|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
224-1340 |
1.19e-176 |
|
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: 565.73 E-value: 1.19e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 224 LLSKGTYWWMNAFIKTAHRKPI---DLRAIGK----LPIAMRALTNYQRLCAAFDAQ------ARKDTQSQQGAR----- 285
Cdd:TIGR00957 209 FLSRITFWWITGMAVYGYRQPLeesDLWSLNKedtsEMVVPVLVENWKKECKKTRKQpvsavyGKKDPSKPKGSSqldan 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 286 -----------------AIWRALCHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVdhlgkeNHVFQPKTQFLGVYFVSS 348
Cdd:TIGR00957 289 eevealivksphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLI------RFVNDPMAPDWQGYFYTG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 349 QEFLgnayvlavllflALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKImhLSTSNLSMGEMTAGQICNLVAIDTNQL 428
Cdd:TIGR00957 363 LLFV------------CACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKA--LVITNSARKSSTVGEIVNLMSVDAQRF 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 429 MWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKL 508
Cdd:TIGR00957 429 MDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 509 LKLYAWENIFCSRVEMTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVT 588
Cdd:TIGR00957 509 LKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRF 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 589 PLFLLSSVVRSTVKALVSVQKLSEFLSSAEIrEEQCAPREPAPQGQAgkyqavplkvvnrkrpareevrdllgplqrltp 668
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRLRIFLSHEEL-EPDSIERRTIKPGEG--------------------------------- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 669 smdgdadnFCVQIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdseg 748
Cdd:TIGR00957 635 --------NSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----------- 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 749 edpryclrtsnperetaadsdaRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQ 828
Cdd:TIGR00957 696 ----------------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 829 IGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQ--AGILELLRDdkRTVVLVTHKLQYLPHADWI 906
Cdd:TIGR00957 754 IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRILVTHGISYLPQVDVI 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 907 IAMKDGTI----------QREGTLKDFQRS------ECQLFEHWKTLMNRQDQE-LEKETVM----------ERK---AP 956
Cdd:TIGR00957 832 IVMSGGKIsemgsyqellQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKEaKLIENGMlvtdvvgkqlQRQlsaSS 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 957 EPSQGLPRAMSSRDGLLLDEDEEEEEAAESEEDDNLSSVlhqRAKIPWractKYLSSAGVLLLSLLVFSQLLKHMVLVAI 1036
Cdd:TIGR00957 912 SDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGQV---ELSVYW----DYMKAIGLFITFLSIFLFVCNHVSALAS 984
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1037 DYWLAKWTDSALVLSPAARNcslsqecALDQSVYAmvftvlcSLGI---ALCLVTSVTVEWTGLKVAKRLHRSLLNRIIL 1113
Cdd:TIGR00957 985 NYWLSLWTDDPMVNGTQNNT-------SLRLSVYG-------ALGIlqgFAVFGYSMAVSIGGIQASRVLHQDLLHNKLR 1050
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1114 APMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASR 1193
Cdd:TIGR00957 1051 SPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSR 1130
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1194 DLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMpgpaavlpqEYIGAC 1273
Cdd:TIGR00957 1131 QLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRL---------ECVGNC 1201
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 1274 VVLIAAATSISNslHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAES 1340
Cdd:TIGR00957 1202 IVLFAALFAVIS--RHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEA 1266
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
679-913 |
2.05e-145 |
|
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: 440.23 E-value: 2.05e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 679 VQIIGGFFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGedpryclrts 758
Cdd:cd03290 1 VQVTNGYFSWGS-GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPS---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 759 nperetAADSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSG 838
Cdd:cd03290 70 ------FEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 839 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 913
Cdd:cd03290 144 GQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
301-610 |
7.68e-142 |
|
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: 434.36 E-value: 7.68e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVA 380
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVSYVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 381 IETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAVYT 540
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 541 SISIFMNTAIPIAAVLITFVGHVsFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYP-YLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
223-1361 |
9.65e-141 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 467.53 E-value: 9.65e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 223 NLLSKGTYWWMNAFIKTAHRKPIDLRAIGKLPIAMRALTNYQRLcaafdaQARKDTQSQQGARAIWRALCHAFGRRLVLS 302
Cdd:PLN03232 233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRF------QRCWTEESRRPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 303 STFRILADLLGFAGPLcifgIVDHLGKENHVFQPKtqFLGvYFVSSQEFLGNAYVlavllflalllqrTFLQASYYVAI- 381
Cdd:PLN03232 307 GIFKIGHDLSQFVGPV----ILSHLLQSMQEGDPA--WVG-YVYAFLIFFGVTFG-------------VLCESQYFQNVg 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 382 ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSAL 461
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 462 IGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAVYTS 541
Cdd:PLN03232 445 FGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 542 ISIFMNTAIPIAAVLITFvgHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSaeirE 621
Cdd:PLN03232 525 FNSFILNSIPVVVTLVSF--GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLS----E 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 622 EQCAPREPapqgqagkyqavplkvvnrkrpareevrdllgPLQRLTPSmdgdadnfcVQIIGGFFTW-TPDGIPTLSNIT 700
Cdd:PLN03232 599 ERILAQNP--------------------------------PLQPGAPA---------ISIKNGYFSWdSKTSKPTLSDIN 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 701 IRIPRGQLTMIVGQVGCGKSSLLLATLGEmqrvsgavfwnssLPDSEgedpryclrtsnperetaaDSDARSRGPVAYAS 780
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGE-------------LSHAE-------------------TSSVVIRGSVAYVP 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 781 QKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLD 860
Cdd:PLN03232 686 QVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFD 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 861 DPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSEcQLFEHWKT---L 937
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSG-SLFKKLMEnagK 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 938 MNRQDQELEKETVMERKAPE-----PSQGLPRAMSSRDGllldedeeeeeaaeseeddnlSSVL-----HQRAKIPWRAC 1007
Cdd:PLN03232 843 MDATQEVNTNDENILKLGPTvtidvSERNLGSTKQGKRG---------------------RSVLvkqeeRETGIISWNVL 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1008 TKYLSSAGVLLLSLLVFSQLLKHMVL-VAIDYWLAKWTDSALVLSpaarncslsqecaLDQSVYAMVFTVLCSLGIALCL 1086
Cdd:PLN03232 902 MRYNKAVGGLWVVMILLVCYLTTEVLrVSSSTWLSIWTDQSTPKS-------------YSPGFYIVVYALLGFGQVAVTF 968
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1087 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYV 1166
Cdd:PLN03232 969 TNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTV 1048
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1167 TPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLF 1246
Cdd:PLN03232 1049 STISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLA 1128
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1247 LTAANRWLEVRMpgpaavlpqEYIGACVVLIAAATSI---SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQ 1323
Cdd:PLN03232 1129 NTSSNRWLTIRL---------ETLGGVMIWLTATFAVlrnGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENS 1199
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 1720421572 1324 LGAVKRIHTLLKTEAESyegllelarPREDSNSKPECA 1361
Cdd:PLN03232 1200 LNSVERVGNYIDLPSEA---------TAIIENNRPVSG 1228
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
1029-1332 |
5.10e-140 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 429.72 E-value: 5.10e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1029 KHMVLVAIDYWLAKWTDSALVLSPAARNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLL 1108
Cdd:cd18602 11 KQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1109 NRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYF 1188
Cdd:cd18602 91 RNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1189 RVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMpgpaavlpqE 1268
Cdd:cd18602 171 RASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL---------D 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 1269 YIGACVVLIAAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHT 1332
Cdd:cd18602 242 YLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLE 305
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
222-1340 |
1.60e-135 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 455.35 E-value: 1.60e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 222 VNLLSKGTYWWMNAFIKTAHRKPIDLRAIGKLPIAMRALTNYQRLCAAFDAQARKDTQsqqgaraiW--RALCHAFGRRL 299
Cdd:PLN03130 232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKP--------WllRALNNSLGGRF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 300 VLSSTFRILADLLGFAGPLcifgIVDHLGKENHVFQPKTQ--------FLGVyfvssqeFLGnayvlavllflalllqrT 371
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGPL----LLNLLLESMQNGEPAWIgyiyafsiFVGV-------VLG-----------------V 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 372 FLQASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 450
Cdd:PLN03130 356 LCEAQYFQNVmRVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMV 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 451 LLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEM 530
Cdd:PLN03130 434 LLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDEL 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 531 TSLRAFAVYTSISIFMNTAIPIAAVLITFvGHVSFFKeSDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:PLN03130 514 SWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLG-GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 611 SEFLSsAEirEEQCAPREPAPQGQagkyqavplkvvnrkrPAreevrdllgplqrltpsmdgdadnfcVQIIGGFFTWTP 690
Cdd:PLN03130 592 EELLL-AE--ERVLLPNPPLEPGL----------------PA--------------------------ISIKNGYFSWDS 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSgavfwnsslpdsegedpryclrtsnperetaaDSD 769
Cdd:PLN03130 627 KAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS--------------------------------DAS 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 849
Cdd:PLN03130 675 VVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARA 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 850 LYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD------- 922
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEElsnngpl 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 923 FQrsecQLFEHWKTLMNRQDQELEKE---TVMERKAPEPSQGLPRAMSSRDgllldedeeeeeaaeseEDDNLSSVLHQR 999
Cdd:PLN03130 833 FQ----KLMENAGKMEEYVEENGEEEddqTSSKPVANGNANNLKKDSSSKK-----------------KSKEGKSVLIKQ 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1000 AK-----IPWRACTKYLSSAGVLLLSLLVFSQLLKHMVL-VAIDYWLAKWTDSALVLS--PAARNcslsqecaldqSVYA 1071
Cdd:PLN03130 892 EEretgvVSWKVLERYKNALGGAWVVMILFLCYVLTEVFrVSSSTWLSEWTDQGTPKThgPLFYN-----------LIYA 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1072 MVF--TVLCSLGIALCLVTSvtvewtGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1149
Cdd:PLN03130 961 LLSfgQVLVTLLNSYWLIMS------SLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMF 1034
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1150 SRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARF 1229
Cdd:PLN03130 1035 LGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRM 1114
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1230 QQKLLEYTDSNNIASLFLTAANRWLEVRMpgpaavlpqEYIGACVVLIAAATSI---SNSLHRELSAGLVGLGLTYALMV 1306
Cdd:PLN03130 1115 AEINGRSMDNNIRFTLVNMSSNRWLAIRL---------ETLGGLMIWLTASFAVmqnGRAENQAAFASTMGLLLSYALNI 1185
|
1130 1140 1150
....*....|....*....|....*....|....
gi 1720421572 1307 SNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAES 1340
Cdd:PLN03130 1186 TSLLTAVLRLASLAENSLNAVERVGTYIDLPSEA 1219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
369-1330 |
3.35e-122 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 416.49 E-value: 3.35e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 369 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDT---NQLMWFfflCPNLWAMPVQI 445
Cdd:PTZ00243 298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVeriNSFMQY---CMYLWSSPMVL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 446 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMT 525
Cdd:PTZ00243 375 LLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 526 RRKEMTSLRAFAVYTSISIFMNTAIP---IAAVLITF--VGHvsffkesDFSPSVAFASLSLFHILVTPLFLLSSVVRST 600
Cdd:PTZ00243 455 RARELRYLRDVQLARVATSFVNNATPtlmIAVVFTVYylLGH-------ELTPEVVFPTIALLGVLRMPFFMIPWVFTTV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 601 VKALVSVQKLSEFLSS---------------AEIREEQCA--------------------PREPA--------------- 630
Cdd:PTZ00243 528 LQFLVSIKRISTFLECdnatcstvqdmeeywREQREHSTAcqlaavlenvdvtafvpvklPRAPKvktsllsralrmlcc 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 631 PQGQAGKYQAVPLKVVNR------KRPAREEVRDLLGPLQRLTPSMDGDADNFCVQIiGGFFTWTPDGIptLSNITIRIP 704
Cdd:PTZ00243 608 EQCRPTKRHPSPSVVVEDtdygspSSASRHIVEGGTGGGHEATPTSERSAKTPKMKT-DDFFELEPKVL--LRDVSVSVP 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 705 RGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfWNsslpdsegedpryclrtsnperetaadsdARSrgpVAYASQKPW 784
Cdd:PTZ00243 685 RGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WA-----------------------------ERS---IAYVPQQAW 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 785 LLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFS 864
Cdd:PTZ00243 732 IMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 865 ALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS---------ECQLFEHWK 935
Cdd:PTZ00243 812 ALDAHVGERVVEECFLGALAG--KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTslyatlaaeLKENKDSKE 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 936 TLMNRQDQELE----KETVMERKAPEP----SQGLPRAMSSRDGLLLdedeeeeeaaeseeddnlssVLHQRA--KIPWR 1005
Cdd:PTZ00243 890 GDADAEVAEVDaapgGAVDHEPPVAKQegnaEGGDGAALDAAAGRLM--------------------TREEKAsgSVPWS 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1006 ACTKYLSS-AGVLLLSLLVFSQLLKHMVLVAIDYWLAKWTdsalvlspaarncslSQECALDQSVYAMVFTVLCSLGIA- 1083
Cdd:PTZ00243 950 TYVAYLRFcGGLHAAGFVLATFAVTELVTVSSGVWLSMWS---------------TRSFKLSAATYLYVYLGIVLLGTFs 1014
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1084 --LCLVTSVTVEWTGlkvAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALT 1161
Cdd:PTZ00243 1015 vpLRFFLSYEAMRRG---SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSIL 1091
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1162 VISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNN 1241
Cdd:PTZ00243 1092 VTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVY 1171
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1242 IASLFLTAANRWLEVRMpgpaavlpqEYIGACVVLIAAATSISNSLHRELS--AGLVGLGLTYALMVSNYLNWMVRNLAD 1319
Cdd:PTZ00243 1172 SCSYLENVANRWLGVRV---------EFLSNIVVTVIALIGVIGTMLRATSqeIGLVSLSLTMAMQTTATLNWLVRQVAT 1242
|
1050
....*....|.
gi 1720421572 1320 MEIQLGAVKRI 1330
Cdd:PTZ00243 1243 VEADMNSVERL 1253
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
679-913 |
1.87e-101 |
|
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: 321.34 E-value: 1.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 679 VQIIGGFFTWTPDGI---PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpdsegedprycl 755
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 756 rtsnperetaadsdarsrgpVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGIN 835
Cdd:cd03250 68 --------------------IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGIN 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 913
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
1034-1331 |
1.30e-82 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 272.84 E-value: 1.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1034 VAIDYWLAKWTDSAlvlspaarncslSQECALDQSVYAMVFTVLCSLG-IALCLVTSVTVEWTGLKVAKRLHRSLLNRII 1112
Cdd:cd18580 16 QFSNIWLDWWSSDW------------SSSPNSSSGYYLGVYAALLVLAsVLLVLLRWLLFVLAGLRASRRLHDKLLRSVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1113 LAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVAS 1192
Cdd:cd18580 84 RAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1193 RDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMpgpaavlpqEYIGA 1272
Cdd:cd18580 164 RQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRL---------DLLGA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 1273 CVVLIAAATSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1331
Cdd:cd18580 235 LLALVVALLAV--LLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERIL 291
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
1030-1331 |
2.41e-79 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 263.57 E-value: 2.41e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1030 HMVLVAIDYWLAKWTDSALVLSPAA---RNCSLSqecaldqsVYAM--VFTVLCSLGIALCLVTSvtvewtGLKVAKRLH 1104
Cdd:cd18603 12 QAFSVGSNIWLSEWSDDPALNGTQDteqRDYRLG--------VYGAlgLGQAIFVFLGSLALALG------CVRASRNLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1105 RSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFI 1184
Cdd:cd18603 78 NKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1185 QKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMpgpaav 1264
Cdd:cd18603 158 QRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRL------ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 1265 lpqEYIGACVVLIAAATSIsnsLHRE-LSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1331
Cdd:cd18603 232 ---EFLGNLIVLFAALFAV---LSRDsLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIK 293
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
1030-1331 |
2.39e-75 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 252.39 E-value: 2.39e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1030 HMVLVAIDYWLAKWT---DSALVLSPAARNcslsqecaldQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRS 1106
Cdd:cd18604 12 QLLSVGQSWWLGIWAsayETSSALPPSEVS----------VLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1107 LLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQK 1186
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1187 YFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMpgpaavlp 1266
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRI-------- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 1267 qEYIGACVVLIAAATSISNslhRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1331
Cdd:cd18604 234 -DLLGALFSFATAALLVYG---PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQ 294
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
223-1330 |
9.38e-73 |
|
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: 267.93 E-value: 9.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 223 NLLSKGTYWWMNAFIKTAHRKPIDLRAIGKLPIAMRALTNYQRLCAAFDaqaRKDTQSQQGARAIwRALCHAFGRRLVLs 302
Cdd:TIGR01271 10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWD---RELASAKKNPKLL-NALRRCFFWRFVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 303 stfriladllgfagplciFGIVDHLGKENHVFQPKT--QFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVA 380
Cdd:TIGR01271 85 ------------------YGILLYFGEATKAVQPLLlgRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 381 IETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:TIGR01271 147 HHLGMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAvyt 540
Cdd:TIGR01271 225 FCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 541 SISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHIL-VTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEI 619
Cdd:TIGR01271 302 YLRYFYSSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 620 R--EEQCAPREpapqgqagkyqavpLKVVNRKRPAREEVRDLLGPLQ-----RLTPsmDGDAdnfcvqiiGGFFT-WTPD 691
Cdd:TIGR01271 382 KtlEYNLTTTE--------------VEMVNVTASWDEGIGELFEKIKqnnkaRKQP--NGDD--------GLFFSnFSLY 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEmqrvsgavfwnssLPDSEGEdpryclrtsnperetaadsdAR 771
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGE-------------LEPSEGK--------------------IK 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 851
Cdd:TIGR01271 485 HSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVY 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 852 QHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE---- 927
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRpdfs 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 928 -----CQLFEHWK----------TL------------------------------------------------------- 937
Cdd:TIGR01271 643 slllgLEAFDNFSaerrnsilteTLrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkfsfvqmgp 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 938 --MNRQDQELEKETVMERK---APEPSQG---LPRAMSSRDGLLLDEDEEEEEAAESEEDDNLSSVLHQRakipwRACTK 1009
Cdd:TIGR01271 723 qkAQATTIEDAVREPSERKfslVPEDEQGeesLPRGNQYHHGLQHQAQRRQSVLQLMTHSNRGENRREQL-----QTSFR 797
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1010 YLSSAGVLLLSLLVF-----------------------------------------------SQLLKHMVLVAI---DYW 1039
Cdd:TIGR01271 798 KKSSITQQNELASELdiysrrlskdsvyeiseeineedlkecfaderenvfetttwntylryITTNRNLVFVLIfclVIF 877
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1040 LAKWTDSALVL-----SPAARNcSLSQECALDQS---VYAMVFTVLCSLGI------------ALCLVTSVTVEWTGLKV 1099
Cdd:TIGR01271 878 LAEVAASLLGLwlitdNPSAPN-YVDQQHANASSpdvQKPVIITPTSAYYIfyiyvgtadsvlALGFFRGLPLVHTLLTV 956
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1100 AKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAV 1179
Cdd:TIGR01271 957 SKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAV 1036
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1180 VCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF----RYEARFQQKLLEYTdsnniASLFLTAAN-RWL 1254
Cdd:TIGR01271 1037 IFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFgrqsYFETLFHKALNLHT-----ANWFLYLSTlRWF 1111
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 1255 EVRMpgpaavlpqEYIgaCVVLIAAATSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 1330
Cdd:TIGR01271 1112 QMRI---------DII--FVFFFIAVTFIAIGTNQD-GEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRV 1175
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
301-610 |
3.25e-72 |
|
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: 243.16 E-value: 3.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENHvfQPKTQ-------FLGVYFVSSqeflgnayvlavllflalllqrTFL 373
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD--EPLSEgyllalaLFLVSLLQS----------------------LLL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 374 QASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLY 453
Cdd:cd18579 57 HQYFFLSFRLGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 454 YILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSL 533
Cdd:cd18579 135 RLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKAL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 534 RAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKEsdFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18579 215 RKFGYLRALNSFLFFSTPVLVSLATFATYVLLGNP--LTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
1035-1331 |
6.36e-70 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 237.04 E-value: 6.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1035 AIDYWLAKWTDSAlvlspaarNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILA 1114
Cdd:cd18605 17 LIDFWLSYWVSHS--------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1115 PMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRD 1194
Cdd:cd18605 89 KMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1195 LQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMpgpaavlpqEYIGACV 1274
Cdd:cd18605 169 LKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRL---------QLLGVLI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 1275 VLIAAATSI-SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1331
Cdd:cd18605 240 VTFVALTAVvQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVR 297
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
1037-1332 |
7.70e-65 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 222.82 E-value: 7.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1037 DYWLAKW------TDSALVLSPAARNCSLSQECALD--QSVYAMVFTVLCSLGIALCLVTSVTVewtgLKVAKRLHRSLL 1108
Cdd:cd18599 23 DWWLSYWlkqgsgNTTNNVDNSTVDSGNISDNPDLNfyQLVYGGSILVILLLSLIRGFVFVKVT----LRASSRLHNKLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1109 NRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYF 1188
Cdd:cd18599 99 QKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1189 RVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMpgpaavlpqE 1268
Cdd:cd18599 179 RRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRL---------D 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 1269 YIGACVVLIAAATSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHT 1332
Cdd:cd18599 250 ILAVLITLITALLVV--LLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILE 311
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
1034-1331 |
2.10e-63 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 217.73 E-value: 2.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1034 VAIDYWLAKWTDSALVLSpaarncslsqecaldQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIIL 1113
Cdd:cd18606 16 VFTNLWLSFWTEDFFGLS---------------QGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1114 APMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASR 1193
Cdd:cd18606 81 APMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1194 DLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASlFLTAAN-RWLEVRMpgpaavlpqEYIGA 1272
Cdd:cd18606 161 ELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAY-FLTIANqRWLAIRL---------DLLGS 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 1273 CVVLIAAATSISNSLHreLSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIH 1331
Cdd:cd18606 231 LLVLIVALLCVTRRFS--ISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLL 287
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
285-919 |
3.07e-61 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 220.81 E-value: 3.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 285 RAIWRALcHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLGkENHVFQPKTQFLGVYFVSsqeFLGNAyvlavllfl 364
Cdd:COG1132 10 RRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSALLLLLLLLLGL---ALLRA--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 365 alllqrTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFF-FLCPNLWAMPV 443
Cdd:COG1132 76 ------LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLaHGLPQLVRSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 444 QIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FC 519
Cdd:COG1132 148 TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERelerFR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 520 SRVEMTRRKEMTSLRAFAVYTSISIFMNTaipIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRS 599
Cdd:COG1132 228 EANEELRRANLRAARLSALFFPLMELLGN---LGLALVLLVG-GLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 600 TVKALVSVQKLSEFLSsaeireeqcaprepAPQGQAGKYQAVPLKvvnrkrPAREEVRdllgpLQRLTpsmdgdadnfcv 679
Cdd:COG1132 304 LQRALASAERIFELLD--------------EPPEIPDPPGAVPLP------PVRGEIE-----FENVS------------ 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 680 qiiggfFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNsslpdseGEDprycLRT 757
Cdd:COG1132 347 ------FSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLvnLLLRFYDPT--SGRILID-------GVD----IRD 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 758 SNPEretaadsDARSRgpVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERG 833
Cdd:COG1132 407 LTLE-------SLRRQ--IGVVPQDTFLFSGTIRENIRYGRPdATDEE---VEEAAkaaQAHEFIEALPDGYDTVVGERG 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 834 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGT 913
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTE-TEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGR 551
|
....*.
