|
Name |
Accession |
Description |
Interval |
E-value |
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
679-907 |
3.91e-150 |
|
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: 443.70 E-value: 3.91e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 679 VQIIGGFFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPDSEGedpsnperet 758
Cdd:cd03290 1 VQVTNGYFSWGS-GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPS---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 759 AADSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRI 838
Cdd:cd03290 70 FEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 907
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
301-610 |
1.55e-147 |
|
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: 440.52 E-value: 1.55e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVA 380
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVSYVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 381 IETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSLRAFAVYT 540
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 541 SISIFMNTAIPIAAVLITFVGHVsFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYP-YLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
224-938 |
1.13e-112 |
|
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: 380.45 E-value: 1.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 224 LLSKGTYWWMNAFIKTAHKKPI---DLRAIGK----LPIAMRALTNYQRLCLAFDAQ------ARKDTQSQQGAR----- 285
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLeesDLWSLNKedtsEMVVPVLVENWKKECKKTRKQpvsavyGKKDPSKPKGSSqldan 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 286 -----------------AIWRALCHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVdhlgkeNHVFQPKTQFLGVYFVSS 348
Cdd:TIGR00957 289 eevealivksphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLI------RFVNDPMAPDWQGYFYTG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 349 QEFLgnayvlavllflALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKImhLSTSNLSMGEMTAGQICNLVAIDTNQL 428
Cdd:TIGR00957 363 LLFV------------CACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKA--LVITNSARKSSTVGEIVNLMSVDAQRF 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 429 MWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKL 508
Cdd:TIGR00957 429 MDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 509 LKLYAWENIFCSRVEKTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVT 588
Cdd:TIGR00957 509 LKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRF 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 589 PLFLLSSVVRSTVKALVSVQKLSEFLSSAEIrEEQCAPREPAPQGQAgkyqavplkvvnrkrpareevrdllgplqrltp 668
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRLRIFLSHEEL-EPDSIERRTIKPGEG--------------------------------- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 669 stdgdadnFCVQIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpdseg 748
Cdd:TIGR00957 635 --------NSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----------- 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 749 edpsnperetaadsdaRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI 828
Cdd:TIGR00957 696 ----------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGV 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 829 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQ--AGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 906
Cdd:TIGR00957 760 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRILVTHGISYLPQVDVIIVMSGG 837
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1958642734 907 TI----------QREGTLKDFQRS------ECQLFEHWKTLMNRQDQE 938
Cdd:TIGR00957 838 KIsemgsyqellQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKE 885
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
679-907 |
9.06e-105 |
|
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: 324.42 E-value: 9.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 679 VQIIGGFFTWTPDGI---PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSlpdsegedpsnpe 755
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 756 retaadsdarsrgpVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQR 835
Cdd:cd03250 68 --------------IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 836 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 907
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
222-916 |
7.63e-104 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 355.97 E-value: 7.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 222 VNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCLAFDAQARKDTQsqqgaraiW--RALCHAFGRRL 299
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKP--------WllRALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 300 VLSSTFRILADLLGFAGPLcifgIVDHLGKENHVFQPKTQ--------FLGVyfvssqeFLGnayvlavllflalllqrT 371
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGPL----LLNLLLESMQNGEPAWIgyiyafsiFVGV-------VLG-----------------V 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 372 FLQASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 450
Cdd:PLN03130 356 LCEAQYFQNVmRVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMV 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 451 LLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEM 530
Cdd:PLN03130 434 LLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDEL 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 531 TSLRAFAVYTSISIFMNTAIPIAAVLITFvGHVSFFKeSDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:PLN03130 514 SWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLG-GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 611 SEFLSsAEirEEQCAPREPAPQGQagkyqavplkvvnrkrPAreevrdllgplqrltpstdgdadnfcVQIIGGFFTWTP 690
Cdd:PLN03130 592 EELLL-AE--ERVLLPNPPLEPGL----------------PA--------------------------ISIKNGYFSWDS 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSgavfwnsslpdsegedpsnperetaaDSDARSRGP 769
Cdd:PLN03130 627 KAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS--------------------------DASVVIRGT 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTN 849
Cdd:PLN03130 681 VAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 850 VVFLDDPFSALDVHLSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEE 825
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
223-943 |
1.18e-103 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 354.67 E-value: 1.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLclafdaQARKDTQSQQGARAIWRALCHAFGRRLVLS 302
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRF------QRCWTEESRRPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 303 STFRILADLLGFAGPLcifgIVDHLGKENHVFQPKtqFLGvYFVSSQEFLGNAYVlavllflalllqrTFLQASYYVAI- 381
Cdd:PLN03232 307 GIFKIGHDLSQFVGPV----ILSHLLQSMQEGDPA--WVG-YVYAFLIFFGVTFG-------------VLCESQYFQNVg 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 382 ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSAL 461
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 462 IGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSLRAFAVYTS 541
Cdd:PLN03232 445 FGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 542 ISIFMNTAIPIAAVLITFvgHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSaeirE 621
Cdd:PLN03232 525 FNSFILNSIPVVVTLVSF--GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLS----E 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 622 EQCAPREPapqgqagkyqavplkvvnrkrpareevrdllgPLQRLTPStdgdadnfcVQIIGGFFTW-TPDGIPTLSNIT 700
Cdd:PLN03232 599 ERILAQNP--------------------------------PLQPGAPA---------ISIKNGYFSWdSKTSKPTLSDIN 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 701 IRIPRGQLTMIVGQVGCGKSSLLLATLGEmqkvsgavfwnssLPDSEgedpsnperetaaDSDARSRGPVAYASQKPWLL 780
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGE-------------LSHAE-------------TSSVVIRGSVAYVPQVSWIF 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 781 NATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSAL 860
Cdd:PLN03232 692 NATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 861 DVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSEcQLFEHWKTLMNRQDQELE 940
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSG-SLFKKLMENAGKMDATQE 848
|
...
gi 1958642734 941 KHT 943
Cdd:PLN03232 849 VNT 851
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
369-920 |
3.14e-87 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 307.09 E-value: 3.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 369 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDT---NQLMWFfflCPNLWAMPVQI 445
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVeriNSFMQY---CMYLWSSPMVL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 446 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKT 525
Cdd:PTZ00243 375 LLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 526 RRKEMTSLRAFAVYTSISIFMNTAIP---IAAVLITF--VGHvsffkesDFSPSVAFASLSLFHILVTPLFLLSSVVRST 600
Cdd:PTZ00243 455 RARELRYLRDVQLARVATSFVNNATPtlmIAVVFTVYylLGH-------ELTPEVVFPTIALLGVLRMPFFMIPWVFTTV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 601 VKALVSVQKLSEFLSS---------------AEIREEQCA--------------------PREPA--------------- 630
Cdd:PTZ00243 528 LQFLVSIKRISTFLECdnatcstvqdmeeywREQREHSTAcqlaavlenvdvtafvpvklPRAPKvktsllsralrmlcc 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 631 PQGQAGKYQAVPLKVVNR------KRPAREEVRDLLGPLQRLTPSTDGDADNFCVQIiGGFFTWTPDGIptLSNITIRIP 704
Cdd:PTZ00243 608 EQCRPTKRHPSPSVVVEDtdygspSSASRHIVEGGTGGGHEATPTSERSAKTPKMKT-DDFFELEPKVL--LRDVSVSVP 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 705 RGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfWNsslpdsegedpsnperetaadsdARSrgpVAYASQKPWLLNATV 784
Cdd:PTZ00243 685 RGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WA-----------------------ERS---IAYVPQQAWIMNATV 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 785 EENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHL 864
Cdd:PTZ00243 738 RGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642734 865 SDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:PTZ00243 818 GERVVEECFLGALAG--KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT 871
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
301-610 |
4.38e-75 |
|
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: 248.55 E-value: 4.38e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENHvfQPKTQ-------FLGVYFVSSqeflgnayvlavllflalllqrTFL 373
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD--EPLSEgyllalaLFLVSLLQS----------------------LLL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 374 QASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLY 453
Cdd:cd18579 57 HQYFFLSFRLGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 454 YILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSL 533
Cdd:cd18579 135 RLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKAL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 534 RAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKEsdFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18579 215 RKFGYLRALNSFLFFSTPVLVSLATFATYVLLGNP--LTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
285-913 |
3.21e-63 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 225.04 E-value: 3.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 285 RAIWRALcHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLGkENHVFQPKTQFLGVYFVSsqeFLGNAyvlavllfl 364
Cdd:COG1132 10 RRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSALLLLLLLLLGL---ALLRA--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 365 alllqrTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFF-FLCPNLWAMPV 443
Cdd:COG1132 76 ------LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 444 QIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FC 519
Cdd:COG1132 148 TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 520 SRVEKTRRKEMTSLRAFAVYTSISIFMNTaipIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRS 599
Cdd:COG1132 228 EANEELRRANLRAARLSALFFPLMELLGN---LGLALVLLVG-GLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 600 TVKALVSVQKLSEFLSsaeireeqcaprepAPQGQAGKYQAVPLKvvnrkrPAREEVRdllgpLQRLTpstdgdadnfcv 679
Cdd:COG1132 304 LQRALASAERIFELLD--------------EPPEIPDPPGAVPLP------PVRGEIE-----FENVS------------ 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 680 qiiggfFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLatLGEMQKVSGAVFWNsslpdseGEDPsnpeRE 757
Cdd:COG1132 347 ------FSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLvnLL--LRFYDPTSGRILID-------GVDI----RD 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 758 TAADSdARSRgpVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGG 833
Cdd:COG1132 407 LTLES-LRRQ--IGVVPQDTFLFSGTIRENIRYGRPdATDEE---VEEAAkaaQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 834 QRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTE-TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
369-610 |
1.82e-61 |
|
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: 210.79 E-value: 1.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 369 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVG 448
Cdd:cd18595 51 QSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 449 VILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRK 528
Cdd:cd18595 129 LYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 529 EMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18595 209 ELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLK 288
|
..
gi 1958642734 609 KL 610
Cdd:cd18595 289 RL 290
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
223-918 |
1.84e-59 |
|
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: 222.86 E-value: 1.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCLAFDaqaRKDTQSQQGARAIwRALCHAFGRRLVLs 302
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWD---RELASAKKNPKLL-NALRRCFFWRFVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 303 stfriladllgfagplciFGIVDHLGKENHVFQPKT--QFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVA 380
Cdd:TIGR01271 85 ------------------YGILLYFGEATKAVQPLLlgRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 381 IETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:TIGR01271 147 HHLGMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSLRAFAvyt 540
Cdd:TIGR01271 225 FCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 541 SISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHIL-VTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEI 619
Cdd:TIGR01271 302 YLRYFYSSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 620 R--EEQCAPREpapqgqagkyqavpLKVVNRKRPAREEVRDLLGPLQ-----RLTPstDGDAdnfcvqiiGGFFT-WTPD 691
Cdd:TIGR01271 382 KtlEYNLTTTE--------------VEMVNVTASWDEGIGELFEKIKqnnkaRKQP--NGDD--------GLFFSnFSLY 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpdsegedpsnperetaadsdaRSRGPVA 771
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---------------------------KHSGRIS 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVV 851
Cdd:TIGR01271 491 FSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLY 570
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 852 FLDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 918
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQ 635
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
371-913 |
9.64e-57 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 209.30 E-value: 9.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 371 TFLQASYYVAIETGINLRgaIQTKIYNKIMHLSTSNL---SMGEMTA-----GQICNLVaidTNQLMWFFFLCPnlwamp 442
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDLASrfrdvESIREFL---TGSLLTALLDLL------ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 443 vQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRV 522
Cdd:COG2274 282 -FVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRW 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 523 EKTRRKEM-TSLRAFAVYTSISIFMNTAIPIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTV 601
Cdd:COG2274 361 ENLLAKYLnARFKLRRLSNLLSTLSGLLQQLATVALLWLG-AYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 602 KALVSVQKLSEFLSsaeireeqcAPREPAPqgqagkyqavplkvvnrkrpareevrdllGPLQRLTPSTDGDadnfcVQI 681
Cdd:COG2274 440 DAKIALERLDDILD---------LPPEREE-----------------------------GRSKLSLPRLKGD-----IEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 682 IGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDpsnperetAAD 761
Cdd:COG2274 477 ENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID-------GID--------LRQ 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 762 SDARS-RGPVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQ 836
Cdd:COG2274 542 IDPASlRRQIGVVLQDVFLFSGTIRENITLGDPdATDEE---IIEAArlaGLHDFIEALPMGYDTVVGEGGSNLSGGQRQ 618
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
372-610 |
3.91e-55 |
|
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: 193.05 E-value: 3.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMT 531
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 532 SLRAFAVYTSISIFMNTAIPIAAVLITFVghVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18597 217 YVRKLQILRSILTAVAFSLPVLASMLSFI--TYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
311-608 |
8.17e-52 |
|
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: 184.24 E-value: 8.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 311 LLGFAGPLCIFGIVDHLgkENHVFQPKTQ--------FLGVyFVSSQeflgnayvlavllflalllqrtFLQASYYVAIE 382
Cdd:cd18596 11 VLSFAPPFFLNRLLRYL--EDPGEDATVRpwvwvlllFLGP-LLSSL----------------------LDQQYLWIGRR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 383 TGINLRGAIQTKIYNKIMHL-----------------STSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQI 445
Cdd:cd18596 66 LSVRLRAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 446 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKT 525
Cdd:cd18596 146 VIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 526 RRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKEsDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALV 605
Cdd:cd18596 226 REEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQ-ELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKV 304
|
...
gi 1958642734 606 SVQ 608
Cdd:cd18596 305 SLD 307
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
445-921 |
2.60e-48 |
|
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: 181.49 E-value: 2.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 445 IIVGVILLYYILGVSALigAAVIILL-AP--------VQYFvATKLSQAQRSTLEysneRLKQT-NEMLRGIKLLKLY-- 512
Cdd:COG4988 143 ALVPLLILVAVFPLDWL--SGLILLVtAPliplfmilVGKG-AAKASRRQWRALA----RLSGHfLDRLRGLTTLKLFgr 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 513 --AWENIFCSRVEKTRRKEMTSLR-AFAVYTSISIFMNTAIPIAAVLITF---VGHVSFFkesdfspsVAFASLslfhIL 586
Cdd:COG4988 216 akAEAERIAEASEDFRKRTMKVLRvAFLSSAVLEFFASLSIALVAVYIGFrllGGSLTLF--------AALFVL----LL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 587 V----TPLFLLSSVVRSTVKALVSVQKLSEFLSsaeireeqcAPREPAPQGQAGKYQAVPLKVvnrkrpareEVRDLLgp 662
Cdd:COG4988 284 ApeffLPLRDLGSFYHARANGIAAAEKIFALLD---------APEPAAPAGTAPLPAAGPPSI---------ELEDVS-- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 663 lqrltpstdgdadnfcvqiiggfFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNss 742
Cdd:COG4988 344 -----------------------FSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-- 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 743 lpdseGEDPSNperetaADSDARSRGpVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQT 821
Cdd:COG4988 398 -----GVDLSD------LDPASWRRQ-IAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDT 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 822 QIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWII 901
Cdd:COG4988 466 PLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRIL 542
|
490 500
....*....|....*....|
gi 1958642734 902 AMKDGTIQREGTLKDFQRSE 921
Cdd:COG4988 543 VLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
372-610 |
4.48e-48 |
|
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: 172.75 E-value: 4.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLStsnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMT 531
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 532 SLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAHVAL--GNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
305-610 |
1.47e-46 |
|
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: 168.50 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 305 FRILADLLGFAGPLCIFGIVDHLgkENHVFQPKTQFL--GVYFVSSqeFLGnayvlavllflalllqrTFLQASY-YVAI 381
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFL--EDSSEPLSDGYLyaLGLVLSS--LLG-----------------ALLSSHYnFQMN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 382 ETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFfflCPNL---WAMPVQIIVGVILLYYILGV 458
Cdd:cd18598 64 KVSLKVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 459 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSLR---- 534
Cdd:cd18598 139 AFLAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKgrky 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 535 --AFAVY--TSISIFMNTaipiaAVLITFV--GHvsffkesDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18598 219 ldALCVYfwATTPVLISI-----LTFATYVlmGN-------TLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLK 286
|
..
gi 1958642734 609 KL 610
Cdd:cd18598 287 RL 288
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
445-913 |
4.59e-43 |
|
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: 166.09 E-value: 4.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 445 IIVGVILLYYILGVSALI---GAAVIILLAPVqyFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLY-AWENiFCS 520
Cdd:COG4987 143 ILAAVAFLAFFSPALALVlalGLLLAGLLLPL--LAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYgALDR-ALA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 521 RVEKTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPS----VAFASLSLFHILVTplflLSSV 596
Cdd:COG4987 220 RLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPllalLVLAALALFEALAP----LPAA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 597 VRSTVKALVSVQKLSEFLSSAeireeqcaPREPAPQGQAGKYQAVPLKVVNrkrpareeVRdllgplqrltpstdgdadn 676
Cdd:COG4987 296 AQHLGRVRAAARRLNELLDAP--------PAVTEPAEPAPAPGGPSLELED--------VS------------------- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 677 fcvqiiggfFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdsegedpsnpER 756
Cdd:COG4987 341 ---------FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG--------------GV 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 757 ETAADSDARSRGPVAYASQKPWLLNATVEENITFESPfNKQRYKM--VIEACSLQPDIDILPHGDQTQIGERGINLSGGQ 834
Cdd:COG4987 398 DLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP-DATDEELwaALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 835 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
692-918 |
3.44e-42 |
|
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: 155.78 E-value: 3.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpdsegedpsnperetaadsdaRSRGPVA 771
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---------------------------KHSGRIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVV 851
Cdd:cd03291 102 FSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 852 FLDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 918
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
686-906 |
5.58e-40 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 145.60 E-value: 5.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPEREtaadsDAR 765
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-------GVDLRDLDLE-----SLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 SRgpVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALY 845
Cdd:cd03228 76 KN--IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642734 846 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 906
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEA-LRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
686-912 |
1.35e-39 |
|
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: 146.20 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSlpDSEGEDPSnperetaadsDAR 765
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT--DIRQLDPA----------DLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 SRgpVAYASQKPWLLNATVEENITFESPF-NKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARAL 844
Cdd:cd03245 78 RN--IGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 912
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
685-913 |
4.90e-39 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 145.07 E-value: 4.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 685 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQkvSGAVFWNsslpdseGEDpsnperetAADS 762
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnLIPRFYDVD--SGRILID-------GHD--------VRDY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 763 DARS-RGPVAYASQKPWLLNATVEENITFESPfNKQRyKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRI 838
Cdd:cd03251 70 TLASlRRQIGLVSQDVFLFNDTVAENIAYGRP-GATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
318-610 |
5.86e-38 |
|
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: 143.93 E-value: 5.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 318 LCIFGIVDHLGKenhVFQPktQFLG---VYFV-SSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQT 393
Cdd:cd18594 2 LGILLFLEESLK---IVQP--LLLGrlvAYFVpDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 394 KIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPV 473
Cdd:cd18594 77 LIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 474 QYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSLR--AFAVYTSISIFMNTAIP 551
Cdd:cd18594 155 QAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRkaAYIRAFNMAFFFFSPTL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 552 IaaVLITFVGHVSFFKESDfsPSVAFASLSLFHILVTPL-FLLSSVVRSTVKALVSVQKL 610
Cdd:cd18594 235 V--SFATFVPYVLTGNTLT--ARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
376-617 |
7.81e-38 |
|
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: 143.52 E-value: 7.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 376 SYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQL-MWFFFLcPNLWAMPVQIIVGVILLYY 454
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 455 ILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSLR 534
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 535 --AFAVYTSISIFMntaipIAAVLITFVGHVSFF-KESDFSPSVAFASLSLFHilvtplfllssVVRSTVKALV--SVQK 609
Cdd:cd18593 217 rtSFLRALNMGLFF-----VSSKLILFLTFLAYIlLGNILTAERVFVTMALYN-----------AVRLTMTLFFpfAIQF 280
|
....*...
