYVPQQS----------WIQng 713
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPlsdwsaaelarhrAYLSQQQsppfampvfqYLA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 714 tikdniLFG-----TEFNEKRYQQVLEACALLPDLemlpggdlaeigEKGIN-LSGGQKQRISLARATYQ-----NLD-- 780
Cdd:COG4138 92 ------LHQpagasSEAVEQLLAQLAEALGLEDKL------------SRPLTqLSGGEWQRVRLAAVLLQvwptiNPEgq 153
|
170
....*....|..
gi 767961632 781 IYLLDDPLSAVD 792
Cdd:COG4138 154 LLLLDEPMNSLD 165
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
660-853 |
1.81e-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: 49.11 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 660 DIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT-AYVPQQswiqngtikdnilfgtefnekryqqvleaca 738
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITpVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 739 llpdlemlpggdlaeigekgINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA----HVGKHIfnKVLGPNGllkGKT 814
Cdd:cd03222 70 --------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAI--RRLSEEG---KKT 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 767961632 815 RLLVTHSMHFLPQVDEIVVLGNGtivEKGSYSALLAKKG 853
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEG---EPGVYGIASQPKG 160
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
643-844 |
2.63e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.19 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 643 SFTWEHDSEAtVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG-------------TTAYVPQQS- 708
Cdd:PRK13652 10 CYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQNPd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 709 -WIQNGTIKDNILFG-------TEFNEKRYQQVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLD 780
Cdd:PRK13652 89 dQIFSPTVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961632 781 IYLLDDPLSAVDAHVGKHIFNKVlgpNGLLK--GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFL---NDLPEtyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGT 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
654-848 |
2.82e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT--TAYVPQQ-----SWIQ------------NGT 714
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdlLGMKDDEwravrSDIQmifqdplaslnpRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNI----------LFGTEFNEkRYQQVLEACALLPDLemlpggdlaeigekgIN-----LSGGQKQRISLARATYQNL 779
Cdd:PRK15079 117 IGEIIaeplrtyhpkLSRQEVKD-RVKAMMLKVGLLPNL---------------INrypheFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 780 DIYLLDDPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSAL 848
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVN-------LLQqlqremGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
325-613 |
2.98e-06 |
|
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: 50.12 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 325 SFLLKLVNDIFTFVSPQLLKLLI-SFASDRDT-YLWIgylCAILLFTAALIQSFC--LQCYF--QLCFKLGVKVRTAIma 398
Cdd:cd18542 4 AILALLLATALNLLIPLLIRRIIdSVIGGGLReLLWL---LALLILGVALLRGVFryLQGYLaeKASQKVAYDLRNDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 399 svYKKaltLSNLARKEYTVGETVNLMS-----VDAqklmdVTNFMHM----LWSSVLQIVLSIFFL----WRelgpsvLA 465
Cdd:cd18542 79 --YDH---LQRLSFSFHDKARTGDLMSrctsdVDT-----IRRFLAFglveLVRAVLLFIGALIIMfsinWK------LT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 466 GVgvMVLVIPINAILSTK-SKTIQvKNMKNKDKRLKIMN----EILSGIKILKYFAWEPS----FRDQVQNLRKKELKNL 536
Cdd:cd18542 143 LI--SLAIIPFIALFSYVfFKKVR-PAFEEIREQEGELNtvlqENLTGVRVVKAFAREDYeiekFDKENEEYRDLNIKLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 537 LAFSQLQCVVIFVFQLTPVLVSVV--------TFSVYVLVdsnnildaqkAFTSitLFNILRFPLSMLPMMISSMLQASV 608
Cdd:cd18542 220 KLLAKYWPLMDFLSGLQIVLVLWVggylvingEITLGELV----------AFIS--YLWMLIWPVRQLGRLINDMSRASA 287
|
....*
gi 767961632 609 STERL 613
Cdd:cd18542 288 SAERI 292
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
657-841 |
3.17e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.39 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAY------------------------VPQQSWIQN 712
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeearaklrakhvgfvfqsfmlIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 GTIKdNILFGTEFNEKRYQ--QVLEACALLPDLEMLPGgdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:PRK10584 109 VELP-ALLRGESSRQSRNGakALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767961632 791 VDAHVGKHIFNKVLGPNGLLkGKTRLLVTHSMHFLPQVDEIVVLGNGTIVE 841
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREH-GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
660-833 |
3.42e-06 |
|
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: 50.94 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 660 DIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQ-SWIQNGTIKDNI--LFGTEFNEKRYQQvlea 736
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYiSPDYDGTVEEFLrsANTDDFGSSYYKT---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 737 callpdlEMLPGGDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLSAVDA----HVGKHIFNKVLGpngllK 811
Cdd:COG1245 438 -------EIIKPLGLEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFAEN-----R 505
|
170 180
....*....|....*....|...
