|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
53-931 |
0e+00 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 710.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPKSvLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEK 132
Cdd:TIGR00957 646 WARDLPPT-LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 133 YNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECI 212
Cdd:TIGR00957 725 LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVI 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 213 --KKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN----------------LRGLQFK 274
Cdd:TIGR00957 805 gpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTyapdeqqghledswtaLVSGEGK 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 275 DPEHIYNVAMVETLKESPAQRDEDAvlASGDEKDEGKE-PETEEFVDTNAPAH--QLIQTESPQEGIVTWKTYHTYIKAS 351
Cdd:TIGR00957 885 EAKLIENGMLVTDVVGKQLQRQLSA--SSSDSGDQSRHhGSSAELQKAEAKEEtwKLMEADKAQTGQVELSVYWDYMKAI 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 352 GgYLVSFLVLCLFFLMMGSSAFSTWWLGIWLDrgSQVVCASQNNKTacnvdqtlqdtkhhmYQL-VYIAsmvsvlmFGII 430
Cdd:TIGR00957 963 G-LFITFLSIFLFVCNHVSALASNYWLSLWTD--DPMVNGTQNNTS---------------LRLsVYGA-------LGIL 1017
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 431 KGFTFTNTTL-------MASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFIL 503
Cdd:TIGR00957 1018 QGFAVFGYSMavsiggiQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGAL 1097
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 504 VIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEN 583
Cdd:TIGR00957 1098 IVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDEN 1177
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 584 SSHLLYFNCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLR 663
Cdd:TIGR00957 1178 QKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLK 1257
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 664 EYILTcvpEHTHPFKV-GTCPKD-WPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFR 741
Cdd:TIGR00957 1258 EYSET---EKEAPWQIqETAPPSgWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFR 1334
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 742 LVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAE 821
Cdd:TIGR00957 1335 INESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHE 1414
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 822 VTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMEN 901
Cdd:TIGR00957 1415 CAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDK 1494
|
890 900 910
....*....|....*....|....*....|
gi 568956771 902 GKVIEFDKPEVLAEKPDSAFAMllAAEVGL 931
Cdd:TIGR00957 1495 GEVAEFGAPSNLLQQRGIFYSM--AKDAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
53-922 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 709.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQM-QLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGE 131
Cdd:PLN03130 624 WDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 132 KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEC 211
Cdd:PLN03130 704 PFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKC 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 212 IKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNLRGLQFKDPEHiyNVAMVETLKES 291
Cdd:PLN03130 784 IKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVEEN--GEEEDDQTSSK 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 292 PAQRDEDAVLA-SGDEKDEGKEPETeefvdtnapahQLIQTESPQEGIVTWKTYHTYIKASGGYLVsflVLCLFFLMMGS 370
Cdd:PLN03130 862 PVANGNANNLKkDSSSKKKSKEGKS-----------VLIKQEERETGVVSWKVLERYKNALGGAWV---VMILFLCYVLT 927
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 371 SAF---STWWLGIWLDRGsqvvcasqnnktacnvdqTLQDTKHHMYQLVYIASMVSVLMFGIIKGFTFTNTTLMASSSLH 447
Cdd:PLN03130 928 EVFrvsSSTWLSEWTDQG------------------TPKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLH 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 448 NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLIL 527
Cdd:PLN03130 990 DAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGA 1069
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 528 LRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRWFALRMDILMNI 607
Cdd:PLN03130 1070 YLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGL 1149
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 608 VTFVVALLVTLSFSSISASSK-----GLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI-----LTCVPEHTHPf 677
Cdd:PLN03130 1150 MIWLTASFAVMQNGRAENQAAfastmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIdlpseAPLVIENNRP- 1228
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 678 kvgtcPKDWPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDI 757
Cdd:PLN03130 1229 -----PPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI 1303
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 758 CTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLL 837
Cdd:PLN03130 1304 SKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLL 1383
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 838 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 917
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNE 1463
|
....*
gi 568956771 918 DSAFA 922
Cdd:PLN03130 1464 GSAFS 1468
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
53-925 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 652.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQM-QLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGE 131
Cdd:PLN03232 624 WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 132 KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEC 211