gi 1958642734 610 LSEFLSSA 617
Cdd:cd18593 281 GSELSVSI 288
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
692-913 |
6.02e-36 |
|
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: 136.20 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERETAadsdaRSRgpVA 771
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID-------GIDIRDISRKSL-----RSM--IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLLNATVEENITFESPFNKQryKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 848
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKeagAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 849 NVVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03254 159 KILILDEATSNIDTE-TEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
445-913 |
3.78e-35 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 142.16 E-value: 3.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 445 IIVG--VILLYYILGVSAligaaVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTN----EMLRGIKLLKLYAWENIF 518
Cdd:TIGR02203 141 TVIGlfIVLLYYSWQLTL-----IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTtvaeETLQGYRVVKLFGGQAYE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 519 CSRVEKT----RRKEMTSLRAFAVYTSISIFmntaipIAAVLITFVGHVSFFKESDFSPSVA-FASLSLFHILV-TPLFL 592
Cdd:TIGR02203 216 TRRFDAVsnrnRRLAMKMTSAGSISSPITQL------IASLALAVVLFIALFQAQAGSLTAGdFTAFITAMIALiRPLKS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 593 LSSVVRSTVKALVSVQKLSEFLSSAeireeqcaprepaPQGQAGKyqavplKVVNRKRpAREEVRDLLgplqrltpstdg 672
Cdd:TIGR02203 290 LTNVNAPMQRGLAAAESLFTLLDSP-------------PEKDTGT------RAIERAR-GDVEFRNVT------------ 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 673 dadnfcvqiiggfFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEmqkvsgavfwnsslPDS---- 746
Cdd:TIGR02203 338 -------------FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYE--------------PDSgqil 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 747 -EGEDpsnperetAADSDARS-RGPVAYASQKPWLLNATVEENITFESP--FNKQRYKMVIEACSLQPDIDILPHGDQTQ 822
Cdd:TIGR02203 391 lDGHD--------LADYTLASlRRQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTP 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 823 IGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIA 902
Cdd:TIGR02203 463 IGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVV 539
|
490
....*....|.
gi 1958642734 903 MKDGTIQREGT 913
Cdd:TIGR02203 540 MDDGRIVERGT 550
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
299-590 |
7.35e-35 |
|
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: 134.31 E-value: 7.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 299 LVLSSTFRILADLLGFAGPLCIFGIVDHLGKENhvfQPKTQFLGVYFVssqeFLGNAYVLAVLlflalllqrtFLQASYY 378
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDG---DPETQALNVYSL----ALLLLGLAQFI----------LSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 379 VAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGV 458
Cdd:pfam00664 64 LLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 459 S-ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSLRAFA 537
Cdd:pfam00664 142 KlTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 538 VYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPL 590
Cdd:pfam00664 222 VANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
379-913 |
6.67e-34 |
|
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: 137.86 E-value: 6.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 379 VAIETGINLRGAIQTKIYNKIMhlsTSNLSMGEMTAGQICNlvaiDTNQLMWF--------FFLCPnlWaMPVQIIVgVI 450
Cdd:TIGR01842 69 VLVRIGEKLDGALNQPIFAASF---SATLRRGSGDGLQALR----DLDQLRQFltgpglfaFFDAP--W-MPIYLLV-CF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 451 LLYYILGVSALIGAAVIILLAPV-QYFVATKLSQAQrstlEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRK- 528
Cdd:TIGR01842 138 LLHPWIGILALGGAVVLVGLALLnNRATKKPLKEAT----EASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKy 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 529 ----EMTSLRAFAVYTSISIFMNtaipIAAVLITFVG-HVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKA 603
Cdd:TIGR01842 214 lsaqSAASDRAGMLSNLSKYFRI----VLQSLVLGLGaYLAI--DGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 604 LVSVQKLSEFLssAEIREEQCAPREPAPQGQagkyqavpLKVvnrkrparEEVrDLLGPLQRLtpstdgdadnfcvqiig 683
Cdd:TIGR01842 288 RQAYKRLNELL--ANYPSRDPAMPLPEPEGH--------LSV--------ENV-TIVPPGGKK----------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 684 gfftwtpdgiPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpDSEGEDPSNPERETAADSd 763
Cdd:TIGR01842 332 ----------PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV-------RLDGADLKQWDRETFGKH- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 764 arsrgpVAYASQKPWLLNATVEENIT-FESPFNKQRykmVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRIS 839
Cdd:TIGR01842 394 ------IGYLPQDVELFPGTVAENIArFGENADPEK---IIEAAKLagvHELILRLPDGYDTVIGPGGATLSGGQRQRIA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
694-913 |
1.55e-33 |
|
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: 137.19 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnssLpdsEGEDPSNPEREtaadsdarSRGP-VAY 772
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR----L---DGADLSQWDRE--------ELGRhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 773 ASQKPWLLNATVEENIT-FESPfNKQRykmVIEACSLqpdIDI------LPHGDQTQIGERGINLSGGQRQRISVARALY 845
Cdd:COG4618 411 LPQDVELFDGTIAENIArFGDA-DPEK---VVAAAKL---AGVhemilrLPDGYDTRIGEGGARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 846 QHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAA--IRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
690-903 |
3.10e-33 |
|
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: 135.49 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSslpdsegedpsnpeRETAADSDARSRGP 769
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG--------------VPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLNATVEENITFESPFNKQ-RYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 848
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 849 NVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAM 903
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEA-LRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
690-913 |
4.83e-33 |
|
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: 128.04 E-value: 4.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSlllaTLGEMQK----VSGAVFWNsslpdsegedpsnperetaaDSDAR 765
Cdd:cd03249 14 PD-VPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERfydpTSGEILLD--------------------GVDIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 S------RGPVAYASQKPWLLNATVEENITFESPFNKQryKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQ 836
Cdd:cd03249 69 DlnlrwlRSQIGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 837 RISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAE-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
690-913 |
7.73e-33 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 127.35 E-value: 7.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQkvSGAVFWNsslpdseGEDPsnpeRETAADSDARSR 767
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTIlrLLFRFYDVS--SGSILID-------GQDI----REVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 GPVAyasQKPWLLNATVEENITFESP--FNKQrykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 842
Cdd:cd03253 78 GVVP---QDTVLFNDTIGYNIRYGRPdaTDEE----VIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642734 843 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03253 151 AILKNPPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGT 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
686-907 |
1.23e-30 |
|
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: 120.26 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdsegedpsnpERETAADSDAR 765
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD--------------GKDLTKLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 SRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 835
Cdd:cd03225 73 LRRKVGLVFQNPddQFFGPTVEEEVAF-GLENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 836 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 907
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
686-911 |
2.42e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.96 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgeMQKVSGAVFWNsslpdseGEDPSNPEREtaadsd 763
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLrlIAGL--EKPTSGEVLVD-------GKPVTGPGPD------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 764 arsrgpVAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNL 830
Cdd:COG1116 82 ------RGVVFQEpallPWL---TVLDNVALglelrgVPK--AERRERArelLELVGLAGFEDAYPH-----------QL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAMKD-- 905
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDELLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSArp 216
|
....*.
gi 1958642734 906 GTIQRE 911
Cdd:COG1116 217 GRIVEE 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
691-921 |
5.53e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPsnperetaadsdARSRGPV 770
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF-------GKPP------------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRIS 839
Cdd:COG1121 78 GYVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADR-PIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIqREGTLKDFQ 918
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVReYFDRVLLLNRGLV-AHGPPEEVL 226
|
...
gi 1958642734 919 RSE 921
Cdd:COG1121 227 TPE 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
686-921 |
1.13e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 118.36 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEDpsnpereTAADSDAR 765
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVL-------VDGHD-------LALADPAW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 SRGPVAYASQKPWLLNATVEENITFESPFNKQRykMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 842
Cdd:cd03252 74 LRRQVGVVLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 843 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
687-913 |
1.38e-29 |
|
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: 118.61 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 687 TWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSN-PERETAadsdaR 765
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD-------GRDLASlSRRELA-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 SrgpVAYASQK---PWLLnaTVEENI--------TFESPFNKQRYKMVIEACslqpdidilphgDQTQIG---ERGIN-L 830
Cdd:COG1120 76 R---IAYVPQEppaPFGL--TVRELValgryphlGLFGRPSAEDREAVEEAL------------ERTGLEhlaDRPVDeL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVTHKL-QYLPHADWIIAMKD 905
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRLVLLKD 213
|
....*...
gi 1958642734 906 GTIQREGT 913
Cdd:COG1120 214 GRIVAQGP 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
690-917 |
2.74e-29 |
|
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: 116.66 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERetaadSDARSRgp 769
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-------GKDITKKNL-----RELRRK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPW--LLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 839
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEEDVAF-GPENlglpreeiRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGTIQREGTLKDF 917
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
305-610 |
1.15e-28 |
|
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: 116.93 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 305 FRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVS--SQEFLGNAYvlavllflalllqrtflqaSYYVAIe 382
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALaiLQGITVFQY-------------------SMAVSI- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 383 TGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALI 462
Cdd:cd18559 65 GGIFASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 463 GAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSLRAFAVYTSI 542
Cdd:cd18559 143 GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRAL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 543 SIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18559 223 AVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
689-913 |
1.37e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 122.26 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ-----KVSGAVFWNSSLPDSegedpsnperetaadsd 763
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGIELRELDPESW----------------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 764 arsRGPVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 842
Cdd:PRK11174 422 ---RKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642734 843 ALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQA--LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
381-935 |
3.93e-28 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 121.60 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 381 IETGINlrGAIQTKIYNKIMHL--------STSNLSMGEMTAGQICNLVAIDT-NQLMWFFFLCPNLWampvqiivgviL 451
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLG-----------L 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAWENIFCSRVE 523
Cdd:TIGR03797 270 MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 524 KTRRKEM------TSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFkesdfspsVAFASLSlfhilvtplfllsSVV 597
Cdd:TIGR03797 350 LELSAQRienlltVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFN--------TAFGSFS-------------GAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 598 RSTVKALVSVqklseflssaeireeqcaprepapqgqagkYQAVPLkvVNRKRP---AREEVRDLLGPLQRLtpSTDGDA 674
Cdd:TIGR03797 409 TQLSNTLISI------------------------------LAVIPL--WERAKPileALPEVDEAKTDPGKL--SGAIEV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 675 DNFCvqiiggfFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPSnp 754
Cdd:TIGR03797 455 DRVT-------FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFY-------DGQDLA-- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 755 eretAADSDA--RSRGPVAYASQkpwLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSG 832
Cdd:TIGR03797 519 ----GLDVQAvrRQLGVVLQNGR---LMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSG 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 833 GQRQRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 912
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQG 666
|
570 580
....*....|....*....|...
gi 1958642734 913 TLKDFQRSECQLFEhwktLMNRQ 935
Cdd:TIGR03797 667 TYDELMAREGLFAQ----LARRQ 685
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
690-913 |
5.49e-28 |
|
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: 112.97 E-value: 5.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSnpereTAADSDARSRgp 769
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID-------GVDIS-----KIGLHDLRSR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 846
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 847 HTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03244 157 KSKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
696-911 |
5.75e-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: 112.57 E-value: 5.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPEREtaadsdarsrgpVAYASQ 775
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD-------GEPVTGPGPD------------RGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 K----PWLlnaTVEENITFesPFN---------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 842
Cdd:cd03293 81 QdallPWL---TVLDNVAL--GLElqgvpkaeaRERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 843 ALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAM--KDGTIQRE 911
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQ-LQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
696-912 |
1.07e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 110.60 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERETAADSdarsrgpVAYASQ 775
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-------GKDLASLSPKELARK-------IAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 kpwllnatveenitfespfnkqrykmVIEACSLqpdidilphgdqTQIGERGIN-LSGGQRQRISVARALYQHTNVVFLD 854
Cdd:cd03214 81 --------------------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 855 DPFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREG 912
Cdd:cd03214 123 EPTSHLDIA-----HQIELLELLRRLARergkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
389-891 |
4.24e-27 |
|
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: 117.08 E-value: 4.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 389 GAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVA--IDTNQLMWFFFLCPNLWAMPVQIIV--GVILLYYILGVSALIGA 464
Cdd:TIGR02868 86 GALRVRVYERLARQALA--GRRRLRRGDLLGRLGadVDALQDLYVRVIVPAGVALVVGAAAvaAIAVLSVPAALILAAGL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 465 AVIILLAPvqyFVATKLSQAQRSTLEYS-NERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEMTSLRAFAVYTSIS 543
Cdd:TIGR02868 164 LLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 544 IFMNTAIPIAAVLITFVGHVSFFKESDFSPS----VAFASLSLFHilvtPLFLLSSVVRSTVKALVSVQKLSEFLSSAEI 619
Cdd:TIGR02868 241 AALTLLAAGLAVLGALWAGGPAVADGRLAPVtlavLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLDAAGP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 620 REEQCAPREpapqgqagkyQAVPLKVVNRkrpareEVRDLLgplqrltpstdgdadnfcvqiiggfFTWtPDGIPTLSNI 699
Cdd:TIGR02868 317 VAEGSAPAA----------GAVGLGKPTL------ELRDLS-------------------------AGY-PGAPPVLDGV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 700 TIRIPRGQLTMIVGQVGCGKSSLLLATLGemqkvsgavfwnsSLPDSEGEDPSNPERETAADSDARSRgPVAYASQKPWL 779
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAG-------------LLDPLQGEVTLDGVPVSSLDQDEVRR-RVSVCAQDAHL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 780 LNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFS 858
Cdd:TIGR02868 421 FDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTE 500
|
490 500 510
....*....|....*....|....*....|....*
gi 1958642734 859 ALDVHLSDHLmqagiLELLRD--DKRTVVLVTHKL 891
Cdd:TIGR02868 501 HLDAETADEL-----LEDLLAalSGRTVVLITHHL 530
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
696-920 |
5.34e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.54 E-value: 5.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPsnpereTAADSDARSRgpVAYASQ 775
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-------GEDV------ARDPAEVRRR--IGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWL-LNATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDilphgdqTQIGergiNLSGGQRQRISVARALYQH 847
Cdd:COG1131 81 EPALyPDLTVRENLRFfarlyglPRKEARERIDELLELFGLTDAAD-------RKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKDFQRS 920
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
693-908 |
5.67e-27 |
|
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: 109.89 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLATLGEMQKV-SGAVFwnsslpdSEGEDPSN-PERETAADsdarSRGPV 770
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKST-LLNILGGLDRPtSGEVR-------VDGTDISKlSEKELAAF----RRRHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPWLLNA-TVEENI----TFESPFNKQRYKMVIEACslqpdidilphgDQTQIGERgIN-----LSGGQRQRISV 840
Cdd:cd03255 85 GFVFQSFNLLPDlTALENVelplLLAGVPKKERRERAEELL------------ERVGLGDR-LNhypseLSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
686-908 |
1.55e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.36 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDpsnpeRETAADSDAR 765
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD-------GKP-----LSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 SRgpVAYASQKPWLLNATVEENITF-----ESPFNKQRYKMVIEACSLQPDIdiLphgdQTQIGErginLSGGQRQRISV 840
Cdd:COG4619 74 RQ--VAYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDI--L----DKPVER----LSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEEL-LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
686-921 |
1.61e-26 |
|
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: 116.38 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQKvsGAVFWNSSlpDSEGEDPSNPEREtaadsd 763
Cdd:TIGR01846 463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQH--GQVLVDGV--DLAIADPAWLRRQ------ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 764 arsrgpVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRISV 840
Cdd:TIGR01846 533 ------MGVVLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAI 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYE-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL 681
|
.
gi 1958642734 921 E 921
Cdd:TIGR01846 682 Q 682
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
686-912 |
1.72e-26 |
|
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: 108.38 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPEREtaadsdar 765
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-------GRDVTGVPPE-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 sRGPVAYASQK----PWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQ 834
Cdd:cd03259 71 -RRNIGMVFQDyalfPHL---TVAENIAFglklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 835 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 912
Cdd:cd03259 136 QQRVALARALAREPSLLLLDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
694-913 |
2.05e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 115.19 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAV-FWNSSLPDSEGEDpsnperetaadsdARSRgpVAY 772
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrFHDIPLTKLQLDS-------------WRSR--LAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 773 ASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVV 851
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 852 FLDDPFSALDVHlSDHlmqaGILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK10789 474 ILDDALSAVDGR-TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
691-904 |
7.48e-26 |
|
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: 106.46 E-value: 7.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPsnperetaadsdARSRGPV 770
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-------GKPL------------EKERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRIS 839
Cdd:cd03235 71 GYVPQRrsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEALER---VGLSELADR-QIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 840 VARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILEL---LRDDKRTVVLVTHKL-QYLPHADWIIAMK 904
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPK-----TQEDIYELlreLRREGMTILVVTHDLgLVLEYFDRVLLLN 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
696-921 |
1.18e-25 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 106.43 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPSnperETAADSDARSRGPVAYASQ 775
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-------DGEDIS----GLSEAELYRLRRRMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARAL 844
Cdd:cd03261 85 SGALFDSlTVFENVAF--PLRehtrlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQR 919
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASG-----VIDDLIRSLKKelglTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
..