gi 767961632 812 GKTRLLVTHSMHFLPQV-DEIVV 833
Cdd:COG1245 506 GKTAMVVDHDIYLIDYIsDRLMV 528
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
637-839 |
4.26e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 637 MQFSEASFTWEhDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI--TIKGTTAyVPQQSWIQNGT 714
Cdd:PLN03073 509 ISFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMA-VFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFgteFNEKRYQQVLEAC--ALLPDLEMlpGGDLAEigEKGINLSGGQKQRISLARATYQNLDIYLLDDP----- 787
Cdd:PLN03073 587 LSSNPLL---YMMRCFPGVPEQKlrAHLGSFGV--TGNLAL--QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPsnhld 659
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767961632 788 LSAVDAhvgkHIFNKVLGPNGLlkgktrLLVTHSMHFLP-QVDEIVVLGNGTI 839
Cdd:PLN03073 660 LDAVEA----LIQGLVLFQGGV------LMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
754-846 |
7.64e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 754 IGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDaHVGKHIFNKVLgpNGLLKGKTR--LLVTHSMHFLPQVDEI 831
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTI--NNLKGNENRitIIIAHRLSTIRYANTI 649
|
90
....*....|....*
gi 767961632 832 VVLGNGtivEKGSYS 846
Cdd:PTZ00265 650 FVLSNR---ERGSTV 661
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
649-787 |
9.78e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 649 DSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHI--TIKGTTAYVPQQS------------WI-QNG 713
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQDHaydfendltlfdWMsQWR 409
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961632 714 TIKDNilfgtefnekryQQVLEACallpdL-EMLPGGDlaEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:PRK15064 410 QEGDD------------EQAVRGT-----LgRLLFSQD--DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
608-857 |
1.17e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 608 VSTERLEKYLGGDDLDTSAirhdcnfdKAMqfSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGE 687
Cdd:PRK14271 1 MACERLGGQSGAADVDAAA--------PAM--AAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 688 MENVHGH-----ITIKGTTAY--------------VPQQSWIQNGTIKDNILFGtefnekryqqvLEACALLPDLEM--L 746
Cdd:PRK14271 71 NDKVSGYrysgdVLLGGRSIFnyrdvlefrrrvgmLFQRPNPFPMSIMDNVLAG-----------VRAHKLVPRKEFrgV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 747 PGGDLAEIG----------EKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVlgpNGLLKGKTRL 816
Cdd:PRK14271 140 AQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI---RSLADRLTVI 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767961632 817 LVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLA--KKGEFAK 857
Cdd:PRK14271 217 IVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSspKHAETAR 260
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
654-838 |
1.31e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLgemENVHGHITIKGTTAYVPQ--------QSWIQNGtikdnilfgtef 725
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---YASGKARLISFLPKFSRNklifidqlQFLIDVG------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 726 nekryqqvleacallpdLEMLPggdlaeIGEKGINLSGGQKQRISLARATYQNLD--IYLLDDPLSAVDAHVGKHIFNKV 803
Cdd:cd03238 76 -----------------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 767961632 804 lgpNGLL-KGKTRLLVTHSMHFLPQVDEIVVLGNGT 838
Cdd:cd03238 133 ---KGLIdLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
762-850 |
1.38e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 762 SGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLKG---KTRL---LVTHSMHFLPQV-DEIVVL 834
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILA-------LLKSlqqKHQLaylFISHDLHVVRALcHQVIVL 499
|
90
....*....|....*.