gi 1720421572 914 IQREGT 919
Cdd:COG1132 552 IVEQGT 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 |
8.46e-60 |
|
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: 207.32 E-value: 8.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 369 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVG 448
Cdd:cd18595 51 QSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 449 VILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRK 528
Cdd:cd18595 129 LYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 529 EMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18595 209 ELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLK 288
|
..
gi 1720421572 609 KL 610
Cdd:cd18595 289 RL 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
371-919 |
8.84e-56 |
|
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: 207.76 E-value: 8.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 371 TFLQASYYVAIETGINLRgaIQTKIYNKIMHLSTSNL---SMGEMTA-----GQICNLVaidTNQLMWFFFLCPnlwamp 442
Cdd:COG2274 213 RLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFesrSVGDLASrfrdvESIREFL---TGSLLTALLDLL------ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 443 vQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRV 522
Cdd:COG2274 282 -FVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRW 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 523 E-MTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTV 601
Cdd:COG2274 361 EnLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLG-AYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 602 KALVSVQKLSEFLSsaeireeqcAPREPAPqgqagkyqavplkvvnrkrpareevrdllGPLQRLTPSMDGDadnfcVQI 681
Cdd:COG2274 440 DAKIALERLDDILD---------LPPEREE-----------------------------GRSKLSLPRLKGD-----IEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 682 IGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPE 761
Cdd:COG2274 477 ENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID-------GID----LRQIDPA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 762 retaadsDARSRgpVAYASQKPWLLNATVEENITFESP-FNKQRykmVIEAC---SLQPDIDILPHGDQTQIGERGINLS 837
Cdd:COG2274 546 -------SLRRQ--IGVVLQDVFLFSGTIRENITLGDPdATDEE---IIEAArlaGLHDFIEALPMGYDTVVGEGGSNLS 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 917
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
..
gi 1720421572 918 GT 919
Cdd:COG2274 691 GT 692
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
1037-1330 |
6.13e-54 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 191.38 E-value: 6.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1037 DYWLAKWTDS-----ALVLSPAARNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRI 1111
Cdd:cd18601 23 DWWLSYWANLeeklnDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1112 ILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVA 1191
Cdd:cd18601 103 LRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1192 SRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIA-SLFLTaANRWLEVRMpgpaavlpqEYI 1270
Cdd:cd18601 183 SREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAwFLFLA-TSRWLAVRL---------DAL 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1271 gaCVVLIAAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 1330
Cdd:cd18601 253 --CALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
372-610 |
1.30e-53 |
|
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: 189.59 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18597 59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMT 531
Cdd:cd18597 137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 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 |
6.24e-50 |
|
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: 179.61 E-value: 6.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 311 LLGFAGPLCIFGIVDHLgkENHVFQPKTQ--------FLGVyFVSSQeflgnayvlavllflalllqrtFLQASYYVAIE 382
Cdd:cd18596 11 VLSFAPPFFLNRLLRYL--EDPGEDATVRpwvwvlllFLGP-LLSSL----------------------LDQQYLWIGRR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 383 TGINLRGAIQTKIYNKIMHL-----------------STSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQI 445
Cdd:cd18596 66 LSVRLRAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 446 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMT 525
Cdd:cd18596 146 VIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 526 RRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKEsDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALV 605
Cdd:cd18596 226 REEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQ-ELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKV 304
|
...
gi 1720421572 606 SVQ 608
Cdd:cd18596 305 SLD 307
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
372-610 |
3.70e-46 |
|
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: 168.12 E-value: 3.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLStsnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18592 55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMT 531
Cdd:cd18592 131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 532 SLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18592 211 ILEKAGYLQSISISLAPIVPVIASVVTFLAHVAL--GNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
690-927 |
5.86e-46 |
|
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: 175.33 E-value: 5.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclrtsnperetAADSD 769
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-------GVDLS------------DLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRGpVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 848
Cdd:COG4988 408 SWRRQ-IAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 849 ALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 927
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAE-TEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
305-610 |
1.53e-44 |
|
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: 163.49 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 305 FRILADLLGFAGPLCIFGIVDHLgkENHVFQPKTQFL--GVYFVSSqeFLGnayvlavllflalllqrTFLQASY-YVAI 381
Cdd:cd18598 5 LKLLADVLGFAGPLLLNKLVEFL--EDSSEPLSDGYLyaLGLVLSS--LLG-----------------ALLSSHYnFQMN 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 382 ETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFfflCPNL---WAMPVQIIVGVILLYYILGV 458
Cdd:cd18598 64 KVSLKVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 459 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLR---- 534
Cdd:cd18598 139 AFLAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKgrky 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 535 --AFAVYtsisiFMNTAiPIAAVLITFVGHVsfFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18598 219 ldALCVY-----FWATT-PVLISILTFATYV--LMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
692-924 |
4.74e-41 |
|
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: 153.09 E-value: 4.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdsegedpryclrtsnperetaadsdaR 771
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---------------------------------K 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 851
Cdd:cd03291 96 HSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 852 QHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 924
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
445-919 |
2.18e-40 |
|
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: 158.78 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 445 IIVGVILLYYILGVSALI---GAAVIILLAPVqyFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSR 521
Cdd:COG4987 143 ILAAVAFLAFFSPALALVlalGLLLAGLLLPL--LAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALAR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 522 VEMTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPS----VAFASLSLFHILVTplflLSSVV 597
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPllalLVLAALALFEALAP----LPAAA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 598 RSTVKALVSVQKLSEFLSSAeireeqcaPREPAPQGQAGKYQAVPLKvvnrkrpareevrdllgpLQRLTpsmdgdadnf 677
Cdd:COG4987 297 QHLGRVRAAARRLNELLDAP--------PAVTEPAEPAPAPGGPSLE------------------LEDVS---------- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 678 cvqiiggfFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclrt 757
Cdd:COG4987 341 --------FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-------GVDLR----- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 758 snpereTAADSDARSRgpVAYASQKPWLLNATVEENITFESPfNKQRYKM--VIEACSLQPDIDILPHGDQTQIGERGIN 835
Cdd:COG4987 401 ------DLDEDDLRRR--IAVVPQRPHLFDTTLRENLRLARP-DATDEELwaALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQ 915
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAG--RTVLLITHRLAGLERMDRILVLEDGRIV 548
|
....
gi 1720421572 916 REGT 919
Cdd:COG4987 549 EQGT 552
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1030-1310 |
1.08e-39 |
|
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: 148.95 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1030 HMVLVAIDYWLAKWTDSALVLSPAARNcslsqecalDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLN 1109
Cdd:pfam00664 12 GAISPAFPLVLGRILDVLLPDGDPETQ---------ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1110 RIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFR 1189
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1190 VASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMpgpaavlpqEY 1269
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGIT---------QF 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720421572 1270 IGACVVLIAAATSISNSLHRELSAGLVGLGLTYALMVSNYL 1310
Cdd:pfam00664 234 IGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
686-912 |
1.38e-39 |
|
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: 144.83 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPEreta 765
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID-------GVD----LRDLDLE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adsDARSRgpVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRIS 845
Cdd:cd03228 73 ---SLRKN--IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 912
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEA-LRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
685-919 |
1.61e-38 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 143.91 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 685 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNsslpdseGEDPRY----CLRTS 758
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnLIPRFYDVD--SGRILID-------GHDVRDytlaSLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 759 nperetaadsdarsrgpVAYASQKPWLLNATVEENITFESPfNKQRyKMVIEA---CSLQPDIDILPHGDQTQIGERGIN 835
Cdd:cd03251 78 -----------------IGLVSQDVFLFNDTVAENIAYGRP-GATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQ 915
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
....
gi 1720421572 916 REGT 919
Cdd:cd03251 216 ERGT 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
686-918 |
2.52e-38 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 143.11 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpDSEGEDPryclrtsnpereta 765
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT--DIRQLDP-------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adSDARSRgpVAYASQKPWLLNATVEENITFESPF-NKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRI 844
Cdd:cd03245 74 --ADLRRN--IGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 845 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 918
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
318-610 |
8.71e-37 |
|
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: 140.85 E-value: 8.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 318 LCIFGIVDHLGKenhVFQPktQFLG---VYFV-SSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQT 393
Cdd:cd18594 2 LGILLFLEESLK---IVQP--LLLGrlvAYFVpDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 394 KIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPV 473
Cdd:cd18594 77 LIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 474 QYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLR--AFAVYTSISIFMNTAIP 551
Cdd:cd18594 155 QAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRkaAYIRAFNMAFFFFSPTL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 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 |
1.59e-36 |
|
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: 140.43 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 376 SYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQL-MWFFFLcPNLWAMPVQIIVGVILLYY 454
Cdd:cd18593 60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 455 ILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLR 534
Cdd:cd18593 137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 535 --AFAVYTSISIFMntaipIAAVLITFVGHVSFF-KESDFSPSVAFASLSLFHilvtplfllssVVRSTVKALV--SVQK 609
Cdd:cd18593 217 rtSFLRALNMGLFF-----VSSKLILFLTFLAYIlLGNILTAERVFVTMALYN-----------AVRLTMTLFFpfAIQF 280
|
....*...
gi 1720421572 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 ... |
692-919 |
9.23e-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: 135.82 E-value: 9.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpDSEGED-PRYCLRTSnperetaadsda 770
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID----GIDIRDiSRKSLRSM------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 rsrgpVAYASQKPWLLNATVEENITFESPFNKQryKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVA 847
Cdd:cd03254 79 -----IGVVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKeagAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTE-TEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
690-919 |
2.00e-34 |
|
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: 132.28 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSlllaTLGEMQR----VSGAVFWNsslpdseGEDprycLRTSNPEReta 765
Cdd:cd03249 14 PD-VPILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERfydpTSGEILLD-------GVD----IRDLNLRW--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adsdarSRGPVAYASQKPWLLNATVEENITFESPFNKQryKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQ 842
Cdd:cd03249 75 ------LRSQIGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 843 RISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAE-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
449-919 |
2.14e-33 |
|
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: 137.54 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 449 VILLYYILGVSAligaaVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTN----EMLRGIKLLKLYAWE----NIFCS 520
Cdd:TIGR02203 147 IVLLYYSWQLTL-----IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTtvaeETLQGYRVVKLFGGQayetRRFDA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 521 RVEMTRRKEMTSLRAFAVYTSISIFmntaipIAAVLITFVGHVSFFKESDFSPSVA-FASLSLFHILV-TPLFLLSSVVR 598
Cdd:TIGR02203 222 VSNRNRRLAMKMTSAGSISSPITQL------IASLALAVVLFIALFQAQAGSLTAGdFTAFITAMIALiRPLKSLTNVNA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 599 STVKALVSVQKLSEFLSSAeireeqcaprepaPQGQAGKyqavplKVVNRKRpAREEVRDLLgplqrltpsmdgdadnfc 678
Cdd:TIGR02203 296 PMQRGLAAAESLFTLLDSP-------------PEKDTGT------RAIERAR-GDVEFRNVT------------------ 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 679 vqiiggfFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFwnssLPDSEGEDprYCLR 756
Cdd:TIGR02203 338 -------FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYEPD--SGQIL----LDGHDLAD--YTLA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 757 tsnperetaadsDARSRgpVAYASQKPWLLNATVEENITFESP--FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI 834
Cdd:TIGR02203 403 ------------SLRRQ--VALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGV 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 835 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 914
Cdd:TIGR02203 469 LLSGGQRQRLAIARALLKDAPILILDEATSALDNE-SERLVQAALERLMQG--RTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
....*
gi 1720421572 915 QREGT 919
Cdd:TIGR02203 546 VERGT 550
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
299-590 |
4.72e-33 |
|
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: 129.69 E-value: 4.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 299 LVLSSTFRILADLLGFAGPLCIFGIVDHLGKEN-HVFQPKTQFLGVYFVssqeflgnayvlavllflALLLQRTFLQASY 377
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGdPETQALNVYSLALLL------------------LGLAQFILSFLQS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 378 YVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILG 457
Cdd:pfam00664 63 YLLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 458 VS-ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAF 536
Cdd:pfam00664 141 WKlTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKK 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 537 AVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPL 590
Cdd:pfam00664 221 AVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
694-919 |
1.01e-32 |
|
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: 135.26 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPERetaadsdarsR 773
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD-------GAD----LSQWDREE----------L 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GP-VAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEACSLqpdIDI------LPHGDQTQIGERGINLSGGQRQRISV 846
Cdd:COG4618 405 GRhIGYLPQDVELFDGTIAENI---ARFGDADPEKVVAAAKL---AGVhemilrLPDGYDTRIGEGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 847 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAA--IRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
690-919 |
7.15e-32 |
|
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: 125.04 E-value: 7.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNsslpdseGEDPRyclrtsnperETAAD 767
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTIlrLLFRFYDVS--SGSILID-------GQDIR----------EVTLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 768 SDARSRGPVAyasQKPWLLNATVEENITFESP--FNKQrykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQRQ 842
Cdd:cd03253 72 SLRRAIGVVP---QDTVLFNDTIGYNIRYGRPdaTDEE----VIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 843 RISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERGT 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
379-919 |
1.18e-31 |
|
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: 131.70 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 379 VAIETGINLRGAIQTKIYNKIMhlsTSNLSMGEMTAGQICNlvaiDTNQLMWF--------FFLCPnlWaMPVQIIVgVI 450
Cdd:TIGR01842 69 VLVRIGEKLDGALNQPIFAASF---SATLRRGSGDGLQALR----DLDQLRQFltgpglfaFFDAP--W-MPIYLLV-CF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 451 LLYYILGVSALIGAAVIILLAPV-QYFVATKLSQAQrstlEYSNERLKQTNEMLRGIKLLK-LYAWENIfcsrVEMTRRK 528
Cdd:TIGR01842 138 LLHPWIGILALGGAVVLVGLALLnNRATKKPLKEAT----EASIRANNLADSALRNAEVIEaMGMMGNL----TKRWGRF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 529 EMTSLRAFAVYTSISIFMNTAIPIAAV----LITFVG-HVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKA 603
Cdd:TIGR01842 210 HSKYLSAQSAASDRAGMLSNLSKYFRIvlqsLVLGLGaYLAI--DGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 604 LVSVQKLSEFLssAEIREEQCAPREPAPQGQagkyqavpLKVvnrkrparEEVrDLLGPLQRLtpsmdgdadnfcvqiig 683
Cdd:TIGR01842 288 RQAYKRLNELL--ANYPSRDPAMPLPEPEGH--------LSV--------ENV-TIVPPGGKK----------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 684 gfftwtpdgiPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpDSEGEDPRyclrtsNPERE 763
Cdd:TIGR01842 332 ----------PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV-------RLDGADLK------QWDRE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 764 TAADSdarsrgpVAYASQKPWLLNATVEENIT-FESPFNKQRykmVIEACSL---QPDIDILPHGDQTQIGERGINLSGG 839
Cdd:TIGR01842 389 TFGKH-------IGYLPQDVELFPGTVAENIArFGENADPEK---IIEAAKLagvHELILRLPDGYDTVIGPGGATLSGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 840 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:TIGR01842 459 QRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA--IKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
690-909 |
2.27e-31 |
|
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: 130.48 E-value: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSslpdsegedpryclrtsnpeRETAADSD 769
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG--------------------VPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRGPVAYASQKPWLLNATVEENITFESPFNKQ-RYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 848
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421572 849 ALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAM 909
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
686-913 |
1.47e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 117.57 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegedpryclrtsnpERETA 765
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD--------------------GKDLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 ADSDARSRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiN 835
Cdd:cd03225 67 KLSLKELRRKVGLVFQNPddQFFGPTVEEEVAF-GLENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------T 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 913
Cdd:cd03225 135 LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
691-927 |
3.58e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclrtsnperetaadsda 770
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF-------GKPPR------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGPVAYASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGG 839
Cdd:COG1121 72 RARRRIGYVPQRaevDWDFPITVRDvvlmgrygRRGLFRRPSRADREAVDEALER---VGLEDLADR-PIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 840 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIqREG 918
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRREGKTILVVTHDLGAVReYFDRVLLLNRGLV-AHG 220
|
....*....
gi 1720421572 919 TLKDFQRSE 927
Cdd:COG1121 221 PPEEVLTPE 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
686-927 |
4.44e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 116.82 E-value: 4.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSslllaTLGEM-QRV----SGAVFwnsslpdSEGEDprycLRTSNP 760
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKS-----TLTKLiQRFyvpeNGRVL-------VDGHD----LALADP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 761 eretaadsdARSRGPVAYASQKPWLLNATVEENITFESPFNKQRykMVIEACSL---QPDIDILPHGDQTQIGERGINLS 837
Cdd:cd03252 72 ---------AWLRRQVGVVLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLagaHDFISELPEGYDTIVGEQGAGLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 917
Cdd:cd03252 141 GGQRQRIAIARALIHNPRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
250
....*....|
gi 1720421572 918 GTLKDFQRSE 927
Cdd:cd03252 218 GSHDELLAEN 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
687-919 |
2.06e-28 |
|
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: 115.53 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 687 TWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclRTSNPERetaa 766
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD-------GRDLA---SLSRREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 767 dsdARSrgpVAYASQK---PWLLnaTVEENI--------TFESPFNKQRYKMVIEACslqpdidilphgDQTQIG---ER 832
Cdd:COG1120 74 ---ARR---IAYVPQEppaPFGL--TVRELValgryphlGLFGRPSAEDREAVEEAL------------ERTGLEhlaDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 833 GIN-LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVTHKL-QYLPHADWI 906
Cdd:COG1120 134 PVDeLSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA---H--QLEVLELLRRlareRGRTVVMVLHDLnLAARYADRL 208
|
250
....*....|...
gi 1720421572 907 IAMKDGTIQREGT 919
Cdd:COG1120 209 VLLKDGRIVAQGP 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
686-917 |
3.98e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.80 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclrtsnpereta 765
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD-------GKPVT------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adsdaRSRGPVAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMV---IEACSLQPDIDILPHgdqtqiger 832
Cdd:COG1116 77 -----GPGPDRGVVFQEpallPWL---TVLDNVALglelrgVPK--AERRERArelLELVGLAGFEDAYPH--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 833 giNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAM 909
Cdd:COG1116 138 --QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDELLRLWQETGKTVLFVTHDVDeavFL--ADRVVVL 212
|
250
....*....|
gi 1720421572 910 KD--GTIQRE 917
Cdd:COG1116 213 SArpGRIVEE 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
690-923 |
4.28e-28 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 113.97 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclrtsnpeRETAADsd 769
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-------GKDIT---------KKNLRE-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRgpVAYASQKPW--LLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGG 839
Cdd:COG1122 73 LRRK--VGLVFQNPDdqLFAPTVEEDVAF-GPENlglpreeiRERVEEALELVGLEHLADRPPH-----------ELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 840 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGTIQREG 918
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADG 216
|
....*
gi 1720421572 919 TLKDF 923
Cdd:COG1122 217 TPREV 221
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
305-610 |
6.12e-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: 115.39 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 305 FRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVS--SQEFLGNAYvlavllflalllqrtflqasYYVAIE 382
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALaiLQGITVFQY--------------------SMAVSI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 383 TGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALI 462
Cdd:cd18559 65 GGIFASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 463 GAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAVYTSI 542
Cdd:cd18559 143 GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRAL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 543 SIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18559 223 AVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
1069-1329 |
9.74e-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: 114.62 E-value: 9.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1069 VYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEC 1148
Cdd:cd18559 39 VYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1149 LSRSTLLCVSALTVISYVTPVFLVAlLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEAR 1228
Cdd:cd18559 119 WMGPLQNVIGLYLLILLAGPMAAVG-IPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1229 FQQKLLEYTDsNNIASLFLTAANRWLEVRMpgpaavlpqEYIGACVVLIAA-ATSISnslhRELSAGLVGLGLTYALMVS 1307
Cdd:cd18559 198 FIRQVDAKRD-NELAYLPSIVYLRALAVRL---------WCVGPCIVLFASfFAYVS----RHSLAGLVALKVFYSLALT 263
|
250 260
....*....|....*....|..
gi 1720421572 1308 NYLNWMVRNLADMEIQLGAVKR 1329
Cdd:cd18559 264 TYLNWPLNMSPEVITNIVAAEV 285
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
689-919 |
1.51e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 119.56 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavFwnssLPdSEGEdprycLRTSNPERETAADS 768
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG---------F----LP-YQGS-----LKINGIELRELDPE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 DARSRgpVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVA 847
Cdd:PRK11174 420 SWRKH--LSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALA 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHSEQLVMQA--LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGD 566
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1095-1330 |
5.07e-27 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 113.36 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1095 TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVAL 1174
Cdd:cd18600 97 TLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLAT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1175 LPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFR----YEARFQQKLLEYTdsnniASLFL-TA 1249
Cdd:cd18600 177 VPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHT-----ANWFLyLS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1250 ANRWLEVRMpgpaavlpqEYIgaCVVLIAAATSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKR 1329
Cdd:cd18600 252 TLRWFQMRI---------EMI--FVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSR 319
|
.
gi 1720421572 1330 I 1330
Cdd:cd18600 320 I 320
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
381-941 |
8.78e-27 |
|
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: 118.14 E-value: 8.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 381 IETGINlrGAIQTKIYNKIMHL--------STSNLSMGEMTAGQICNLVAIDT-NQLMWFFFLCPNLWampvqiivgviL 451
Cdd:TIGR03797 203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLG-----------L 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAWENIFCSRVE 523
Cdd:TIGR03797 270 MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 524 MTRRKEM------TSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFkesdfspsVAFASLSlfhilvtplfllsSVV 597
Cdd:TIGR03797 350 LELSAQRienlltVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFN--------TAFGSFS-------------GAV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 598 RSTVKALVSVqklseflssaeireeqcaprepapqgqagkYQAVPLkvVNRKRP---AREEVRDLLGPLQRLTPSMDgdA 674
Cdd:TIGR03797 409 TQLSNTLISI------------------------------LAVIPL--WERAKPileALPEVDEAKTDPGKLSGAIE--V 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 675 DNFCvqiiggfFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpDSEGEDPRyC 754
Cdd:TIGR03797 455 DRVT-------FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQ--DLAGLDVQ-A 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 755 LRtsnperetaadsdaRSRGPVAYASQkpwLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI 834
Cdd:TIGR03797 525 VR--------------RQLGVVLQNGR---LMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGG 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 835 NLSGGQRQRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 914
Cdd:TIGR03797 588 TLSGGQRQRLLIARALVRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRV 662
|
570 580
....*....|....*....|....*..
gi 1720421572 915 QREGTLKDFQRSECQLFEhwktLMNRQ 941
Cdd:TIGR03797 663 VQQGTYDELMAREGLFAQ----LARRQ 685
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
690-919 |
1.07e-26 |
|
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: 109.51 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN----SSLPdsegedprycLRtsnpereta 765
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvdiSKIG----------LH--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adsDARSRgpVAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQ 842
Cdd:cd03244 75 ---DLRSR--ISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 843 RISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
696-918 |
3.96e-26 |
|
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: 106.37 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclRTSNPERetaadsdARSrgp 775
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-------GKDLA---SLSPKEL-------ARK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQkpwllnatveenitfespfnkqrykmVIEACSLqpdidilphgdqTQIGERGIN-LSGGQRQRISVARALYQHT 854
Cdd:cd03214 75 IAYVPQ--------------------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 855 NVVFLDDPFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREG 918
Cdd:cd03214 117 PILLLDEPTSHLDIA-----HQIELLELLRRLARergkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
696-917 |
5.71e-26 |
|
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: 107.56 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemqrvsgavfwnssLPDSEGEdpryCLRTSNPERETAADsdarsr 773
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLriIAGL---------------ERPTSGE----VLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 gpVAYASQK----PWLlnaTVEENITFesPFN---------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQ 840
Cdd:cd03293 75 --RGYVFQQdallPWL---TVLDNVAL--GLElqgvpkaeaRERAEELLELVGLSGFENAYPH-----------QLSGGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAM--KDGTIQ 915
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQ-LQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIV 213
|
..