gi 1958642734 920 SE 921
Cdd:cd03261 227 SD 228
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
445-913 |
2.11e-25 |
|
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: 112.10 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 445 IIVGVILLYYILGV--SALIGAAVIILLAPVqYFVATKLSQAQRStleySNERLKQTN----EMLRGIKLLKLYAWENI- 517
Cdd:TIGR02204 145 MCIGGLIMMFITSPklTSLVLLAVPLVLLPI-LLFGRRVRKLSRE----SQDRIADAGsyagETLGAIRTVQAFGHEDAe 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 518 ---FCSRVEKTRRKEMTSLRAFAVYTSISIFMNTAipiAAVLITFVGhVSFFKESDFSPSV--AFASLSLFhiLVTPLFL 592
Cdd:TIGR02204 220 rsrFGGAVEKAYEAARQRIRTRALLTAIVIVLVFG---AIVGVLWVG-AHDVIAGKMSAGTlgQFVFYAVM--VAGSIGT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 593 LSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPREPAPQGQAgkyqAVPLKVVNRKRPAREEVrdllgplqrltpstdg 672
Cdd:TIGR02204 294 LSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRG----EIEFEQVNFAYPARPDQ---------------- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 673 dadnfcvqiiggfftwtpdgiPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnssLPDseGEDPS 752
Cdd:TIGR02204 354 ---------------------PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRI-----LLD--GVDLR 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 753 NPEREtaadsDARSRgpVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEAC-SLQPD--IDILPHGDQTQIGERGIN 829
Cdd:TIGR02204 406 QLDPA-----ELRAR--MALVPQDPVLFAASVMENIRYGRP--DATDEEVEAAArAAHAHefISALPEGYDTYLGERGVT 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQ 909
Cdd:TIGR02204 477 LSGGQRQRIAIARAILKDAPILLLDEATSALDA-ESEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIV 553
|
....
gi 1958642734 910 REGT 913
Cdd:TIGR02204 554 AQGT 557
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
693-912 |
2.68e-25 |
|
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: 105.28 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPSNPEREtaadsDARSRGP-VA 771
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF-------DGKDLLKLSRR-----LRKIRRKeIQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVI--EACSLQPDIDIL---PHGdqtqigerginLSGGQRQRI 838
Cdd:cd03257 86 MVFQDPMSsLNPrmTIGEQIAeplriHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMKDGTIQRE 911
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKLQEelglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEE 227
|
.
gi 1958642734 912 G 912
Cdd:cd03257 228 G 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
686-916 |
2.72e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 111.65 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQkvsgavfwnsslpdsEGE---DPSNPERETAA 760
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDID---------------EGEillDGHDLRDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 761 DSdarsRGPVAYASQKPWLLNATVEENITFESpfnKQRY--KMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQR 835
Cdd:PRK11176 414 SL----RNQVALVSQNVHLFNDTIANNIAYAR---TEQYsrEQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 836 QRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 915
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHA 563
|
.
gi 1958642734 916 D 916
Cdd:PRK11176 564 E 564
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
692-907 |
8.58e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 101.55 E-value: 8.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERETAadsdarsRGPVA 771
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-------GKDIAKLPLEEL-------RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVV 851
Cdd:cd00267 77 YVPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 852 FLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 907
Cdd:cd00267 103 LLDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
685-913 |
1.35e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.84 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 685 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERETAADSdA 764
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD-------GKDLTKLSRRSLREL-R 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 765 RSRGPV---AYASqkpwlLNA--TVEENITfESPFN------KQRYKMV---IEACSLQPD-IDILPHGdqtqigergin 829
Cdd:COG1123 342 RRVQMVfqdPYSS-----LNPrmTVGDIIA-EPLRLhgllsrAERRERVaelLERVGLPPDlADRYPHE----------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIA 902
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLavvRYI--ADRVAV 477
|
250
....*....|.
gi 1958642734 903 MKDGTIQREGT 913
Cdd:COG1123 478 MYDGRIVEDGP 488
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
693-911 |
1.56e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.81 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQKV-SGAVFWNsslpdseGEDPSnperetAADSDARSR-- 767
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLniLGGL---DRPtSGEVLID-------GQDIS------SLSERELARlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 ----GpvaYASQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 835
Cdd:COG1136 85 rrhiG---FVFQFFNLLpELTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642734 836 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 911
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
692-916 |
3.25e-24 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 109.06 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERETAadsdarsRGPVA 771
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN-------GFSLKDIDRHTL-------RQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLLNATVEENITFESPFNKQRyKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHT 848
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLGAKENVSQ-DEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 849 NVVFLDDPFSALDVhlsdhLMQAGILE-LLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:TIGR01193 631 KVLILDESTSNLDT-----ITEKKIVNnLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
686-920 |
4.09e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 102.57 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERetaadsdAR 765
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD-------GRPVTRRRR-------KA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 SRGPVAYASQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVIEACSLQPDI-DILPHgdqtQigerginLSGGQRQ 836
Cdd:COG1124 77 FRRRVQMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFlDRYPH----Q-------LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 837 RISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 911
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEE 220
|
....*....
gi 1958642734 912 GTLKDFQRS 920
Cdd:COG1124 221 LTVADLLAG 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
690-920 |
6.58e-24 |
|
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: 101.61 E-value: 6.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDpsnpereTAADSDARSRGP 769
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-------GED-------IREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLL-NATVEENIT-------FESPFNKQRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRIS 839
Cdd:cd03295 77 IGYVIQQIGLFpHMTVEENIAlvpkllkWPKEKIRERADELLALVGLDPAefADRYPH-----------ELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 840 VARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQ 918
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
..
gi 1958642734 919 RS 920
Cdd:cd03295 225 RS 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
686-912 |
1.42e-23 |
|
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: 98.54 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERETaadsdar 765
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD-------GVPVSDLEKAL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 sRGPVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALY 845
Cdd:cd03247 74 -SSLISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 846 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 912
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSL-IFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
696-858 |
1.47e-23 |
|
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: 97.72 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPEREtaadsdaRSRGPVAYASQ 775
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD-------GQDLTDDERK-------SLRKEIGYVFQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLLNA-TVEENITFESPFnKQRYKMVIEAcslQPDIDI----LPHGDQTQIGERGINLSGGQRQRISVARALYQHTNV 850
Cdd:pfam00005 67 DPQLFPRlTVRENLRLGLLL-KGLSKREKDA---RAEEALeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKL 142
|
....*...
gi 1958642734 851 VFLDDPFS 858
Cdd:pfam00005 143 LLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
690-918 |
1.92e-23 |
|
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: 100.34 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNpeRETAADSDARSRgp 769
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID-------GTDINK--LKGKALRQLRRQ-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLN-ATVEENI---------TFESPFN------KQRykmvieACSLQPDIDILPHGDQtqigeRGINLSGG 833
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVlsgrlgrrsTWRSLFGlfpkeeKQR------ALAALERVGLLDKAYQ-----RADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 834 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 912
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDL-LKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDG 227
|
....*.
gi 1958642734 913 TLKDFQ 918
Cdd:cd03256 228 PPAELT 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
694-908 |
2.37e-23 |
|
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: 98.06 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnssLPDseGEDPSnperetAADSDARsRGPVAYA 773
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----RLD--GADIS------QWDPNEL-GDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNVVFL 853
Cdd:cd03246 82 PQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 854 DDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03246 121 DEPNSHLDVEGERALNQA--IAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
694-921 |
5.46e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.39 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWNsslpdseGEDPSNperetaADSDARSRgPVA 771
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLsmISRLLPPD--SGEVLVD-------GLDVAT------TPSRELAK-RLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWL-LNATVEENITF-ESPFNKQR-----YKMVIEAcslqpdIDILphgDQTQIGERGIN-LSGGQRQRISVARA 843
Cdd:COG4604 79 ILRQENHInSRLTVRELVAFgRFPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDK-RTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
691-923 |
7.16e-23 |
|
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: 98.78 E-value: 7.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPEREtaadsdARSRgpV 770
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-------GEDVRKEPRE------ARRQ--I 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPWL-LNATVEENITFESPFN-------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVAR 842
Cdd:COG4555 77 GVLPDERGLyDRLTVRENIRYFAELYglfdeelKKRIEELIELLGLEEFLDRRVGE-----------LSTGMKKKVALAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 843 ALYQHTNVVFLDDPFSALDVhLSDHLMQaGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDV-MARRLLR-EILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEI 223
|
..
gi 1958642734 922 CQ 923
Cdd:COG4555 224 GE 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
692-907 |
1.55e-22 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 95.72 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERETAAdsdarSRGPVA 771
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------GEDLTDLEDELPP-----LRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLL-NATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNV 850
Cdd:cd03229 80 MVFQDFALFpHLTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 851 VFLDDPFSALDVhlsdhLMQAGILELLRD----DKRTVVLVTHKLQYLPH-ADWIIAMKDGT 907
Cdd:cd03229 122 LLLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
690-908 |
4.40e-22 |
|
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: 96.00 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQKvsGAVFWNSS-LPDSEGEdpsnperetaadsdaRS 766
Cdd:cd03248 25 PD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQG--GQVLLDGKpISQYEHK---------------YL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 767 RGPVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 843
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQ--SCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03248 165 LIRNPQVLILDEATSALDAE-SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
686-924 |
8.82e-22 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 100.36 E-value: 8.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQKVSGAVFWNsslpdseGEDPsnpereTAADS 762
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLD-------GRDL------LELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 763 DARSRGpVAYASQKPW--LLNATVEENITfESPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSG 832
Cdd:COG1123 79 ALRGRR-IGMVFQDPMtqLNPVTVGDQIA-EALENlglsraeaRARVLELLEAVGLERRLDRYPH-----------QLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQY-LPHADWIIAMKDGT 907
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTT-----QAEILDLLRELQRergtTVLLITHDLGVvAEIADRVVVMDDGR 220
|
250
....*....|....*..
gi 1958642734 908 IQREGTLKDFQRSECQL 924
Cdd:COG1123 221 IVEDGPPEEILAAPQAL 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
696-908 |
1.24e-20 |
|
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: 90.15 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPEREtaadsdARSRgpVAYASQ 775
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-------GKDIKKEPEE------VKRR--IGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLL-NATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFLD 854
Cdd:cd03230 81 EPSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 855 DPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:cd03230 121 EPTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
688-908 |
1.98e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 90.55 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 688 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpDSEGEDPSNPEREtaadsDARSR 767
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-------EIDGIDISTIPLE-----DLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 gpVAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEACSlqpdidilphgdqtqIGERGINLSGGQRQRISVARALYQH 847
Cdd:cd03369 84 --LTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642734 848 TNVVFLDDPFSALDVHlSDHLMQAGILELLRDDkrTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03369 144 PRVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
691-913 |
3.51e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.21 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWNsslpdseGEDpsnperetAADSDARSRG 768
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrmIAGLEDPT--SGEILIG-------GRD--------VTDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 pVAYASQKPWLL-NATVEENITF------ESPfnKQRYKMVIEAcslqpdIDILphgdqtQIGE----RGINLSGGQRQR 837
Cdd:COG3839 77 -IAMVFQSYALYpHMTVYENIAFplklrkVPK--AEIDRRVREA------AELL------GLEDlldrKPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 838 ISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQRE 911
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAKLRVE-MRAEIKRLHRRLGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQV 215
|
..
gi 1958642734 912 GT 913
Cdd:COG3839 216 GT 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
696-921 |
3.79e-20 |
|
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: 90.81 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGED-PSNPERETAAdsdARSRgpVAYAS 774
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-------GQDiTGLSEKELYE---LRRR--IGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 775 QKPWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARA 843
Cdd:COG1127 89 QGGALFDSlTVFENVAF--PLRehtdlseaeiRELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLS---DHLmqagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQR 919
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSaviDEL----IRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
..
gi 1958642734 920 SE 921
Cdd:COG1127 232 SD 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
691-891 |
8.41e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpdsegedpsnpERETAAdsdarsrgPV 770
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------------RRAGGA--------RV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQK---PWLLNATVEENITF-----ESPFNKQRY--KMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISV 840
Cdd:NF040873 58 AYVPQRsevPDSLPLTVRDLVAMgrwarRGLWRRLTRddRAAVDDALERVGLADLAG---RQLGE----LSGGQRQRALL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTHKL 891
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDL 179
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
696-889 |
1.17e-19 |
|
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: 88.30 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPsnperetaADSDARSRGPVAYASQ 775
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-------GEPI--------RDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLLNA-TVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHTN 849
Cdd:COG4133 83 ADGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958642734 850 VVFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTH 889
Cdd:COG4133 152 LWLLDEPFTALDAAGVALL--AELIAAHLARGGAVLLTTH 189
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
690-915 |
1.34e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnssLPDseGEDPSnperetaaDSDARS-RG 768
Cdd:TIGR00958 492 PD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV-----LLD--GVPLV--------QYDHHYlHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQKPWLLNATVEENITFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 847
Cdd:TIGR00958 556 QVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMaAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 848 TNVVFLDDPFSALDVHlSDHLMQagilELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 915
Cdd:TIGR00958 636 PRVLILDEATSALDAE-CEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
696-927 |
2.65e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.59 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgEMQKvSGAVFWNsslpdseGEDpsnpereTAADSDARSRGpVAYA 773
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLriIAGL-ETPD-SGRIVLN-------GRD-------LFTNLPPRERR-VGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKPWLL-NATVEENITF----ESPFNKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 845
Cdd:COG1118 81 FQHYALFpHMTVAENIAFglrvRPPSKAEIRARVeelLELVQLEGLADRYPS-----------QLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 846 QHTNVVFLDDPFSALDVHLSDHLMQaGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDfqrsecqL 924
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRR-WLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDE-------V 221
|
...
gi 1958642734 925 FEH 927
Cdd:COG1118 222 YDR 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
686-926 |
2.95e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.65 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPDSEGEdpsnperetaadSDAR 765
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF------------EKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 SRGPVAYASQKPWLLNATVEENITFESPFNKQRY-KMVIEACSLQPDIDILPHGD-QTQigergiNLSGGQRQRISVARA 843
Cdd:PRK13648 83 KHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYdEMHRRVSEALKQVDMLERADyEPN------ALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQ 923
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
...
gi 1958642734 924 LFE 926
Cdd:PRK13648 236 LTR 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
696-892 |
3.14e-19 |
|
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: 87.62 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQKVSGAVFWNSSLPDSEGEDPSNPEREtaadsdarsrgpV 770
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELRRR------------V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPWLLNATVEENITF------ESPfNKQRYKMVIEACS---LQPDIDILPHGDQtqigerginLSGGQRQRISVA 841
Cdd:cd03260 84 GMVFQKPNPFPGSIYDNVAYglrlhgIKL-KEELDERVEEALRkaaLWDEVKDRLHALG---------LSGGQQQRLCLA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELlrDDKRTVVLVTHKLQ 892
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQ 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
673-908 |
7.13e-19 |
|
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: 91.28 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 673 DADNFCV--QIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGeMQKVSGAVFWNsslpdseGED 750
Cdd:COG4172 277 EARDLKVwfPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFD-------GQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 751 PSNpeRETAADSDARSR------GPvaYASQKPWLlnaTVEENIT------FESPFNKQRYKMVIEACS---LQPD-IDI 814
Cdd:COG4172 349 LDG--LSRRALRPLRRRmqvvfqDP--FGSLSPRM---TVGQIIAeglrvhGPGLSAAERRARVAEALEevgLDPAaRHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 815 LPHgdqtqigErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVLVTHK 890
Cdd:COG4172 422 YPH-------E----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV-----QAQILDLLRDlqREHglAYLFISHD 485
|
250 260
....*....|....*....|.
gi 1958642734 891 LQ---YLphADWIIAMKDGTI 908
Cdd:COG4172 486 LAvvrAL--AHRVMVMKDGKV 504
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
654-907 |
7.59e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.41 E-value: 7.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 654 EEVRDLLGPLQRLTPSTDGD--ADNFCVQiiggfftwTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemq 731
Cdd:COG4178 343 EAADALPEAASRIETSEDGAlaLEDLTLR--------TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 732 kvsgavFWNS-----SLPDSEGedpsnperetaadsdarsrgpVAYASQKPWLLNATVEENITF---ESPFNKQRYKMVI 803
Cdd:COG4178 412 ------LWPYgsgriARPAGAR---------------------VLFLPQRPYLPLGTLREALLYpatAEAFSDAELREAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 804 EACSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRT 883
Cdd:COG4178 465 EAVGLG---HLAERLDEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG--TT 536
|
250 260
....*....|....*....|....
gi 1958642734 884 VVLVTHKLQYLPHADWIIAMKDGT 907
Cdd:COG4178 537 VISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
686-913 |
8.49e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.42 E-value: 8.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLgemqkvsgavFWNsslPDSeGEDPSNpERETAADSDA 764
Cdd:PRK11160 346 FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLqLLTR----------AWD---PQQ-GEILLN-GQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 765 RSRGPVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDIlPHGDQTQIGERGINLSGGQRQRISVARA 843
Cdd:PRK11160 411 ALRQAISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRD---DKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQ-----ILELLAEhaqNK-TVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
686-913 |
9.96e-19 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 91.54 E-value: 9.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLgeMQKVSGAVFWnsslpdsEGEDPSNPERETAADSd 763
Cdd:TIGR03796 485 FGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIakLVAGL--YQPWSGEILF-------DGIPREEIPREVLANS- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 764 arsrgpVAYASQKPWLLNATVEENITFESPFNKQryKMVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQRISV 840
Cdd:TIGR03796 555 ------VAMVDQDIFLFEGTVRDNLTLWDPTIPD--ADLVRACkdaAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEI 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:TIGR03796 627 ARALVRNPSILILDEATSALDP-----ETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
691-913 |
1.23e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.62 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSN--PERetaadsdarsRg 768
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD-------GRDVTGlpPEK----------R- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQR 837
Cdd:COG3842 78 NVGMVFQDyalfPHL---TVAENVAFglrmrgVPK--AEIRARVAELLEL---VGLEGLAD------RYPHqLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 838 ISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKlQY--LPHADWIIAMKDGTIQREGT 913
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREE-MREELRRLQRELGITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
692-908 |
2.35e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 83.25 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQKVSGAVFWNsslpdseGEdpsnpERETAADSDARSRGp 769
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMkiLS--GLYKPDSGEILVD-------GK-----EVSFASPRDARRAG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTN 849
Cdd:cd03216 77 IAMVYQ------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 850 VVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
694-913 |
2.82e-18 |
|
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: 89.88 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQkvSGAVFWNsslpdseGEDPsnpeRETAADSDARSRGPVA 771
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLarLLFRFYDVT--SGRILID-------GQDI----RDVTQASLRAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 yasQKPWLLNATVEENItfespfnkqRY----------KMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVA 841
Cdd:COG5265 439 ---QDTVLFNDTIAYNI---------AYgrpdaseeevEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSR-TERAIQAALREVARG--RTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
703-912 |
4.03e-18 |
|
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: 84.08 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 703 IPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDpsnperETAADSDARsrgPVAYASQKPWLL-N 781
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-------GVD------VTAAPPADR---PVSMLFQENNLFaH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 782 ATVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARALYQHTNVVFLD 854
Cdd:cd03298 85 LTVEQNVGLGlspglklTAEDRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 855 DPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 912
Cdd:cd03298 154 EPFAALDPALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
691-903 |
5.53e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.00 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWnsslpdsEGEDPS--NPERetaadsdarS 766
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLkiVASLISPT--SGTLLF-------EGEDIStlKPEI---------Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 767 RGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQ----PDidilphgdqtQIGERGIN-LSGGQRQRISVA 841
Cdd:PRK10247 80 RQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLErfalPD----------TILTKNIAeLSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 903
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
695-921 |
1.14e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 83.27 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 695 TLSNITIR-----------IPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDpsnperETAADSD 763
Cdd:COG3840 3 RLDDLTYRygdfplrfdltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-------GQD------LTALPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 764 ARsrgPVAYASQK----PWLlnaTVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgDQtqigerginLSG 832
Cdd:COG3840 70 ER---PVSMLFQEnnlfPHL---TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ---------LSG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQRE 911
Cdd:COG3840 133 GQRQRVALARCLVRKRPILLLDEPFSALDPALRQE-MLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAAD 211
|
250
....*....|
gi 1958642734 912 GTLKDFQRSE 921
Cdd:COG3840 212 GPTAALLDGE 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
692-917 |
1.90e-17 |
|
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: 82.48 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDpsnperETAADSDARSRGPVA 771
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-------DGRD------ITGLPPHERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLL-NATVEENITF-ESPFNKQRYKMVIE-ACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVARALYQHT 848
Cdd:cd03224 79 YVPEGRRIFpELTVEENLLLgAYARRRAKRKARLErVYELFPRL-------KERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 849 NVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 917
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEA--IRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
691-913 |
2.94e-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: 82.39 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDpsnperetAADSDARSRGpV 770
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-------GED--------ATDVPVQERN-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 838
Cdd:cd03296 77 GFVFQHYALFrHMTVFDNVAFglrvkprsERPPEaeiRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKEL-RRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
691-912 |
3.69e-17 |
|
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: 81.15 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDpsnperetAADSDARSRGpV 770
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-------GRD--------VTDLPPKDRD-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPWLL-NATVEENITFESPFNKQRyKMVIE------ACSLQpdIDILPHGDQTQigerginLSGGQRQRISVARA 843
Cdd:cd03301 75 AMVFQNYALYpHMTVYDNIAFGLKLRKVP-KDEIDervrevAELLQ--IEHLLDRKPKQ-------LSGGQRQRVALGRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 912
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQ-MRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
698-921 |
3.91e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.34 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPsnpeRETAADSDARSRGPVAYasqkp 777
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-------DGEHI----QHYASKEVARRIGLLAQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 778 wllNATVEENITFESPFNKQRYKMvieacslQP--------DIDILPHGDQ----TQIGERGIN-LSGGQRQRISVARAL 844
Cdd:PRK10253 89 ---NATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 845 YQHTNVVFLDDPFSALDVhlsDHlmQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQR 919
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT 233
|
..