Cdd:PLN03232 704 DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 212 IKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNLRGLqfkDPEHIYNVAMVETLKES 291
Cdd:PLN03232 784 MKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKM---DATQEVNTNDENILKLG 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 292 P-AQRD-EDAVLASGDEKDEGKEpeteefvdtnapahQLIQTESPQEGIVTWKTYHTYIKASGG-YLVSFLVLCLFFLMM 368
Cdd:PLN03232 861 PtVTIDvSERNLGSTKQGKRGRS--------------VLVKQEERETGIISWNVLMRYNKAVGGlWVVMILLVCYLTTEV 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 369 GSSAFSTWwLGIWLDRgsqvvcasqnnktacnvdQTLQDTKHHMYQLVYiasmvSVLMFGIIkGFTFTNT------TLMA 442
Cdd:PLN03232 927 LRVSSSTW-LSIWTDQ------------------STPKSYSPGFYIVVY-----ALLGFGQV-AVTFTNSfwlissSLHA 981
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 443 SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAV 522
Cdd:PLN03232 982 AKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLI 1061
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 523 IFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYdKKDDCISKF--KTLnDENSSHLLYFNCALRWFALR 600
Cdd:PLN03232 1062 LFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAY-KAYDRMAKIngKSM-DNNIRFTLANTSSNRWLTIR 1139
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 601 MDILMNIVTFVVALLVTLSF-----SSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI-----LTCV 670
Cdd:PLN03232 1140 LETLGGVMIWLTATFAVLRNgnaenQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIdlpseATAI 1219
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 671 PEHTHPfkvgtcPKDWPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI 750
Cdd:PLN03232 1220 IENNRP------VSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 751 IIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFS 830
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFS 1373
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 831 VGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP 910
Cdd:PLN03232 1374 VGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSP 1453
|
890
....*....|....*
gi 568956771 911 EVLAEKPDSAFAMLL 925
Cdd:PLN03232 1454 QELLSRDTSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-927 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 619.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 22 AQIQKRHVFKKQRPELYSEQSRSDQGVASPEWQSGS-----PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQM 96
Cdd:PTZ00243 631 PSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDffelePKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 97 QLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQR 176
Cdd:PTZ00243 711 EISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKAR 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 177 ISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 256
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 257 ergryAKLIHNLRGLQFKDPEhiynvamvetLKESPAQRDEDAV-LASGDEKDEGKEPETEEFVD-------TNAPAHQL 328
Cdd:PTZ00243 871 -----TSLYATLAAELKENKD----------SKEGDADAEVAEVdAAPGGAVDHEPPVAKQEGNAeggdgaaLDAAAGRL 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 329 IQTESPQEGIVTWKTYHTYIKASGGYLVSFLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVVCASqnnktacnvdqtlqdt 408
Cdd:PTZ00243 936 MTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMWSTRSFKLSAAT---------------- 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 409 khhmYQLVYIAsMVSVLMFGIIKGFTFTNTTL-MASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPF 487
Cdd:PTZ00243 1000 ----YLYVYLG-IVLLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPM 1074
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 488 HAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYD 567
Cdd:PTZ00243 1075 SYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYG 1154
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 568 KKDDCISKFKTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSK----GLSLSYIIQLSGLLQ 643
Cdd:PTZ00243 1155 KAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSQEiglvSLSLTMAMQTTATLN 1234
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 644 VCVRTGTETQAKFTSAELLREYIL-----------------------------TCVPEHTHPfkVGTCPKDWPSrGEITF 694
Cdd:PTZ00243 1235 WLVRQVATVEADMNSVERLLYYTDevphedmpeldeevdalerrtgmaadvtgTVVIEPASP--TSAAPHPVQA-GSLVF 1311
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 695 KDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQ 774
Cdd:PTZ00243 1312 EGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQ 1391
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 775 DPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL-RNSKIILLD 853
Cdd:PTZ00243 1392 DPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMD 1471
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 854 EATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAA 927
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
353-666 |
2.37e-152 |
|
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: 451.25 E-value: 2.37e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 353 GYLVSFLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVVcASQNNKTACNVDQTLQDTKHHMYQLVYIASMVSVLMFGIIKG 432
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNT-TNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 433 FTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPV 512
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 513 VLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNC 592