gi 767961632 835 GNGTIVEKGSYSALLA 850
Cdd:PRK15134 500 RQGEVVEQGDCERVFA 515
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
654-900 |
2.08e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 47.41 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT---------AYVPqqswiqngtikdnilfgte 724
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPldpedrrriGYLP------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 725 fnEKR--YQQ--VLEACALLPDLEMLPGGD-------------LAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDD 786
Cdd:COG4152 78 --EERglYPKmkVGEQLVYLARLKGLSKAEakrradewlerlgLGDRANKKVeELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 787 PLSAVDAhVGKHIFNKVlgpngLL----KGKTRLLVTHSMHflpQV----DEIVVLGNGTIVEKGSYSALlakKGEFAKN 858
Cdd:COG4152 156 PFSGLDP-VNVELLKDV-----IRelaaKGTTVIFSSHQME---LVeelcDRIVIINKGRKVLSGSVDEI---RRQFGRN 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767961632 859 lKTFLRHTGPEEEATVHDG--SEEEDDDYGLIssveEIPEDAAS 900
Cdd:COG4152 224 -TLRLEADGDAGWLRALPGvtVVEEDGDGAEL----KLEDGADA 262
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
656-857 |
2.22e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 656 DVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNG-TIKDNI-LFGTEFNEKRyQQV 733
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQlTGIENIeLKGLMMGLTK-EKI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 734 LEacaLLPDLEmlpggDLAEIGeKGIN-----LSGGQKQRISLARATYQNLDIYLLDDPLSavdahVGKHIF-NKVLGPN 807
Cdd:PRK13545 121 KE---IIPEII-----EFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQTFtKKCLDKM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 808 GLLK--GKTRLLVTHSmhfLPQVDEIVV----LGNGTIVEKGSYSALLAKKGEFAK 857
Cdd:PRK13545 187 NEFKeqGKTIFFISHS---LSQVKSFCTkalwLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
654-844 |
6.83e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.88 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGT-TAYVPQQSW------IQ----------NG--T 714
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELrplrrrMQmvfqdpyaslNPrmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 715 IKDNILFGTEFN--------EKRYQQVLEACALLPD-LEMLPGgdlaeigEkginLSGGQKQRISLARATYQNLDIYLLD 785
Cdd:COG4608 114 VGDIIAEPLRIHglaskaerRERVAELLELVGLRPEhADRYPH-------E----FSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 786 DPLSAVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGS 844
Cdd:COG4608 183 EPVSALDVSIQAQVLN-------LLEdlqdelGLTYLFISHDLSVVRHIsDRVAVMYLGKIVEIAP 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
646-822 |
8.44e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.87 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 646 WEHDSEA------TVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKG------TTAYVP-------- 705
Cdd:PRK10908 4 FEHVSKAylggrqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlKNREVPflrrqigm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 706 ---QQSWIQNGTIKDNILF-------GTEFNEKRYQQVLEACALLPDLEMLPggdlaeigekgINLSGGQKQRISLARAT 775
Cdd:PRK10908 84 ifqDHHLLMDRTVYDNVAIpliiagaSGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767961632 776 YQNLDIYLLDDPLSAVDAHVGKHI------FNKVlgpngllkGKTRLLVTHSM 822
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGIlrlfeeFNRV--------GVTVLMATHDI 197
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
654-794 |
9.97e-05 |
|
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: 44.73 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISamlgemenvhghiTIKGTtaYVPQQSWI----QNGTIkdNILFGTEfnekr 729
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLK-------------CIYGN--YLPDSGSIlvrhDGGWV--DLAQASP----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 730 yQQVLE------------------ACALlpDLEMLP----GGDLAEIGEKGINL------------------SGGQKQRI 769
Cdd:COG4778 85 -REILAlrrrtigyvsqflrviprVSAL--DVVAEPllerGVDREEARARARELlarlnlperlwdlppatfSGGEQQRV 161
|
170 180
....*....|....*....|....*
gi 767961632 770 SLARATYQNLDIYLLDDPLSAVDAH 794
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAA 186
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
648-834 |
1.11e-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: 43.50 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 648 HDSEATVRDVNLDimAGQLVAVIGPVGSGKSSLISAM----LGEMENVHGHITIKgTTAYVPQQSwiqngtikdnilfgt 723