gi 1958642734 920 SE 921
Cdd:PRK10253 234 AE 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
686-916 |
5.44e-17 |
|
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: 81.09 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMQKvSGAVFWN----SSLPDSEgedpsnpEREtaa 760
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrCINGLERPT-SGSVLVDgtdlTLLSGKE-------LRK--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 761 dsdARSRgpVAYASQKPWLLNA-TVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSG 832
Cdd:cd03258 80 ---ARRR--IGMIFQHFNLLSSrTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGT 907
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGE 218
|
....*....
gi 1958642734 908 IQREGTLKD 916
Cdd:cd03258 219 VVEEGTVEE 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
698-913 |
8.33e-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: 81.54 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPSNperetAADSDARS--RGPVAYASQ 775
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-------DGQDIAA-----MSRKELRElrRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLL-NATVEENITF------ESPFNKQRYKM-VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQH 847
Cdd:cd03294 110 SFALLpHRTVLENVAFglevqgVPRAEREERAAeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 848 TNVVFLDDPFSALDvHLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:cd03294 179 PDILLMDEAFSALD-PLIRREMQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGT 244
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
711-947 |
9.66e-17 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 82.54 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 711 IVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSN--PERetaadsdaRSRGPV--AYAsqkpWLLNATVEE 786
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLD-------GEDVTNvpPHL--------RHINMVfqSYA----LFPHMTVEE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 787 NITFESPFNK----QRYKMVIEACSLqpdidilphgdqTQIGERG----INLSGGQRQRISVARALYQHTNVVFLDDPFS 858
Cdd:TIGR01187 62 NVAFGLKMRKvpraEIKPRVLEALRL------------VQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 859 ALDVHLSDhLMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQRS-----------ECQLFE 926
Cdd:TIGR01187 130 ALDKKLRD-QMQLELKTIQEQLGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEpanlfvarfigEINVFE 208
|
250 260
....*....|....*....|.
gi 1958642734 927 hwKTLMNRQDQELEKHTVETR 947
Cdd:TIGR01187 209 --ATVIERKSEQVVLAGVEGR 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
690-889 |
9.86e-17 |
|
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: 80.14 E-value: 9.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNpERETAADSDARSRGp 769
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-------GQDVSD-LRGRAIPYLRRKIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKpWLLNATVEENITF------ESPFN-KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVAR 842
Cdd:cd03292 82 VVFQDFR-LLPDRNVYENVAFalevtgVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958642734 843 ALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD-DKR--TVVLVTH 889
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTT-----WEIMNLLKKiNKAgtTVVVATH 194
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
698-920 |
1.03e-16 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 84.94 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQKVSGavfwnsslPDS-----EGEDPSNPERETAadsdarsRGPVAY 772
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLI----NLLQRVYD--------PTVgqiliDGIDINTVTRESL-------RKSIAT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 773 ASQKPWLLNATVEENITF--ESPFNKQRYKMViEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNV 850
Cdd:TIGR01192 414 VFQDAGLFNRSIRENIRLgrEGATDEEVYEAA-KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPI 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 851 VFLDDPFSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:TIGR01192 493 LVLDEATSALDVETEARVKNA--IDALRKN-RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
693-913 |
1.08e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 85.47 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQKVSGAVFWNSSLPDSEGEDPSNPERE------------- 757
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVmsLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEqnvgmknvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 758 TAADSDARS-------------------------RGPVAYASQKPWLLNATVEENITF-ESPFNKQRYKMVIEACSLQPD 811
Cdd:PTZ00265 1261 TKEGGSGEDstvfknsgkilldgvdicdynlkdlRNLFSIVSQEPMLFNMSIYENIKFgKEDATREDVKRACKFAAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 812 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKL 891
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
250 260
....*....|....*....|....*..
gi 1958642734 892 QYLPHADWIIAM----KDGT-IQREGT 913
Cdd:PTZ00265 1420 ASIKRSDKIVVFnnpdRTGSfVQAHGT 1446
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
691-916 |
1.21e-16 |
|
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: 80.36 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPSN---PERetaadsdarsr 767
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL-------DGKDITNlppHKR----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 gPVAYASQKPWLL-NATVEENITF-----ESPFNKQRYKmVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRISV 840
Cdd:cd03300 73 -PVNTVFQNYALFpHLTVFENIAFglrlkKLPKAEIKER-VAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHLSDHlMQagiLELLRDDKR---TVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKD-MQ---LELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
690-916 |
1.76e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.05 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPDsegedpsnpereTAADSDARSRGP 769
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID------------YSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRIS 839
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSF-GAVNlklpedevRKRVDNALKRTGIEHLKDKPTHC-----------LSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 840 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL-LVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
694-889 |
2.11e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.29 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqkvsgavFwnssLPDSEGEDPSNPERETAADSDarsRGPVAya 773
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAG---------F----LAPSSGEITLDGVPVTGPGAD---RGVVF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 sQK----PWLlnaTVEENITFESPFNK----QRYKMVIEACSLqpdIDiLPHGDQTQIGErginLSGGQRQRISVARALY 845
Cdd:COG4525 83 -QKdallPWL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VG-LADFARRRIWQ----LSGGMRQRVGIARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958642734 846 QHTNVVFLDDPFSALDVhLSDHLMQAGILELLRDDKRTVVLVTH 889
Cdd:COG4525 151 ADPRFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
696-892 |
2.41e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.21 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQKVSGAV-FWNSSLPDSEgEDPSnperetaadsDARSRgp 769
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVtFHGKNLYAPD-VDPV----------EVRRR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLNATVEENITFESPFNKQRYKM--VIEACSLQPdidILPHGDQTQIGERGINLSGGQRQRISVARALYQH 847
Cdd:PRK14243 93 IGMVFQKPNPFPKSIYDNIAYGARINGYKGDMdeLVERSLRQA---ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958642734 848 TNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHKLQ 892
Cdd:PRK14243 170 PEVILMDEPCSAL-----DPISTLRIEELMHELKEqyTIIIVTHNMQ 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
696-910 |
2.64e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.62 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQKVSGAVFWNSslpdseGEDPSNPERETAAdsdARSRGPVAYASQ 775
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLDKPTSGTYRVA------GQDVATLDADALA---QLRREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLL-NATVEENITFESPF-------NKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQH 847
Cdd:PRK10535 94 RYHLLsHLTAAQNVEVPAVYaglerkqRLLRAQELLQRLGLEDRVEYQPS-----------QLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQR 910
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
689-889 |
3.14e-16 |
|
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: 77.19 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsSLPDSEGedpsnperetaadsdarsrg 768
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----GMPEGED-------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 pVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidILPHGDqtqigergiNLSGGQRQRISVARALYQHT 848
Cdd:cd03223 66 -LLFLPQRPYLPLGTLREQL-------------------------IYPWDD---------VLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958642734 849 NVVFLDDPFSALDVHLSDHLMQagileLLRDDKRTVVLVTH 889
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQ-----LLKELGITVISVGH 146
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
706-912 |
3.54e-16 |
|
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: 78.49 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 706 GQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSS-LPDSEGEDPSNPERetaadsdarsRGpVAYASQKPWLL-NAT 783
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvLFDSRKKINLPPQQ----------RK-IGLVFQQYALFpHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 784 VEENITFESPFNKQRYKMVieacslQPDiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTNVVFLDDPFSALDV 862
Cdd:cd03297 92 VRENLAFGLKRKRNREDRI------SVD-ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 863 HLSDHLMQAgILELLRDDKRTVVLVTHKL---QYLphADWIIAMKDGTIQREG 912
Cdd:cd03297 165 ALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
686-903 |
3.67e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.29 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---KVSGAVFWN----SSLPdsegedpsnPERet 758
Cdd:COG4136 7 LTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNgrrlTALP---------AEQ-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 759 aadsdarsRGpVAYASQKPWLL-NATVEENITF---ESPFNKQRYKMVIEAcsLQpDIDiLPHgdqtqIGERGIN-LSGG 833
Cdd:COG4136 76 --------RR-IGILFQDDLLFpHLSVGENLAFalpPTIGRAQRRARVEQA--LE-EAG-LAG-----FADRDPAtLSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 834 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 903
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLDAALRAQ-FREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
696-913 |
6.09e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.90 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSslpdsegedpsNPERETAADSDARSrgpVAYASQ 775
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD-----------KPISMLSSRQLARR---LALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPwllnaTVEENITFE-------SPFNK------QRYKMVIEAcSLQpdidilphgdQTQIGE----RGINLSGGQRQRI 838
Cdd:PRK11231 84 HH-----LTPEGITVRelvaygrSPWLSlwgrlsAEDNARVNQ-AME----------QTRINHladrRLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
694-913 |
7.63e-16 |
|
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: 77.55 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdsegedpsnpERETAADSDARsRGPVAYA 773
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--------------GYSIRTDRKAA-RQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQK---PWLLnaTVEENITFESPF---NKQRYKMVIEA----CSLQPDIDilphgdqTQIGergiNLSGGQRQRISVARA 843
Cdd:cd03263 81 PQFdalFDEL--TVREHLRFYARLkglPKSEIKEEVELllrvLGLTDKAN-------KRAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRddKRTVVLVTHKLQ---YLphADWIIAMKDGTIQREGT 913
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDL-ILEVRK--GRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
691-913 |
9.16e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 81.69 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqkvsgavfwnsSLPDSEGE---DpsnpERETAADSDARSR 767
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG-------------YYPLTEGEirlD----GRPLSSLSHSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 GPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 847
Cdd:PRK10790 415 QGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHLMQAgiLELLRdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQA--LAAVR-EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
690-916 |
1.44e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.20 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEdpsnperetAADSDARS--- 766
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL-------IKGE---------PIKYDKKSlle 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 767 -RGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 835
Cdd:PRK13639 76 vRKTVGIVFQNPddQLFAPTVEEDVAF-GPLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 836 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTL 914
Cdd:PRK13639 144 KRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTP 221
|
..
gi 1958642734 915 KD 916
Cdd:PRK13639 222 KE 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
694-913 |
1.47e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.16 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQKV----SGAVfwnssLPDseGEDPSNPERETAadsdarsRGP 769
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQRVfdpqSGRI-----LID--GTDIRTVTRASL-------RRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLNATVEENITFESPfNKQRYKMVIEACSLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 847
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAA--LDELMKG-RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
687-912 |
2.02e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 76.05 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 687 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSlpDSEGEDPSnperetaadsdars 766
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPY-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 767 RGPVAYASQKPWLL-NATVEENITFE-SPFNK----QRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRI 838
Cdd:TIGR01277 69 QRPVSMLFQENNLFaHLTVRQNIGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 912
Cdd:TIGR01277 138 ALARCLVRPNPILLLDEPFSALDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
696-916 |
2.11e-15 |
|
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: 76.61 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSN--PERETaadsdarsrgpVAYA 773
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN-------GKDITNlpPEKRD-----------ISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKPWLL-NATVEENITF----ESPFNKQRYKMVIE-ACSLqpDIDILPHGDQTqigergiNLSGGQRQRISVARALYQH 847
Cdd:cd03299 77 PQNYALFpHMTVYKNIAYglkkRKVDKKEIERKVLEiAEML--GIDHLLNRKPE-------TLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHLMqagilELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLR-----EELKKIRKefgvTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
696-921 |
2.60e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.75 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpdSEGEDPSNPERETAADSDARSRgpVAYASQ 775
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV--------TIGERVITAGKKNKKLKPLRKK--VGIVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALY 845
Cdd:PRK13634 93 FPehQLFEETVEKDICF-GPMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 846 QHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL----QYlphADWIIAMKDGTIQREGTLKD-FQRS 920
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEM-FYKLHKEKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREiFADP 237
|
.
gi 1958642734 921 E 921
Cdd:PRK13634 238 D 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
686-917 |
2.68e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---KVSGAV-FWNSSLPdsegedpsnpERETA 759
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELEsevRVEGRVeFFNQNIY----------ERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 760 ADsdaRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKM----VIEACSLQPDI-DILPHgdqtQIGERGINLSGGQ 834
Cdd:PRK14258 83 LN---RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLwDEIKH----KIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 835 RQRISVARALYQHTNVVFLDDPFSALDVHLS---DHLMQAGILEllrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 911
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
....*.
gi 1958642734 912 GTLKDF 917
Cdd:PRK14258 232 GQLVEF 237
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
683-911 |
3.14e-15 |
|
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: 76.77 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 683 GGFFtWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPS--NPERETAA 760
Cdd:TIGR02769 15 GGLF-GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF-------RGQDLYqlDRKQRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 761 DSDARSRGPVAYASQKP-----WLLNATVEENITFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQ 834
Cdd:TIGR02769 87 RRDVQLVFQDSPSAVNPrmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 835 RQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQ 909
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
..
gi 1958642734 910 RE 911
Cdd:TIGR02769 231 EE 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
696-890 |
5.21e-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: 75.39 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQK---VSGAVFWNSSlpdsegedPSNPeretaadsdARSRGPVAY 772
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ--------PRKP---------DQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 773 ASQKPWLL-NATVEENITFESPF-------NKQRYKMVieacslqpDIDILPHGDQTQIGERGI-NLSGGQRQRISVARA 843
Cdd:cd03234 86 VRQDDILLpGLTVRETLTYTAILrlprkssDAIRKKRV--------EDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHK 890
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
696-908 |
5.24e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQKVSGAVFWNSSLPDSEGEDpsnperetaaDS-----DARsrg 768
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLrlLAGL---ETPSAGELLAGTAPLAEARE----------DTrlmfqDAR--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 pvayasQKPWllnATVEENITFESPFN-KQRYKMVIEACSLQPdidilphgdqtQIGERGINLSGGQRQRISVARALYQH 847
Cdd:PRK11247 92 ------LLPW---KKVIDNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 848 TNVVFLDDPFSALDVhLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 908
Cdd:PRK11247 152 PGLLLLDEPLGALDA-LTRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
696-937 |
7.20e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.82 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlatlgemQKVSGAVFWNSSlPDSEGEDPSNP-ERETAADSDAR-SRGPVAYA 773
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKS-AGSHIELLGRTvQREGRLARDIRkSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKPWLLNA-TVEENITF----ESPFNKQRYKMVIEAcSLQPDIDILphgdqTQIG------ERGINLSGGQRQRISVAR 842
Cdd:PRK09984 92 FQQFNLVNRlSVLENVLIgalgSTPFWRTCFSWFTRE-QKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 843 ALYQHTNVVFLDDPFSALDVHLSDHLMqagilELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 917
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVM-----DTLRDinqnDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
|
250 260
....*....|....*....|
gi 1958642734 918 QRSEcqlFEHWKTLMNRQDQ 937
Cdd:PRK09984 241 DNER---FDHLYRSINRVEE 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
692-921 |
7.44e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQKVSGAVFWNsslpdseGE--DPSNPeretaadSDARSR 767
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMkiLS--GVYQPDSGEILLD-------GEpvRFRSP-------RDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 GpVAYASQKPWLL-NATVEENITFESPFNK----QRYKMVIEACSL--QPDIDILPHgdqTQIGErginLSGGQRQRISV 840
Cdd:COG1129 80 G-IAIIHQELNLVpNLSVAENIFLGREPRRggliDWRAMRRRARELlaRLGLDIDPD---TPVGD----LSVAQQQLVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQR 919
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVAELTE 229
|
..