Cdd:cd18599 160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 593 ALRWFALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 666
Cdd:cd18599 240 AMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
61-908 |
2.85e-141 |
|
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: 457.06 E-value: 2.85e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNHQRYQH 140
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 141 TVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKT 220
Cdd:TIGR01271 521 VIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKT 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 221 VVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNL-------------------------------- 268
Cdd:TIGR01271 601 RILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLeafdnfsaerrnsiltetlrrvsidgdstvfs 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 269 ----RGLQFKDPEHIYNVAMVETLKESP------------------AQRDEDAVLASGD-------EKDEGKEPETEEFV 319
Cdd:TIGR01271 681 gpetIKQSFKQPPPEFAEKRKQSIILNPiasarkfsfvqmgpqkaqATTIEDAVREPSErkfslvpEDEQGEESLPRGNQ 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 320 DTNAPAHQ---------LIQTESPQEGIV--------------------------------------------------- 339
Cdd:TIGR01271 761 YHHGLQHQaqrrqsvlqLMTHSNRGENRReqlqtsfrkkssitqqnelaseldiysrrlskdsvyeiseeineedlkecf 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 340 -----------TWKTYHTYIKASGGyLVSFLVLCLFFLMMGSSAFstwWLGIWLDRGSQVVCASQNNKTACNVDQTLQ-- 406
Cdd:TIGR01271 841 aderenvfettTWNTYLRYITTNRN-LVFVLIFCLVIFLAEVAAS---LLGLWLITDNPSAPNYVDQQHANASSPDVQkp 916
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 407 ----DTKHHMYQLVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD 482
Cdd:TIGR01271 917 viitPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIID 996
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 483 VRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGV 562
Cdd:TIGR01271 997 DMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWT 1076
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 563 IHAYDKKDDCISKF-KTLNDENSSHLLYFNcALRWFALRMDILMnIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGL 641
Cdd:TIGR01271 1077 IRAFGRQSYFETLFhKALNLHTANWFLYLS-TLRWFQMRIDIIF-VFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILST 1154
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 642 LQVCVRTGTETQAKFTSAELLREYIlTCVPEHTHPFKVGT--------------CPKDWPSRGEITFKDYRMRYRDNTPL 707
Cdd:TIGR01271 1155 LQWAVNSSIDVDGLMRSVSRVFKFI-DLPQEEPRPSGGGGkyqlstvlvienphAQKCWPSGGQMDVQGLTAKYTEAGRA 1233
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEpASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL 787
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 788 DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLV 867
Cdd:TIGR01271 1313 DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQII 1392
|
970 980 990 1000
....*....|....*....|....*....|....*....|.
gi 568956771 868 QSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFD 908
Cdd:TIGR01271 1393 RKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
690-910 |
1.50e-130 |
|
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: 391.47 E-value: 1.50e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 690 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 769
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 849
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 850 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP 910
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
415-930 |
1.83e-109 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 349.46 E-value: 1.83e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 415 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQ 494
Cdd:COG1132 65 LLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 495 QFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCIS 574
Cdd:COG1132 145 SVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 575 KFKTLNDENSSHLLYFNCALRWFALRMDILMNIVTFVVALLVTLSFSSisassKGLS-------LSYIIQLSGLLQVCVR 647
Cdd:COG1132 225 RFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLS-----GSLTvgdlvafILYLLRLFGPLRQLAN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 648 TGTETQAKFTSAELLREYILTCV----PEHTHPFKvgtcpkdwPSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVG 723
Cdd:COG1132 300 VLNQLQRALASAERIFELLDEPPeipdPPGAVPLP--------PVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 724 IVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDpLG--SHTDEMLWHV 801
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGrpDATDEEVEEA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 802 LERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVL 881
Cdd:COG1132 450 AKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTI 529
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 568956771 882 TIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKpDSAFAMLLAAEVG 930
Cdd:COG1132 530 VIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQFG 577
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
49-244 |
4.34e-108 |
|
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: 332.13 E-value: 4.34e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 49 ASPEWQSGS--PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIFHGNVREN 126
Cdd:cd03250 6 ASFTWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 206
Cdd:cd03250 86 ILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 568956771 207 VFEECIKKTLK-GKTVVLVTHQLQFLESCDEVILLEDGE 244
Cdd:cd03250 166 IFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
686-910 |