gi 1720421572 916 RE 917
Cdd:cd03293 214 AE 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
686-914 |
6.27e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.82 E-value: 6.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPEreta 765
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLD-------GKP----LSAMPPP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adsDARSRgpVAYASQKPWLLNATVEENITF-----ESPFNKQRYKMVIEACSLQPDIdiLphgdQTQIGErginLSGGQ 840
Cdd:COG4619 71 ---EWRRQ--VAYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDI--L----DKPVER----LSGGE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 914
Cdd:COG4619 136 RQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEEL-LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
686-927 |
7.56e-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: 115.22 E-value: 7.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQRvsGAVFwnsslpdSEGEDprycLRTSNPere 763
Cdd:TIGR01846 463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQH--GQVL-------VDGVD----LAIADP--- 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 764 taadsdARSRGPVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQ 840
Cdd:TIGR01846 527 ------AWLRRQMGVVLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQ 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 920
Cdd:TIGR01846 599 RQRIAIARALVGNPRILIFDEATSALDYE-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRH 675
|
....*..
gi 1720421572 921 KDFQRSE 927
Cdd:TIGR01846 676 EELLALQ 682
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
696-926 |
9.87e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 107.07 E-value: 9.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclrtsnperetAADSDARSRgp 775
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVL-------GEDVA------------RDPAEVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWL-LNATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDilphgdqTQIGergiNLSGGQRQRISVA 847
Cdd:COG1131 75 IGYVPQEPALyPDLTVRENLRFfarlyglPRKEARERIDELLELFGLTDAAD-------RKVG----TLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKDF 923
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWE--LLRELAAEGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDEL 218
|
...
gi 1720421572 924 QRS 926
Cdd:COG1131 219 KAR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
693-914 |
1.43e-25 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 106.03 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQRV-SGAVFWNSSLPDSEGEDPRYCLRtsnpeRETaadsdar 771
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVRVDGTDISKLSEKELAAFR-----RRH------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 srgpVAYASQKPWLLNA-TVEENI----TFESPFNKQRYKMVIEACslqpdidilphgDQTQIGERgIN-----LSGGQR 841
Cdd:cd03255 84 ----IGFVFQSFNLLPDlTALENVelplLLAGVPKKERRERAEELL------------ERVGLGDR-LNhypseLSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 842 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 914
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
694-965 |
1.64e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 113.27 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAV-FWNSSLPDsegedprycLRTSnperetaadsDARS 772
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrFHDIPLTK---------LQLD----------SWRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 RgpVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 851
Cdd:PRK10789 390 R--LAVVSQTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 852 QHTNVVFLDDPFSALDVHlSDHlmqaGILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKdfqrsecQ 929
Cdd:PRK10789 468 LNAEILILDDALSAVDGR-TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHD-------Q 535
|
250 260 270
....*....|....*....|....*....|....*...
gi 1720421572 930 LFEH--WKTLMNRQdQELEKETvmeRKAPEPSQGLPRA 965
Cdd:PRK10789 536 LAQQsgWYRDMYRY-QQLEAAL---DDAPEIREEAVDA 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
686-922 |
2.40e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 112.80 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNsslpdseGEDPR-YCLRTSnper 762
Cdd:PRK11176 349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDID--EGEILLD-------GHDLRdYTLASL---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 763 etaadsdarsRGPVAYASQKPWLLNATVEENITFESpfnKQRY--KMVIEACSLQPDIDI---LPHGDQTQIGERGINLS 837
Cdd:PRK11176 416 ----------RNQVALVSQNVHLFNDTIANNIAYAR---TEQYsrEQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 917
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVER 559
|
....*
gi 1720421572 918 GTLKD 922
Cdd:PRK11176 560 GTHAE 564
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
686-918 |
5.09e-25 |
|
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: 104.52 E-value: 5.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPryclrTSNPEReta 765
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-------GRDV-----TGVPPE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adsdarsRGPVAYASQK----PWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigergi 834
Cdd:cd03259 71 -------RRNIGMVFQDyalfPHL---TVAENIAFglklrgvPKAEIRARVRELLELVGLEGLLNRYPHE---------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 835 nLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGT 913
Cdd:cd03259 131 -LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGR 208
|
....*
gi 1720421572 914 IQREG 918
Cdd:cd03259 209 IVQVG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
691-910 |
7.41e-25 |
|
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: 104.15 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclrtsnperetaadsda 770
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-------GKPLE------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGPVAYASQK---PWLLNATVEE--------NITFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGG 839
Cdd:cd03235 65 KERKRIGYVPQRrsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEALER---VGLSELADR-QIGE----LSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 840 QRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILEL---LRDDKRTVVLVTHKL-QYLPHADWIIAMK 910
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPK-----TQEDIYELlreLRREGMTILVVTHDLgLVLEYFDRVLLLN 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
696-927 |
9.62e-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: 104.51 E-value: 9.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDpryclRTSNPEREtaadsDARSRGP 775
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-------DGED-----ISGLSEAE-----LYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 844
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAF--PLRehtrlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 845 SVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQ-YLPHADWIIAMKDGTIQREGT 919
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASG-----VIDDLIRSLKKelglTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGT 220
|
....*...
gi 1720421572 920 LKDFQRSE 927
Cdd:cd03261 221 PEELRASD 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
389-897 |
2.98e-24 |
|
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: 108.60 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 389 GAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVA--IDTNQLMWFFFLCPNLWAMPVQIIV--GVILLYYILGVSALIGA 464
Cdd:TIGR02868 86 GALRVRVYERLARQALA--GRRRLRRGDLLGRLGadVDALQDLYVRVIVPAGVALVVGAAAvaAIAVLSVPAALILAAGL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 465 AVIILLAPvqyFVATKLSQAQRSTLEYS-NERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAVYTSIS 543
Cdd:TIGR02868 164 LLAGFVAP---LVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 544 IFMNTAIPIAAVLITFVGHVSFFKESDFSPS----VAFASLSLFHilvtPLFLLSSVVRSTVKALVSVQKLSEFLSSAEI 619
Cdd:TIGR02868 241 AALTLLAAGLAVLGALWAGGPAVADGRLAPVtlavLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLDAAGP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 620 REEQCAPREpapqgqagkyQAVPLKVVNRkrpareEVRDLLgplqrltpsmdgdadnfcvqiiggfFTWtPDGIPTLSNI 699
Cdd:TIGR02868 317 VAEGSAPAA----------GAVGLGKPTL------ELRDLS-------------------------AGY-PGAPPVLDGV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 700 TIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavfwnsSLPDSEGEdpryclRTSNPERETAADSDARSRgPVAYA 779
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAG-------------LLDPLQGE------VTLDGVPVSSLDQDEVRR-RVSVC 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 780 SQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVF 858
Cdd:TIGR02868 415 AQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILL 494
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1720421572 859 LDDPFSALDVHLSDHLmqagiLELLRD--DKRTVVLVTHKL 897
Cdd:TIGR02868 495 LDEPTEHLDAETADEL-----LEDLLAalSGRTVVLITHHL 530
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
445-919 |
4.44e-24 |
|
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: 108.63 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 445 IIVGVILLYYILGV--SALIGAAVIILLAPVqYFVATKLSQAQRStleySNERLKQTN----EMLRGIKLLKLYAWENI- 517
Cdd:TIGR02204 145 MCIGGLIMMFITSPklTSLVLLAVPLVLLPI-LLFGRRVRKLSRE----SQDRIADAGsyagETLGAIRTVQAFGHEDAe 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 518 ---FCSRVEMTRRKEMTSLRAFAVYTSISIFMNTAipiAAVLITFVGhVSFFKESDFSPSV--AFASLSLFhiLVTPLFL 592
Cdd:TIGR02204 220 rsrFGGAVEKAYEAARQRIRTRALLTAIVIVLVFG---AIVGVLWVG-AHDVIAGKMSAGTlgQFVFYAVM--VAGSIGT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 593 LSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPREPAPQGQAgkyqAVPLKVVNRKRPAREEVrdllgplqrltpsmdg 672
Cdd:TIGR02204 294 LSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRG----EIEFEQVNFAYPARPDQ---------------- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 673 dadnfcvqiiggfftwtpdgiPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnssLPDseGEDpr 752
Cdd:TIGR02204 354 ---------------------PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRI-----LLD--GVD-- 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 753 ycLRTSNPEretaadsDARSRgpVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEAC-SLQPD--IDILPHGDQTQI 829
Cdd:TIGR02204 404 --LRQLDPA-------ELRAR--MALVPQDPVLFAASVMENIRYGRP--DATDEEVEAAArAAHAHefISALPEGYDTYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 830 GERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAM 909
Cdd:TIGR02204 471 GERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA-ESEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVM 547
|
490
....*....|
gi 1720421572 910 KDGTIQREGT 919
Cdd:TIGR02204 548 DQGRIVAQGT 557
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
693-918 |
7.25e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 101.43 E-value: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDpryclrtsnpeRETAADSDARS 772
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF-------DGKD-----------LLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 RGP-VAYASQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVI--EACSLQPDIDIL---PHGdqtqigerginLSG 838
Cdd:cd03257 80 RRKeIQMVFQDPMSsLNPrmTIGEQIAeplriHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 839 GQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMKD 911
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKLQEelglTLLFITHDLgvvAKI--ADRVAVMYA 221
|
....*..
gi 1720421572 912 GTIQREG 918
Cdd:cd03257 222 GKIVEEG 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
693-917 |
1.81e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 100.50 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQRV-SGAVFWNsslpdseGEDPryclrtsnpereTAADSD 769
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLniLGGL---DRPtSGEVLID-------GQDI------------SSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSR------GpvaYASQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiN 835
Cdd:COG1136 79 ELARlrrrhiG---FVFQFFNLLpELTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQ 915
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL-LRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
..
gi 1720421572 916 RE 917
Cdd:COG1136 224 SD 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
685-919 |
2.38e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 105.76 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 685 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPryclrTSNPERET 764
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD-------GKDL-----TKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 765 AAdsDARSRGPV---AYASqkpwlLNA--TVEENITfESPFN------KQRYKMV---IEACSLQPD-IDILPHGdqtqi 829
Cdd:COG1123 338 RE--LRRRVQMVfqdPYSS-----LNPrmTVGDIIA-EPLRLhgllsrAERRERVaelLERVGLPPDlADRYPHE----- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 830 gerginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLph 902
Cdd:COG1123 405 ------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSV-----QAQILNLLRDLQRelglTYLFISHDLavvRYI-- 471
|
250
....*....|....*..
gi 1720421572 903 ADWIIAMKDGTIQREGT 919
Cdd:COG1123 472 ADRVAVMYDGRIVEDGP 488
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
692-913 |
3.44e-23 |
|
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: 97.32 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegedpryclrtsnpERETAADSDAR 771
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID--------------------GKDIAKLPLEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGPVAYASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALY 851
Cdd:cd00267 71 LRRRIGYVPQ------------------------------------------------------LSGGQRQRVALARALL 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 852 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 913
Cdd:cd00267 97 LNPDLLLLDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1070-1339 |
3.93e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.63 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1070 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1149
Cdd:COG1132 63 LLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1150 SRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1225
Cdd:COG1132 143 VRSVVTLIGALVVLFVIDWrlalIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAE----LNGRLQESLSGIRVVKAFGR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1226 EARFQQKLLEYTDSNNIASLfltAANRWLEVRMPGPAAVLpqeYIGACVVLIAAATSIsnsLHRELSAGLVGLGLTYALM 1305
Cdd:COG1132 219 EERELERFREANEELRRANL---RAARLSALFFPLMELLG---NLGLALVLLVGGLLV---LSGSLTVGDLVAFILYLLR 289
|
250 260 270
....*....|....*....|....*....|....
gi 1720421572 1306 VSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAE 1339
Cdd:COG1132 290 LFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
690-926 |
7.78e-23 |
|
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: 98.91 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPERetaadsd 769
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-------GED----IREQDPVE------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 arSRGPVAYASQKPWLL-NATVEENIT-------FESPFNKQRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGG 839
Cdd:cd03295 73 --LRRKIGYVIQQIGLFpHMTVEENIAlvpkllkWPKEKIRERADELLALVGLDPAefADRYPH-----------ELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 840 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 918
Cdd:cd03295 140 QQQRVGVARALAADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVG 218
|
....*...
gi 1720421572 919 TLKDFQRS 926
Cdd:cd03295 219 TPDEILRS 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
692-922 |
2.14e-22 |
|
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: 104.05 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLpdsegedpryclrTSNPERETAadsdar 771
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-------------LKDIDRHTL------ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 sRGPVAYASQKPWLLNATVEENITFESPFNKQRyKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 848
Cdd:TIGR01193 547 -RQFINYLPQEPYIFSGSILENLLLGAKENVSQ-DEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 849 ALYQHTNVVFLDDPFSALDVhlsdhLMQAGILE-LLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 922
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDT-----ITEKKIVNnLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
690-924 |
3.14e-22 |
|
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: 97.25 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSslpdsegedpryclrTSNPERETAADSD 769
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDG---------------TDINKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRgpVAYASQKPWLLN-ATVEENI---------TFESPFN------KQRykmvieACSLQPDIDILPHGDQtqigeRG 833
Cdd:cd03256 76 LRRQ--IGMIFQQFNLIErLSVLENVlsgrlgrrsTWRSLFGlfpkeeKQR------ALAALERVGLLDKAYQ-----RA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 834 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDG 912
Cdd:cd03256 143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDL-LKRINREEGITVIVSLHQVDLaREYADRIVGLKDG 221
|
250
....*....|..
gi 1720421572 913 TIQREGTLKDFQ 924
Cdd:cd03256 222 RIVFDGPPAELT 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
686-918 |
3.54e-22 |
|
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: 95.07 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEdpryCLRTSnpereta 765
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----ALSSL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adsdarsrgpVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRIS 845
Cdd:cd03247 77 ----------ISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 918
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSL-IFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
694-914 |
3.54e-22 |
|
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: 94.98 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnssLPDseGEDprycLRTSNPERetaadsdarSR 773
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----RLD--GAD----ISQWDPNE---------LG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GPVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQH 853
Cdd:cd03246 76 DHVGYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421572 854 TNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 914
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQA--IAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
686-926 |
8.34e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 96.03 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSslpdsegedpryclrtsnpeRETA 765
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG--------------------RPVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 ADSDARSRGPVAYASQKPWL-LNA--TVEENIT-----FESPFNKQRYKMVIEACSLQPDI-DILPHgdqtQigerginL 836
Cdd:COG1124 71 RRRRKAFRRRVQMVFQDPYAsLHPrhTVDRILAeplriHGLPDREERIAELLEQVGLPPSFlDRYPH----Q-------L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKD 911
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVS-----VQAEILNLLKDLREerglTYLFVSHDLAVVAHlCDRVAVMQN 214
|
250
....*....|....*
gi 1720421572 912 GTIQREGTLKDFQRS 926
Cdd:COG1124 215 GRIVEELTVADLLAG 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
696-864 |
1.02e-21 |
|
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: 92.71 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRYclrtsnperetaaDSDARSRGP 775
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD-------GQDLTD-------------DERKSLRKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLLNA-TVEENITFESPFnKQRYKMVIEAcslQPDIDI----LPHGDQTQIGERGINLSGGQRQRISVARAL 850
Cdd:pfam00005 61 IGYVFQDPQLFPRlTVRENLRLGLLL-KGLSKREKDA---RAEEALeklgLGDLADRPVGERPGTLSGGQRQRVAIARAL 136
|
170
....*....|....
gi 1720421572 851 YQHTNVVFLDDPFS 864
Cdd:pfam00005 137 LTKPKLLLLDEPTA 150
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
694-927 |
1.67e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.54 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNsslpdseGEDPryclrtsnpereTAADSDAR 771
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLsmISRLLPPD--SGEVLVD-------GLDV------------ATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRgPVAYASQKPWL-LNATVEENITF-ESPFNKQR-----YKMVIEAcslqpdIDILphgDQTQIGERGIN-LSGGQRQR 843
Cdd:COG4604 74 AK-RLAILRQENHInSRLTVRELVAFgRFPYSKGRltaedREIIDEA------IAYL---DLEDLADRYLDeLSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDK-RTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLK 921
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMK--LLRRLADELgKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPE 221
|
....*.
gi 1720421572 922 DFQRSE 927
Cdd:COG4604 222 EIITPE 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
690-914 |
3.35e-21 |
|
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: 93.69 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSS-LPDSEGedpRYCLRTsnperetaads 768
Cdd:cd03248 25 PD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpISQYEH---KYLHSK----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 darsrgpVAYASQKPWLLNATVEENITFESPfnKQRYKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRIS 845
Cdd:cd03248 90 -------VSLVGQEPVLFARSLQDNIAYGLQ--SCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 914
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAE-SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
691-929 |
4.60e-21 |
|
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: 93.77 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRYCLRTsnperetaadsdA 770
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-------GEDVRKEPRE------------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRgpVAYASQKPWL-LNATVEENITFESPFN-------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQ 842
Cdd:COG4555 73 RRQ--IGVLPDERGLyDRLTVRENIRYFAELYglfdeelKKRIEELIELLGLEEFLDRRVGE-----------LSTGMKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 843 RISVARALYQHTNVVFLDDPFSALDVhLSDHLMQaGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLK 921
Cdd:COG4555 140 KVALARALVHDPKVLLLDEPTNGLDV-MARRLLR-EILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLD 217
|
....*...
gi 1720421572 922 DFQRSECQ 929
Cdd:COG4555 218 ELREEIGE 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
692-913 |
4.64e-21 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 91.86 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPERETaadsdar 771
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------GED----LTDLEDELPP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGPVAYASQKPWLL-NATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARAL 850
Cdd:cd03229 74 LRRRIGMVFQDFALFpHLTVLENIAL--------------------------------------GLSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 851 YQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRD----DKRTVVLVTHKLQYLPH-ADWIIAMKDGT 913
Cdd:cd03229 116 AMDPDVLLLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
686-930 |
7.58e-21 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 98.05 E-value: 7.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQRVSGAVFWNsslpdseGEDPRyclrtsnper 762
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLD-------GRDLL---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 763 etAADSDARSRGpVAYASQKPW--LLNATVEENITfESPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqiger 832
Cdd:COG1123 75 --ELSEALRGRR-IGMVFQDPMtqLNPVTVGDQIA-EALENlglsraeaRARVLELLEAVGLERRLDRYPH--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 833 giNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQY-LPHADWII 907
Cdd:COG1123 142 --QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTT-----QAEILDLLRELQRergtTVLLITHDLGVvAEIADRVV 214
|
250 260
....*....|....*....|...
gi 1720421572 908 AMKDGTIQREGTLKDFQRSECQL 930
Cdd:COG1123 215 VMDDGRIVEDGPPEEILAAPQAL 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
696-927 |
2.40e-19 |
|
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: 88.88 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpryclRTSNPERETAAdsdARSRgp 775
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-------GQD-----ITGLSEKELYE---LRRR-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLLNA-TVEENITFesPFN----------KQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRI 844
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAF--PLRehtdlseaeiRELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 845 SVARALYQHTNVVFLDDPFSALDVHLS---DHLmqagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTL 920
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSaviDEL----IRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
....*..
gi 1720421572 921 KDFQRSE 927
Cdd:COG1127 227 EELLASD 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
696-914 |
3.35e-19 |
|
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: 86.30 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclrtSNPEretaadsDARSRgp 775
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-------GKDIK-----KEPE-------EVKRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLL-NATVEENItfespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHT 854
Cdd:cd03230 75 IGYLPEEPSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421572 855 NVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 914
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
688-914 |
3.49e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 87.47 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 688 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGavfwnsslpdsegedpryCLRTSNPERETAAD 767
Cdd:cd03369 16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEG------------------KIEIDGIDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 768 SDARSRgpVAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEACSlqpdidilphgdqtqIGERGINLSGGQRQRISVA 847
Cdd:cd03369 78 EDLRSS--LTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDkrTVVLVTHKLQYLPHADWIIAMKDGTI 914
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
691-919 |
4.97e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 90.52 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQrvSGAVFWNsslpdseGEDpryclrtsnperetAADS 768
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrmIAGLEDPT--SGEILIG-------GRD--------------VTDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 DARSRGpVAYASQKPWLL-NATVEENITF------ESPfnKQRYKMVIEAcslqpdIDILphgdqtQIGE----RGINLS 837
Cdd:COG3839 71 PPKDRN-IAMVFQSYALYpHMTVYENIAFplklrkVPK--AEIDRRVREA------AELL------GLEDlldrKPKQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKD 911
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVE-MRAEIKRLHRRLGTTTIYVTHdqveamTL-----ADRIAVMND 209
|
....*...
gi 1720421572 912 GTIQREGT 919
Cdd:COG3839 210 GRIQQVGT 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
696-895 |
1.23e-18 |
|
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: 85.61 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRyclrtsnperetaaDSDARSRGP 775
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-------GEPIR--------------DAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLLNA-TVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 849
Cdd:COG4133 77 LAYLGHADGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720421572 850 LYQHTNVVFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTH 895
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALL--AELIAAHLARGGAVLLTTH 189
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
696-933 |
1.55e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.67 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgEMQRvSGAVFWNsslpdseGEDpryclrtsnpereTAADSDARSR 773
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLriIAGL-ETPD-SGRIVLN-------GRD-------------LFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GpVAYASQKPWLL-NATVEENITF----ESPFNKQRYKMV---IEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 845
Cdd:COG1118 76 R-VGFVFQHYALFpHMTVAENIAFglrvRPPSKAEIRARVeelLELVQLEGLADRYPS-----------QLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHLSDHLMQaGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDfq 924
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAKVRKELRR-WLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGRIEQVGTPDE-- 220
|
....*....
gi 1720421572 925 rsecqLFEH 933
Cdd:COG1118 221 -----VYDR 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
690-921 |
2.16e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 91.32 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlPDSEgEDPRYcLRTSnperetaadsd 769
Cdd:TIGR00958 492 PD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-PLVQ-YDHHY-LHRQ----------- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 arsrgpVAYASQKPWLLNATVEENITFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 848
Cdd:TIGR00958 557 ------VALVGQEPVLFSGSVRENIAYGLTDTPDEEIMaAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 849 ALYQHTNVVFLDDPFSALDVHlSDHLMQagilELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 921
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAE-CEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
686-932 |
3.27e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.34 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEdpryclrtsnpereta 765
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF---------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRY-KMVIEACSLQPDIDILPHGD-QTQigergiNLSGGQRQR 843
Cdd:PRK13648 79 --EKLRKHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYdEMHRRVSEALKQVDMLERADyEPN------ALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDF 923
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
....*....