gi 1958642734 920 SE 921
Cdd:COG1129 230 DE 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
696-889 |
9.11e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 9.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsSLPDSEGEDPSNPERetaadsdarsrgpVAYASQ 775
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI----KLDGGDIDDPDVAEA-------------CHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 ----KPWLlnaTVEENITFESPFNKQRYKMV---IEACSLQPDIDiLPHGdqtqigergiNLSGGQRQRISVARALYQHT 848
Cdd:PRK13539 81 rnamKPAL---TVAENLEFWAAFLGGEELDIaaaLEAVGLAPLAH-LPFG----------YLSAGQKRRVALARLLVSNR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958642734 849 NVVFLDDPFSALDVH--------LSDHLMQAGIlellrddkrtVVLVTH 889
Cdd:PRK13539 147 PIWILDEPTAALDAAavalfaelIRAHLAQGGI----------VIAATH 185
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
689-889 |
1.65e-14 |
|
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: 75.47 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQKVSGAVFWnsslpdsEGEDPSN-PERETAAdsd 763
Cdd:COG0444 13 TRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILF-------DGEDLLKlSEKELRK--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 764 ARSRGpVAYASQKPwlLNA-----TVEENITfESPFN------KQRYKMVIEA---CSLQPDIDIL---PHgdqtqiger 826
Cdd:COG0444 83 IRGRE-IQMIFQDP--MTSlnpvmTVGDQIA-EPLRIhgglskAEARERAIELlerVGLPDPERRLdryPH--------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 827 giNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTH 889
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITH 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
690-912 |
2.53e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.16 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSN-PERETAAdsdARSR- 767
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-------GQDLSRlKRREIPY---LRRRi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 GPVAyasQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 839
Cdd:COG2884 82 GVVF---QDFRLLpDRTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 840 VARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPHADW-IIAMKDGTIQREG 912
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSW-----EIMELLEEINRrgtTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
692-912 |
2.66e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEDPSnperetAADSDARSRgPVA 771
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL-------VAGDDVE------ALSARAASR-RVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWL-LNATVEENITFESPFNKQRYKMVIEACSLQPDiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTN 849
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 850 VVFLDDPFSALDVHlsdHLMQAgiLELLR---DDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 912
Cdd:PRK09536 160 VLLLDEPTASLDIN---HQVRT--LELVRrlvDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAG 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
691-889 |
4.02e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.26 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPSN--PEREtaadsdarsrg 768
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-------DGVDLSHvpPYQR----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQKPWLL-NATVEENITFESPFNK-------QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISV 840
Cdd:PRK11607 92 PINMMFQSYALFpHMTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH 889
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDR-MQLEVVDILERVGVTCVMVTH 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
691-892 |
4.92e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsSLPDSEGEDPSnPERETAADSDArsrgpv 770
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI----TLDGKPVEGPG-AERGVVFQNEG------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 ayasQKPWLlnaTVEENITFespfnKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTN 849
Cdd:PRK11248 81 ----LLPWR---NVQDNVAF-----GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958642734 850 VVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ 892
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
686-913 |
5.87e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.30 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMqkvsgavfwnssLPDSegedpsNPERETAADS--- 762
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL------------LPDD------NPNSKITVDGitl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 763 ------DARSRGPVAYASQKPWLLNATVEENITFESPfNKQ--RYKMVIEACSLQPDIDILPHGDQTQIgergiNLSGGQ 834
Cdd:PRK13640 75 taktvwDIREKVGIVFQNPDNQFVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 835 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKL-IRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
684-903 |
6.90e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.85 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 684 GFFTwTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQKVSGAVFWNsslpdseGEDPSNPERETAADs 762
Cdd:PRK11308 20 GLFK-PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIE-TPTGGELYYQ-------GQDLLKADPEAQKL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 763 dARSR------GPvaYASQKP-WLLNATVEE----NITFESPFNKQRYKMVIEACSLQPD-IDILPHgdqtqigergiNL 830
Cdd:PRK11308 90 -LRQKiqivfqNP--YGSLNPrKKVGQILEEplliNTSLSAAERREKALAMMAKVGLRPEhYDRYPH-----------MF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 903
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQelglSYVFISHDLSVVEHiADEVMVM 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
690-913 |
8.74e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.71 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEDPSNPERETAAdsdarsRGP 769
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-------VSGIDTGDFSKLQGI------RKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKP--WLLNATVEENITFeSPFNkqrykmvieACslQPDIDILPHGDQTqIGERGI---------NLSGGQRQRI 838
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAF-GPEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
694-908 |
9.74e-14 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 72.25 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEDPSNPERETAadsdaRSRgpVAYA 773
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV-------IDGIDISKLPLHTL-----RSR--LSII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFL 853
Cdd:cd03288 101 LQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 854 DDPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:cd03288 181 DEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
691-889 |
1.12e-13 |
|
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: 70.85 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSlpdsegedPSNPERETAADSdarsrgpV 770
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT--------PLAEQRDEPHEN-------I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPWLLNA-TVEENITFESPFNKQRYKMVIEACslqpdidilphgdqTQIGERGIN------LSGGQRQRISVARA 843
Cdd:TIGR01189 76 LYLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 844 LYQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 889
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
696-908 |
1.64e-13 |
|
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: 70.64 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWNsslpdseGEDPSNPERETAAdsdARSRgpVAYA 773
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTIIID-------GLKLTDDKKNINE---LRQK--VGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKPWLL-NATVEENITfESP---FNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTN 849
Cdd:cd03262 82 FQQFNLFpHLTVLENIT-LAPikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 850 VVFLDDPFSALDVHlsdhlMQAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:cd03262 156 VMLFDEPTSALDPE-----LVGEVLDVMKDlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
691-916 |
1.78e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSN--PEREtaadsdarsrg 768
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-------GQDITHvpAENR----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQKPWLL-NATVEENITF-----ESPfNKQRYKMVIEA---CSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 839
Cdd:PRK09452 87 HVNTVFQSYALFpHMTVFENVAFglrmqKTP-AAEITPRVMEAlrmVQLEEFAQRKPH-----------QLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 840 VARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQ-MQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
687-891 |
2.74e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 687 TWTpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpdSEGEDPSNperetaadsDARS 766
Cdd:PRK15056 15 TWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI--------SILGQPTR---------QALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 767 RGPVAYASQKP---WLLNATVEENIT---------FESPfnKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQ 834
Cdd:PRK15056 77 KNLVAYVPQSEevdWSFPVLVEDVVMmgryghmgwLRRA--KKRDRQIVTAALARVDMVEFRH---RQIGE----LSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 835 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL 891
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNL 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
696-919 |
2.89e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.42 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPEretaadsdARSRgPVAYASQ 775
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-------GTDVSRLH--------ARDR-KVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPhgdqTQigerginLSGGQRQRISVARA 843
Cdd:PRK10851 82 HYALFrHMTVFDNIAFgltvlprrERPNAaaiKAKVTQLLEMVQLAHLADRYP----AQ-------LSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQR 919
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKEL-RRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
819-912 |
3.30e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.77 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 819 DQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-A 897
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvS 219
|
90
....*....|....*
gi 1958642734 898 DWIIAMKDGTIQREG 912
Cdd:PRK10619 220 SHVIFLHQGKIEEEG 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
688-893 |
4.21e-13 |
|
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: 69.12 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 688 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQKVSGAVFWNSSlpdsegedPSNPERetaadsdar 765
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLnaLAGRRTGLGVSGEVLINGR--------PLDKRS--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 766 SRGPVAYASQKPWLL-NATVEENITFespfnkqrykmvieACSLQpdidilphgdqtqigergiNLSGGQRQRISVARAL 844
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALEL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY 893
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSS 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
676-913 |
8.18e-13 |
|
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: 73.06 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 676 NFCVQiiggfftWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllaTLGEMQKVSGAvfwnsslpdsEGE---DPS 752
Cdd:TIGR00957 1289 NYCLR-------YREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSL---TLGLFRINESA----------EGEiiiDGL 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 753 NperetAAD---SDARSRgpVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGIN 829
Cdd:TIGR00957 1349 N-----IAKiglHDLRFK--ITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGEN 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQ 909
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEVA 1498
|
....
gi 1958642734 910 REGT 913
Cdd:TIGR00957 1499 EFGA 1502
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
673-913 |
8.54e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.42 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 673 DADNFCVQIiggfftwtpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsSLPDSEGEDPS 752
Cdd:PRK13548 4 EARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV----RLNGRPLADWS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 753 NPERetaadsdARSRgpvAYASQK-----PWllnaTVEENITF-ESPF--NKQRYKMVIEACSLQPDIDILPHGDQTQig 824
Cdd:PRK13548 71 PAEL-------ARRR---AVLPQHsslsfPF----TVEEVVAMgRAPHglSRAEDDALVAAALAQVDLAHLAGRDYPQ-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 825 erginLSGGQRQRISVARALYQHTN------VVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVTHKL--- 891
Cdd:PRK13548 135 -----LSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLA---H--QHHVLRLARQlaheRGLAVIVVLHDLnla 204
|
250 260
....*....|....*....|...
gi 1958642734 892 -QYlphADWIIAMKDGTIQREGT 913
Cdd:PRK13548 205 aRY---ADRIVLLHQGRLVADGT 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
696-892 |
9.02e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.30 E-value: 9.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEM------QKVSGAVFWNsslpdseGEDPSNPERETAAdsdARSRgp 769
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLL-RCLNRMndlipgARVEGEILLD-------GEDIYDPDVDVVE---LRRR-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLNATVEENITFESPFNKQRYKMVIEA--------CSLQPDI-DILphgdqtqiGERGINLSGGQRQRISV 840
Cdd:COG1117 94 VGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWDEVkDRL--------KKSALGLSGGQQQRLCI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD--DKRTVVLVTHKLQ 892
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPIST-----AKIEELILElkKDYTIVIVTHNMQ 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
699-920 |
9.39e-13 |
|
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: 70.91 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 699 ITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQKVSGAVFWNSSlpdSEGEDPSnPERETaadsdarsrgpVAYA 773
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIrliagLTRPDEGEIVLNGRTLFDS---RKGIFLP-PEKRR-----------IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKPWLL-NATVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQH 847
Cdd:TIGR02142 81 FQEARLFpHLSVRGNLRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:TIGR02142 150 PRLLLMDEPLAALDDPRKYEILP--YLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
676-912 |
1.04e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.38 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 676 NFCVQIIGGFFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG--EMQKVSGAVFwnsslpdsegedpsn 753
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiyLPQRGRVKVM--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 754 pERETAADSDARSRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqi 823
Cdd:PRK13647 66 -GREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAF-GPVNmgldkdevERRVEEALKAVRMWDFRDKPPY------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 824 gergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIA 902
Cdd:PRK13647 138 -----HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIV 210
|
250
....*....|
gi 1958642734 903 MKDGTIQREG 912
Cdd:PRK13647 211 LKEGRVLAEG 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
683-903 |
1.09e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 70.15 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 683 GGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPSNPERETAADs 762
Cdd:COG4608 21 GGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF-------DGQDITGLSGRELRP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 763 dARSR------GPvaYASqkpwlLNA--TVEENItfESPF-------NKQRYKMV---IEACSLQPD-IDILPHgdqtqi 823
Cdd:COG4608 93 -LRRRmqmvfqDP--YAS-----LNPrmTVGDII--AEPLrihglasKAERRERVaelLELVGLRPEhADRYPH------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 824 gErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-AD 898
Cdd:COG4608 157 -E----FSGGQRQRIGIARALALNPKLIVCDEPVSALDV--S---IQAQVLNLLEDLQDelglTYLFISHDLSVVRHiSD 226
|
....*
gi 1958642734 899 WIIAM 903
Cdd:COG4608 227 RVAVM 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
699-903 |
3.26e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGED----PSNPERETAADSDARSRGPVAyaS 774
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL-------GKDllgmKDDEWRAVRSDIQMIFQDPLA--S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 775 QKPWLlnaTVEENI-----TFESPFNKQ----RYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVARAL 844
Cdd:PRK15079 111 LNPRM---TIGEIIaeplrTYHPKLSRQevkdRVKAMMLKVGLLPNlINRYPH-----------EFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 903
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
695-892 |
3.48e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.49 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 695 TLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---KVSGAVFWNsslpdseGEDPSNPERETAadsdaRSRGP 769
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsINRMNDLNpevTITGSIVYN-------GHNIYSPRTDTV-----DLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLNATVEENITFESPFN----KQRYKMVIEACSLQPDI-----DILpHgdqtqigERGINLSGGQRQRISV 840
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdevkDRL-H-------DSALGLSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELlrDDKRTVVLVTHKLQ 892
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQ 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
687-891 |
3.55e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 687 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDpsnpERETAAdsdarS 766
Cdd:PRK10771 8 TWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN-------GQD----HTTTPP-----S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 767 RGPVAYASQKPWLLN-ATVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 838
Cdd:PRK10771 70 RRPVSMLFQENNLFShLTVAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVLVTHKL 891
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDPAL-----RQEMLTLVSQvcQERqlTLLMVSHSL 190
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
696-914 |
3.63e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSlpdsegedpSNPERETAADSDARSRgPVAYASQ 775
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ---------PMSKLSSAAKAELRNQ-KLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLL-NATVEENITFESPFNKQRYKMVIEACSlqpdiDILPH-GDQTQIGERGINLSGGQRQRISVARALYQHTNVVFL 853
Cdd:PRK11629 95 FHHLLpDFTALENVAMPLLIGKKKPAEINSRAL-----EMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642734 854 DDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 914
Cdd:PRK11629 170 DEPTGNLDARNADSIFQL-LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
696-914 |
4.02e-12 |
|
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: 65.81 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEmqkvSGAVFWNSSLPdsegedpsnperetaadsdARSRGPVAYASQ 775
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLP-------------------KFSRNKLIFIDQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 kpwlLNATVEENITFespfnkqrykmvieacslqpdidiLPHGDQTQigergiNLSGGQRQRISVARALYQHT-NVVF-L 853
Cdd:cd03238 68 ----LQFLIDVGLGY------------------------LTLGQKLS------TLSGGELQRVKLASELFSEPpGTLFiL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642734 854 DDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 914
Cdd:cd03238 114 DEPSTGLHQQDINQLL--EVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKV 172
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
686-916 |
4.08e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.71 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLA--------------------TLGEMQKVSGAVFWNssl 743
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTIskILTgllkpqsgeikidgitiskeNLKEIRKKIGIIFQN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 744 PDSEgedpsnperetaadsdarsrgpvayasqkpwLLNATVEENITFeSPFNKQ--RYKM--VIEACSLQPDI-DILPHG 818
Cdd:PRK13632 92 PDNQ-------------------------------FIGATVEDDIAF-GLENKKvpPKKMkdIIDDLAKKVGMeDYLDKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 819 DQtqigergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHAD 898
Cdd:PRK13632 140 PQ--------NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI-MVDLRKTRKKTLISITHDMDEAILAD 210
|
250
....*....|....*...
gi 1958642734 899 WIIAMKDGTIQREGTLKD 916
Cdd:PRK13632 211 KVIVFSEGKLIAQGKPKE 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
688-908 |
4.61e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 688 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSlpdsegedpsnperETAADSDARSR 767
Cdd:PLN03232 1244 YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDC--------------DVAKFGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 GPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 847
Cdd:PLN03232 1310 RVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958642734 848 TNVVFLDDPFSALDVHlSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:PLN03232 1390 SKILVLDEATASVDVR-TDSLIQRTIREEFK--SCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-930 |
5.18e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.86 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQKVSGAVFWnsslpdsEGEDPSNPERetaadSDARSRGPV 770
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVYL-------DGQDIFKMDV-----IELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPwLLNATVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVA 841
Cdd:PRK14247 87 VFQIPNP-IPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDdkRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKD- 916
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKD--MTIVLVTH---FPQQAarisDYVAFLYKGQIVEWGPTREv 232
|
250
....*....|....
gi 1958642734 917 FQRSECQLFEHWKT 930
Cdd:PRK14247 233 FTNPRHELTEKYVT 246
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
689-916 |
5.31e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSS-------LLLATLGEMQkvsgAVFWNSSLPDSEGEDPSNPE------ 755
Cdd:PRK13651 16 LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIE----WIFKDEKNKKKTKEKEKVLEklviqk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 756 ---RETAADSDARSRGPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLqpDIDILPHGDqtqig 824
Cdd:PRK13651 92 trfKKIKKIKEIRRRVGVVFQFAEYQLFEQTIEKDIIF-GPVSmgvskeeaKKRAAKYIELVGL--DESYLQRSP----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 825 ergINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAM 903
Cdd:PRK13651 164 ---FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRTIFF 238
|
250
....*....|....*..
gi 1958642734 904 KDGTIQREG----TLKD 916
Cdd:PRK13651 239 KDGKIIKDGdtydILSD 255
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
691-889 |
5.37e-12 |
|
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: 65.98 E-value: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSlPDSEGEDpsnperetaadSDARSrgpV 770
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDFQRD-----------SIARG---L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPWLLNA-TVEENITFESPFNKQrykmviEACslqpdIDILPHGDQTQIGERGIN-LSGGQRQRISVARALYQHT 848
Cdd:cd03231 76 LYLGHAPGIKTTlSVLENLRFWHADHSD------EQV-----EEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958642734 849 NVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 889
Cdd:cd03231 145 PLWILDEPTTALDKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
692-921 |
6.25e-12 |
|
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: 66.31 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDpsnperETAADSDARSRGPVA 771
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-------GED------ITGLPPHEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLL-NATVEENI----------TFESPFNKQRYKMVIEACSlqpdiDILphgDQTQIGERG----INLSGGQRQ 836
Cdd:cd03219 79 RTFQIPRLFpELTVLENVmvaaqartgsGLLLARARREEREARERAE-----ELL---ERVGLADLAdrpaGELSYGQQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLK 915
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPD 228
|
....*.
gi 1958642734 916 DFQRSE 921
Cdd:cd03219 229 EVRNNP 234
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
378-610 |
9.97e-12 |
|
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: 66.81 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 378 YVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYIL 456
Cdd:cd07346 61 YLAARLGQRVVFDLRRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIGALVILFYLN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 457 GVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEKTRRKEM-TSLRA 535
Cdd:cd07346 139 WKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRdANLRA 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 536 FAVYTSISIFMNTAIPIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd07346 219 ARLSALFSPLIGLLTALGTALVLLYG-GYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
694-916 |
1.23e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.26 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKS-------SLLLATlgemqkvSGAVFwnsslpdSEGEDPSNPERETaadsDARS 766
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKStiakhmnALLIPS-------EGKVY-------VDGLDTSDEENLW----DIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 767 RGPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 838
Cdd:PRK13633 86 KAGMVFQNPDNQIVATIVEEDVAF-GPENlgippeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
830-935 |
1.93e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
90 100
....*....|....*....|....*..
gi 1958642734 909 QREGTLKdfqrsecQLFEHWKTLMNRQ 935
Cdd:PRK11264 223 VEQGPAK-------ALFADPQQPRTRQ 242
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
696-917 |
2.32e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 65.02 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQkvSGAVFWNsslpdseGEDPSNPERETAAdsdARSRgpVAYA 773
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTITVD-------GEDLTDSKKDINK---LRRK--VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQK----PwllNATVEENITfESP-----FNKQrykmviEACSLQpdIDILphgDQTQIGERG----INLSGGQRQRISV 840
Cdd:COG1126 83 FQQfnlfP---HLTVLENVT-LAPikvkkMSKA------EAEERA--MELL---ERVGLADKAdaypAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 916
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELV-----GEVLDVMRDlakEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEE 222
|
.
gi 1958642734 917 F 917
Cdd:COG1126 223 F 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
689-913 |
2.38e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.80 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdsegeDPSNPERETAADSDARSRG 768
Cdd:PRK13645 20 TPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG---------DYAIPANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQKP--WLLNATVEENITFeSPFN-----KQRYKMVIEACSLQPdidiLPhgdQTQIGERGINLSGGQRQRISVA 841
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAF-GPVNlgenkQEAYKKVPELLKLVQ----LP---EDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
698-925 |
2.46e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.28 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEDpsnperetAADSDARSRGpVAYASQKP 777
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF-------IDGED--------VTHRSIQQRD-ICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 778 WLL-NATVEENITF-------ESPFNKQRYKmviEACSLqpdIDILPHGDQ--TQIgerginlSGGQRQRISVARALYQH 847
Cdd:PRK11432 88 ALFpHMSLGENVGYglkmlgvPKEERKQRVK---EALEL---VDLAGFEDRyvDQI-------SGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLF 925
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-930 |
2.93e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQKVSGAVFWNSSLPDSEGEDPSNPERETaadsdarsrGPV 770
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRREV---------GMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 -AYASQKPWLlnaTVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISV 840
Cdd:PRK14267 91 fQYPNPFPHL---TIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 841 ARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHK-LQYLPHADWIIAMKDGTIQREG-TLKD 916
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANI-----DPVGTAKIEELLFELKKeyTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGpTRKV 235
|
250
....*....|....