Cdd:cd03227 7 FPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILDAIglalGGAQSATRRRSGVK-AGCIVAAVS--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 efnekryqqvLEACALLPdlemlpggdlaeigekgiNLSGGQKQRISLA----RATYQNLDIYLLDDPLSAVDAHVGKHI 799
Cdd:cd03227 69 ----------AELIFTRL------------------QLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 767961632 800 FNKVLgpnGLLKGKTRLLVThsMHFLPQVDEIVVL 834
Cdd:cd03227 121 AEAIL---EHLVKGAQVIVI--THLPELAELADKL 150
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
754-844 |
1.53e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 754 IGEKGINLSGGQKQRISLA-----RATYQNLdiYLLDDPLSAVDAHVGKHIFNkVLGpnGLL-KGKTRLLVTHSMHFLPQ 827
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAkelskRSTGRTL--YILDEPTTGLHFDDIKKLLE-VLQ--RLVdKGNTVVVIEHNLDVIKT 897
|
90 100
....*....|....*....|...
gi 767961632 828 VDEIVVLG------NGTIVEKGS 844
Cdd:TIGR00630 898 ADYIIDLGpeggdgGGTVVASGT 920
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
762-858 |
1.98e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 762 SGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVgkhifnkVLG-PNGLLK-GKTRLLVTHSMHFLPQ-VDEIVVLGNGT 838
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA-------VLWlETYLLKwPKTFIVVSHAREFLNTvVTDILHLHGQK 418
|
90 100
....*....|....*....|.
gi 767961632 839 IVE-KGSYSALLAKKGEFAKN 858
Cdd:PLN03073 419 LVTyKGDYDTFERTREEQLKN 439
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
666-697 |
2.10e-04 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 44.70 E-value: 2.10e-04
10 20 30
....*....|....*....|....*....|....
gi 767961632 666 LVAVIGPVGSGKSSLISAMLGEM-ENVHGHI-TI 697
Cdd:COG2805 127 LVLVTGPTGSGKSTTLAAMIDYInETRAKHIiTI 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
654-787 |
2.48e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.63 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT--------------AYVPQ--QSW--IQNGTI 715
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitglsprerrrlgvAYIPEdrLGRglVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNILFGTEFNEK-------RYQQVLEACA-LLPDLEMLPGGDLAEIGekgiNLSGGQKQRISLARATYQNLDIYLLDDP 787
Cdd:COG3845 354 AENLILGRYRRPPfsrggflDRKAIRAFAEeLIEEFDVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQP 429
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
654-851 |
4.37e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.54 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGttaYVPQQSWIQNgtiKDNI--LFGT-------- 723
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKRRKEF---ARRIgvVFGQrsqlwwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 -------------EFNEKRYQQVLEACAllpdlEMLpggDLAEIGEKGI-NLSGGQKQRISLARATYQNLDIYLLDDPLS 789
Cdd:COG4586 112 paidsfrllkaiyRIPDAEYKKRLDELV-----ELL---DLGELLDTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767961632 790 AVDAHVGKHIFNkvlgpngLLK------GKTRLLVTHSMHFLPQV-DEIVVLGNGTIVEKGSYSALLAK 851
Cdd:COG4586 184 GLDVVSKEAIRE-------FLKeynrerGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
322-612 |
4.43e-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: 43.27 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 322 LLKSFLLKLVNDIFTFVSPQLLKLLI---SFASDRDTYLWIGYLCAILLFTAALIQSFC--LQCYfqLCFKLGVKVRTAI 396
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIddvLIQLGPGGNTSLLLLLVLGLAGAYVLSALLgiLRGR--LLARLGERITADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 397 MASVYKKA--LTLSNLARKEytVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSIFFL----WRelgpsvLAgvgV 469
Cdd:cd18563 79 RRDLYEHLqrLSLSFFDKRQ--TGSLMSRVTSDTDRLQDfLSDGLPDFLTNILMIIGIGVVLfslnWK------LA---L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 470 MVLV-IPINAILSTK-SKTIQVKNMKNKDKRLK---IMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKNLLAFS 540
Cdd:cd18563 148 LVLIpVPLVVWGSYFfWKKIRRLFHRQWRRWSRlnsVLNDTLPGIRVVKAFGQEKReikrFDEANQELLDANIRAEKLWA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 541 QLQCVVIFVFQLTPVLVSVV--------TFSVYVLVdsnnildaqkAFTS-ITLFNilrFPLSMLPMMISSMLQASVSTE 611
Cdd:cd18563 228 TFFPLLTFLTSLGTLIVWYFggrqvlsgTMTLGTLV----------AFLSyLGMFY---GPLQWLSRLNNWITRALTSAE 294
|
.