gi 1720421572 924 QRSECQLFE 932
Cdd:PRK13648 230 FDHAEELTR 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
696-898 |
4.01e-18 |
|
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: 84.92 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWNSSLPDSEGEDPrYCLRTSnperetaadsda 770
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDV-LELRRR------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 rsrgpVAYASQKPWLLNATVEENITF------ESPfNKQRYKMVIEACS---LQPDIDILPHGDQtqigerginLSGGQR 841
Cdd:cd03260 83 -----VGMVFQKPNPFPGSIYDNVAYglrlhgIKL-KEELDERVEEALRkaaLWDEVKDRLHALG---------LSGGQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 842 QRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELlrDDKRTVVLVTHKLQ 898
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQ 201
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
691-897 |
4.31e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdsegedpryclrtsnpERETAAdsda 770
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------------------RRAGGA---- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 rsrgPVAYASQK---PWLLNATVEENITF-----ESPFNKQRY--KMVIEACSLQPDIDILPHgdqTQIGErginLSGGQ 840
Cdd:NF040873 56 ----RVAYVPQRsevPDSLPLTVRDLVAMgrwarRGLWRRLTRddRAAVDDALERVGLADLAG---RQLGE----LSGGQ 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLmqAGILELLRDDKRTVVLVTHKL 897
Cdd:NF040873 125 RQRALLAQGLAQEADLLLLDEPTTGLDAESRERI--IALLAEEHARGATVVVVTHDL 179
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
691-909 |
5.24e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRvsGAVFWnsslpdsEGEDprycLRTSNPERetaads 768
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLkiVASLISPTS--GTLLF-------EGED----ISTLKPEI------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 darSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQ----PDidilphgdqtQIGERGIN-LSGGQRQR 843
Cdd:PRK10247 79 ---YRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLErfalPD----------TILTKNIAeLSGGEKQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 909
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
686-919 |
1.31e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATlgemqRvsgavFWNsslPDSeGEdprycLRTSNpeRET 764
Cdd:PRK11160 346 FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLqLLT-----R-----AWD---PQQ-GE-----ILLNG--QPI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 765 AADSDARSRGPVAYASQKPWLLNATVEENITFESP-FNKQRYKMVIEACSLQPDIDIlPHGDQTQIGERGINLSGGQRQR 843
Cdd:PRK11160 405 ADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQ-----ILELLAEhaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
692-914 |
1.40e-17 |
|
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: 81.32 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQRVSGAVFWNsslpdseGEdpryclrtsnpERETAADSD 769
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMkiLS--GLYKPDSGEILVD-------GK-----------EVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRGpVAYASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARA 849
Cdd:cd03216 72 ARRAG-IAMVYQ------------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 850 LYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 914
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
691-919 |
1.46e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 85.92 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN----SSLPdsegedpryclrtsnPERetaa 766
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLP---------------PEK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 767 dsdarsRgPVAYASQK----PWLlnaTVEENITF------ESPfnKQRYKMVIEACSLqpdIDILPHGDqtqigeRGIN- 835
Cdd:COG3842 77 ------R-NVGMVFQDyalfPHL---TVAENVAFglrmrgVPK--AEIRARVAELLEL---VGLEGLAD------RYPHq 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKlQY--LPHADWIIAMKDGT 913
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREE-MREELRRLQRELGITFIYVTHD-QEeaLALADRIAVMNDGR 213
|
....*.
gi 1720421572 914 IQREGT 919
Cdd:COG3842 214 IEQVGT 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
654-913 |
2.13e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.56 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 654 EEVRDLLGPLQRLTPSMDGD--ADNFCVQiiggfftwTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemq 731
Cdd:COG4178 343 EAADALPEAASRIETSEDGAlaLEDLTLR--------TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 732 rvsgavFWnsslPDSEGedpryclRTSNPERETaadsdarsrgpVAYASQKPWLLNATVEENITF---ESPFNKQRYKMV 808
Cdd:COG4178 412 ------LW----PYGSG-------RIARPAGAR-----------VLFLPQRPYLPLGTLREALLYpatAEAFSDAELREA 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 809 IEACSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDdkR 888
Cdd:COG4178 464 LEAVGLG---HLAERLDEEADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREELPG--T 535
|
250 260
....*....|....*....|....*
gi 1720421572 889 TVVLVTHKLQYLPHADWIIAMKDGT 913
Cdd:COG4178 536 TVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
673-914 |
2.64e-17 |
|
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: 87.05 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 673 DADNFCV--QIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGeMQRVSGAVFWNsslpdseGED 750
Cdd:COG4172 277 EARDLKVwfPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFD-------GQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 751 PRyclrtsnpERETAADSDARSRGPVA----YASQKPWLlnaTVEENIT------FESPFNKQRYKMVIEACS---LQPD 817
Cdd:COG4172 349 LD--------GLSRRALRPLRRRMQVVfqdpFGSLSPRM---TVGQIIAeglrvhGPGLSAAERRARVAEALEevgLDPA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 818 -IDILPHgdqtqigErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVL 892
Cdd:COG4172 418 aRHRYPH-------E----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV-----QAQILDLLRDlqREHglAYLF 481
|
250 260
....*....|....*....|....*
gi 1720421572 893 VTHKLQ---YLphADWIIAMKDGTI 914
Cdd:COG4172 482 ISHDLAvvrAL--AHRVMVMKDGKV 504
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
693-919 |
3.37e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.16 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQRVSGAVFWNSSLPDSEG-------EDPRYCLRTSNPERE 763
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVmsLLMRFYDLKNDHHIVFKNEHTNDMTNeqdyqgdEEQNVGMKNVNEFSL 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 764 TAADSDARS-------------------------RGPVAYASQKPWLLNATVEENITF-ESPFNKQRYKMVIEACSLQPD 817
Cdd:PTZ00265 1261 TKEGGSGEDstvfknsgkilldgvdicdynlkdlRNLFSIVSQEPMLFNMSIYENIKFgKEDATREDVKRACKFAAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 818 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKL 897
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
250 260
....*....|....*....|....*..
gi 1720421572 898 QYLPHADWIIAM----KDGT-IQREGT 919
Cdd:PTZ00265 1420 ASIKRSDKIVVFnnpdRTGSfVQAHGT 1446
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
694-919 |
5.32e-17 |
|
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: 86.41 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLGEMQrvSGAVFWNsslpdseGEDPRyclrtsnperETAADSDAR 771
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLarLLFRFYDVT--SGRILID-------GQDIR----------DVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGPVAyasQKPWLLNATVEENItfespfnkqRY----------KMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQR 841
Cdd:COG5265 433 AIGIVP---QDTVLFNDTIAYNI---------AYgrpdaseeevEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEK 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 842 QRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSR-TERAIQAALREVARG--RTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
686-919 |
6.48e-17 |
|
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: 86.54 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLATLgeMQRVSGAVFWnsslpdsEGEDpryclRTSNPeRE 763
Cdd:TIGR03796 485 FGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIakLVAGL--YQPWSGEILF-------DGIP-----REEIP-RE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 764 TAADSdarsrgpVAYASQKPWLLNATVEENITFESPFNKQryKMVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQ 840
Cdd:TIGR03796 550 VLANS-------VAMVDQDIFLFEGTVRDNLTLWDPTIPD--ADLVRACkdaAIHDVITSRPGGYDAELAEGGANLSGGQ 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:TIGR03796 621 RQRLEIARALVRNPSILILDEATSALDP-----ETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
703-918 |
8.96e-17 |
|
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: 80.61 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 703 IPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpryclrtsnperETAADSDARsrgPVAYASQK 782
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-------GVD------------VTAAPPADR---PVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 783 PWLL-NATVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARALYQHT 854
Cdd:cd03298 79 NNLFaHLTVEQNVGLGlspglklTAEDRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 855 NVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 918
Cdd:cd03298 148 PVLLLDEPFAALDPALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
686-922 |
8.98e-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: 8.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMQRvSGAVFWNsslpdseGEDpryCLRTSNPERET 764
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrCINGLERPT-SGSVLVD-------GTD---LTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 765 AadsdaRSRgpVAYASQKPWLLNA-TVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNL 836
Cdd:cd03258 80 A-----RRR--IGMIFQHFNLLSSrTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKD 911
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEK 216
|
250
....*....|.
gi 1720421572 912 GTIQREGTLKD 922
Cdd:cd03258 217 GEVVEEGTVEE 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
692-923 |
1.46e-16 |
|
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: 80.17 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDpryclrtsnperETAADSDAR 771
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-------DGRD------------ITGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGPVAYASQKPWLL-NATVEENITF-ESPFNKQRYKMVIE-ACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVAR 848
Cdd:cd03224 73 ARAGIGYVPEGRRIFpELTVEENLLLgAYARRRAKRKARLErVYELFPRL-------KERRKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 849 ALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 923
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEA--IRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
686-909 |
2.05e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.45 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---RVSGAVFWNsslpdseGEDprycLRTSNPER 762
Cdd:COG4136 7 LTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLN-------GRR----LTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 763 etaadsdarsRGpVAYASQKPWLL-NATVEENITF---ESPFNKQRYKMVIEAcsLQpDIDiLPHgdqtqIGERGIN-LS 837
Cdd:COG4136 76 ----------RR-IGILFQDDLLFpHLSVGENLAFalpPTIGRAQRRARVEQA--LE-EAG-LAG-----FADRDPAtLS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 909
Cdd:COG4136 136 GGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ-FREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
695-927 |
2.38e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.80 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 695 TLSNITIR-----------IPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpryCLRTSNPERe 763
Cdd:COG3840 3 RLDDLTYRygdfplrfdltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-------GQD---LTALPPAER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 764 taadsdarsrgPVAYASQK----PWLlnaTVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPhgDQtqiger 832
Cdd:COG3840 72 -----------PVSMLFQEnnlfPHL---TVAQNIGLGlrpglklTAEQRAQVEQALERVGLAGLLDRLP--GQ------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 833 ginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKD 911
Cdd:COG3840 130 ---LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE-MLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVAD 205
|
250
....*....|....*.
gi 1720421572 912 GTIQREGTLKDFQRSE 927
Cdd:COG3840 206 GRIAADGPTAALLDGE 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
691-919 |
3.55e-16 |
|
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: 79.69 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpryclrtsnperetAADSDA 770
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-------GED--------------ATDVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGpVAYASQKPWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSG 838
Cdd:cd03296 72 QERN-VGFVFQHYALFrHMTVFDNVAFglrvkprsERPPEaeiRAKVHELLKLVQLDWLADRYPA-----------QLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 839 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQRE 917
Cdd:cd03296 140 GQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL-RRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQV 218
|
..
gi 1720421572 918 GT 919
Cdd:cd03296 219 GT 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
698-927 |
3.91e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGED-PRYclrtsnperetAADSDARSRGPV 776
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-------DGEHiQHY-----------ASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 777 AYasqkpwllNATVEENITFESPFNKQRYKMvieacslQP--------DIDILPHGDQ----TQIGERGIN-LSGGQRQR 843
Cdd:PRK10253 87 AQ--------NATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVhlsDHlmQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREG 918
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnQACRYASHLIALREGKIVAQG 226
|
....*....
gi 1720421572 919 TLKDFQRSE 927
Cdd:PRK10253 227 APKEIVTAE 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
696-898 |
4.27e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 4.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAV-FWNSSLPDSEgEDPryclrtsnperetaadSD 769
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVtFHGKNLYAPD-VDP----------------VE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRgpVAYASQKPWLLNATVEENITFESPFNKQRYKM--VIEACSLQPdidILPHGDQTQIGERGINLSGGQRQRISVA 847
Cdd:PRK14243 89 VRRR--IGMVFQKPNPFPKSIYDNIAYGARINGYKGDMdeLVERSLRQA---ALWDEVKDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 848 RALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHKLQ 898
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSAL-----DPISTLRIEELMHELKEqyTIIIVTHNMQ 211
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
689-895 |
5.65e-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: 76.81 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMqrvsgavfWnsslpdsegedPRYCLRTSNPERETaads 768
Cdd:cd03223 10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGL--------W-----------PWGSGRIGMPEGED---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 darsrgpVAYASQKPWLLNATVEENItfespfnkqrykmvieacslqpdidILPHGDqtqigergiNLSGGQRQRISVAR 848
Cdd:cd03223 66 -------LLFLPQRPYLPLGTLREQL-------------------------IYPWDD---------VLSGGEQQRLAFAR 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720421572 849 ALYQHTNVVFLDDPFSALDVHLSDHLMQagileLLRDDKRTVVLVTH 895
Cdd:cd03223 105 LLLHKPKFVFLDEATSALDEESEDRLYQ-----LLKELGITVISVGH 146
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
691-918 |
6.31e-16 |
|
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: 78.07 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpryclrtsnperetAADSDA 770
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-------GRD--------------VTDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGpVAYASQKPWLL-NATVEENITFESPFNKQRyKMVIE------ACSLQpdIDILPHGDQTQigerginLSGGQRQR 843
Cdd:cd03301 70 KDRD-IAMVFQNYALYpHMTVYDNIAFGLKLRKVP-KDEIDervrevAELLQ--IEHLLDRKPKQ-------LSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 918
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQ-MRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
694-919 |
1.18e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.93 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQRV----SGAVfwnssLPDseGEDPRYCLRTSnperetaadsd 769
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQRVfdpqSGRI-----LID--GTDIRTVTRAS----------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 arSRGPVAYASQKPWLLNATVEENITFESPfNKQRYKMVIEACSLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVA 847
Cdd:PRK13657 407 --LRRNIAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHdfIERKPDGYDTVVGERGRQLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAA--LDELMKG-RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
691-922 |
1.69e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 77.28 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDpryCLRTSNPERetaadsda 770
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL-------DGKD---ITNLPPHKR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 rsrgPVAYASQKPWLL-NATVEENITF-----ESPFNKQRYKmVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQR 843
Cdd:cd03300 73 ----PVNTVFQNYALFpHLTVFENIAFglrlkKLPKAEIKER-VAEALDL---VQLEGYAN------RKPSqLSGGQQQR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHlMQagiLELLRDDKR---TVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 919
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKD-MQ---LELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGT 214
|
...
gi 1720421572 920 LKD 922
Cdd:cd03300 215 PEE 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
694-895 |
1.90e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 77.98 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdsegedpryclrTSNPERETAADSDarsR 773
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-------------------TLDGVPVTGPGAD---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GPVAyasQK----PWLlnaTVEENITFESPFNK----QRYKMVIEACSLqpdIDiLPHGDQTQIGErginLSGGQRQRIS 845
Cdd:COG4525 79 GVVF---QKdallPWL---NVLDNVAFGLRLRGvpkaERRARAEELLAL---VG-LADFARRRIWQ----LSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVhLSDHLMQAGILELLRDDKRTVVLVTH 895
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDA-LTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
690-922 |
2.18e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.20 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEDPRYclrtsnperetaadsD 769
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL-------IKGEPIKY---------------D 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARS----RGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiN 835
Cdd:PRK13639 70 KKSllevRKTVGIVFQNPddQLFAPTVEEDVAF-GPLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------H 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTI 914
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKI 215
|
....*...
gi 1720421572 915 QREGTLKD 922
Cdd:PRK13639 216 IKEGTPKE 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
690-922 |
2.24e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.35 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDsegedpryclrtsnpereTAADSD 769
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID------------------YSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGG 839
Cdd:PRK13636 78 MKLRESVGMVFQDPdnQLFSASVYQDVSF-GAVNlklpedevRKRVDNALKRTGIEHLKDKPTHC-----------LSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 840 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 918
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL-LVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224
|
....
gi 1720421572 919 TLKD 922
Cdd:PRK13636 225 NPKE 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
696-919 |
2.44e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.36 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlPDSEGEDPRYCLRTSNPERETAADSDARSRGP 775
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK-PISMLSSRQLARRLALLPQHHLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYAsQKPWLlnatveeniTFESPFNKQRYKMVIEACslqpdidilphgDQTQIGE----RGINLSGGQRQRISVARALY 851
Cdd:PRK11231 97 VAYG-RSPWL---------SLWGRLSAEDNARVNQAM------------EQTRINHladrRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 852 QHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 919
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
698-926 |
2.79e-15 |
|
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: 80.70 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 698 NITIRIPRGQLTMIVGQVGCGKSSLLlatlGEMQRVSGavfwnsslPDS-----EGEDPRYCLRTSnperetaadsdarS 772
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLI----NLLQRVYD--------PTVgqiliDGIDINTVTRES-------------L 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 RGPVAYASQKPWLLNATVEENITF--ESPFNKQRYKMViEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARAL 850
Cdd:TIGR01192 408 RKSIATVFQDAGLFNRSIRENIRLgrEGATDEEVYEAA-KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 851 YQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 926
Cdd:TIGR01192 487 LKNAPILVLDEATSALDVETEARVKNA--IDALRKN-RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
706-918 |
3.13e-15 |
|
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: 76.18 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 706 GQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDsegeDPRYCLRTSNPEREtaadsdarsrgpVAYASQKPWL 785
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF----DSRKKINLPPQQRK------------IGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 786 L-NATVEENITFESPFNKQRYKMVIEAcslqpdiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHTNVVFLDDPF 863
Cdd:cd03297 87 FpHLNVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 864 SALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL---QYLphADWIIAMKDGTIQREG 918
Cdd:cd03297 160 SALDRALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
691-919 |
3.19e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.53 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavfwnsSLPDSEGEdprycLRTSNpeRETAADSDA 770
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG-------------YYPLTEGE-----IRLDG--RPLSSLSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARAL 850
Cdd:PRK10790 412 VLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 851 YQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQA--LAAVR-EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
698-919 |
3.36e-15 |
|
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: 77.30 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPRyclrtsnpereTAADSDARS--RGP 775
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-------DGQDIA-----------AMSRKELRElrRKK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLL-NATVEENITF------ESPFNKQRYKM-VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVA 847
Cdd:cd03294 104 ISMVFQSFALLpHRTVLENVAFglevqgVPRAEREERAAeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 848 RALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 919
Cdd:cd03294 173 RALAVDPDILLMDEAFSALD-PLIRREMQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGT 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
690-895 |
3.92e-15 |
|
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: 75.91 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN----SSLPDSEGEDPRyclrtsnpereta 765
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvSDLRGRAIPYLR------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adsdaRSRGpVAYASQKpWLLNATVEENITF------ESPFN-KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSG 838
Cdd:cd03292 78 -----RKIG-VVFQDFR-LLPDRNVYENVAFalevtgVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 839 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD-DKR--TVVLVTH 895
Cdd:cd03292 140 GEQQRVAIARAIVNSPTILIADEPTGNLDPDTT-----WEIMNLLKKiNKAgtTVVVATH 194
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
696-914 |
6.93e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.25 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEDPRYCLRtsnperetaadsDARsrgp 775
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQ------------DAR---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 vayasQKPWllnATVEENITFESPFN-KQRYKMVIEACSLQPdidilphgdqtQIGERGINLSGGQRQRISVARALYQHT 854
Cdd:PRK11247 92 -----LLPW---KKVIDNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421572 855 NVVFLDDPFSALDVhLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 914
Cdd:PRK11247 153 GLLLLDEPLGALDA-LTRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
711-919 |
7.77e-15 |
|
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: 77.15 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 711 IVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPERetaadsdaRSRGPV--AYAsqkpWLLNA 788
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLD-------GED----VTNVPPHL--------RHINMVfqSYA----LFPHM 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 789 TVEENITFESPFNK----QRYKMVIEACSLqpdidilphgdqTQIGERG----INLSGGQRQRISVARALYQHTNVVFLD 860
Cdd:TIGR01187 58 TVEENVAFGLKMRKvpraEIKPRVLEALRL------------VQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLD 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 861 DPFSALDVHLSDhLMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 919
Cdd:TIGR01187 126 EPLSALDKKLRD-QMQLELKTIQEQLGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
696-943 |
1.67e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.05 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlatlgemQRVSGAVFWNSSlPDSEGEdprycLRTSNPERETAADSDAR-SRG 774
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKS-AGSHIE-----LLGRTVQREGRLARDIRkSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 775 PVAYASQKPWLLNA-TVEENITF----ESPFNKQRYKMVIEAcSLQPDIDILphgdqTQIG------ERGINLSGGQRQR 843
Cdd:PRK09984 87 NTGYIFQQFNLVNRlSVLENVLIgalgSTPFWRTCFSWFTRE-QKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMqagilELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 918
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVM-----DTLRDinqnDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDG 235
|
250 260
....*....|....*....|....*
gi 1720421572 919 TLKDFQRSEcqlFEHWKTLMNRQDQ 943
Cdd:PRK09984 236 SSQQFDNER---FDHLYRSINRVEE 257
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1069-1351 |
1.72e-14 |
|
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: 78.72 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1069 VYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPSTLEC 1148
Cdd:COG2274 197 VLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLT 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1149 LSRSTLLCVSALTVISY----VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFR 1224
Cdd:COG2274 276 ALLDLLFVLIFLIVLFFysppLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQ----SLLVETLRGIETIKALG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1225 YEARFQQKLLEYTD---SNNIASLFLTAANRWLevrmpgpAAVLPQeyIGACVVLIAAATSIsnsLHRELSAGlvglGLT 1301
Cdd:COG2274 352 AESRFRRRWENLLAkylNARFKLRRLSNLLSTL-------SGLLQQ--LATVALLWLGAYLV---IDGQLTLG----QLI 415
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 1302 YALMVSNYLNWMVRNLADM--EIQ--LGAVKRIHTLLKTEAESYEGLLELARPR 1351
Cdd:COG2274 416 AFNILSGRFLAPVAQLIGLlqRFQdaKIALERLDDILDLPPEREEGRSKLSLPR 469
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
696-922 |
1.75e-14 |
|
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: 74.29 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPERETaadsdarsrgp 775
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN-------GKD----ITNLPPEKRD----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLL-NATVEENITF----ESPFNKQRYKMVIE-ACSLqpDIDILPHGDQTqigergiNLSGGQRQRISVARA 849
Cdd:cd03299 73 ISYVPQNYALFpHMTVYKNIAYglkkRKVDKKEIERKVLEiAEML--GIDHLLNRKPE-------TLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 850 LYQHTNVVFLDDPFSALDVHLSDHLMqagilELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 922
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLR-----EELKKIRKefgvTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
686-923 |
1.76e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.07 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---RVSGAV-FWNSSLpdsegedprYclrtsn 759
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELEsevRVEGRVeFFNQNI---------Y------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 760 pERETAADsdaRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKM----VIEACSLQPDI-DILPHgdqtQIGERGI 834
Cdd:PRK14258 78 -ERRVNLN---RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLwDEIKH----KIHKSAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 835 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLS---DHLMQAGILEllrdDKRTVVLVTHKLQYLPHADWIIAMKD 911
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVSRLSDFTAFFK 225
|
250
....*....|..
gi 1720421572 912 GTIQREGTLKDF 923
Cdd:PRK14258 226 GNENRIGQLVEF 237
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
694-919 |
2.38e-14 |
|
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: 73.69 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRYclrtsnpERETAadsdarsR 773
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-------GYSIRT-------DRKAA-------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GPVAYASQK---PWLLnaTVEENITFESPF---NKQRYKMVIEA----CSLQPDIDilphgdqTQIGergiNLSGGQRQR 843
Cdd:cd03263 75 QSLGYCPQFdalFDEL--TVREHLRFYARLkglPKSEIKEEVELllrvLGLTDKAN-------KRAR----TLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRddKRTVVLVTHKLQ---YLphADWIIAMKDGTIQREGT 919
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL-ILEVRK--GRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGS 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
696-916 |
3.77e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQRVSGAVFWNSslpdseGEDPryclrtsnpereTAADSDARS--- 772
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLDKPTSGTYRVA------GQDV------------ATLDADALAqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 RGPVAYASQKPWLL-NATVEENITFESPF-------NKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 844
Cdd:PRK10535 85 REHFGFIFQRYHLLsHLTAAQNVEVPAVYaglerkqRLLRAQELLQRLGLEDRVEYQPS-----------QLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421572 845 SVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQR 916
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
683-917 |
3.79e-14 |
|
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: 74.07 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 683 GGFFtWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDprycLRTSNPER 762
Cdd:TIGR02769 15 GGLF-GAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSF-------RGQD----LYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 763 ETAADSDARSRGPVAYASQKP-----WLLNATVEENITFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNL 836
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSPSAVNPrmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKD 911
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDK 226
|
....*.