gi 1958642734 917 FQRSECQLFEHWKT 930
Cdd:PRK14267 236 FENPEHELTEKYVT 249
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
697-898 |
3.07e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 697 SNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgeMQKVSGAVFWNsslpdseGEDpsnperetaadsdaRSRGPVAYAS 774
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLriLAGL--ARPDAGEVLWQ-------GEP--------------IRRQRDEYHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 775 QKPWL--LNA-----TVEENITFespfnkqrykmvieACSLQPDIDilphGDQT-----QIGERGI------NLSGGQRQ 836
Cdd:PRK13538 75 DLLYLghQPGiktelTALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 837 RISVARALYQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTHklQYLPHAD 898
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH--QDLPVAS 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
696-916 |
8.12e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.91 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNperETAADSDARSRgpVAYASQ 775
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-------GVDITD---KKVKLSDIRKK--VGLVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDI--DILPhgdqtqigergINLSGGQRQRISVARA 843
Cdd:PRK13637 91 YPeyQLFEETIEKDIAF-GPINlglseeeiENRVKRAMNIVGLDYEDykDKSP-----------FELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEIL-NKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
698-916 |
8.65e-11 |
|
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: 64.74 E-value: 8.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSLL--LATL-----GEMQkVSGAVFWNSS----LPdsegedpsnPERetaadsdars 766
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLraIAGLerpdsGRIR-LGGEVLQDSArgifLP---------PHR---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 767 RgPVAYASQK----PWLlnaTVEENITF---ESPFNKQRYKM--VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQR 837
Cdd:COG4148 77 R-RIGYVFQEarlfPHL---SVRGNLLYgrkRAPRAERRISFdeVVELLGIGHLLDRRPA-----------TLSGGERQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 838 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKL---QYLphADWIIAMKDGTIQREGT 913
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDLARKAEILP--YLERLRDELDIpILYVSHSLdevARL--ADHVVLLEQGRVVASGP 217
|
...
gi 1958642734 914 LKD 916
Cdd:COG4148 218 LAE 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
689-913 |
1.20e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAV----FWNSslPDSEGEDPSNPERETAADSDA 764
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIG--DKKNNHELITNPYSKKIKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 765 RSRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGG 833
Cdd:PRK13631 113 ELRRRVSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 834 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagileLLRDDK---RTVVLVTHKL-QYLPHADWIIAMKDGTIQ 909
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-----LILDAKannKTVFVITHTMeHVLEVADEVIVMDKGKIL 255
|
....
gi 1958642734 910 REGT 913
Cdd:PRK13631 256 KTGT 259
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
689-918 |
1.67e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPDSegedpSNPERETAAdsdARSRG 768
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS-----TSKQKEIKP---VRKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQKPWLLNATVEENITFeSPFNKQRYKMVIEACSLQpDIDILphGDQTQIGERG-INLSGGQRQRISVARALYQH 847
Cdd:PRK13643 87 GVVFQFPESQLFEETVLKDVAF-GPQNFGIPKEKAEKIAAE-KLEMV--GLADEFWEKSpFELSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQ 918
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDvFQ 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
689-924 |
1.74e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPDSEGEDPS-NPERETaadsdarsr 767
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYiRPVRKR--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 gpVAYASQKP--WLLNATVEENITFeSPFNkqrYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARAL 844
Cdd:PRK13646 87 --IGMVFQFPesQLFEDTVEREIIF-GPKN---FKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSECQ 923
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRL-LKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
.
gi 1958642734 924 L 924
Cdd:PRK13646 240 L 240
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
696-927 |
2.00e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERETAAD---------SDArs 766
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-------GEPLAKLNRAQRKAfrrdiqmvfQDS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 767 rgPVAYASQKP--WLLNATVEENITFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISVARA 843
Cdd:PRK10419 99 --ISAVNPRKTvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVlDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLkdfq 918
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQqfgtACLFITHDLRLVERfCQRVMVMDNGQIVETQPV---- 236
|
....*....
gi 1958642734 919 rSECQLFEH 927
Cdd:PRK10419 237 -GDKLTFSS 244
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
689-890 |
2.09e-10 |
|
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: 64.77 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLATLGEMQKVSGAVFwnsSLPdsegedpsnperetaadsdarSRG 768
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGGRL---TKP---------------------AKG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQKPWLLNATVEENITF-ESPFNKQRYKMvieacSLQPDIDILPHGDQTQIGERGIN----------LSGGQRQR 837
Cdd:TIGR00954 516 KLFYVPQRPYMTLGTLRDQIIYpDSSEDMKRRGL-----SDKDLEQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQR 590
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 838 ISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHK 890
Cdd:TIGR00954 591 IAMARLFYHKPQFAILDECTSAVSVD-----VEGYMYRLCREFGITLFSVSHR 638
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
698-912 |
2.39e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWN----SSLPDSEgedpsnperetaadsdaRSRGPV--A 771
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmNDVPPAE-----------------RGVGMVfqS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQkPWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARAL 844
Cdd:PRK11000 84 YALY-PHL---SVAENMSFglklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 912
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
812-905 |
2.94e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 812 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELLRDDKRTVVLVTHKL 891
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
90
....*....|....
gi 1958642734 892 QYLPHADWIIAMKD 905
Cdd:PTZ00265 641 STIRYANTIFVLSN 654
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
694-927 |
3.72e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.95 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSsLPDSEgedpsnperETAADSdarsRGPVAYA 773
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSE---------ETVWDV----RRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKP--WLLNATVEENITF--EspfNKQ--RYKMV------IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVA 841
Cdd:PRK13635 87 FQNPdnQFVGATVQDDVAFglE---NIGvpREEMVervdqaLRQVGMEDFLNREPH-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKR-TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKdfqrs 920
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVL--ETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPE----- 225
|
....*..
gi 1958642734 921 ecQLFEH 927
Cdd:PRK13635 226 --EIFKS 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
696-889 |
6.07e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 62.02 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMqkvsgavfwnsslPDS-----EGEDPSN-PERETAAdsdARSRg 768
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrCINLLER-------------PTSgsvlvDGVDLTAlSERELRA---ARRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 pVAYASQKPWLLNA-TVEENITFesPF------NKQRYKMVIEACSLqpdIDILPHGDQ--TQigerginLSGGQRQRIS 839
Cdd:COG1135 84 -IGMIFQHFNLLSSrTVAENVAL--PLeiagvpKAEIRKRVAELLEL---VGLSDKADAypSQ-------LSGGQKQRVG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 840 VARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTH 889
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTR-----SILDLLKDINRelglTIVLITH 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
691-913 |
7.91e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQKVSGAVFWNSSL---------PDSEGE---------- 749
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvLRGMDQYEPTSGRIIYHVALcekcgyverPSKVGEpcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 750 -------DPSNPERetaadsdARSRGPVAYASQKPWLL--NATVEENITfeSPFNKQRYKmviEACSLQPDIDILphgDQ 820
Cdd:TIGR03269 91 peevdfwNLSDKLR-------RRIRKRIAIMLQRTFALygDDTVLDNVL--EALEEIGYE---GKEAVGRAVDLI---EM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 821 TQIGER----GINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhLMQAGILELLRDDKRTVVLVTHKLQYLPH 896
Cdd:TIGR03269 156 VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250
....*....|....*...
gi 1958642734 897 -ADWIIAMKDGTIQREGT 913
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGT 252
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
688-908 |
9.02e-10 |
|
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: 60.14 E-value: 9.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 688 WTPDGIPT-LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGemQKVSGAVFWNsslpdseGEDPsnpereTAADSDA 764
Cdd:COG4181 19 GTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLglLAGLD--RPTSGTVRLA-------GQDL------FALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 765 RSR------GPVAYASQkpwLLNA-TVEENITFESPFN-----KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSG 832
Cdd:COG4181 84 RARlrarhvGFVFQSFQ---LLPTlTALENVMLPLELAgrrdaRARARALLERVGLGHRLDHYPAQ-----------LSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 833 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKDGTI 908
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQ-----IIDLLFELNRergtTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
693-911 |
9.18e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.79 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsEGEDPSNPERETAADSDARSRGPVAY 772
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL-------VGQPLHQMDEEARAKLRAKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 773 ASQKPWLLNATveENITFESPFNKQRykmviEACSLQPDIDILphgDQTQIGER----GINLSGGQRQRISVARALYQHT 848
Cdd:PRK10584 96 SFMLIPTLNAL--ENVELPALLRGES-----SRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 849 NVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 911
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADL-LFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
696-921 |
1.35e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.19 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQkvsgavfwnsslPDSEGEDPSNPERETAADSDARSRgPVAYASQ 775
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQ------------PPSEGEILLDAQPLESWSSKAFAR-KVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 K-PWLLNATVEENITF-ESP-------FNKQRYKMVIEACSLqpdIDILPhgdqtqIGERGIN-LSGGQRQRISVARALY 845
Cdd:PRK10575 93 QlPAAEGMTVRELVAIgRYPwhgalgrFGAADREKVEEAISL---VGLKP------LAHRLVDsLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 846 QHTNVVFLDDPFSALDV-HLSDHLmqAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIaHQVDVL--ALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
691-921 |
1.51e-09 |
|
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: 59.23 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPsnpereTAADSDARSRGPV 770
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-------GEDI------TGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQK----PWLlnaTVEENIT--FESPFNKQRYKMVIEACslqpdIDILPhgdqtQIGER----GINLSGGQRQRISV 840
Cdd:COG0410 81 GYVPEGrrifPSL---TVEENLLlgAYARRDRAEVRADLERV-----YELFP-----RLKERrrqrAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 841 ARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDFQR 919
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFE--IIRRLNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
..
gi 1958642734 920 SE 921
Cdd:COG0410 226 DP 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
685-908 |
1.57e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 59.71 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 685 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAtlgemqkVSGAVfwnssLPDS-----EGEDPSN-PERET 758
Cdd:COG1101 11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA-------IAGSL-----PPDSgsiliDGKDVTKlPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 759 AADsdarsrgpVAYASQKPwLL----NATVEENI----------TFESPFNKQRYKMVIEACSlqpDIDI-LPHGDQTQI 823
Cdd:COG1101 79 AKY--------IGRVFQDP-MMgtapSMTIEENLalayrrgkrrGLRRGLTKKRRELFRELLA---TLGLgLENRLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 824 GergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagiL--ELLRDDKRTVVLVTHKLQY-LPHADWI 900
Cdd:COG1101 147 G----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTHNMEQaLDYGNRL 219
|
....*...
gi 1958642734 901 IAMKDGTI 908
Cdd:COG1101 220 IMMHEGRI 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
831-908 |
1.71e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.55 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL---QYLPHAdwIIAM 903
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRElglaVVIVTHDLavaRLLAHR--LLVM 225
|
....*
gi 1958642734 904 KDGTI 908
Cdd:PRK11701 226 KQGRV 230
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
696-913 |
1.76e-09 |
|
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: 59.55 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL---------------GEMQKVSGA------VFWNSSLPdseGEDP-SN 753
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLehidkvIVIDQSPI---GRTPrSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 754 PERETAADSDARS------RGP--------VAYASQK-PWLLNATVEENITFESPFNKQRYKmvieacsLQPDIDIlphG 818
Cdd:cd03271 88 PATYTGVFDEIRElfcevcKGKrynretleVRYKGKSiADVLDMTVEEALEFFENIPKIARK-------LQTLCDV---G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 819 -DQTQIGERGINLSGGQRQRISVARALYQ---HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL 894
Cdd:cd03271 158 lGYIKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLE--VLQRLVDKGNTVVVIEHNLDVI 235
|
250 260
....*....|....*....|....*
gi 1958642734 895 PHADWIIAM------KDGTIQREGT 913
Cdd:cd03271 236 KCADWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
696-912 |
1.87e-09 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 58.74 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGqLTMIVGQVGCGKSSLL--LATLgeMQKVSGAVFWNsslpdseGEDPSNPERETaadsdarsRGPVAYA 773
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMriLATL--TPPSSGTIRID-------GQDVLKQPQKL--------RRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKP-WLLNATVEENITF-------ESPFNKQRYKMVIEAcslqpdIDILPHGDQtQIGErginLSGGQRQRISVARALY 845
Cdd:cd03264 78 PQEFgVYPNFTVREFLDYiawlkgiPSKEVKARVDEVLEL------VNLGDRAKK-KIGS----LSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 846 QHTNVVFLDDPFSALD----VHLSDHLMQAGilellrdDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 912
Cdd:cd03264 147 GDPSILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
830-917 |
2.65e-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: 60.85 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL----QYlphADWII 901
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLgvvrRF---ADRVA 228
|
90
....*....|....*.
gi 1958642734 902 AMKDGTIQREGTLKDF 917
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
831-913 |
2.98e-09 |
|
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: 58.15 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDG 906
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHG 208
|
....*..
gi 1958642734 907 TIQREGT 913
Cdd:cd03265 209 RIIAEGT 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
699-912 |
5.23e-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: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpDSEGEDPSNPEREtaadsdARSRGPVAYASQK-- 776
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-------TVDGFDVVKEPAE------ARRRLGFVSDSTGly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 777 PWLlnaTVEENITFESPFN-------KQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARALYQHTN 849
Cdd:cd03266 91 DRL---TARENLEYFAGLYglkgdelTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 850 VVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 912
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
696-928 |
6.33e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 57.72 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-------LATLGEMQkVSGAVFWNSSLPDsegedpsnperetaaDSDARS-R 767
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLrvlnlleMPRSGTLN-IAGNHFDFSKTPS---------------DKAIRElR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 GPVAYASQK----PWLlnaTVEENITfESPFN---------KQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQ 834
Cdd:PRK11124 82 RNVGMVFQQynlwPHL---TVQQNLI-EAPCRvlglskdqaLARAEKLLERLRLKPYADRFP-----------LHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 835 RQRISVARALYQHTNVVFLDDPFSALD-------VHLSDHLMQAGIlellrddkrTVVLVTHKLQYLPH-ADWIIAMKDG 906
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAETGI---------TQVIVTHEVEVARKtASRVVYMENG 217
|
250 260
....*....|....*....|..
gi 1958642734 907 TIQREGTLKDFQRSECQLFEHW 928
Cdd:PRK11124 218 HIVEQGDASCFTQPQTEAFKNY 239
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
830-906 |
6.75e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 57.93 E-value: 6.75e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 906
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINL-MLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
696-921 |
8.53e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ--------KVSGAVFWNsslpdseGEdpsnPERETAADSDARSR 767
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLN-------GE----PLAAIDAPRLARLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 GPVAYASQKPWLLnaTVEENITFespfnkQRYKMVIEACSL-QPDIDILPH-----GDQTQIGERGINLSGGQRQRISVA 841
Cdd:PRK13547 86 AVLPQAAQPAFAF--SAREIVLL------GRYPHARRAGALtHRDGEIAWQalalaGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 842 RALYQ---------HTNVVFLDDPFSALDV-HlsDHLMQAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQR 910
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDLaH--QHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVA 235
|
250
....*....|.
gi 1958642734 911 EGTLKDFQRSE 921
Cdd:PRK13547 236 HGAPADVLTPA 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-913 |
9.20e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.36 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ----KVSGAVFWNsslpdseGEDpsnperetAADSDA-RSRG 768
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvLNRLIEIYdskiKVDGKVLYF-------GKD--------IFQIDAiKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQKP-WLLNATVEENITFesPF------NKQRYKMVIEACSLQPDIDILPHgdqTQIGERGINLSGGQRQRISVA 841
Cdd:PRK14246 91 EVGMVFQQPnPFPHLSIYDNIAY--PLkshgikEKREIKKIVEECLRKVGLWKEVY---DRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVhLSDHLMQAGILELlrDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 913
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDI-VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
696-913 |
1.03e-08 |
|
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: 59.26 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL---------------GEMQKVSGA------VFWNSSLPdseGEDP-SN 753
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanrlngaktvpGRYTSIEGLehldkvIHIDQSPI---GRTPrSN 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 754 PERET----------AADSDARSRGpvaYaSQKPWLLNA--------------TVEEN------ITFES----PFNKQ-- 797
Cdd:TIGR00630 701 PATYTgvfdeirelfAETPEAKVRG---Y-TPGRFSFNVkggrceacqgdgviKIEMHflpdvyVPCEVckgkRYNREtl 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 798 --RYK---------MVI-EACSLQPDIDILPHGDQT---------QIGERGINLSGGQRQRISVARALYQ---HTNVVFL 853
Cdd:TIGR00630 777 evKYKgkniadvldMTVeEAYEFFEAVPSISRKLQTlcdvglgyiRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYIL 856
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 854 DDPFSALdvHLSD--HLMQagILELLRDDKRTVVLVTHKLQYLPHADWII------AMKDGTIQREGT 913
Cdd:TIGR00630 857 DEPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKTADYIIdlgpegGDGGGTVVASGT 920
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
696-908 |
1.13e-08 |
|
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: 55.90 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGED--PSNPeretaadSDARSRGpVAYA 773
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-------GKPvtRRSP-------RDAIRAG-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 S----QKPWLLNATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQHTN 849
Cdd:cd03215 81 PedrkREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 850 VVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
694-918 |
1.30e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.08 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPsnPERETAADSDARSRGPVAYA 773
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD-------GENI--PAMSRSRLYTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SqKPWLLNATVEENITF--------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 845
Cdd:PRK11831 92 S-GALFTDMNVFDNVAYplrehtqlPAPLLHSTVMMKLEAVGLRGAAKLMPS-----------ELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 846 QHTNVVFLDDPFSALD-------VHLSDHLMQA-GIlellrddkrTVVLVTHKL-QYLPHAD--WIIAmkDGTIQREGTL 914
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDpitmgvlVKLISELNSAlGV---------TCVVVSHDVpEVLSIADhaYIVA--DKKIVAHGSA 228
|
....