gi 767961632 612 R 612
Cdd:cd18563 295 R 295
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
321-613 |
4.56e-04 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. 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. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 43.20 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 321 VLLKSFLLKLVNDIFTFVSPQLLKLLIsfasdrDTYLWIG-----YLCAILLFTAALIQSFcLQcYFQ--LCFKLGVKVR 393
Cdd:cd18570 3 LLILILLLSLLITLLGIAGSFFFQILI------DDIIPSGdinllNIISIGLILLYLFQSL-LS-YIRsyLLLKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 394 TAIMASVYKKALTL-----SNlaRKeytVGETVNLMSvDAQKLMD-VTNFMHMLWSSVLQIVLSIFFLWR---ELGPSVL 464
Cdd:cd18570 75 IRLILGYFKHLLKLplsffET--RK---TGEIISRFN-DANKIREaISSTTISLFLDLLMVIISGIILFFynwKLFLITL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 465 AGVGVMVLVIpinAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQC 544
Cdd:cd18570 149 LIIPLYILII---LLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSN 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961632 545 VVIFVFQLTPVLVSVVTF---SVYVLvdsNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18570 226 LQSSIKGLISLIGSLLILwigSYLVI---KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
646-820 |
6.26e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.86 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 646 WEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTT------------AYVPQQSWIQ-N 712
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdlctyqkqlCFVGHRSGINpY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 713 GTIKDNILFGTEFNEKRYQqVLEACAL--LPDLEMLPGGdlaeigekgiNLSGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAVG-ITELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|
gi 767961632 791 VDAHVGKHIFNKVLGPNGllKGKTRLLVTH 820
Cdd:PRK13540 158 LDELSLLTIITKIQEHRA--KGGAVLLTSH 185
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
654-850 |
1.16e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 42.36 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSslISAM-----LGE-MENVHGHITIKGTtayvpqqswiqngtikdNILfgtEFNE 727
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKS--VTALsilrlLPDpAAHPSGSILFDGQ-----------------DLL---GLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 728 KR------------YQ--------------QVLEACAL---LPD-------LEMlpggdLAEIG----EKGIN-----LS 762
Cdd:COG4172 84 RElrrirgnriamiFQepmtslnplhtigkQIAEVLRLhrgLSGaaararaLEL-----LERVGipdpERRLDayphqLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 763 GGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNkvlgpngLLKGKTR------LLVTHSMHFLPQV-DEIVVLG 835
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHDLGVVRRFaDRVAVMR 231
|
250
....*....|....*
gi 767961632 836 NGTIVEKGSYSALLA 850
Cdd:COG4172 232 QGEIVEQGPTAELFA 246
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
654-706 |
1.22e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 1.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767961632 654 VRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIkGT---TAYVPQ 706
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTkleVAYFDQ 389
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
761-850 |
1.39e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.38 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 761 LSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFnkvlgpnGLLK------GKTRLLVTHSMHFLPQV-DEIVV 833
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL-------QLLRelqqelNMGLLFITHNLSIVRKLaDRVAV 229
|
90
....*....|....*..