gi 1720421572 912 GTIQRE 917
Cdd:TIGR02769 227 GQIVEE 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
696-896 |
4.12e-14 |
|
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: 73.07 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---RVSGAVFWNSSlpdsegedPRyclrtsnpERETAADSdars 772
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQ--------PR--------KPDQFQKC---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 rgpVAYASQKPWLL-NATVEENITFESPF-------NKQRYKMVieacslqpDIDILPHGDQTQIGERGI-NLSGGQRQR 843
Cdd:cd03234 83 ---VAYVRQDDILLpGLTVRETLTYTAILrlprkssDAIRKKRV--------EDVLLRDLALTRIGGNLVkGISGGERRR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHK 896
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
696-927 |
4.26e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 74.29 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdSEGEdpryclRTSNPERETAADSDARSRgp 775
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV--------TIGE------RVITAGKKNKKLKPLRKK-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRIS 845
Cdd:PRK13634 87 VGIVFQFPehQLFEETVEKDICF-GPMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL----QYlphADWIIAMKDGTIQREGTLK 921
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEM-FYKLHKEKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPR 231
|
....*..
gi 1720421572 922 D-FQRSE 927
Cdd:PRK13634 232 EiFADPD 238
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
687-918 |
5.17e-14 |
|
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: 72.59 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 687 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpDSEGEDPryclrtsnperetaa 766
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAP--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 767 dsdarSRGPVAYASQKPWLL-NATVEENITFE-SPFNK----QRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSG 838
Cdd:TIGR01277 68 -----YQRPVSMLFQENNLFaHLTVRQNIGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 839 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 917
Cdd:TIGR01277 132 GQRQRVALARCLVRPNPILLLDEPFSALDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKIKVV 210
|
.
gi 1720421572 918 G 918
Cdd:TIGR01277 211 S 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
686-919 |
8.27e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.30 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMqrvsgavfwnssLPDsegEDPRYCLRTSNPERETA 765
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL------------LPD---DNPNSKITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 ADSDARSRGPVAYASQKPWLLNATVEENITFESPfNKQ--RYKMVIEACSLQPDIDILPHGDQTQIgergiNLSGGQRQR 843
Cdd:PRK13640 78 TVWDIREKVGIVFQNPDNQFVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 919
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKL-IRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
689-895 |
9.30e-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: 73.93 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG---EMQRVSGAVFWnsslpdsEGEDpryCLRTSNPEREt 764
Cdd:COG0444 13 TRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILF-------DGED---LLKLSEKELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 765 aadsdaRSRGP-VAYASQKPwlLNA-----TVEENITfESPFN------KQRYKMVIEA---CSLQPDIDIL---PHgdq 826
Cdd:COG0444 82 ------KIRGReIQMIFQDP--MTSlnpvmTVGDQIA-EPLRIhgglskAEARERAIELlerVGLPDPERRLdryPH--- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 827 tqigergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTH 895
Cdd:COG0444 150 --------ELSGGMRQRVMIARALALEPKLLIADEPTTALDV-----TIQAQILNLLKDLQRelglAILFITH 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
690-918 |
9.64e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.01 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN----SSLPDSEgeDPRycLRtsnpereta 765
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlSRLKRRE--IPY--LR--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 adsdaRSRGPVAyasQKPWLL-NATVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLS 837
Cdd:COG2884 79 -----RRIGVVF---QDFRLLpDRTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPHADW-IIAMKDGT 913
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPETSW-----EIMELLEEINRrgtTVLIATHDLELVDRMPKrVLELEDGR 214
|
....*
gi 1720421572 914 IQREG 918
Cdd:COG2884 215 LVRDE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
692-927 |
9.97e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 9.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQRVSGAVFWNsslpdseGEDprycLRTSNPeretaadSD 769
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMkiLS--GVYQPDSGEILLD-------GEP----VRFRSP-------RD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRGpVAYASQKPWLL-NATVEENITFESPFNK----QRYKMVIEACSL--QPDIDILPHgdqTQIGErginLSGGQRQ 842
Cdd:COG1129 76 AQAAG-IAIIHQELNLVpNLSVAENIFLGREPRRggliDWRAMRRRARELlaRLGLDIDPD---TPVGD----LSVAQQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 843 RISVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLK 921
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLF--RIIRRLKAQGVAIIYISHRLdEVFEIADRVTVLRDGRLVGTGPVA 225
|
....*.
gi 1720421572 922 DFQRSE 927
Cdd:COG1129 226 ELTEDE 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
696-895 |
3.51e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsSLPDSEGEDPRYclrtsnperetaadsdarsRGP 775
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI----KLDGGDIDDPDV-------------------AEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQ----KPWLlnaTVEENITFESPFNKQRYKMV---IEACSLQPDIDiLPHGdqtqigergiNLSGGQRQRISVAR 848
Cdd:PRK13539 75 CHYLGHrnamKPAL---TVAENLEFWAAFLGGEELDIaaaLEAVGLAPLAH-LPFG----------YLSAGQKRRVALAR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 849 ALYQHTNVVFLDDPFSALDVH--------LSDHLMQAGIlellrddkrtVVLVTH 895
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAavalfaelIRAHLAQGGI----------VIAATH 185
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
691-895 |
3.72e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.95 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGED----PRYclrtsnperetaa 766
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-------DGVDlshvPPY------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 767 dsdarsRGPVAYASQKPWLL-NATVEENITFESPFNK-------QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSG 838
Cdd:PRK11607 90 ------QRPINMMFQSYALFpHMTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 839 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH 895
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDR-MQLEVVDILERVGVTCVMVTH 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
825-918 |
4.83e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.77 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 825 DQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-A 903
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvS 219
|
90
....*....|....*
gi 1720421572 904 DWIIAMKDGTIQREG 918
Cdd:PRK10619 220 SHVIFLHQGKIEEEG 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
692-918 |
7.17e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.18 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEDPryclrtsnpereTAADSDAR 771
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL-------VAGDDV------------EALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRgPVAYASQKPWL-LNATVEENITFESPFNKQRYKMVIEACSLQPDiDILPHGDQTQIGERGI-NLSGGQRQRISVARA 849
Cdd:PRK09536 76 SR-RVASVPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 850 LYQHTNVVFLDDPFSALDVHlsdHLMQAgiLELLR---DDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 918
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDIN---HQVRT--LELVRrlvDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAG 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
694-914 |
1.41e-12 |
|
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: 69.17 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN----SSLPdsegedprycLRTsnperetaadsd 769
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDgidiSKLP----------LHT------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRgpVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 849
Cdd:cd03288 93 LRSR--LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 850 LYQHTNVVFLDDPFSALDVhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 914
Cdd:cd03288 171 FVRKSSILIMDEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
691-898 |
1.76e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.96 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsSLPDSEGEDPryclrtsNPERETAADSDA 770
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI----TLDGKPVEGP-------GAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSrgpvayasqkPWLlnaTVEENITFespfnKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI-NLSGGQRQRISVARA 849
Cdd:PRK11248 81 LL----------PWR---NVQDNVAF-----GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720421572 850 LYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKLQ 898
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1089-1240 |
2.36e-12 |
|
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: 69.37 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1089 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYV-- 1166
Cdd:cd18552 60 TYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdw 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 1167 --TPVFLVALLPLAVVCYFIQKYFRVASRDLQ-QLDDttqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSN 1240
Cdd:cd18552 140 klTLIALVVLPLAALPIRRIGKRLRKISRRSQeSMGD-----LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERL 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
676-919 |
2.46e-12 |
|
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: 71.90 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 676 NFCVQiiggfftWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllaTLGeMQRVSGAvfwnsslpdSEGEdprycL 755
Cdd:TIGR00957 1289 NYCLR-------YREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSL---TLG-LFRINES---------AEGE-----I 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 756 RTSNPERETAADSDARSRgpVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGIN 835
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFK--ITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGEN 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQ 915
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEVA 1498
|
....
gi 1720421572 916 REGT 919
Cdd:TIGR00957 1499 EFGA 1502
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
835-922 |
3.23e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.98 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 835 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGT 913
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ-MQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGR 222
|
....*....
gi 1720421572 914 IQREGTLKD 922
Cdd:PRK09452 223 IEQDGTPRE 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
687-897 |
3.63e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 687 TWTpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnSSLpdseGEDPRYCLRTSnperetaa 766
Cdd:PRK15056 15 TWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI---SIL----GQPTRQALQKN-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 767 dsdarsrgPVAYASQKP---WLLNATVEENIT---------FESPfnKQRYKMVIEACSLQPDIDILPHgdqTQIGErgi 834
Cdd:PRK15056 79 --------LVAYVPQSEevdWSFPVLVEDVVMmgryghmgwLRRA--KKRDRQIVTAALARVDMVEFRH---RQIGE--- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 835 nLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKL 897
Cdd:PRK15056 143 -LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNL 202
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
699-909 |
3.91e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPE--RETAADSDARSRGPV 776
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL-------GKD----LLGMKDDewRAVRSDIQMIFQDPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 777 AyaSQKPWLlnaTVEENI-----TFESPFNKQ----RYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGGQRQRISV 846
Cdd:PRK15079 109 A--SLNPRM---TIGEIIaeplrTYHPKLSRQevkdRVKAMMLKVGLLPNlINRYPH-----------EFSGGQCQRIGI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 847 ARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 909
Cdd:PRK15079 173 ARALILEPKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
690-919 |
5.11e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.09 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEDpryclrTSNPERETAAdsd 769
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-------VSGID------TGDFSKLQGI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 arsRGPVAYASQKP--WLLNATVEENITFeSPFNkqrykmvieACslQPDIDILPHGDQTqIGERGI---------NLSG 838
Cdd:PRK13644 76 ---RKLVGIVFQNPetQFVGRTVEEDLAF-GPEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 839 GQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 918
Cdd:PRK13644 140 GQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEG 217
|
.
gi 1720421572 919 T 919
Cdd:PRK13644 218 E 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1070-1330 |
5.12e-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: 68.35 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1070 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1149
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1150 SRSTLLCVSALTVISYVTPV-FLVALLPLAVVCYFIQKYF---RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1225
Cdd:cd07346 121 LSDVLTLIGALVILFYLNWKlTLVALLLLPLYVLILRYFRrriRKASREVRESLAE----LSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1226 EARFQQKLLEYTDSNNIASLfltAANRWLEVRMPGPAAVLpqeYIGACVVLIAAATSIsnsLHRELSAGlvglGLTYALM 1305
Cdd:cd07346 197 EEREIERFREANRDLRDANL---RAARLSALFSPLIGLLT---ALGTALVLLYGGYLV---LQGSLTIG----ELVAFLA 263
|
250 260
....*....|....*....|....*....
gi 1720421572 1306 VSNYLNWMVRNLADM--EIQ--LGAVKRI 1330
Cdd:cd07346 264 YLGMLFGPIQRLANLynQLQqaLASLERI 292
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
691-895 |
5.43e-12 |
|
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: 66.23 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSslpdsegedpryclrtsnpeRETAADSDA 770
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG--------------------TPLAEQRDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGpVAYASQKPWLLNA-TVEENITFESPFNKQRYKMVIEACslqpdidilphgdqTQIGERGIN------LSGGQRQR 843
Cdd:TIGR01189 71 PHEN-ILYLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 895
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
696-899 |
6.49e-12 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 66.04 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWNSSlpdsegedPRYclrtsnperetaadsDARSR 773
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLnaLAGRRTGLGVSGEVLINGR--------PLD---------------KRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GPVAYASQKPWLL-NATVEENITFespfnkqrykmvieACSLQpdidilphgdqtqigergiNLSGGQRQRISVARALYQ 852
Cdd:cd03213 82 KIIGYVPQDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALELVS 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720421572 853 HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY 899
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSS 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
696-898 |
6.56e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 67.37 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEM------QRVSGAVFWNsslpdseGED---PRYclrtsNPEREtaa 766
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLL-RCLNRMndlipgARVEGEILLD-------GEDiydPDV-----DVVEL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 767 dsdaRSRgpVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEA--------CSLQPDI-DILphgdqtqiGERGINLS 837
Cdd:COG1117 91 ----RRR--VGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWDEVkDRL--------KKSALGLS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD--DKRTVVLVTHKLQ 898
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPIST-----AKIEELILElkKDYTIVIVTHNMQ 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
676-918 |
6.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 676 NFCVQIIGGFFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLG--EMQRVSGAVFwnsslpdsegedpry 753
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiyLPQRGRVKVM--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 754 clrtsnpERETAADSDARSRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPH 823
Cdd:PRK13647 66 -------GREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAF-GPVNmgldkdevERRVEEALKAVRMWDFRDKPPY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 824 gdqtqigergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPH 902
Cdd:PRK13647 138 -----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEW 204
|
250
....*....|....*.
gi 1720421572 903 ADWIIAMKDGTIQREG 918
Cdd:PRK13647 205 ADQVIVLKEGRVLAEG 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
684-909 |
6.90e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.45 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 684 GFFTwTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQRVSGAVFWNsslpdseGEDpryclrTSNPER 762
Cdd:PRK11308 20 GLFK-PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIE-TPTGGELYYQ-------GQD------LLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 763 ETAADsdARSR------GPvaYASQKP-WLLNATVEE----NITFESPFNKQRYKMVIEACSLQPD-IDILPHgdqtqig 830
Cdd:PRK11308 85 EAQKL--LRQKiqivfqNP--YGSLNPrKKVGQILEEplliNTSLSAAERREKALAMMAKVGLRPEhYDRYPH------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 831 ergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADW 905
Cdd:PRK11308 154 ----MFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQelglSYVFISHDLSVVEHiADE 224
|
....
gi 1720421572 906 IIAM 909
Cdd:PRK11308 225 VMVM 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
836-914 |
7.69e-12 |
|
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: 66.01 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKD 911
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE-----LVGEVLDVMKDlaeEGMTMVVVTHEMGFAREvADRVIFMDD 210
|
...
gi 1720421572 912 GTI 914
Cdd:cd03262 211 GRI 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
696-925 |
7.80e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.57 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpryclrtsnperetAADSDARSRgP 775
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-------GTD--------------VSRLHARDR-K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLL-NATVEENITF--------ESPFN---KQRYKMVIEACSLQPDIDILPhgdqTQigerginLSGGQRQR 843
Cdd:PRK10851 76 VGFVFQHYALFrHMTVFDNIAFgltvlprrERPNAaaiKAKVTQLLEMVQLAHLADRYP----AQ-------LSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 922
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKEL-RRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
...
gi 1720421572 923 FQR 925
Cdd:PRK10851 224 VWR 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
688-961 |
1.24e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 688 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlatlgemqrvsgavfwNSSLPDSEGEDPRYCLRTSNPERETAAD 767
Cdd:PLN03232 1244 YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSML----------------NALFRIVELEKGRIMIDDCDVAKFGLTD 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 768 SdarsRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVA 847
Cdd:PLN03232 1308 L----RRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLA 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 927
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVR-TDSLIQRTIREEFK--SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
250 260 270
....*....|....*....|....*....|....
gi 1720421572 928 CQLFEHWKTLMNRQDQELEKETVMERKAPEPSQG 961
Cdd:PLN03232 1461 TSAFFRMVHSTGPANAQYLSNLVFERRENGMSLG 1494
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
699-926 |
1.58e-11 |
|
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: 67.44 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 699 ITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWNSSlpdsegeDPRYCLrtsNPERETaadsdarsr 773
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIrliagLTRPDEGEIVLNGRTLFDS-------RKGIFL---PPEKRR--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 gpVAYASQKPWLL-NATVEENITF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVA 847
Cdd:TIGR02142 77 --IGYVFQEARLFpHLSVRGNLRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQR 925
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALDDPRKYEILP--YLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
.
gi 1720421572 926 S 926
Cdd:TIGR02142 222 S 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
689-922 |
1.72e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.03 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSS-------LLLATLGEMQrvsgaVFWNSSLPDSEGEDPRYCLRTSNPE 761
Cdd:PRK13651 16 LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnaLLLPDTGTIE-----WIFKDEKNKKKTKEKEKVLEKLVIQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 762 RETAAD----SDARSRGPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLqpDIDILPHGDqtqi 829
Cdd:PRK13651 91 KTRFKKikkiKEIRRRVGVVFQFAEYQLFEQTIEKDIIF-GPVSmgvskeeaKKRAAKYIELVGL--DESYLQRSP---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 830 gergINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIA 908
Cdd:PRK13651 164 ----FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRTIF 237
|
250
....*....|....*...
gi 1720421572 909 MKDGTIQREG----TLKD 922
Cdd:PRK13651 238 FKDGKIIKDGdtydILSD 255
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
694-922 |
1.94e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.26 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLllatlgemqrvsgAVFWNSSLPDSEGEDPRYCLRTSNPERETaadsDARSR 773
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTI-------------AKHMNALLIPSEGKVYVDGLDTSDEENLW----DIRNK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GPVAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 845
Cdd:PRK13633 87 AGMVFQNPDNQIVATIVEEDVAF-GPENlgippeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 922
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
836-941 |
2.27e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 914
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
90 100
....*....|....*....|....*..
gi 1720421572 915 QREGTLKdfqrsecQLFEHWKTLMNRQ 941
Cdd:PRK11264 223 VEQGPAK-------ALFADPQQPRTRQ 242
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
696-920 |
2.56e-11 |
|
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: 63.88 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEmqrvSGAVFWNSSLPdsegedpryclrtsnperetaadsdARSRGP 775
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLP-------------------------KFSRNK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQkpwlLNATVEENITFespfnkqrykmvieacslqpdidiLPHGDQTQigergiNLSGGQRQRISVARALYQHT- 854
Cdd:cd03238 62 LIFIDQ----LQFLIDVGLGY------------------------LTLGQKLS------TLSGGELQRVKLASELFSEPp 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 855 NVVF-LDDPFSALDVHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 920
Cdd:cd03238 108 GTLFiLDEPSTGLHQQDINQLL--EVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKV 172
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
673-919 |
3.25e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.18 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 673 DADNFCVQIiggfftwtpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlpdsegedpr 752
Cdd:PRK13548 4 EARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 753 yclrtsnPERETAADSDARSRgpvAYASQK-----PWllnaTVEENITF-ESPF--NKQRYKMVIEACSLQPDIDILPHG 824
Cdd:PRK13548 65 -------PLADWSPAELARRR---AVLPQHsslsfPF----TVEEVVAMgRAPHglSRAEDDALVAAALAQVDLAHLAGR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 825 DQTQigerginLSGGQRQRISVARALYQHTN------VVFLDDPFSALDVHlsdHlmQAGILELLRD----DKRTVVLVT 894
Cdd:PRK13548 131 DYPQ-------LSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLA---H--QHHVLRLARQlaheRGLAVIVVL 198
|
250 260
....*....|....*....|....*....
gi 1720421572 895 HKL----QYlphADWIIAMKDGTIQREGT 919
Cdd:PRK13548 199 HDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
683-909 |
3.36e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 66.29 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 683 GGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDpryclrtsnper 762
Cdd:COG4608 21 GGLFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF-------DGQD------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 763 etAADSDARSRGPVA----------YASqkpwlLNA--TVEENItfESPF-------NKQRYKMV---IEACSLQPD-ID 819
Cdd:COG4608 82 --ITGLSGRELRPLRrrmqmvfqdpYAS-----LNPrmTVGDII--AEPLrihglasKAERRERVaelLELVGLRPEhAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 820 ILPHgdqtqigErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSdhlMQAGILELLRDDKR----TVVLVTH 895
Cdd:COG4608 153 RYPH-------E----FSGGQRQRIGIARALALNPKLIVCDEPVSALDV--S---IQAQVLNLLEDLQDelglTYLFISH 216
|
250
....*....|....*
gi 1720421572 896 KLQYLPH-ADWIIAM 909
Cdd:COG4608 217 DLSVVRHiSDRVAVM 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
687-897 |
3.74e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.60 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 687 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpryCLRTSnPeretaa 766
Cdd:PRK10771 8 TWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN-------GQD---HTTTP-P------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 767 dsdarSRGPVAYASQKPWLLN-ATVEENITFE-------SPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSG 838
Cdd:PRK10771 69 -----SRRPVSMLFQENNLFShLTVAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSG 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 839 GQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRD--DKR--TVVLVTHKL 897
Cdd:PRK10771 133 GQRQRVALARCLVREQPILLLDEPFSALDPAL-----RQEMLTLVSQvcQERqlTLLMVSHSL 190
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1070-1330 |
4.10e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 65.64 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1070 YAMVFTVLCSLGIALC-LVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEC 1148
Cdd:cd18572 37 RAVLLLLLLSVLSGLFsGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1149 LSRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQQ-LDDTTQLpllshfAETVEGL-TTIRA 1222
Cdd:cd18572 117 FLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYYRKLSKEIQDaLAEANQV------AEEALSNiRTVRS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1223 F---RYEA-RFQQKLLEYTDSN---NIASLFLTAANRWLevrmpgpaavlpqEYIGACVVLIAAATSIsnsLHRELSAG- 1294
Cdd:cd18572 191 FateEREArRYERALDKALKLSvrqALAYAGYVAVNTLL-------------QNGTQVLVLFYGGHLV---LSGRMSAGq 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720421572 1295 LVGLGLtYALMVSNYLNWMVRNLADMEIQLGAVKRI 1330
Cdd:cd18572 255 LVTFML-YQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
692-927 |
5.34e-11 |
|
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: 64.38 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDpryclrtsnperETAADSDAR 771
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-------GED------------ITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGPVAYASQKPWLL-NATVEENI----------TFESPFNKQRYKMVIEACSlqpdiDILphgDQTQIGERG----INL 836
Cdd:cd03219 73 ARLGIGRTFQIPRLFpELTVLENVmvaaqartgsGLLLARARREEREARERAE-----ELL---ERVGLADLAdrpaGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQ 915
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVI 222
|
250
....*....|..
gi 1720421572 916 REGTLKDFQRSE 927
Cdd:cd03219 223 AEGTPDEVRNNP 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-936 |
5.40e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.55 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWnsslpdsEGEDPRyclrtsnpereTAADSDA 770
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVYL-------DGQDIF-----------KMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGPVAYASQKPwLLNATVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQR 841
Cdd:PRK14247 81 RRRVQMVFQIPNP-IPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 842 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLmQAGILELLRDdkRTVVLVTHklqYLPHA----DWIIAMKDGTIQRE 917
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKD--MTIVLVTH---FPQQAarisDYVAFLYKGQIVEW 226
|
250 260
....*....|....*....|
gi 1720421572 918 GTLKD-FQRSECQLFEHWKT 936
Cdd:PRK14247 227 GPTREvFTNPRHELTEKYVT 246
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1066-1330 |
5.49e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 65.27 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1066 DQSVYAMVFTVLCSLGIALCLVTSVTV---EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHI 1142
Cdd:cd18557 31 DLDVLNELALILLAIYLLQSVFTFVRYylfNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1143 PSTLECLSRSTLLCVSA---LTVISY-VTPVFLVALLPLAVVCYFIQKYFRVASRDLQQlddttQLPLLSHFA-ETVEGL 1217
Cdd:cd18557 111 TDNLSQLLRNILQVIGGliiLFILSWkLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQD-----ALAKAGQVAeESLSNI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1218 TTIRAF---RYE-ARFQQKLLEYTDSnNIASLFLTAANRWLevrmpgpAAVLpqEYIGACVVLIAAATSISNSlhrELSA 1293
Cdd:cd18557 186 RTVRSFsaeEKEiRRYSEALDRSYRL-ARKKALANALFQGI-------TSLL--IYLSLLLVLWYGGYLVLSG---QLTV 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720421572 1294 GLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRI 1330
Cdd:cd18557 253 GELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
696-920 |
5.99e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSslpdsegedpryclrTSNPERETAADSDARSRgP 775
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG---------------QPMSKLSSAAKAELRNQ-K 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLL-NATVEENITFESPFNKQRYKMVIEACSlqpdiDILPH-GDQTQIGERGINLSGGQRQRISVARALYQH 853
Cdd:PRK11629 89 LGFIYQFHHLLpDFTALENVAMPLLIGKKKPAEINSRAL-----EMLAAvGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 854 TNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 920
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQL-LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
691-956 |
6.92e-11 |
|
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: 66.36 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWNSSL---------PDSEGEDPRYCLRTSN 759
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvLRGMDQYEPTSGRIIYHVALcekcgyverPSKVGEPCPVCGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 760 PERETAADSD----ARSRGPVAYASQKPWLL--NATVEENITfeSPFNKQRYKmviEACSLQPDIDILphgDQTQIGER- 832
Cdd:TIGR03269 91 PEEVDFWNLSdklrRRIRKRIAIMLQRTFALygDDTVLDNVL--EALEEIGYE---GKEAVGRAVDLI---EMVQLSHRi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 833 ---GINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIA 908
Cdd:TIGR03269 163 thiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIW 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720421572 909 MKDGTIQREGTLKDFQRSECQLFEhwktlmnrqdqELEKETVMERKAP 956
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVAVFMEGVS-----------EVEKECEVEVGEP 278
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1073-1233 |
1.01e-10 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. 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.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 64.46 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1073 VFTV--LCSLGIALCLVTSvtvewtGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1150
Cdd:cd18573 50 VFVVgaAANFGRVYLLRIA------GERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1151 RSTLLCVSALTVISYVTP-VFLVALL---PLAVVCYFIQKYFRVASRDLQQ-LDDTTQLPllshfAETVEGLTTIRAF-- 1223
Cdd:cd18573 124 RSLVSGVGGIGMMLYISPkLTLVMLLvvpPIAVGAVFYGRYVRKLSKQVQDaLADATKVA-----EERLSNIRTVRAFaa 198
|
170
....*....|..