gi 1958642734 915 KDFQ 918
Cdd:PRK11831 229 QALQ 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
696-916 |
1.42e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.12 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEdPSNPE--RETaadsdarsRGPVAYA 773
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL-------IRGE-PITKEniREV--------RKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 843
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAF-GPINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 844 LYQHTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEE 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
696-891 |
1.62e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSL--LLAtlGEMQKVSGAVFWNsslpdseGE--DPSNPeretaadSDARSRGpVA 771
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLmkILY--GLYQPDSGEILID-------GKpvRIRSP-------RDAIALG-IG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLLNA-TVEENI------TFESPFNKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQRQRISVARAL 844
Cdd:COG3845 84 MVHQHFMLVPNlTVAENIvlglepTKGGRLDRKAARARIRELSERYGLDVDPD---AKVED----LSVGEQQRVEILKAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL 891
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKL 201
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
696-921 |
1.63e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsslpdsegedPSNPERETAADS-DARSRGPVAYAS 774
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV-------------KIDGELLTAENVwNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 775 QKPWLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHTNV 850
Cdd:PRK13642 90 PDNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDF-----KTREPAR---LSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 851 VFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 921
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRV-IHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSElFATSE 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
691-907 |
1.78e-08 |
|
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: 54.38 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPdsegedpsnperetaadsdarsrgpV 770
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-------------------------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHTNV 850
Cdd:cd03221 66 GYFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 851 VFLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGT 907
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEA-----LKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
694-921 |
2.17e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEdpsnperETAADSDARSRGPVAYA 773
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII-------IDGD-------LLTEENVWDIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKP--WLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQH 847
Cdd:PRK13650 87 FQNPdnQFVGATVEDDVAFglenKGIPHEEMKERVNEALELVGMQDF-----KEREPAR---LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 848 TNVVFLDDPFSALDvhlsdhlmQAGILELLRDDKR-------TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQR 919
Cdd:PRK13650 159 PKIIILDEATSMLD--------PEGRLELIKTIKGirddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRElFSR 230
|
..
gi 1958642734 920 SE 921
Cdd:PRK13650 231 GN 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
689-921 |
2.80e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.29 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPDSegedpsnpereTAADSDARS-R 767
Cdd:PRK13649 16 TPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS-----------TSKNKDIKQiR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 GPVAYASQKP--WLLNATVEENITFeSPFNKQRYKmvIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 845
Cdd:PRK13649 85 KKVGLVFQFPesQLFEETVLKDVAF-GPQNFGVSQ--EEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 846 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQRSE 921
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDiFQDVD 237
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
696-903 |
3.08e-08 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 55.34 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL-GEMQK-----VSGAV---FWNSSLPDS---EGEDPS-NPERETAADS 762
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyAEGQRryvesLSAYArqfLGQMDKPDVdsiEGLSPAiAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 763 DARSRGPVAYASQKPWLLNATVeeNItfespfnKQRYKMVIEacslqpdidilphgdqtqIG------ERGIN-LSGGQR 835
Cdd:cd03270 91 PRSTVGTVTEIYDYLRLLFARV--GI-------RERLGFLVD------------------VGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 836 QRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 903
Cdd:cd03270 144 QRIRLATQIgSGLTGVLYvLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
696-913 |
3.58e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEDPSNperetAADSDARS--RGPVAYA 773
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL-------IDGVDIAK-----ISDAELREvrRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKPWLL-NATVEENITFESPFN----KQRYKMVIEACSlQPDIDILPHGDQTQigerginLSGGQRQRISVARALYQHT 848
Cdd:PRK10070 112 FQSFALMpHMTVLDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642734 849 NVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
692-912 |
5.05e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEdpsnpERETAADSDARSRGpVA 771
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-------GQ-----EMRFASTTAALAAG-VA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLL-NATVEENI---TFESPFNKQRYKMVIEACSLQPD---IDILPhgdQTQIGErginLSGGQRQRISVARAL 844
Cdd:PRK11288 83 IIYQELHLVpEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEhlgVDIDP---DTPLKY----LSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLqylphaDWIIAMKDG-TIQREG 912
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
690-913 |
5.66e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFwnsslpdSEGEDPSnpereTAADSDARSRgp 769
Cdd:PLN03130 1249 PELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL-------IDGCDIS-----KFGLMDLRKV-- 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 846
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESlerAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 847 HTNVVFLDDPFSALDVHlSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 913
Cdd:PLN03130 1392 RSKILVLDEATAAVDVR-TDALIQKTIREEFK--SCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDT 1455
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
830-912 |
5.79e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.71 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 908
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
|
....
gi 1958642734 909 QREG 912
Cdd:PRK09493 215 AEDG 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
692-889 |
6.00e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 55.96 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQKVSGAVFWNsslpdseGEDPsnpereTAADSDA--RSRG 768
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrCINLLE-RPTSGRVLVD-------GQDL------TALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQKPWLLNA-TVEENITFespfnkqrykmvieacSLQpdidiLPHGDQTQIGER--------GI---------NL 830
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNVAL----------------PLE-----LAGTPKAEIKARvtellelvGLsdkadrypaQL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTH 889
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITH 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
693-920 |
7.95e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPDSEGEDPSNPERETAADSDaRSRGP-VA 771
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMR-HVRGAdMA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWL-LNA--TVEENITfESPFNKQ---RYKMVIEACSLQPDIDIlPHGdQTQIGERGINLSGGQRQRISVARALY 845
Cdd:PRK10261 108 MIFQEPMTsLNPvfTVGEQIA-ESIRLHQgasREEAMVEAKRMLDQVRI-PEA-QTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 846 QHTNVVFLDDPFSALDVhlsdhLMQAGILELLR----DDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 920
Cdd:PRK10261 185 CRPAVLIADEPTTALDV-----TIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
691-925 |
1.06e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIP-TLSNITIRIPRGQLTMIVGQVGCGKSSLLLaTLGEMQKVSGavfwnsslpdseGEDPSNpERETAADSDARSRGP 769
Cdd:PTZ00243 1320 EGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLL-TFMRMVEVCG------------GEIRVN-GREIGAYGLRELRRQ 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPWLLNATVEENItfeSPFNKQRYKMV---IEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 846
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNV---DPFLEASSAEVwaaLELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 847 HTNVVFLDDPFSALDVHLSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLF 925
Cdd:PTZ00243 1463 KGSGFILMDEATANIDPALDRQIQATVMSAF--SAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
691-861 |
1.10e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.42 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLA---TLGEMQKVSGAVFWNSslpdsegedpsnperETAADSDARSR 767
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanRTEGNVSVEGDIHYNG---------------IPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 768 GPVAYASQK----PWLlnaTVEENITFespfnkqrykmvieACSLQpdidilphGDQTQigeRGInlSGGQRQRISVARA 843
Cdd:cd03233 83 GEIIYVSEEdvhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEA 132
|
170
....*....|....*...
gi 1958642734 844 LYQHTNVVFLDDPFSALD 861
Cdd:cd03233 133 LVSRASVLCWDNSTRGLD 150
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
698-920 |
1.30e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGeMQKVSGAVFWNS-SLPDSEGEDPSNPERETAADSDarsrgpVAYASQK 776
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMAEKlEFNGQDLQRISEKERRNLVGAE------VAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 777 PWL-LNA--TVEENI-----TFESPFNKQRYKMVIEACSLQ--PD----IDILPHgdqtqigergiNLSGGQRQRISVAR 842
Cdd:PRK11022 98 PMTsLNPcyTVGFQImeaikVHQGGNKKTRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 843 ALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELL----RDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 917
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDV-----TIQAQIIELLlelqQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
...
gi 1958642734 918 QRS 920
Cdd:PRK11022 242 FRA 244
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
703-900 |
2.10e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.14 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 703 IPR-GQLTMIVGQVGCGKSSLLLATLGEMQ----KVSGAVFWNSSLPDSEGEDPSNpERETAADSDARSRGPVAYASQKP 777
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKpnlgKFDDPPDWDEILDEFRGSELQN-YFTKLLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 778 WLLNATVEENITFESPFNKQRYkmVIEACSLQPdidilphgdqtqIGERGI-NLSGGQRQRISVARALYQHTNVVFLDDP 856
Cdd:cd03236 101 KAVKGKVGELLKKKDERGKLDE--LVDQLELRH------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958642734 857 FSALDVHlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWI 900
Cdd:cd03236 167 SSYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
691-919 |
2.13e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.69 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPdsegedpsnperetaadsdarsrgpV 770
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK-------------------------I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPWLL--NATVEENItfeSPFNKQRYKMVIEACsLQpdiDILPHGDQ--TQIGergiNLSGGQRQRISVARALYQ 846
Cdd:COG0488 381 GYFDQHQEELdpDKTVLDEL---RDGAPGGTEQEVRGY-LG---RFLFSGDDafKPVG----VLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 847 HTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ-REGTLKDFQR 919
Cdd:COG0488 450 PPNVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHdryfldRV-----ATRILEFEDGGVReYPGGYDDYLE 519
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
830-916 |
2.31e-07 |
|
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: 53.16 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP----HAdwiIAMKD 905
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAL-LDKLAAEGAPTLVLVTHHVEEIPpgitHV---LLLKD 218
|
90
....*....|.
gi 1958642734 906 GTIQREGTLKD 916
Cdd:COG1119 219 GRVVAAGPKEE 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
696-906 |
3.90e-07 |
|
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: 51.90 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPDSEGEDPSN--PEretaadsdarSRGpvAYA 773
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylPE----------ERG--LYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SQKpwllnatVEENITFESpfnkQRYKMVIEACSLQPD-----IDILPHGDQtQIGErginLSGGQRQRISVARALYQHT 848
Cdd:cd03269 84 KMK-------VIDQLVYLA----QLKGLKKEEARRRIDewlerLELSEYANK-RVEE----LSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 849 NVVFLDDPFSALDVHLSDHLMQAgILElLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 906
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDV-IRE-LARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
831-894 |
4.11e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 4.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 831 SGGQRQRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRtvvlvTHKLQYL 894
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSL-----DKTVQAQILALLKSLQQ-----KHQLAYL 480
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
830-913 |
4.75e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.92 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTI 908
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLEIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
....*
gi 1958642734 909 QREGT 913
Cdd:PRK11650 214 EQIGT 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
696-941 |
5.40e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.53 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQKVSGAVFWNSS-----LPDSEGEDPSNPERETAADSDARSRG 768
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLkiLA--GELEPDSGEVSIPKGlrigyLPQEPPLDDDLTVLDTVLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVA---YASQKPWLLNATVEENITFESPFNkqrykmVIEACSLQPDIDI------LPHGDQTQ-IGErginLSGGQRQRI 838
Cdd:COG0488 92 LEAeleELEAKLAEPDEDLERLAELQEEFE------ALGGWEAEARAEEilsglgFPEEDLDRpVSE----LSGGWRRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 839 SVARALYQHTNVVFLDDPFSALDVHlsdhlmqaGIL---ELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ 909
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLE--------SIEwleEFLKNYPGTVLVVSHdryfldRV-----ATRILELDRGKLT 228
|
250 260 270
....*....|....*....|....*....|...
gi 1958642734 910 R-EGTLKDFQRSECQLFEHWKTLMNRQDQELEK 941
Cdd:COG0488 229 LyPGNYSAYLEQRAERLEQEAAAYAKQQKKIAK 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
692-921 |
5.81e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllatlgeMQKVSGAVfwnssLPDSeGEDPSNPERET-AADSDARSRGpV 770
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTL-------MKIIAGIV-----PPDS-GTLEIGGNPCArLTPAKAHQLG-I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 771 AYASQKPWLL-NATVEENITFESPFNKQRYKMVIE-----ACSLQPDIdilphgdqtQIGergiNLSGGQRQRISVARAL 844
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDS---------SAG----SLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSE 921
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDD 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
826-912 |
5.91e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.99 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 826 RGIN--LSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsDHL-MQAGILELLRDDKRTVVLVTHKLQYLPH--ADWI 900
Cdd:cd03217 99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRV 175
|
90
....*....|..
gi 1958642734 901 IAMKDGTIQREG 912
Cdd:cd03217 176 HVLYDGRIVKSG 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
693-892 |
8.57e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 51.18 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPSNPERETAAdsdarsRGPVAY 772
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-------GLVPWKRRKKFLR------RIGVVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 773 A--SQKPWLLNA----TVEENITFESPFnkqRYKMVIEACSlqpdiDILPHGDQTQIGERgiNLSGGQRQRISVARALYQ 846
Cdd:cd03267 101 GqkTQLWWDLPVidsfYLLAAIYDLPPA---RFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLH 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958642734 847 HTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQ 892
Cdd:cd03267 171 EPEILFLDEPTIGLDVV-AQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
696-916 |
9.29e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.75 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLllatlgeMQKVSGAVFWNSSLPDSEGEDpSNPERETAADSDARSRGPVAYASQ 775
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTL-------MQHFNALLKPSSGTITIAGYH-ITPETGNKNLKKLRKKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALYQH 847
Cdd:PRK13641 95 EAQLFENTVLKDVEF-GPKNfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHLMQagileLLRDDKR---TVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 916
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQ-----LFKDYQKaghTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKE 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
691-906 |
9.92e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlatlgemqKV----------SGAVFWN------SSLPDSEgedpsnp 754
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLM--------KVlsgvyphgtyEGEIIFEgeelqaSNIRDTE------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 755 eretaadsdarsRGPVAYASQKPWLL-NATVEENItF---E-SPFNKQRY-KMVIEACSL--QPDIDILPHgdqTQIGer 826
Cdd:PRK13549 81 ------------RAGIAIIHQELALVkELSVLENI-FlgnEiTPGGIMDYdAMYLRAQKLlaQLKLDINPA---TPVG-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 827 giNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLmqagiLELLRDDKR---TVVLVTHKLQYLPH-ADWIIA 902
Cdd:PRK13549 143 --NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVL-----LDIIRDLKAhgiACIYISHKLNEVKAiSDTICV 215
|
....
gi 1958642734 903 MKDG 906
Cdd:PRK13549 216 IRDG 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
696-889 |
1.04e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.73 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNssLPDsegeDPSNPEReTAADSDARsRGPVAYASQ 775
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--VPD----NQFGREA-SLIDAIGR-KGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 kpwLLNAT-VEENITFESPFNkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHTNVVFLD 854
Cdd:COG2401 118 ---LLNAVgLSDAVLWLRRFK---------------------------------ELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1958642734 855 DPFSALDVHLSdHLMQAGILELLRDDKRTVVLVTH 889
Cdd:COG2401 162 EFCSHLDRQTA-KRVARNLQKLARRAGITLVVATH 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
644-891 |
1.04e-06 |
|
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: 53.09 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 644 KVVNRKRPAREEVRDLLGP-------LQRLTPstdGDADNFCVQIIGGFFTwtPDGIPTLSNITIRIPRGQLTMIVGQVG 716
Cdd:TIGR01257 892 RALEKTEPLTEEMEDPEHPegindsfFERELP---GLVPGVCVKNLVKIFE--PSGRPAVDRLNITFYENQITAFLGHNG 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 717 CGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPsnperETAADSDARSRGpvaYASQKPWLLN-ATVEENITFESPFN 795
Cdd:TIGR01257 967 AGKTTTLSILTGLLPPTSGTVLVG-------GKDI-----ETNLDAVRQSLG---MCPQHNILFHhLTVAEHILFYAQLK 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 796 KQRYkmviEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILE 875
Cdd:TIGR01257 1032 GRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY-----SRRSIWD 1102
|
250
....*....|....*...
gi 1958642734 876 LLRDDK--RTVVLVTHKL 891
Cdd:TIGR01257 1103 LLLKYRsgRTIIMSTHHM 1120
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
694-919 |
1.15e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEM----QKVSGAVfwnssLPDSEgedpsnpereTAADSDARSRgP 769
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRV-----LLDGK----------PVAPCALRGR-K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPwllnatveenitfESPFNKQRyKM---VIEAC---SLQPDIDILPH-------GDQTQIGER-GINLSGGQR 835
Cdd:PRK10418 81 IATIMQNP-------------RSAFNPLH-TMhthARETClalGKPADDATLTAaleavglENAARVLKLyPFEMSGGML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 836 QRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRT----VVLVTHKLQYLPH-ADWIIAMKDGTIQR 910
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDV-----VAQARILDLLESIVQKralgMLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
250
....*....|
gi 1958642734 911 EGTLKD-FQR 919
Cdd:PRK10418 222 QGDVETlFNA 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
830-906 |
1.17e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMK 904
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 1958642734 905 DG 906
Cdd:PRK15134 232 NG 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
691-906 |
1.32e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.13 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQKVSGAVFWNSSlpdsegedpsnpERETAADSDARSRG 768
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYWSGS------------PLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 769 PVAYASQKPWLLNATVEENI----TFESPFNKQRYKMVIEACS---LQPDIDILPhgDQTQIGERGinlsGGQRQRISVA 841
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKnllRELQLDADN--VTRPVGDYG----GGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 906
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETE-----ILLDIIRDLKAhgvACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
705-889 |
1.33e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.91 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 705 RGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdsegedpsNPERETAADSDARSrgpvayasqkpwllnatv 784
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI------------DGEDILEEVLDQLL------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 785 eenitfespfnkqrykmvieacslqpdidilphgdQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHL 864
Cdd:smart00382 51 -----------------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQ 95
|
170 180
....*....|....*....|....*....
gi 1958642734 865 SDHLMQAGILELL----RDDKRTVVLVTH 889
Cdd:smart00382 96 EALLLLLEELRLLlllkSEKNLTVILTTN 124
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
683-882 |
2.09e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.78 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 683 GGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPDSEGEDPSNPER------ 756
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRrdiqfi 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 757 --ETAADSDARSrgPVAYASQKPWLLNATVEENITfespfnKQRYKMVIEACSLQPDIDI-LPHgdqtqigergiNLSGG 833
Cdd:PRK10261 407 fqDPYASLDPRQ--TVGDSIMEPLRVHGLLPGKAA------AARVAWLLERVGLLPEHAWrYPH-----------EFSGG 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958642734 834 QRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR 882
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSI-----RGQIINLLLDLQR 511
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
693-913 |
2.51e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSlpDSEGEDPSNPERETAAdsdARSRGPVAY 772
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK--DITDWQTAKIMREAVA---IVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 773 ASQkpwllnaTVEENITFESPF-NKQRYKMVIEACslqpdIDILPHGDQTQIgERGINLSGGQRQRISVARALYQHTNVV 851
Cdd:PRK11614 93 SRM-------TVEENLAMGGFFaERDQFQERIKWV-----YELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 852 FLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 913
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFD--TIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
696-889 |
2.87e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.20 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlatlgemqkvsgAVFWNSSLPDSEGeDPS---NPERETAADSDARSrgpvAY 772
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLM------------NALAFRSPKGVKG-SGSvllNGMPIDAKEMRAIS----AY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 773 ASQKPWLLNA-TVEENITFESPF----------NKQRYKMVIEACSLQPDIDILphgdqTQIGERGINLSGGQRQRISVA 841
Cdd:TIGR00955 104 VQQDDLFIPTlTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCANTR-----IGVPGRVKGLSGGERKRLAFA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTH 889
Cdd:TIGR00955 179 SELLTDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
692-916 |
5.61e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdsegedpsNPERETAADSDARSRGpVA 771
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN------------NINYNKLDHKLAAQLG-IG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLLNA-TVEENI--------------TFESPFNKQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQ 836
Cdd:PRK09700 84 IIYQELSVIDElTVLENLyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 837 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLK 915
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVS 230
|
.