gi 767961632 834 LGNGTIVEKGSYSALLA 850
Cdd:PRK15134 230 MQNGRCVEQNRAATLFS 246
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
325-613 |
2.32e-03 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 40.87 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 325 SFLLKLVNDIFTFVSPQLLKLLI--SFASDRDTYLWigYLCAILLFTAAL------IQSFCLQcyfqlcfKLGVKVRTAI 396
Cdd:cd18552 4 AILGMILVAATTAALAWLLKPLLddIFVEKDLEALL--LVPLAIIGLFLLrglasyLQTYLMA-------YVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 397 MASVYKKALTLSnLAR-KEYTVGETVNLMSVDAQKLMD-VTNFMHMLWSSVLQIVLSIFFL----WReLgpSVLAGVGVM 470
Cdd:cd18552 75 RNDLFDKLLRLP-LSFfDRNSSGDLISRITNDVNQVQNaLTSALTVLVRDPLTVIGLLGVLfyldWK-L--TLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 471 VLVIPINAI---LSTKSKTIQVK--NMknkdkrLKIMNEILSGIKILKYFAWEPS----FRDQVQNLRKKELKnLLAFSQ 541
Cdd:cd18552 151 LAALPIRRIgkrLRKISRRSQESmgDL------TSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMK-IARARA 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961632 542 LqcvvifvfqLTPV--LVSVVTFSVYVLVDSNNILDAQK---AFTS-ITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18552 224 L---------SSPLmeLLGAIAIALVLWYGGYQVISGELtpgEFISfITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
655-696 |
2.84e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.68 E-value: 2.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767961632 655 RDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHIT 696
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
433-613 |
3.83e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 40.20 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 433 DVTNFMHMLWSSVL----QIVLSIFFLWRELGPSVLAGV-GVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILS 507
Cdd:cd18583 105 SINDLLEQILFQIVpmiiDLVIAIVYLYYLFDPYMGLIVaVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 508 GIKILKYFAWEP----SFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTpvLVSVVTFSVYvlvdsnNILDAQKA---F 580
Cdd:cd18583 185 NWETVKYFNREPyekeRYREAVKNYQKAERKYLFSLNLLNAVQSLILTLG--LLAGCFLAAY------QVSQGQATvgdF 256
|
170 180 190
....*....|....*....|....*....|....
gi 767961632 581 -TSITLFNILRFPLSMLPMMISSMLQASVSTERL 613
Cdd:cd18583 257 vTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
657-793 |
3.86e-03 |
|
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: 40.96 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGemenVHGHITIKGTTAYVPQQ---------------------SWIQNGTI 715
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSG----VYPHGTWDGEIYWSGSPlkasnirdteragiviihqelTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 716 KDNILFGTEFNEKRY-----QQVLEACALLPDLEMLPGGDLAEIGEKGinlsGGQKQRISLARATYQNLDIYLLDDPLSA 790
Cdd:TIGR02633 96 AENIFLGNEITLPGGrmaynAMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSS 171
|
...
gi 767961632 791 VDA 793
Cdd:TIGR02633 172 LTE 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
657-792 |
5.58e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 39.53 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 657 VNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENvHGHITIKGTT-------------AYVPQQSwiqngtikdnilfGT 723
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPleawsaaelarhrAYLSQQQ-------------TP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961632 724 EFNEKRYQ----------QVLEACALLPDL-EMLPGGDLAeigEKGIN-LSGGQKQRISLARATYQ-----NLD--IYLL 784
Cdd:PRK03695 81 PFAMPVFQyltlhqpdktRTEAVASALNEVaEALGLDDKL---GRSVNqLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLL 157
|
....*...
gi 767961632 785 DDPLSAVD 792
Cdd:PRK03695 158 DEPMNSLD 165
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
668-693 |
8.50e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 38.00 E-value: 8.50e-03
10 20 30
....*....|....*....|....*....|
gi 767961632 668 AVIGPVGSGKSSLISAMLGEM----ENVHG 693
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQNvgivSPIPG 30
|
|
| |