gi 1720421572 1224 -RYE-ARFQQKL 1233
Cdd:cd18573 199 eRKEvERYAKKV 210
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
378-610 |
1.16e-10 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 64.11 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 378 YVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYIL 456
Cdd:cd07346 61 YLAARLGQRVVFDLRRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIGALVILFYLN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 457 GVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWE----NIFCSRVEMTRRKEMTS 532
Cdd:cd07346 139 WKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANRDLRDANLRA 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 533 LRAFAVYTSISIFMNTaipIAAVLITFVGhVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd07346 219 ARLSALFSPLIGLLTA---LGTALVLLYG-GYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
695-898 |
1.42e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.26 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 695 TLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ---RVSGAVFWNsslpdseGEDPrYCLRTSNPERetaadsd 769
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsINRMNDLNpevTITGSIVYN-------GHNI-YSPRTDTVDL------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 arsRGPVAYASQKPWLLNATVEENITFESPFN----KQRYKMVIEACSLQPDI-----DILpHgdqtqigERGINLSGGQ 840
Cdd:PRK14239 85 ---RKEIGMVFQQPNPFPMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdevkDRL-H-------DSALGLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELlrDDKRTVVLVTHKLQ 898
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQ 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
698-931 |
1.48e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEDpryCLRTSNPERETAADSDARSRGP-- 775
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF-------IDGED---VTHRSIQQRDICMVFQSYALFPhm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 -----VAYASQkpwLLNATVEENitfespfnKQRYKmviEACSLqpdIDILPHGDQ--TQIgerginlSGGQRQRISVAR 848
Cdd:PRK11432 94 slgenVGYGLK---MLGVPKEER--------KQRVK---EALEL---VDLAGFEDRyvDQI-------SGGQQQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 849 ALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 927
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
....
gi 1720421572 928 CQLF 931
Cdd:PRK11432 229 ASRF 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
686-922 |
1.78e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.47 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 686 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLA--------------------TLGEMQRVSGAVFWNssl 743
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTIskILTgllkpqsgeikidgitiskeNLKEIRKKIGIIFQN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 744 PDSEgedpryclrtsnperetaadsdarsrgpvayasqkpwLLNATVEENITFeSPFNKQ--RYKM--VIEACSLQPDI- 818
Cdd:PRK13632 92 PDNQ-------------------------------------FIGATVEDDIAF-GLENKKvpPKKMkdIIDDLAKKVGMe 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 819 DILPHGDQtqigergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQ 898
Cdd:PRK13632 134 DYLDKEPQ--------NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI-MVDLRKTRKKTLISITHDMD 204
|
250 260
....*....|....*....|....
gi 1720421572 899 YLPHADWIIAMKDGTIQREGTLKD 922
Cdd:PRK13632 205 EAILADKVIVFSEGKLIAQGKPKE 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
697-904 |
2.05e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 697 SNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgeMQRVSGAVFWNsslpdseGEDPRYClrtsnpeREtaadsdarsrg 774
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLriLAGL--ARPDAGEVLWQ-------GEPIRRQ-------RD----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 775 pvAYASQKPWL--LNA-----TVEENITFespfnkqrykmvieACSLQPDIDilphGDQT-----QIGERGI------NL 836
Cdd:PRK13538 71 --EYHQDLLYLghQPGiktelTALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTHklQYLPHAD 904
Cdd:PRK13538 131 SAGQQRRVALARLWLTRAPLWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH--QDLPVAS 194
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
696-919 |
2.64e-10 |
|
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: 62.63 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL---------------GEMQRVSGA------VFWNSSLPdseGEDPRyc 754
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlkkeqpGNHDRIEGLehidkvIVIDQSPI---GRTPR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 755 lrtSNPERETAADSDARS------RGP--------VAYASQK-PWLLNATVEENITFESPFNKQRYKmvieacsLQPDID 819
Cdd:cd03271 86 ---SNPATYTGVFDEIRElfcevcKGKrynretleVRYKGKSiADVLDMTVEEALEFFENIPKIARK-------LQTLCD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 820 IlphG-DQTQIGERGINLSGGQRQRISVARALYQ---HTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTH 895
Cdd:cd03271 156 V---GlGYIKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLE--VLQRLVDKGNTVVVIEH 230
|
250 260 270
....*....|....*....|....*....|
gi 1720421572 896 KLQYLPHADWIIAM------KDGTIQREGT 919
Cdd:cd03271 231 NLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
691-895 |
2.89e-10 |
|
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: 61.35 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlPDSEGEDpryclrtsnperetaadSDA 770
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDFQRD-----------------SIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSrgpVAYASQKPWLLNA-TVEENITFESPFNKQrykmviEACslqpdIDILPHGDQTQIGERGIN-LSGGQRQRISVAR 848
Cdd:cd03231 73 RG---LLYLGHAPGIKTTlSVLENLRFWHADHSD------EQV-----EEALARVGLNGFEDRPVAqLSAGQQRRVALAR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 849 ALYQHTNVVFLDDPFSALDV--------HLSDHLMQAGIlellrddkrtVVLVTH 895
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDKagvarfaeAMAGHCARGGM----------VVLTTH 183
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
689-930 |
3.71e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEDPRycLRTsnperetaads 768
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKY--IRP----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 dARSRGPVAYASQKPWLLNATVEENITFeSPFNkqrYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVA 847
Cdd:PRK13646 83 -VRKRIGMVFQFPESQLFEDTVEREIIF-GPKN---FKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRS 926
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRL-LKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKD 236
|
....
gi 1720421572 927 ECQL 930
Cdd:PRK13646 237 KKKL 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
818-911 |
4.49e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 818 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDvHLSDHLMQAGILELLRDDKRTVVLVTHKL 897
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
90
....*....|....
gi 1720421572 898 QYLPHADWIIAMKD 911
Cdd:PTZ00265 641 STIRYANTIFVLSN 654
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1074-1330 |
4.66e-10 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 62.12 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1074 FTVLCSLGIALCLVTSV---TVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1150
Cdd:cd18575 39 FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1151 RSTLLCVSALTVISYVTP---VFLVALLPLAVV-CYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAFRY 1225
Cdd:cd18575 119 RNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQdRLADLS-----AFAEETLSAIKTVQAFTR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1226 EARFQQKLLEYTDSNniaslfLTAANRWLEVRmpgpaAVLpqeyIGACVVLIAAATS------ISNSLHRELSAGLVGLG 1299
Cdd:cd18575 194 EDAERQRFATAVEAA------FAAALRRIRAR-----ALL----TALVIFLVFGAIVfvlwlgAHDVLAGRMSAGELSQF 258
|
250 260 270
....*....|....*....|....*....|.
gi 1720421572 1300 LTYALMVSNYLNWMVRNLADMEIQLGAVKRI 1330
Cdd:cd18575 259 VFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-936 |
5.04e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LATLGEMQRVSGAVFWNSSLPDSEGEDPryclrtsnperetaadsdA 770
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVRLFGRNIYSPDVDP------------------I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGPVAYASQKP-WLLNATVEENITFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQ 840
Cdd:PRK14267 82 EVRREVGMVFQYPnPFPHLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKR--TVVLVTHK-LQYLPHADWIIAMKDGTIQRE 917
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANI-----DPVGTAKIEELLFELKKeyTIVLVTHSpAQAARVSDYVAFLYLGKLIEV 229
|
250 260
....*....|....*....|
gi 1720421572 918 G-TLKDFQRSECQLFEHWKT 936
Cdd:PRK14267 230 GpTRKVFENPEHELTEKYVT 249
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
696-895 |
5.91e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 62.40 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQRV-SGAVFWN----SSLPDSEgedprycLRtsnperetaads 768
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLL---ERPtSGSVLVDgvdlTALSERE-------LR------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 DARSRgpVAYASQKPWLLNA-TVEENITFesPF------NKQRYKMVIEACSLqpdIDILPHGDQ--TQigerginLSGG 839
Cdd:COG1135 79 AARRK--IGMIFQHFNLLSSrTVAENVAL--PLeiagvpKAEIRKRVAELLEL---VGLSDKADAypSQ-------LSGG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 840 QRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTH 895
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTR-----SILDLLKDINRelglTIVLITH 199
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
689-896 |
6.30e-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: 63.61 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLATLGEMqrvsgavfWnsslpdsegedPRYCLRTSNPeretaads 768
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGEL--------W-----------PVYGGRLTKP-------- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 darSRGPVAYASQKPWLLNATVEENITF-ESPFNKQRYKMvieacSLQPDIDILPHGDQTQIGERGIN----------LS 837
Cdd:TIGR00954 513 ---AKGKLFYVPQRPYMTLGTLRDQIIYpDSSEDMKRRGL-----SDKDLEQILDNVQLTHILEREGGwsavqdwmdvLS 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHK 896
Cdd:TIGR00954 585 GGEKQRIAMARLFYHKPQFAILDECTSAVSVD-----VEGYMYRLCREFGITLFSVSHR 638
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
689-919 |
7.50e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSslpdsegedprYCLrtsnPERETAADS 768
Cdd:PRK13645 20 TPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGD-----------YAI----PANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 DARSRGPVAYASQKP--WLLNATVEENITFeSPFN-----KQRYKMVIEACSLQPdidiLPhgdQTQIGERGINLSGGQR 841
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAF-GPVNlgenkQEAYKKVPELLKLVQ----LP---EDYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 842 QRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 919
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
836-923 |
7.56e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 60.78 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSdhlmqAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKD 911
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELV-----GEVLDVMRDlakEGMTMVVVTHEMGFAREvADRVVFMDG 211
|
90
....*....|..
gi 1720421572 912 GTIQREGTLKDF 923
Cdd:COG1126 212 GRIVEEGPPEEF 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
689-919 |
9.54e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.79 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsSLPDSEGEDPRYCLRTSNPERETAADS 768
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI----QVGDIYIGDKKNNHELITNPYSKKIKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 DARSRGPVAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPD-IDILPHGdqtqigerginLS 837
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------LS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagileLLRDDK---RTVVLVTHKL-QYLPHADWIIAMKDGT 913
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-----LILDAKannKTVFVITHTMeHVLEVADEVIVMDKGK 253
|
....*.
gi 1720421572 914 IQREGT 919
Cdd:PRK13631 254 ILKTGT 259
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
698-922 |
1.13e-09 |
|
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: 61.66 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 698 NITIRIPRGQLTMIVGQVGCGKSSLL--LATL-----GEMqRVSGAVFWNSS----LPdsegedpryclrtsnPERetaa 766
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLraIAGLerpdsGRI-RLGGEVLQDSArgifLP---------------PHR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 767 dsdarsRgPVAYASQK----PWLlnaTVEENITF---ESPFNKQRYKM--VIEACSLQPDIDILPHgdqtqigergiNLS 837
Cdd:COG4148 77 ------R-RIGYVFQEarlfPHL---SVRGNLLYgrkRAPRAERRISFdeVVELLGIGHLLDRRPA-----------TLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRT-VVLVTHKL---QYLphADWIIAMKDGT 913
Cdd:COG4148 136 GGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP--YLERLRDELDIpILYVSHSLdevARL--ADHVVLLEQGR 211
|
....*....
gi 1720421572 914 IQREGTLKD 922
Cdd:COG4148 212 VVASGPLAE 220
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1070-1232 |
1.39e-09 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 60.86 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1070 YAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1149
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1150 SRSTLLCVSALTVISYV----TPVFLVALLPLAVVCYFIQKYFRVASRDL-QQLDDttqlpLLSHFAETVEGLTTIRAFR 1224
Cdd:cd18544 123 IGDLLLLIGILIAMFLLnwrlALISLLVLPLLLLATYLFRKKSRKAYREVrEKLSR-----LNAFLQESISGMSVIQLFN 197
|
....*...
gi 1720421572 1225 YEARFQQK 1232
Cdd:cd18544 198 REKREFEE 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
689-924 |
1.69e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLpdsegedprycLRTSNPERETAAds 768
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIV-----------VSSTSKQKEIKP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 dARSRGPVAYASQKPWLLNATVEENITFeSPFNKQRYKMVIEACSLQpDIDILphGDQTQIGERG-INLSGGQRQRISVA 847
Cdd:PRK13643 82 -VRKKVGVVFQFPESQLFEETVLKDVAF-GPQNFGIPKEKAEKIAAE-KLEMV--GLADEFWEKSpFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQ 924
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDvFQ 233
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1097-1233 |
1.97e-09 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 60.54 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1097 LKVAKRLHRSLL----NRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPST-LECLSRSTLLCVSALTVISYVTPVFL 1171
Cdd:cd18570 67 LKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFLDLLMVIISGIILFFYNWKLFL 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 1172 VALLPL---AVVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFRYEARFQQKL 1233
Cdd:cd18570 146 ITLLIIplyILIILLFNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKKI 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
698-918 |
2.15e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.20 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN----SSLPDSEgedpryclrtsnperetaadsdaRSR 773
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmNDVPPAE-----------------------RGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GPV--AYASQkPWLlnaTVEENITF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRI 844
Cdd:PRK11000 78 GMVfqSYALY-PHL---SVAENMSFglklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 845 SVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 918
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1089-1236 |
2.66e-09 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 59.80 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1089 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP 1168
Cdd:cd18576 57 IYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 1169 ---VFLVALLP-LAVVCYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAF---RYEA-RFQQKLLEY 1236
Cdd:cd18576 137 kltLLMLATVPvVVLVAVLFGRRIRKLSKKVQdELAEAN-----TIVEETLQGIRVVKAFtreDYEIeRYRKALERV 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
696-922 |
3.05e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 59.68 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPryclrTSnperETAADSDARSRgp 775
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-------GVDI-----TD----KKVKLSDIRKK-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDI--DILPhgdqtqigergINLSGGQRQR 843
Cdd:PRK13637 85 VGLVFQYPeyQLFEETIEKDIAF-GPINlglseeeiENRVKRAMNIVGLDYEDykDKSP-----------FELSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 922
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEIL-NKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
694-933 |
3.86e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSL------LLA----------------TLGEMQRVSGAVFWNsslPDSEgedp 751
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLakllngLLLpeagtitvggmvlseeTVWDVRRQVGMVFQN---PDNQ---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 752 ryclrtsnperetaadsdarsrgpvayasqkpwLLNATVEENITF--EspfNKQ--RYKMV------IEACSLQPDIDIL 821
Cdd:PRK13635 94 ---------------------------------FVGATVQDDVAFglE---NIGvpREEMVervdqaLRQVGMEDFLNRE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 822 PHgdqtqigergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMqaGILELLRDDKR-TVVLVTHKLQYL 900
Cdd:PRK13635 138 PH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVL--ETVRQLKEQKGiTVLSITHDLDEA 204
|
250 260 270
....*....|....*....|....*....|...
gi 1720421572 901 PHADWIIAMKDGTIQREGTLKdfqrsecQLFEH 933
Cdd:PRK13635 205 AQADRVIVMNKGEILEEGTPE-------EIFKS 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
696-919 |
3.92e-09 |
|
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: 61.18 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL---------------GEMQRVSGA------VFWNSSLPdseGEDPRyc 754
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanrlngaktvpGRYTSIEGLehldkvIHIDQSPI---GRTPR-- 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 755 lrtSNPERET----------AADSDARSRGpvaYaSQKPWLLNA--------------TVEEN------ITFES----PF 800
Cdd:TIGR00630 699 ---SNPATYTgvfdeirelfAETPEAKVRG---Y-TPGRFSFNVkggrceacqgdgviKIEMHflpdvyVPCEVckgkRY 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 801 NKQ----RYK---------MVI-EACSLQPDIDILPHGDQT---------QIGERGINLSGGQRQRISVARALYQ---HT 854
Cdd:TIGR00630 772 NREtlevKYKgkniadvldMTVeEAYEFFEAVPSISRKLQTlcdvglgyiRLGQPATTLSGGEAQRIKLAKELSKrstGR 851
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 855 NVVFLDDPFSALdvHLSD--HLMQagILELLRDDKRTVVLVTHKLQYLPHADWII------AMKDGTIQREGT 919
Cdd:TIGR00630 852 TLYILDEPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKTADYIIdlgpegGDGGGTVVASGT 920
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
837-914 |
4.04e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL---QYLPHAdwIIAM 909
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRElglaVVIVTHDLavaRLLAHR--LLVM 225
|
....*
gi 1720421572 910 KDGTI 914
Cdd:PRK11701 226 KQGRV 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
837-919 |
4.31e-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: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDG 912
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHG 208
|
....*..
gi 1720421572 913 TIQREGT 919
Cdd:cd03265 209 RIIAEGT 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
836-923 |
5.34e-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: 60.47 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKRT----VVLVTHKL----QYlphADWII 907
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKDLQRElgmaLLLITHDLgvvrRF---ADRVA 228
|
90
....*....|....*.
gi 1720421572 908 AMKDGTIQREGTLKDF 923
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
688-914 |
6.68e-09 |
|
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: 57.83 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 688 WTPDGIPT-LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLgemQRV-SGAVFWNSSLPDSEGEDPRYCLRtsnpere 763
Cdd:COG4181 19 GTGAGELTiLKGISLEVEAGESVAIVGASGSGKSTLLglLAGL---DRPtSGTVRLAGQDLFALDEDARARLR------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 764 taadsdARSRGPVAYASQkpwLLNA-TVEENITFESPFN-----KQRYKMVIEACSLQPDIDILPHGdqtqigerginLS 837
Cdd:COG4181 89 ------ARHVGFVFQSFQ---LLPTlTALENVMLPLELAgrrdaRARARALLERVGLGHRLDHYPAQ-----------LS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKDGT 913
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQ-----IIDLLFELNRergtTLVLVTHDPALAARCDRVLRLRAGR 223
|
.
gi 1720421572 914 I 914
Cdd:COG4181 224 L 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
693-917 |
1.02e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEDPRYCLRTSNperetaadsdars 772
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKH------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 rgpVAYASQKPWL---LNATveENITFESPFNKQRykmviEACSLQPDIDILphgDQTQIGER----GINLSGGQRQRIS 845
Cdd:PRK10584 90 ---VGFVFQSFMLiptLNAL--ENVELPALLRGES-----SRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 917
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADL-LFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
836-912 |
1.07e-08 |
|
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: 1.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 912
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINL-MLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
691-927 |
1.34e-08 |
|
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: 56.91 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLrtsnpereTAADSDA 770
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-------GED----I--------TGLPPHR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGPVAYASQK----PWLlnaTVEENIT--FESPFNKQRYKMVIEACslqpdIDILPhgdqtQIGER----GINLSGGQ 840
Cdd:COG0410 75 IARLGIGYVPEGrrifPSL---TVEENLLlgAYARRDRAEVRADLERV-----YELFP-----RLKERrrqrAGTLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGT 919
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFE--IIRRLNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGT 219
|
....*...
gi 1720421572 920 LKDFQRSE 927
Cdd:COG0410 220 AAELLADP 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
696-914 |
1.74e-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: 55.52 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPeretaadSDARSRGp 775
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-------GKP----VTRRSP-------RDAIRAG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYAS----QKPWLLNATVEENITFespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALY 851
Cdd:cd03215 77 IAYVPedrkREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 852 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 914
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
696-909 |
1.84e-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: 56.50 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATL-GEMQR-----VSGAV---FWNSSLPDS---EGEDPRYCL---RTSNP 760
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyAEGQRryvesLSAYArqfLGQMDKPDVdsiEGLSPAIAIdqkTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 761 ERETAadsdarsrGPVAYASQKPWLLNATVeeNItfespfnKQRYKMVIEacslqpdidilphgdqtqIG------ERGI 834
Cdd:cd03270 91 PRSTV--------GTVTEIYDYLRLLFARV--GI-------RERLGFLVD------------------VGlgyltlSRSA 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 835 N-LSGGQRQRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 909
Cdd:cd03270 136 PtLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
696-933 |
1.85e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.00 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN-SSLPDSEGEDPRYCLRTSNperetAADSDArsrg 774
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgEPLAKLNRAQRKAFRRDIQ-----MVFQDS---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 775 PVAYASQKP--WLLNATVEENITFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISVARALY 851
Cdd:PRK10419 99 ISAVNPRKTvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVlDKRPP-----------QLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 852 QHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLkdfqrS 926
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQqfgtACLFITHDLRLVERfCQRVMVMDNGQIVETQPV-----G 237
|
....*..
gi 1720421572 927 ECQLFEH 933
Cdd:PRK10419 238 DKLTFSS 244
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
685-914 |
2.40e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 56.63 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 685 FFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAtlgemqrVSGAVfwnssLPDS-----EGED----PRYcL 755
Cdd:COG1101 11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA-------IAGSL-----PPDSgsiliDGKDvtklPEY-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 756 RTS-------NPERETAAdsdarsrgpvayasqkpwllNATVEENI----------TFESPFNKQRYKMVIEACSlqpDI 818
Cdd:COG1101 78 RAKyigrvfqDPMMGTAP--------------------SMTIEENLalayrrgkrrGLRRGLTKKRRELFRELLA---TL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 819 DI-LPHGDQTQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagiL--ELLRDDKRTVVLVTH 895
Cdd:COG1101 135 GLgLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE---LteKIVEENNLTTLMVTH 207
|
250 260
....*....|....*....|
gi 1720421572 896 KLQY-LPHADWIIAMKDGTI 914
Cdd:COG1101 208 NMEQaLDYGNRLIMMHEGRI 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
692-961 |
2.49e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.50 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEmQRVSGAVFWNsslpdseGEDpryclRTSNPERETAAdsdA 770
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrCINLLE-RPTSGRVLVD-------GQD-----LTALSEKELRK---A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRgpVAYASQKPWLLNA-TVEENITFespfnkqrykmvieacSLQpdidiLPHGDQTQIGER--------GI------- 834
Cdd:PRK11153 81 RRQ--IGMIFQHFNLLSSrTVFDNVAL----------------PLE-----LAGTPKAEIKARvtellelvGLsdkadry 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 835 --NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWII 907
Cdd:PRK11153 138 paQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVA 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 908 AMKDGTIQREGTLKDfqrsecqLFEHWKTLMNRQ------DQELEkETVMERKAPEPSQG 961
Cdd:PRK11153 213 VIDAGRLVEQGTVSE-------VFSHPKHPLTREfiqstlHLDLP-EDYLARLQAEPTTG 264
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
696-934 |
2.61e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.18 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL-LATLGEMqrvsgavfwnsslPDSeGEdprycLRTSNPERETAADSDARS-- 772
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLrVLNLLEM-------------PRS-GT-----LNIAGNHFDFSKTPSDKAir 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 --RGPVAYASQK----PWLlnaTVEENITfESPFN---------KQRYKMVIEACSLQPDIDILPhgdqtqigergINLS 837
Cdd:PRK11124 79 elRRNVGMVFQQynlwPHL---TVQQNLI-EAPCRvlglskdqaLARAEKLLERLRLKPYADRFP-----------LHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALD-------VHLSDHLMQAGIlellrddkrTVVLVTHKLQYLPH-ADWIIAM 909
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELAETGI---------TQVIVTHEVEVARKtASRVVYM 214
|
250 260
....*....|....*....|....*
gi 1720421572 910 KDGTIQREGTLKDFQRSECQLFEHW 934
Cdd:PRK11124 215 ENGHIVEQGDASCFTQPQTEAFKNY 239
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
698-926 |
2.83e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.06 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 698 NITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ---RVSGavfwnsslpDSEGEDPRYCLRTSNPERETAADSDarsrg 774
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgRVMA---------EKLEFNGQDLQRISEKERRNLVGAE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 775 pVAYASQKPWL-LNA--TVEENI-----TFESPFNKQRYKMVIEACSLQ--PD----IDILPHgdqtqigergiNLSGGQ 840
Cdd:PRK11022 91 -VAMIFQDPMTsLNPcyTVGFQImeaikVHQGGNKKTRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELL----RDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQ 915
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDV-----TIQAQIIELLlelqQKENMALVLITHDLALVAEaAHKIIVMYAGQVV 233
|
250
....*....|.