gi 1958642734 916 D 916
Cdd:PRK09700 231 D 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
831-891 |
8.88e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 8.88e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTHKL 891
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
696-861 |
1.10e-05 |
|
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: 47.92 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPsnpereTAADSDARSRGPVAYASQ 775
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD-------GQDI------TKLPMHKRARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLL-NATVEENI--TFESpFNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNVVF 852
Cdd:cd03218 83 EASIFrKLTVEENIlaVLEI-RGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLL 156
|
....*....
gi 1958642734 853 LDDPFSALD 861
Cdd:cd03218 157 LDEPFAGVD 165
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
825-921 |
1.43e-05 |
|
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: 49.24 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 825 ERGIN-LSGGQRQRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWII 901
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGL--HQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|....*.
gi 1958642734 902 AM------KDGTIQREGTLKDFQRSE 921
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEILANP 586
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
706-916 |
1.64e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.48 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 706 GQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSlPDSEGEDPSNPERETAADSD-ARSRGPVAYASQkpwLLNATV 784
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-PLHFGDYSYRSQRIRMIFQDpSTSLNPRQRISQ---ILDFPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 785 EENITFESPFNKQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVH 863
Cdd:PRK15112 115 RLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 864 LSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 916
Cdd:PRK15112 184 MRSQLINL-MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
828-889 |
2.47e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 2.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 828 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTH 889
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE-----GILRLFEEFNRvgvTVLMATH 195
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
698-889 |
3.04e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 47.11 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnsSLPDSegedpSNPEREtaadSDARSRGPVA--YASQ 775
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI----SLCGE-----PVPSRA----RHARQRVGVVpqFDNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPwllNATVEENI-TFESPFN------KQRYKMVIEACSLQPDIDilphgdqTQIGErginLSGGQRQRISVARALYQHT 848
Cdd:PRK13537 92 DP---DFTVRENLlVFGRYFGlsaaaaRALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958642734 849 NVVFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 889
Cdd:PRK13537 158 DVLVLDEPTTGLDPQ-ARHLMWERLRSLLARGK-TILLTTH 196
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
820-912 |
4.66e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 820 QTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRD--DKRTVVLVTHKL-QYLPH 896
Cdd:PRK14271 154 KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK-----IEEFIRSlaDRLTVIIVTHNLaQAARI 228
|
90
....*....|....*.
gi 1958642734 897 ADWIIAMKDGTIQREG 912
Cdd:PRK14271 229 SDRAALFFDGRLVEEG 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
828-914 |
6.04e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.41 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 828 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVL-VTHKLQYLPH-ADWIIAMKD 905
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQ 204
|
....*....
gi 1958642734 906 GTIQREGTL 914
Cdd:PRK11144 205 GKVKAFGPL 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
711-911 |
8.10e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.16 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 711 IVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGE--DPSNPeretaadSDARSRGpVAYAS----QKPWLLNATV 784
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLD-------GKpvRIRSP-------RDAIRAG-IAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 785 EENITFeSPFNKQRYKMVI-------EACSLQPDIDILPHGDQTQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPF 857
Cdd:COG1129 348 RENITL-ASLDRLSRGGLLdrrreraLAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 858 SALDVhlsdhlmqaG----ILELLR---DDKRTVVLVThklQYLP----HADWIIAMKDGTIQRE 911
Cdd:COG1129 423 RGIDV---------GakaeIYRLIRelaAEGKAVIVIS---SELPellgLSDRILVMREGRIVGE 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
692-906 |
8.93e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWnsslpdsegedpSNPERETAADSDARSRGPVA 771
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF------------QGKEIDFKSSKEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQKPWLLNATVEENITF-----ESPFNKQRyKMVIEACSL--QPDIDILPHgdqtqigERGINLSGGQRQRISVARAL 844
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLgryptKGMFVDQD-KMYRDTKAIfdELDIDIDPR-------AKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 845 YQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDG 906
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMeEIFQLCDEITILRDG 210
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
696-861 |
9.03e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQK----VSGAVFWNSSLPDsegedpsnperetaaDSDARSRGPVA 771
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfhigVEGVITYDGITPE---------------EIKKHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 772 YASQK----PWLlnaTVEENITF----ESPFNkqRYKMVIEACSLQPDIDI------LPHGDQTQIGE---RGInlSGGQ 834
Cdd:TIGR00956 142 YNAETdvhfPHL---TVGETLDFaarcKTPQN--RPDGVSREEYAKHIADVymatygLSHTRNTKVGNdfvRGV--SGGE 214
|
170 180
....*....|....*....|....*..
gi 1958642734 835 RQRISVARALYQHTNVVFLDDPFSALD 861
Cdd:TIGR00956 215 RKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
391-608 |
9.94e-05 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 45.49 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 391 IQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYI---LGVSALIGAAV 466
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTsALTVLVRDPLTVIGLLGVLFYLdwkLTLIALVVLPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 467 IILlaPVQYFvATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FCSRVEKTRRKEMTSLRAFAVYTSI 542
Cdd:cd18552 152 AAL--PIRRI-GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSSPL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642734 543 SIFMnTAIPIAAVLItFVGHVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18552 229 MELL-GAIAIALVLW-YGGYQVI--SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
828-891 |
1.03e-04 |
|
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: 44.10 E-value: 1.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 828 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL 891
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA-IRRLSEEGKKTALVVEHDL 132
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
699-908 |
1.12e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnssLPDSEGEDPSNPERETAAD-----SDARSRGPVAYA 773
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV-----YLDGKPIDIRSPRDAIRAGimlcpEDRKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 774 SqkpwllnatVEENITFESPFNKQRYKMVI----EACSLQPDIDIL----PHGDQtQIGergiNLSGGQRQRISVARALY 845
Cdd:PRK11288 347 S---------VADNINISARRHHLRAGCLInnrwEAENADRFIRSLniktPSREQ-LIM----NLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 846 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 908
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYN--VIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRI 474
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
827-892 |
1.14e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 1.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 827 GINLSGGQRQRISVARALYQHTNVVFLDDPFSALD-VHLSDhlmQAGILELLRDDKRTVVLVTHKLQ 892
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVR 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
696-893 |
1.21e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPdsegedpsnperetaadsdarsrgpVAYASQ 775
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLE-------------------------VAYFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLLNA--TVEENITfESpfnKQ------RYKMVIEacSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQH 847
Cdd:PRK11147 390 HRAELDPekTVMDNLA-EG---KQevmvngRPRHVLG--YLQ---DFLFHPKRAMTPVKA--LSGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958642734 848 TNVVFLDDPFSALDVHLSDHLMqagilELLRDDKRTVVLVTHKLQY 893
Cdd:PRK11147 459 SNLLILDEPTNDLDVETLELLE-----ELLDSYQGTVLLVSHDRQF 499
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
698-916 |
1.46e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.55 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGED--PSNPeretaadSDARSRGpVAYASQ 775
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN-------GKDisPRSP-------LDAVKKG-MAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KP----WLLNATVEENITFESPFNKQRYKMVI----------EACSLQPDIDILPHGDQTQIGErginLSGGQRQRISVA 841
Cdd:PRK09700 346 SRrdngFFPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCHSVNQNITE----LSGGNQQKVLIS 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 842 RALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLR---DDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 916
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVG-----AKAEIYKVMRqlaDDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
830-889 |
1.71e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 44.82 E-value: 1.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 889
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
696-891 |
1.79e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 44.33 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSSLPdsegedpsnperetaadsdarsrgpVAYASQ 775
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLR-------------------------IGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 776 KPWLlNATVeenitfesPFNKQRYKMvieacsLQPDI---DILPHGDQTQIGERgIN-----LSGGQRQRISVARALYQH 847
Cdd:PRK09544 75 KLYL-DTTL--------PLTVNRFLR------LRPGTkkeDILPALKRVQAGHL-IDapmqkLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958642734 848 TNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRT----VVLVTHKL 891
Cdd:PRK09544 139 PQLLVLDEPTQGVDVN-----GQVALYDLIDQLRREldcaVLMVSHDL 181
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
783-861 |
1.88e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 44.25 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 783 TVEENI-----TFESPFNKQRYKMVieacSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNVVFLDDPF 857
Cdd:COG1137 94 TVEDNIlavleLRKLSKKEREERLE----ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
....
gi 1958642734 858 SALD 861
Cdd:COG1137 165 AGVD 168
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
830-904 |
1.99e-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: 43.12 E-value: 1.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958642734 830 LSGGQRQRISVARAL----YQHTNVVFLDDPFSALDvhLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMK 904
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLD--PRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
445-561 |
2.74e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 44.04 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 445 IIVGVILLYY--ILGVSALIGAAVIILLApvqYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAW 514
Cdd:cd18555 130 VIYLIYMLYYspLLTLIVLLLGLLIVLLL---LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKslgsekniYKKW 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1958642734 515 ENIFCSRVEKTRRKEMTSlrafAVYTSISIFMNTAIPIaavLITFVG 561
Cdd:cd18555 207 ENLFKKQLKAFKKKERLS----NILNSISSSIQFIAPL---LILWIG 246
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
708-889 |
2.86e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.41 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 708 LTMIVGQVGCGKSSLLLAtlgemqkVSGAVFWNSSLPDSEGEDPS--NPERETAadsdarsrgpvayasqkpwllnatve 785
Cdd:cd03279 30 LFLICGPTGAGKSTILDA-------ITYALYGKTPRYGRQENLRSvfAPGEDTA-------------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 786 eNITFESPFNKQRYKmVIEACSLQPD----IDILPHGDQTQIGERGI-NLSGGQRQRISVARAL------YQHTNVV--- 851
Cdd:cd03279 77 -EVSFTFQLGGKKYR-VERSRGLDYDqftrIVLLPQGEFDRFLARPVsTLSGGETFLASLSLALalsevlQNRGGARlea 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958642734 852 -FLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTH 889
Cdd:cd03279 155 lFIDEGFGTLDPEALEAVATA--LELIRTENRMVGVISH 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
829-900 |
2.90e-04 |
|
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: 44.54 E-value: 2.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 829 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWI 900
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH-----LQEYPGTVVAVTHDRYFLDNvAGWI 228
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
779-914 |
7.49e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 779 LLNATVEE-NITFesPFNKQrykmvIEAcSLQPDIDI----LPhgdqtqIGERGINLSGGQRQRISVARALY---QHTNV 850
Cdd:PRK00635 1658 LLQTPIEEvAETF--PFLKK-----IQK-PLQALIDNglgyLP------LGQNLSSLSLSEKIAIKIAKFLYlppKHPTL 1723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 851 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 914
Cdd:PRK00635 1724 FLLDEIATSLDNQQKSALLV--QLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKI 1785
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
698-909 |
8.16e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.04 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRipRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVfwnssLPDSEGEDPSNPEretaadsdarsrgpvAYASqkp 777
Cdd:PRK10522 343 NLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-----LLDGKPVTAEQPE---------------DYRK--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 778 wLLNATVEENITFESPFNKQryKMVIEACSLQPDIDILPHGDQTQIGE---RGINLSGGQRQRISVARALYQHTNVVFLD 854
Cdd:PRK10522 398 -LFSAVFTDFHLFDQLLGPE--GKPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLD 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958642734 855 DPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQ 909
Cdd:PRK10522 475 EWAADQDPHFRREFYQV-LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
818-863 |
9.15e-04 |
|
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: 43.00 E-value: 9.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958642734 818 GDQTQ-IGErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVH 863
Cdd:TIGR03719 435 SDQQKkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
829-891 |
9.19e-04 |
|
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: 43.23 E-value: 9.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958642734 829 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSDHLMQAGILELLRDDKRTVVLVTHKL 891
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
378-608 |
1.04e-03 |
|
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: 42.39 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 378 YVAIETGINLRgaiqTKIYNKIMHLSTSNlsMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAM-PVQIIVGVILLYYIL 456
Cdd:cd18548 65 KASQGFGRDLR----KDLFEKIQSFSFAE--IDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRaPIMLIGAIIMAFRIN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 457 GVSALIGAAVIILLAPVQYFVATK---LSQAQRSTLEYSNERLKqtnEMLRGIKLLKLYAWENIFCSRVEKT----RRKE 529
Cdd:cd18548 139 PKLALILLVAIPILALVVFLIMKKaipLFKKVQKKLDRLNRVVR---ENLTGIRVIRAFNREDYEEERFDKAnddlTDTS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 530 MTSLRAFAVYT-SISIFMNTAIpiaAVLITFVGHvsFFKESDFSPSVAFASLS-LFHILvTPLFLLSSVVRSTVKALVSV 607
Cdd:cd18548 216 LKAGRLMALLNpLMMLIMNLAI---VAILWFGGH--LINAGSLQVGDLVAFINyLMQIL-MSLMMLSMVFVMLPRASASA 289
|
.
gi 1958642734 608 Q 608
Cdd:cd18548 290 K 290
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
817-936 |
1.36e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 817 HGDQ-TQIGERginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHKLQYL- 894
Cdd:PRK10636 420 QGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQALTEALIDFEGALVVVSHDRHLLr 491
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958642734 895 PHADWIIAMKDGTIQR-EGTLKDFQRsecqlfehWKTLMNRQD 936
Cdd:PRK10636 492 STTDDLYLVHDGKVEPfDGDLEDYQQ--------WLSDVQKQE 526
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
830-913 |
1.47e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 830 LSGGQRQRISVA---------RALYqhtnvvFLDDPFSAL---DVHlsdHLMQagILELLRDDKRTVVLVTHKLQYLPHA 897
Cdd:PRK00349 831 LSGGEAQRVKLAkelskrstgKTLY------ILDEPTTGLhfeDIR---KLLE--VLHRLVDKGNTVVVIEHNLDVIKTA 899
|
90 100
....*....|....*....|..
gi 1958642734 898 DWIIAM------KDGTIQREGT 913
Cdd:PRK00349 900 DWIIDLgpeggdGGGEIVATGT 921
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
825-901 |
1.63e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 825 ERGIN-LSGGQRQRISVARALYQHTNVV--FLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWII 901
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
831-894 |
2.01e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642734 831 SGGQRQRISVARALYQHTNVVFLDDPFSALDVH----LSDHLMQAgilellrddKRTVVLVTHKLQYL 894
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwLETYLLKW---------PKTFIVVSHAREFL 404
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
698-889 |
2.51e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 698 NITIRIPRGQLTMIVGQVGCGKSSlllaTlgeMQKVSGAvfwnssLPDSEGE--------DPSnperetaaDSDARSRgp 769
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKST----T---MKMLTGL------LPASEGEawlfgqpvDAG--------DIATRRR-- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQkpwllnA-------TVEENIT-----FESPFNK--QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 835
Cdd:NF033858 341 VGYMSQ------AfslygelTVRQNLElharlFHLPAAEiaARVAEMLERFDLADVADALPD-----------SLPLGIR 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958642734 836 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTH 889
Cdd:NF033858 404 QRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL-LIELSREDGVTIFISTH 456
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
818-906 |
2.71e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 818 GDQTQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHA 897
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQL-IAELAKKDKGIIIISSEMPELLGIT 458
|
....*....
gi 1958642734 898 DWIIAMKDG 906
Cdd:PRK10982 459 DRILVMSNG 467
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
816-921 |
4.09e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 816 PHGDQtQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYL 894
Cdd:PRK10762 387 PSMEQ-AIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ--LINQFKAEGLSIILVSSEMpEVL 459
|
90 100
....*....|....*....|....*..
gi 1958642734 895 PHADWIIAMKDGTIQREgtlkdFQRSE 921
Cdd:PRK10762 460 GMSDRILVMHEGRISGE-----FTREQ 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
696-890 |
5.29e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlgemQKVSGAVFwnsslpdSEGEDPSN-PERETaadSDARSRGPVay 772
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLnvLA-----ERVTTGVI-------TGGDRLVNgRPLDS---SFQRSIGYV-- 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 773 ASQKPWLLNATVEENITFE---------SPFNKQRY-KMVIEACSLQPDIDILphgdqtqIGERGINLSGGQRQRISVAR 842
Cdd:TIGR00956 842 QQQDLHLPTSTVRESLRFSaylrqpksvSKSEKMEYvEEVIKLLEMESYADAV-------VGVPGEGLNVEQRKRLTIGV 914
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 843 ALYQHTN-VVFLDDPFSALDVHLSdhlmqAGILELLR---DDKRTVVLVTHK 890
Cdd:TIGR00956 915 ELVAKPKlLLFLDEPTSGLDSQTA-----WSICKLMRklaDHGQAILCTIHQ 961
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
690-908 |
6.31e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.40 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNsslpdseGEDPsnpereTAADSDARSRGP 769
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD-------GEDI------TGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 770 VAYASQKPW----LLNATVEENITFES----PFNK----QRYKMVIEACSLQPDIDILPHGDQTQIGergiNLSGGQRQR 837
Cdd:COG3845 335 VAYIPEDRLgrglVPDMSVAENLILGRyrrpPFSRggflDRKAIRAFAEELIEEFDVRTPGPDTPAR----SLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958642734 838 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILElLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTI 908
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQR-LLE-LRDAGAAVLLISEDLDeILALSDRIAVMYEGRI 480
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
825-891 |
7.08e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.18 E-value: 7.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 825 ERGI-NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVH--LSdhlMQAGILELLRDdkRTVVLVTHKL 891
Cdd:PRK13409 207 DRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrLN---VARLIRELAEG--KYVLVVEHDL 271
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
378-561 |
8.46e-03 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 39.51 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 378 YVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAG--QICNLVAIDTNQLMWFFFLCPnlWAmPVQIIVgVILLYYI 455
Cdd:cd18586 64 RILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLlrDLDTLRNFLTGPSLFAFFDLP--WA-PLFLAV-IFLIHPP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 456 LGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNErlkQTNEMLRG---IKLLKLyaWENIFCSRVEKTRRKEMTS 532
Cdd:cd18586 140 LGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDA---LAAETLRNaetIKALGM--LGNLRRRWEARHAETLELQ 214
|
170 180 190
....*....|....*....|....*....|..
gi 1958642734 533 LRA---FAVYTSISIFMNTAIpiaAVLITFVG 561
Cdd:cd18586 215 IRAsdlAGAISAIGKTLRMAL---QSLILGVG 243
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
825-916 |
9.47e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 38.76 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642734 825 ERGIN-LSGGQRQRISVARALYQ-------HTNVVFLDDPFSALDV-------HLSDHLMQAGIlellrddkrTVVLVTH 889
Cdd:PRK03695 121 GRSVNqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVaqqaaldRLLSELCQQGI---------AVVMSSH 191
|
90 100
....*....|....*....|....*...
gi 1958642734 890 KLQY-LPHADWIIAMKDGTIQREGTLKD 916
Cdd:PRK03695 192 DLNHtLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
829-900 |
9.94e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 9.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958642734 829 NLSGGQRQRISVARALYQHTNVVFLDDPFSALD---VH-LSDHlmqagilelLRDDKRTVVLVTHKLQYLPH-ADWI 900
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDaesVAwLEQF---------LHDYPGTVVAVTHDRYFLDNvAGWI 230
|
|
| |