gi 1720421572 916 REGTLKDFQRS 926
Cdd:PRK11022 234 ETGKAHDIFRA 244
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
696-927 |
4.43e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQ--------RVSGAVFWNsslpdseGEdpryclrtsnPERETAAD 767
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLN-------GE----------PLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 768 SDARSRGPVAYASQKPWLLnaTVEENITFespfnkQRYKMVIEACSL-QPDIDILPH-----GDQTQIGERGINLSGGQR 841
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFAF--SAREIVLL------GRYPHARRAGALtHRDGEIAWQalalaGATALVGRDVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 842 QRISVARALYQ---------HTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKD 911
Cdd:PRK13547 152 ARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLA-HQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLAD 230
|
250
....*....|....*.
gi 1720421572 912 GTIQREGTLKDFQRSE 927
Cdd:PRK13547 231 GAIVAHGAPADVLTPA 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
693-926 |
4.97e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdsegEDPRYCLRTSNPE----RETAADS 768
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLV-----------QCDKMLLRRRSRQvielSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 DARSRGP-VAYASQKPWL-LNA--TVEENITfESPFNKQ---RYKMVIEACSLQPDIDIlPHGdQTQIGERGINLSGGQR 841
Cdd:PRK10261 98 MRHVRGAdMAMIFQEPMTsLNPvfTVGEQIA-ESIRLHQgasREEAMVEAKRMLDQVRI-PEA-QTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 842 QRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLR----DDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQR 916
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDV-----TIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
250
....*....|
gi 1720421572 917 EGTLKDFQRS 926
Cdd:PRK10261 250 TGSVEQIFHA 259
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
696-918 |
6.31e-08 |
|
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: 54.51 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGqLTMIVGQVGCGKSSLL--LATLgeMQRVSGAVFWNsslpdseGEDPRyclrtsnperetaaDSDARSR 773
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMriLATL--TPPSSGTIRID-------GQDVL--------------KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GPVAYASQKP-WLLNATVEENITF-------ESPFNKQRYKMVIEAcslqpdIDILPHGDQtQIGErginLSGGQRQRIS 845
Cdd:cd03264 72 RRIGYLPQEFgVYPNFTVREFLDYiawlkgiPSKEVKARVDEVLEL------VNLGDRAKK-KIGS----LSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 846 VARALYQHTNVVFLDDPFSALD----VHLSDHLMQAGilellrdDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 918
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
696-927 |
6.35e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.56 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLlATLGEMQrvsgavfwnsslPDSEGEdpryCLRTSNPERETAADSDARSrgp 775
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQ------------PPSEGE----ILLDAQPLESWSSKAFARK--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQK-PWLLNATVEENITF-ESP-------FNKQRYKMVIEACSLqpdIDILPhgdqtqIGERGIN-LSGGQRQRIS 845
Cdd:PRK10575 87 VAYLPQQlPAAEGMTVRELVAIgRYPwhgalgrFGAADREKVEEAISL---VGLKP------LAHRLVDsLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDV-HLSDHLmqAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDF 923
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIaHQVDVL--ALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAEL 235
|
....
gi 1720421572 924 QRSE 927
Cdd:PRK10575 236 MRGE 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
836-919 |
7.41e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.20 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 914
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEV 243
|
....*
gi 1720421572 915 QREGT 919
Cdd:PRK10070 244 VQVGT 248
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1098-1232 |
7.82e-08 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 55.49 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1098 KVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-LVALL- 1175
Cdd:cd18547 75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLtLIVLVt 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 1176 -PLAVVC-YFI----QKYFRVASRDLQQLDdttqlpllSHFAETVEGLTTIRAFRYEARFQQK 1232
Cdd:cd18547 155 vPLSLLVtKFIakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEE 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
836-918 |
8.40e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.71 E-value: 8.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 914
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
|
....
gi 1720421572 915 QREG 918
Cdd:PRK09493 215 AEDG 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
696-922 |
8.90e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.19 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEDPryclrTSNPERETaadsdarsRGP 775
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL-------IRGEPI-----TKENIREV--------RKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKP--WLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 845
Cdd:PRK13652 80 VGLVFQNPddQIFSPTVEQDIAF-GPINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 922
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEE 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
692-918 |
1.12e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDPRYclrtsnpeRETAADSDAr 771
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID-------GQEMRF--------ASTTAALAA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 srGpVAYASQKPWLL-NATVEENI---TFESPFNKQRYKMVIEACSLQPD---IDILPhgdQTQIGErginLSGGQRQRI 844
Cdd:PRK11288 80 --G-VAIIYQELHLVpEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEhlgVDIDP---DTPLKY----LSIGQRQMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 845 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLqylphaDWIIAMKDG-TIQREG 918
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
691-913 |
1.27e-07 |
|
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: 52.07 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPdsegedpryclrtsnperetaadsda 770
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK-------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 rsrgpVAYASQkpwllnatveenitfespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARAL 850
Cdd:cd03221 65 -----IGYFEQ------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 851 YQHTNVVFLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGT 913
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEA-----LKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
696-927 |
1.62e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.33 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpdsegedpryclrTSNPERETAADS-DARSRG 774
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV-------------------KIDGELLTAENVwNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 775 PVAYASQKPWLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARAL 850
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDF-----KTREPAR---LSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 851 YQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 927
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRV-IHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSElFATSE 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
696-919 |
1.68e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.28 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQ----RVSGAVFWNsslpdseGEDpryclrtsnperetAADSD 769
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvLNRLIEIYdskiKVDGKVLYF-------GKD--------------IFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 A-RSRGPVAYASQKP-WLLNATVEENITFesPF------NKQRYKMVIEACSLQPDIDILPHgdqTQIGERGINLSGGQR 841
Cdd:PRK14246 85 AiKLRKEVGMVFQQPnPFPHLSIYDNIAY--PLkshgikEKREIKKIVEECLRKVGLWKEVY---DRLNSPASQLSGGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 842 QRISVARALYQHTNVVFLDDPFSALDVhLSDHLMQAGILELlrDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 919
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
694-927 |
2.29e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.97 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFwnsslpdSEGEdpryclrtsnperETAADSDARSR 773
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII-------IDGD-------------LLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 GPVAYASQKP--WLLNATVEENITF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVA 847
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFglenKGIPHEEMKERVNEALELVGMQDF-----KEREPAR---LSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 848 RALYQHTNVVFLDDPFSALDvhlsdhlmQAGILELLRDDKR-------TVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 920
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLD--------PEGRLELIKTIKGirddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTP 224
|
....*...
gi 1720421572 921 KD-FQRSE 927
Cdd:PRK13650 225 RElFSRGN 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
689-927 |
2.44e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.98 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 689 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSegedpryclrtsnpereTAADS 768
Cdd:PRK13649 16 TPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITS-----------------TSKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 DARS-RGPVAYASQKP--WLLNATVEENITFeSPFNKQRYKmvIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRIS 845
Cdd:PRK13649 79 DIKQiRKKVGLVFQFPesQLFEETVLKDVAF-GPQNFGVSQ--EEAEALAREKLALVGISESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-F 923
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDiF 233
|
....
gi 1720421572 924 QRSE 927
Cdd:PRK13649 234 QDVD 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
699-918 |
2.52e-07 |
|
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: 53.14 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVfwnsslpDSEGEDPryclrTSNPeretaadSDARSRGPVAY 778
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-------TVDGFDV-----VKEP-------AEARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 779 ASQK--PWLlnaTVEENITFESPFN-------KQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARA 849
Cdd:cd03266 85 DSTGlyDRL---TARENLEYFAGLYglkgdelTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 850 LYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 918
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
690-919 |
2.55e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 690 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlatlgemqrvsGAVFwnsslpdsegedpryclRTSNPERE--TAAD 767
Cdd:PLN03130 1249 PELPPVLHGLSFEISPSEKVGIVGRTGAGKSSML-----------NALF-----------------RIVELERGriLIDG 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 768 SDARS------RGPVAYASQKPWLLNATVEENItfeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSG 838
Cdd:PLN03130 1301 CDISKfglmdlRKVLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESlerAHLKDVIRRNSLGLDAEVSEAGENFSV 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 839 GQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 918
Cdd:PLN03130 1378 GQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIQKTIREEFK--SCTMLIIAHRLNTIIDCDRILVLDAGRVVEFD 1454
|
.
gi 1720421572 919 T 919
Cdd:PLN03130 1455 T 1455
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
836-922 |
4.00e-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: 52.78 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP----HAdwiIAMKD 911
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAL-LDKLAAEGAPTLVLVTHHVEEIPpgitHV---LLLKD 218
|
90
....*....|.
gi 1720421572 912 GTIQREGTLKD 922
Cdd:COG1119 219 GRVVAAGPKEE 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
703-906 |
4.35e-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: 52.75 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 703 IPR-GQLTMIVGQVGCGKSSLLLATLGEMQrvsgavfwnsslpdsegedPRYCLRTSNPE--------RETA-------- 765
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLK-------------------PNLGKFDDPPDwdeildefRGSElqnyftkl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 766 ADSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYkmVIEACSLQPdidilphgdqtqIGERGI-NLSGGQRQRI 844
Cdd:cd03236 83 LEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDERGKLDE--LVDQLELRH------------VLDRNIdQLSGGELQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 845 SVARALYQHTNVVFLDDPFSALDVHlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWI 906
Cdd:cd03236 149 AIAAALARDADFYFFDEPSSYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
835-897 |
6.21e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 6.21e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 835 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL 897
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE--ILRRLAAEGKSIIFITHKL 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
836-919 |
7.44e-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: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTI 914
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLEIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
....*
gi 1720421572 915 QREGT 919
Cdd:PRK11650 214 EQIGT 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
832-918 |
8.49e-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: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 832 RGIN--LSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsDHL-MQAGILELLRDDKRTVVLVTHKLQYLPH--ADWI 906
Cdd:cd03217 99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRV 175
|
90
....*....|..
gi 1720421572 907 IAMKDGTIQREG 918
Cdd:cd03217 176 HVLYDGRIVKSG 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
837-900 |
8.60e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 8.60e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALdvhlsDHLMQAGILELLRDDKRtvvlvTHKLQYL 900
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSL-----DKTVQAQILALLKSLQQ-----KHQLAYL 480
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
691-931 |
9.33e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIP-TLSNITIRIPRGQLTMIVGQVGCGKSSLLLaTLGEMQRVSGavfwnsslpdseGEdprycLRTSNpeRETAADSD 769
Cdd:PTZ00243 1320 EGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLL-TFMRMVEVCG------------GE-----IRVNG--REIGAYGL 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRGPVAYASQKPWLLNATVEENItfeSPFNKQRYKMV---IEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISV 846
Cdd:PTZ00243 1380 RELRRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVwaaLELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCM 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 847 ARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 926
Cdd:PTZ00243 1457 ARALLKKGSGFILMDEATANIDPALDRQIQATVMSAF--SAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMN 1534
|
....*
gi 1720421572 927 ECQLF 931
Cdd:PTZ00243 1535 RQSIF 1539
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
691-867 |
1.01e-06 |
|
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: 50.72 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLA---TLGEMQRVSGAVFWNSSLPDsegEDPRYClrtsnperetaad 767
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanRTEGNVSVEGDIHYNGIPYK---EFAEKY------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 768 sdarsRGPVAYASQK----PWLlnaTVEENITFespfnkqrykmvieACSLQpdidilphGDQTQigeRGInlSGGQRQR 843
Cdd:cd03233 82 -----PGEIIYVSEEdvhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKR 126
|
170 180
....*....|....*....|....
gi 1720421572 844 ISVARALYQHTNVVFLDDPFSALD 867
Cdd:cd03233 127 VSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
692-927 |
1.09e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllatlgeMQRVSGAVfwnssLPDSeGEdprycLRTSNPERETAADSDAR 771
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTL-------MKIIAGIV-----PPDS-GT-----LEIGGNPCARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGpVAYASQKPWLL-NATVEENITFESPFNKQRYKMVIE-----ACSLQPDIdilphgdqtQIGergiNLSGGQRQRIS 845
Cdd:PRK15439 85 QLG-IYLVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDS---------SAG----SLEVADRQIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 846 VARALYQHTNVVFLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQ 924
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLS 228
|
...
gi 1720421572 925 RSE 927
Cdd:PRK15439 229 TDD 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
696-912 |
1.31e-06 |
|
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: 50.74 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN-SSLPDSEGEDPRYClrtsnPEretaadsdarSRG 774
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgKPLDIAARNRIGYL-----PE----------ERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 775 pvAYASQKpwllnatVEENITFESpfnkQRYKMVIEACSLQPD-----IDILPHGDQtQIGErginLSGGQRQRISVARA 849
Cdd:cd03269 81 --LYPKMK-------VIDQLVYLA----QLKGLKKEEARRRIDewlerLELSEYANK-RVEE----LSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 850 LYQHTNVVFLDDPFSALDVHLSDHLMQAgILElLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 912
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDV-IRE-LARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1065-1252 |
1.37e-06 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 51.65 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1065 LDQSVYAMVFTVLCSLGIALCL------VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTI 1138
Cdd:cd18554 37 LDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1139 DQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVA---LLPLAVVC-YFIQKYFRVASRDLQQLDDTTQlpllSHFAETV 1214
Cdd:cd18554 117 KDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFYILAvKYFFGRLRKLTKERSQALAEVQ----GFLHERI 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720421572 1215 EGLTTIRAFRYEARFQQkllEYTDSNNiasLFLTAANR 1252
Cdd:cd18554 193 QGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
691-912 |
2.00e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWnsslpdsEGEDprycLRTSNPeRETaads 768
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMkvLSGVYPHGTYEGEIIF-------EGEE----LQASNI-RDT---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 darSRGPVAYASQKPWLL-NATVEENItF---E-SPFNKQRY-KMVIEACSL--QPDIDILPHgdqTQIGergiNLSGGQ 840
Cdd:PRK13549 80 ---ERAGIAIIHQELALVkELSVLENI-FlgnEiTPGGIMDYdAMYLRAQKLlaQLKLDINPA---TPVG----NLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 841 RQRISVARALYQHTNVVFLDDPFSALDVHLSDHLmqagiLELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 912
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVL-----LDIIRDLKAhgiACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
836-912 |
2.29e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.01 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMK 910
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231
|
..
gi 1720421572 911 DG 912
Cdd:PRK15134 232 NG 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
696-922 |
2.41e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.98 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLllatlgeMQRVSGAVFWNSSLPDSEGEdpryclrTSNPERETAADSDARSRGP 775
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTL-------MQHFNALLKPSSGTITIAGY-------HITPETGNKNLKKLRKKVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLLNATVEENITFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVA 847
Cdd:PRK13641 89 LVFQFPEAQLFENTVLKDVEF-GPKNfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHLSDHLMQagileLLRDDKR---TVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 922
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQ-----LFKDYQKaghTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKE 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
696-895 |
2.68e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.97 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATlgeMQRVSGAVFWNSSlpdsegedpryclRTSNPERETAADSDARSrgp 775
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL---AFRSPKGVKGSGS-------------VLLNGMPIDAKEMRAIS--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 vAYASQKPWLLNA-TVEENITFESPF----------NKQRYKMVIEACSLQPDIDILphgdqTQIGERGINLSGGQRQRI 844
Cdd:TIGR00955 102 -AYVQQDDLFIPTlTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCANTR-----IGVPGRVKGLSGGERKRL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720421572 845 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTH 895
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
691-925 |
3.06e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.60 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPdsegedpryclrtsnperetaadsda 770
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVK-------------------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 rsrgpVAYASQKPWLL--NATVEENItfeSPFNKQRYKMVIEACsLQpdiDILPHGDQ--TQIGergiNLSGGQRQRISV 846
Cdd:COG0488 380 -----IGYFDQHQEELdpDKTVLDEL---RDGAPGGTEQEVRGY-LG---RFLFSGDDafKPVG----VLSGGEKARLAL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 847 ARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTH------KLqylphADWIIAMKDGTIQ-REGT 919
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIE-----TLEALEEALDDFPGTVLLVSHdryfldRV-----ATRILEFEDGGVReYPGG 513
|
....*.
gi 1720421572 920 LKDFQR 925
Cdd:COG0488 514 YDDYLE 519
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1076-1246 |
3.96e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 50.10 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1076 VLCSLGIALCLVTS-VTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTL 1154
Cdd:cd18541 47 LLLALLIGIFRFLWrYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1155 LCVSALTVISYVTPVF-LVALLPL---AVVCYFIQKYFRVASRDLQQ----LDDTTQlpllshfaETVEGLTTIRAF--- 1223
Cdd:cd18541 127 LGVLVLVMMFTISPKLtLIALLPLpllALLVYRLGKKIHKRFRKVQEafsdLSDRVQ--------ESFSGIRVIKAFvqe 198
|
170 180
....*....|....*....|....*...
gi 1720421572 1224 -RYEARFQQKLLEYTDSNN----IASLF 1246
Cdd:cd18541 199 eAEIERFDKLNEEYVEKNLrlarVDALF 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
683-888 |
4.91e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 683 GGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWN----SSLPDSEGEDPRYCLRTS 758
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqriDTLSPGKLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 759 NPERETAADSdarsRGPVAYASQKPWLLNATVEENITfespfnKQRYKMVIEACSLQPDIDI-LPHgdqtqigergiNLS 837
Cdd:PRK10261 407 FQDPYASLDP----RQTVGDSIMEPLRVHGLLPGKAA------AARVAWLLERVGLLPEHAWrYPH-----------EFS 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720421572 838 GGQRQRISVARALYQHTNVVFLDDPFSALDVHLsdhlmQAGILELLRDDKR 888
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDVSI-----RGQIINLLLDLQR 511
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1067-1239 |
8.14e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 49.35 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1067 QSVYAMVFTVLcsLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTL 1146
Cdd:cd18551 37 GLLALLVALFL--LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1147 ECLSRSTLLCVSALTVISYVTPV-FLVAL--LPLAVVCYF-IQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLTTIR 1221
Cdd:cd18551 115 PQLVTGVLTVVGAVVLMFLLDWVlTLVTLavVPLAFLIILpLGRRIRKASKRAQD-----ALGELSAALErALSAIRTVK 189
|
170
....*....|....*...
gi 1720421572 1222 AFRYEARFQQKLLEYTDS 1239
Cdd:cd18551 190 ASNAEERETKRGGEAAER 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
835-898 |
9.94e-06 |
|
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: 48.48 E-value: 9.94e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 835 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKRTVVLVTHKLQ 898
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV-AQENIRNFLKEYNRERGTTVLLTSHYMK 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
691-912 |
1.01e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.82 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 691 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LATLGEMQRVSGAVFWnsslpdsEGEDprycLRTSNPeretaadS 768
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMkiLSGVYPHGTWDGEIYW-------SGSP----LKASNI-------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 769 DARSRGPVAYASQKPWLLNATVEENI----TFESPFNKQRYKMVIEACS---LQPDIDILPhgDQTQIGERGinlsGGQR 841
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKnllRELQLDADN--VTRPVGDYG----GGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 842 QRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 912
Cdd:TIGR02633 148 QLVEIAKALNKQARLLILDEPSSSLTEKETE-----ILLDIIRDLKAhgvACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
694-925 |
1.15e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.54 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 694 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEM----QRVSGAVfwnssLPDSEgedpryclrtsnpereTAADSD 769
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRV-----LLDGK----------------PVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 770 ARSRgPVAYASQKPwllnatveenitfESPFNKQRyKM---VIEAC---SLQPDIDILPH-------GDQTQIGER-GIN 835
Cdd:PRK10418 76 LRGR-KIATIMQNP-------------RSAFNPLH-TMhthARETClalGKPADDATLTAaleavglENAARVLKLyPFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKRT----VVLVTHKLQYLPH-ADWIIAMK 910
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDV-----VAQARILDLLESIVQKralgMLLVTHDMGVVARlADDVAVMS 215
|
250
....*....|....*.
gi 1720421572 911 DGTIQREGTLKD-FQR 925
Cdd:PRK10418 216 HGRIVEQGDVETlFNA 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
693-919 |
1.17e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWnsslpdsEGEDPRYcLRTSNPERETAAdsdARS 772
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF-------DGKDITD-WQTAKIMREAVA---IVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 RGPVAYASQkpwllnaTVEENITFESPF-NKQRYKMVIEACslqpdIDILPHGDQTQIgERGINLSGGQRQRISVARALY 851
Cdd:PRK11614 87 EGRRVFSRM-------TVEENLAMGGFFaERDQFQERIKWV-----YELFPRLHERRI-QRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 852 QHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 919
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFD--TIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1064-1249 |
1.22e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 48.64 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1064 ALDQSVYAMVFTVL--CSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILA--------PMRFFETTPLGSILNRFSS 1133
Cdd:cd18546 25 GIDSGVRAGDLGVLllAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRvfahlqrlSLDFHERETSGRIMTRMTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1134 DCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVALLPLAVVCYFiqkyFRVASRDLQQLDDTTQLPLLSH 1209
Cdd:cd18546 105 DIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRW----FRRRSSRAYRRARERIAAVNAD 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720421572 1210 FAETVEGLTTIRAFRYEARFQQKLLEYTDSN---NIASLFLTA 1249
Cdd:cd18546 181 LQETLAGIRVVQAFRRERRNAERFAELSDDYrdaRLRAQRLVA 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
696-948 |
1.23e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.68 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlGEMQRVSGAVFWnsslpdsegedpryclrtsnperetaaDSDARsr 773
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLkiLA--GELEPDSGEVSI---------------------------PKGLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 774 gpVAYASQKPWLL-NATVEENItFESpfNKQRYKMV-----IEACSLQPDIDILPHGD-QTQIGER-------------- 832
Cdd:COG0488 63 --IGYLPQEPPLDdDLTVLDTV-LDG--DAELRALEaeleeLEAKLAEPDEDLERLAElQEEFEALggweaearaeeils 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 833 --GI----------NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlmqaGIL---ELLRDDKRTVVLVTH-- 895
Cdd:COG0488 138 glGFpeedldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE--------SIEwleEFLKNYPGTVLVVSHdr 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 896 ----KLqylphADWIIAMKDGTIQR-EGTLKDFQRSECQLFEHWKTLMNRQDQELEKE 948
Cdd:COG0488 210 yfldRV-----ATRILELDRGKLTLyPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKE 262
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
837-897 |
1.30e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 1.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDVhlsdhLMQAGILELLRDDKR----TVVLVTHKL 897
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 222
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
705-895 |
1.57e-05 |
|
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: 46.21 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 705 RGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegedpryclrtsNPERETAADSDARSrgpvayasqkpw 784
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI------------------DGEDILEEVLDQLL------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 785 llnatveenitfespfnkqrykmvieacslqpdidilphgdQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFS 864
Cdd:smart00382 51 -----------------------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITS 89
|
170 180 190
....*....|....*....|....*....|....*
gi 1720421572 865 ALDVHLSDHLMQAGILELL----RDDKRTVVLVTH 895
Cdd:smart00382 90 LLDAEQEALLLLLEELRLLlllkSEKNLTVILTTN 124
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
831-927 |
2.10e-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: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 831 ERGIN-LSGGQRQRISVARAL-YQHTNVVF-LDDPFSALdvHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWII 907
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEPSIGL--HQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|....*.
gi 1720421572 908 AM------KDGTIQREGTLKDFQRSE 927
Cdd:TIGR00630 561 DIgpgageHGGEVVASGTPEEILANP 586
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
696-895 |
2.20e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.26 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNssLPDSEgedpryclrtsNPERETAADSDARsRGP 775
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD--VPDNQ-----------FGREASLIDAIGR-KGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQkpwLLNAT-VEENITFESPFNkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHT 854
Cdd:COG2401 112 FKDAVE---LLNAVgLSDAVLWLRRFK---------------------------------ELSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720421572 855 NVVFLDDPFSALDVHLSdHLMQAGILELLRDDKRTVVLVTH 895
Cdd:COG2401 156 KLLVIDEFCSHLDRQTA-KRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
834-895 |
3.55e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.79 E-value: 3.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720421572 834 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDhlmqaGILELLRDDKR---TVVLVTH 895
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE-----GILRLFEEFNRvgvTVLMATH 195
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1064-1232 |
3.99e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 47.24 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1064 ALDQSVYAMVFTVLcsLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIP 1143
Cdd:cd18780 40 ALNQAVLILLGVVL--IGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1144 STLECLSRSTLLCVSALTVISYV----TPVFLVALLPLAVVCYFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLT 1218
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTswklTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQD-----ALAAASTVAEeSISNIR 192
|
170
....*....|....
gi 1720421572 1219 TIRAFRYEARFQQK 1232
Cdd:cd18780 193 TVRSFAKETKEVSR 206
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1089-1240 |
4.02e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 47.08 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1089 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP 1168
Cdd:cd18545 61 IYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1169 VF-LVAL--LP-LAVVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFRYE----ARFQQKLLEYTDSN 1240
Cdd:cd18545 141 RLaLVTLavLPlLVLVVFLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSFAREdeneEIFDELNRENRKAN 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
706-922 |
4.92e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.71 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 706 GQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSlPDSEGEdprYCLRtSNPERETAADSdARSRGPVAYASQkpwL 785
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-PLHFGD---YSYR-SQRIRMIFQDP-STSLNPRQRISQ---I 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 786 LNATVEENITFESPFNKQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQRQRISVARALYQHTNVVFLDDPFS 864
Cdd:PRK15112 110 LDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 865 ALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 922
Cdd:PRK15112 179 SLDMSMRSQLINL-MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1099-1233 |
5.58e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.79 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1099 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVAL 1174
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrltmVTLINL 311
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 1175 LPLAVVCYFIQKYFRVASRDLQQ-LDDTTQLPLlshfaETVEGLTTIRAF---RYEA-RFQQKL 1233
Cdd:TIGR00958 312 PLVFLAEKVFGKRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFaaeEGEAsRFKEAL 370
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
692-922 |
5.94e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 692 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdsegedpryclrtsNPERETAADSDAR 771
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN------------------NINYNKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGpVAYASQKPWLLNA-TVEENI--------------TFESPFNKQRYKMVIEACSLQPDIDilphgdqtqigERGINL 836
Cdd:PRK09700 79 QLG-IGIIYQELSVIDElTVLENLyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLD-----------EKVANL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQ 915
Cdd:PRK09700 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
....*..
gi 1720421572 916 REGTLKD 922
Cdd:PRK09700 225 CSGMVSD 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
826-918 |
6.76e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 826 QTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHlmqagILELLRD--DKRTVVLVTHKL-QYLPH 902
Cdd:PRK14271 154 KDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK-----IEEFIRSlaDRLTVIIVTHNLaQAARI 228
|
90
....*....|....*.
gi 1720421572 903 ADWIIAMKDGTIQREG 918
Cdd:PRK14271 229 SDRAALFFDGRLVEEG 244
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
1071-1254 |
9.10e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 45.92 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1071 AMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLECLS 1150
Cdd:cd18567 45 AIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1151 RSTLLCVSALTVI-SYVTPVFLVALlpLAVVCYFI-----QKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFR 1224
Cdd:cd18567 124 LDGLMAILTLVMMfLYSPKLALIVL--AAVALYALlrlalYPPLRRATEEQIVASAKEQ----SHFLETIRGIQTIKLFG 197
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720421572 1225 YEARFQQKLLE-YTDSNN------IASLFLTAANRWL 1254
Cdd:cd18567 198 REAEREARWLNlLVDAINadirlqRLQILFSAANGLL 234
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
834-920 |
1.07e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.02 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 834 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVL-VTHKLQYLPH-ADWIIAMKD 911
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQ 204
|
....*....
gi 1720421572 912 GTIQREGTL 920
Cdd:PRK11144 205 GKVKAFGPL 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
771-867 |
1.09e-04 |
|
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: 45.23 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 771 RSRGPVAYASQKPWLL-NATVEENI--TFESpFNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVA 847
Cdd:cd03218 72 RARLGIGYLPQEASIFrKLTVEENIlaVLEI-RGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIA 145
|
90 100
....*....|....*....|
gi 1720421572 848 RALYQHTNVVFLDDPFSALD 867
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVD 165
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
836-895 |
1.25e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 45.57 E-value: 1.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 895
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLARGK-TILLTTH 196
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
834-897 |
1.47e-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: 1.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 834 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKL 897
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA-IRRLSEEGKKTALVVEHDL 132
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
833-898 |
1.65e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 1.65e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 833 GINLSGGQRQRISVARALYQHTNVVFLDDPFSALD-VHLSDhlmQAGILELLRDDKRTVVLVTHKLQ 898
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVR 198
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1093-1240 |
1.85e-04 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 45.11 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1093 EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-L 1171
Cdd:cd18542 64 EKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLtL 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 1172 VALLPLAVVCYFIQKYFRVASRDLQQLDDttQLPLLSHFA-ETVEGLTTIRAF---RYE-ARFQQKLLEYTDSN 1240
Cdd:cd18542 144 ISLAIIPFIALFSYVFFKKVRPAFEEIRE--QEGELNTVLqENLTGVRVVKAFareDYEiEKFDKENEEYRDLN 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
836-895 |
2.49e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 44.82 E-value: 2.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlSDHLMQAGILELLRDDKrTVVLVTH 895
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
789-867 |
2.71e-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: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 789 TVEENI-----TFESPFNKQRYKMVieacSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHTNVVFLDDPF 863
Cdd:COG1137 94 TVEDNIlavleLRKLSKKEREERLE----ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
....
gi 1720421572 864 SALD 867
Cdd:COG1137 165 AGVD 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
711-917 |
2.75e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.01 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 711 IVGQVGCGKSSLLLATLGEMQRVSGAVFWNsslpdseGEDprycLRTSNPeretaadSDARSRGpVAYAS----QKPWLL 786
Cdd:COG1129 283 IAGLVGAGRTELARALFGADPADSGEIRLD-------GKP----VRIRSP-------RDAIRAG-IAYVPedrkGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 787 NATVEENITFeSPFNKQRYKMVI-------EACSLQPDIDILPHGDQTQIGergiNLSGGQRQRISVARALYQHTNVVFL 859
Cdd:COG1129 344 DLSIRENITL-ASLDRLSRGGLLdrrreraLAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 860 DDPFSALDVhlsdhlmqaG----ILELLR---DDKRTVVLVThklQYLP----HADWIIAMKDGTIQRE 917
Cdd:COG1129 419 DEPTRGIDV---------GakaeIYRLIRelaAEGKAVIVIS---SELPellgLSDRILVMREGRIVGE 475
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
836-910 |
2.85e-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: 42.73 E-value: 2.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720421572 836 LSGGQRQRISVARAL----YQHTNVVFLDDPFSALDvhLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMK 910
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLD--PRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1094-1330 |
3.13e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 44.42 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1094 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVF-LV 1172
Cdd:cd18563 69 RLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLaLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1173 ALLPLAVVCYFIQKYFRVASRDLQQL----DDTTqlpllSHFAETVEGLTTIRAF---RYE-ARFQQKLLEYTDSNnias 1244
Cdd:cd18563 149 VLIPVPLVVWGSYFFWKKIRRLFHRQwrrwSRLN-----SVLNDTLPGIRVVKAFgqeKREiKRFDEANQELLDAN---- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1245 lfLTAANRWLevrMPGPAAVLPQEyIGACVVLIAAATSIsnsLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQL 1324
Cdd:cd18563 220 --IRAEKLWA---TFFPLLTFLTS-LGTLIVWYFGGRQV---LSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRAL 290
|
....*.
gi 1720421572 1325 GAVKRI 1330
Cdd:cd18563 291 TSAERI 296
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
708-895 |
3.89e-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: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 708 LTMIVGQVGCGKSSLLLAtlgemqrVSGAVFwnsslpdseGEDPRYclRTSNPERETAADSDARSRgpvayasqkpwlln 787
Cdd:cd03279 30 LFLICGPTGAGKSTILDA-------ITYALY---------GKTPRY--GRQENLRSVFAPGEDTAE-------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 788 atveenITFESPFNKQRYKmVIEACSLQPD----IDILPHGDQTQIGERGI-NLSGGQRQRISVARAL------YQHTNV 856
Cdd:cd03279 78 ------VSFTFQLGGKKYR-VERSRGLDYDqftrIVLLPQGEFDRFLARPVsTLSGGETFLASLSLALalsevlQNRGGA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720421572 857 V----FLDDPFSALDVHLSDHLMQAgiLELLRDDKRTVVLVTH 895
Cdd:cd03279 151 RlealFIDEGFGTLDPEALEAVATA--LELIRTENRMVGVISH 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
835-906 |
4.24e-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: 4.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 835 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWI 906
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH-----LQEYPGTVVAVTHDRYFLDNvAGWI 228
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
445-561 |
4.70e-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: 43.65 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 445 IIVGVILLYY--ILGVSALIGAAVIILLApvqYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAW 514
Cdd:cd18555 130 VIYLIYMLYYspLLTLIVLLLGLLIVLLL---LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKslgsekniYKKW 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1720421572 515 ENIFCSRVEMTRRKEMTSlrafAVYTSISIFMNTAIPIaavLITFVG 561
Cdd:cd18555 207 ENLFKKQLKAFKKKERLS----NILNSISSSIQFIAPL---LILWIG 246
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
699-914 |
5.56e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 699 ITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSS--LPDSEGEDPR----YClrtsnPEretaadsDARS 772
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRagimLC-----PE-------DRKA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 RGPVAYASqkpwllnatVEENITFESPFNKQRYKMVI----EACSLQPDIDIL----PHGDQtQIGergiNLSGGQRQRI 844
Cdd:PRK11288 340 EGIIPVHS---------VADNINISARRHHLRAGCLInnrwEAENADRFIRSLniktPSREQ-LIM----NLSGGNQQKA 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421572 845 SVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 914
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDVGAKHEIYN--VIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRI 474
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
817-912 |
6.39e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 817 DIDILPHgdqtqigERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHK 896
Cdd:PRK10982 123 DIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHK 193
|
90
....*....|....*..
gi 1720421572 897 L-QYLPHADWIIAMKDG 912
Cdd:PRK10982 194 MeEIFQLCDEITILRDG 210
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
696-867 |
7.50e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQR----VSGAVFWNSSLPDsegedpryclrtsnperetaaDSDAR 771
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfhigVEGVITYDGITPE---------------------EIKKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 772 SRGPVAYASQK----PWLlnaTVEENITF----ESPFNkqRYKMVIEACSLQPDIDI------LPHGDQTQIGE---RGI 834
Cdd:TIGR00956 136 YRGDVVYNAETdvhfPHL---TVGETLDFaarcKTPQN--RPDGVSREEYAKHIADVymatygLSHTRNTKVGNdfvRGV 210
|
170 180 190
....*....|....*....|....*....|...
gi 1720421572 835 nlSGGQRQRISVARALYQHTNVVFLDDPFSALD 867
Cdd:TIGR00956 211 --SGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1068-1187 |
8.76e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 42.85 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1068 SVYAMVFTVLcslGIALCLVTSVTV---EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID----Q 1140
Cdd:cd18577 47 NKYALYFVYL---GIGSFVLSYIQTacwTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQdgigE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 1141 HIPSTLECLSrstlLCVSALtVISYV---------TPVFLVALLPLAVVCYFIQKY 1187
Cdd:cd18577 124 KLGLLIQSLS----TFIAGF-IIAFIyswkltlvlLATLPLIAIVGGIMGKLLSKY 174
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1076-1310 |
9.67e-04 |
|
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: 42.77 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1076 VLCSLGIALC-LVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTL 1154
Cdd:cd18548 46 LLLALLGLIAgILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1155 LCVSALTVISYVTP----VFLVALLPLAVVCYFIQKYFRVASRDLQ-QLDDTTQLpllshFAETVEGLTTIRAF---RYE 1226
Cdd:cd18548 126 MLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKAIPLFKKVQkKLDRLNRV-----VRENLTGIRVIRAFnreDYE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1227 -ARFQQKLLEYTDSNniaslflTAANRWLEVRMPGPAAVLpqeYIGACVVLIAAATSISNSlhrELSAG-LVGLgLTYAL 1304
Cdd:cd18548 201 eERFDKANDDLTDTS-------LKAGRLMALLNPLMMLIM---NLAIVAILWFGGHLINAG---SLQVGdLVAF-INYLM 266
|
....*.
gi 1720421572 1305 MVSNYL 1310
Cdd:cd18548 267 QILMSL 272
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
785-920 |
1.05e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 785 LLNATVEE-NITFesPFNKQrykmvIEAcSLQPDIDI----LPhgdqtqIGERGINLSGGQRQRISVARALY---QHTNV 856
Cdd:PRK00635 1658 LLQTPIEEvAETF--PFLKK-----IQK-PLQALIDNglgyLP------LGQNLSSLSLSEKIAIKIAKFLYlppKHPTL 1723
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720421572 857 VFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 920
Cdd:PRK00635 1724 FLLDEIATSLDNQQKSALLV--QLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKI 1785
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
696-899 |
1.18e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPdsegedpryclrtsnperetaadsdarsrgp 775
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLE------------------------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 776 VAYASQKPWLLNA--TVEENITfESpfnKQ------RYKMVIEacSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVA 847
Cdd:PRK11147 384 VAYFDQHRAELDPekTVMDNLA-EG---KQevmvngRPRHVLG--YLQ---DFLFHPKRAMTPVKA--LSGGERNRLLLA 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720421572 848 RALYQHTNVVFLDDPFSALDVHLSDHLMqagilELLRDDKRTVVLVTHKLQY 899
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVETLELLE-----ELLDSYQGTVLLVSHDRQF 499
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
693-918 |
1.21e-03 |
|
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: 43.25 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 693 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGemqrvsgavfwnsSLPDSEGEdprYCLRTSNPEretaadSDARS 772
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG-------------VLEPTSGE---VNVRVGDEW------VDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 RGPVAYASQKPWL----------LNATVEENIT----FESPFNKQRYKMVI----------EACSLqpdIDILPHgdqtq 828
Cdd:TIGR03269 355 PGPDGRGRAKRYIgilhqeydlyPHRTVLDNLTeaigLELPDELARMKAVItlkmvgfdeeKAEEI---LDKYPD----- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 829 igergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALD----VHLSDHLMQAGIlELlrddKRTVVLVTHKLQY-LPHA 903
Cdd:TIGR03269 427 ------ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKARE-EM----EQTFIIVSHDMDFvLDVC 495
|
250
....*....|....*
gi 1720421572 904 DWIIAMKDGTIQREG 918
Cdd:TIGR03269 496 DRAALMRDGKIVKIG 510
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1102-1330 |
1.23e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 42.47 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1102 RLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIdQHIPSTLECLSRSTLLCVSALTVISYVTP----VFLVALLPL 1177
Cdd:cd18543 73 DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPplalVALASLPPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1178 AVVCYFIQKYFRVASRDLQQL--DDTTqlpllsHFAETVEGLTTIRAFRYEARFQQKlleytdsnniaslFLTAANRWLE 1255
Cdd:cd18543 152 VLVARRFRRRYFPASRRAQDQagDLAT------VVEESVTGIRVVKAFGRERRELDR-------------FEAAARRLRA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1256 VRM--------PGPA-AVLPQEYIGACVVLIAAATsisnsLHRELSAGLVGLGLTYALMvsnyLNWMVRNLADM--EIQL 1324
Cdd:cd18543 213 TRLraarlrarFWPLlEALPELGLAAVLALGGWLV-----ANGSLTLGTLVAFSAYLTM----LVWPVRMLGWLlaMAQR 283
|
....*...
gi 1720421572 1325 G--AVKRI 1330
Cdd:cd18543 284 AraAAERV 291
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
824-869 |
1.33e-03 |
|
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: 1.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720421572 824 GDQTQ-IGErginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVH 869
Cdd:TIGR03719 435 SDQQKkVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
835-897 |
1.34e-03 |
|
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: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720421572 835 NLSGGQRQRISVARALYQHTNVVFLDDPFSALDVhlSDHLMQAGILELLRDDKRTVVLVTHKL 897
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
391-608 |
1.75e-03 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 42.02 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 391 IQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYI---LGVSALIGAAV 466
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTsALTVLVRDPLTVIGLLGVLFYLdwkLTLIALVVLPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 467 IILlaPVQYFvATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FCSRVEMTRRKEMTSLRAFAVYTSI 542
Cdd:cd18552 152 AAL--PIRRI-GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSSPL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720421572 543 SIFMnTAIPIAAVLItFVGHVSFfkESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18552 229 MELL-GAIAIALVLW-YGGYQVI--SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
834-915 |
1.76e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.65 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 834 INLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 913
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV-LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
..
gi 1720421572 914 IQ 915
Cdd:PRK10522 527 LS 528
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1066-1250 |
1.98e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter 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.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 41.91 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1066 DQSVYAMVFTVLCSLGIALCL-----VTSVTVEWTGLKVAKRLHRSLLNRIIlapmRFFETTPLGSILNRFSSDCNTIDQ 1140
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAgirggLFTLAMARLNIRIRNLLFRSIVSQEI----GFFDTVKTGDITSRLTSDTTTMSD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1141 HIPSTLECLSRSTllcVSALTVIsyvtpVFLVAL-----------LPL-AVVCYFIQKYFRVASRDLQqlddtTQLPLLS 1208
Cdd:cd18784 109 TVSLNLNIFLRSL---VKAIGVI-----VFMFKLswqlslvtligLPLiAIVSKVYGDYYKKLSKAVQ-----DSLAKAN 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720421572 1209 HFA-ETVEGLTTIRAF--------RYEARFQQ----KLLE------YTDSNNIASLFLTAA 1250
Cdd:cd18784 176 EVAeETISSIRTVRSFanedgeanRYSEKLKDtyklKIKEalayggYVWSNELTELALTVS 236
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
836-919 |
2.15e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 836 LSGGQRQRISVA---------RALYqhtnvvFLDDPFSAL---DVHlsdHLMQagILELLRDDKRTVVLVTHKLQYLPHA 903
Cdd:PRK00349 831 LSGGEAQRVKLAkelskrstgKTLY------ILDEPTTGLhfeDIR---KLLE--VLHRLVDKGNTVVVIEHNLDVIKTA 899
|
90 100
....*....|....*....|..
gi 1720421572 904 DWIIAM------KDGTIQREGT 919
Cdd:PRK00349 900 DWIIDLgpeggdGGGEIVATGT 921
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
823-942 |
2.17e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 823 HGDQ-TQIGERginLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHlsdhlMQAGILELLRDDKRTVVLVTHKLQYL- 900
Cdd:PRK10636 420 QGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQALTEALIDFEGALVVVSHDRHLLr 491
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720421572 901 PHADWIIAMKDGTIQR-EGTLKDFQRsecqlfehWKTLMNRQD 942
Cdd:PRK10636 492 STTDDLYLVHDGKVEPfDGDLEDYQQ--------WLSDVQKQE 526
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
831-907 |
2.26e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 831 ERGIN-LSGGQRQRISVARALYQHTNVV--FLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWII 907
Cdd:PRK00635 471 ERALAtLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
837-900 |
2.93e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 837 SGGQRQRISVARALYQHTNVVFLDDPFSALDVH----LSDHLMQAgilellrddKRTVVLVTHKLQYL 900
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwLETYLLKW---------PKTFIVVSHAREFL 404
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
824-912 |
3.67e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 824 GDQTQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHA 903
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQL-IAELAKKDKGIIIISSEMPELLGIT 458
|
....*....
gi 1720421572 904 DWIIAMKDG 912
Cdd:PRK10982 459 DRILVMSNG 467
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1096-1240 |
5.34e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 40.61 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 1096 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCntidQHIPSTLE-CLS---RSTLL---CVSALTVISYVTP 1168
Cdd:cd18574 70 GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADV----QEFKSSFKqCVSqglRSVTQtvgCVVSLYLISPKLT 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720421572 1169 VFLVALLPLAVVC-YFIQKYFRVASRDLQQLDDTTqlplLSHFAETVEGLTTIRAFRYEAR----FQQKLLEYTDSN 1240
Cdd:cd18574 146 LLLLVIVPVVVLVgTLYGSFLRKLSRRAQAQVAKA----TGVADEALGNIRTVRAFAMEDRelelYEEEVEKAAKLN 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
822-927 |
5.93e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 822 PHGDQtQIGergiNLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQagILELLRDDKRTVVLVTHKL-QYL 900
Cdd:PRK10762 387 PSMEQ-AIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ--LINQFKAEGLSIILVSSEMpEVL 459
|
90 100
....*....|....*....|....*..
gi 1720421572 901 PHADWIIAMKDGTIQREgtlkdFQRSE 927
Cdd:PRK10762 460 GMSDRILVMHEGRISGE-----FTREQ 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
696-896 |
6.96e-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: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 696 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAtlgemQRVSGAVFwnsslpdSEGEdpryclRTSN-PERETaadSDARS 772
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLnvLA-----ERVTTGVI-------TGGD------RLVNgRPLDS---SFQRS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720421572 773 RGPVayASQKPWLLNATVEENITFE---------SPFNKQRY-KMVIEACSLQPDIDILphgdqtqIGERGINLSGGQRQ 842
Cdd:TIGR00956 838 IGYV--QQQDLHLPTSTVRESLRFSaylrqpksvSKSEKMEYvEEVIKLLEMESYADAV-------VGVPGEGLNVEQRK 908
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720421572 843 RISVARALYQHTN-VVFLDDPFSALDVHLSdhlmqAGILELLR---DDKRTVVLVTHK 896
Cdd:TIGR00956 909 RLTIGVELVAKPKlLLFLDEPTSGLDSQTA-----WSICKLMRklaDHGQAILCTIHQ 961
|
|
| |