1.89e-90 |
|
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: 285.85 E-value: 1.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 686 WPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL 765
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 766 RTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLertfmrdtimklpeklqaEVTENGENFSVGERQLLCMARALLR 845
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 846 NSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP 910
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
415-929 |
1.09e-85 |
|
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: 289.81 E-value: 1.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 415 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSkDMDELDVRLPFHAENFLQ 494
Cdd:COG2274 200 IGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 495 QFFMVVFILVIMAAV-FPVVLVVLAGLAVIFLILLRIFHRGVQ-ELKQVENISRSpwFSHITSSIQGLGVIHAYDkkddC 572
Cdd:COG2274 279 DLLFVLIFLIVLFFYsPPLALVVLLLIPLYVLLGLLFQPRLRRlSREESEASAKR--QSLLVETLRGIETIKALG----A 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 573 ISKFKTLNDENSSHLLYFNCALRWFALRMDILMN--------IVTFVVALLV-----TLSFSSISASSKGLSLSYIIQLS 639
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGllqqlatvALLWLGAYLVidgqlTLGQLIAFNILSGRFLAPVAQLI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 640 GLLQvcvrtgtETQAKFTSAELLREyILTCVPEHTHPFKVGTCPKDwpsRGEITFKDYRMRYRDNTPLVLDGLNLNIQSG 719
Cdd:COG2274 433 GLLQ-------RFQDAKIALERLDD-ILDLPPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPVLDNISLTIKPG 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 720 QTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL---DPlgSHTDE 796
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 797 MLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK 876
Cdd:COG2274 580 EIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK 659
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 877 SCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKpDSAFAMLLAAEV 929
Cdd:COG2274 660 GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQQQL 711
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
357-666 |
1.62e-83 |
|
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: 270.53 E-value: 1.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 357 SFLVLCLFFLMMGSSAFSTWWLGIWLDRgsqvvcasqnnktacNVDQTLQDTKHHMYqLVYIASMVSVLMFGIIKGFTFT 436
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSD---------------WSSSPNSSSGYYLG-VYAALLVLASVLLVLLRWLLFV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 437 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 516
Cdd:cd18580 65 LAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 517 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 596
Cdd:cd18580 145 LPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 597 FALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 666
Cdd:cd18580 225 LGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
690-928 |
1.35e-77 |
|
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: 253.29 E-value: 1.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 690 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 769
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 849
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 850 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAE 928
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTD 256
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
444-916 |
1.43e-72 |
|
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: 250.06 E-value: 1.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 444 SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvrlPFHAeNFLQQFFMVVFI-LVIMAAVFP------VVLVV 516
Cdd:COG4988 91 RRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALD---GYFA-RYLPQLFLAALVpLLILVAVFPldwlsgLILLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 517 LAGLAVIFLILLRIFHRGVQElKQVENISR-SpwfSHITSSIQGLGVIHAYDKKDDCISKFKTLNDE------------- 582
Cdd:COG4988 167 TAPLIPLFMILVGKGAAKASR-RQWRALARlS---GHFLDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrtmkvlrvaf 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 583 NSShllyfncalrwFALrmDILMNIVTFVVALLVtlsfssisasskGLSLSYI-IQLSGLLQVCV---------RT-GTE 651
Cdd:COG4988 243 LSS-----------AVL--EFFASLSIALVAVYI------------GFRLLGGsLTLFAALFVLLlapefflplRDlGSF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 652 TQAKF---TSAELLREYILTCVPEHTHpfkvGTCPKDWPSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRT 728
Cdd:COG4988 298 YHARAngiAAAEKIFALLDAPEPAAPA----GTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 729 GSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDpLGSH--TDEMLWHVLERTF 806
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR-LGRPdaSDEELEAALEAAG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 807 MRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR 886
Cdd:COG4988 452 LDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR 531
|
490 500 510
....*....|....*....|....*....|
gi 568956771 887 LNTVLNCDLVLVMENGKVIEFDKPEVLAEK 916
Cdd:COG4988 532 LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
357-665 |
2.40e-71 |
|
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: 237.76 E-value: 2.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 357 SFLVLCLFFLMMGSSAFSTWWLGIWldrgsqvvcaSQNNktACNVDQTLQDTkhHMYQLVYIASMVSVLMFGIIKGFTFT 436
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEW----------SDDP--ALNGTQDTEQR--DYRLGVYGALGLGQAIFVFLGSLALA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 437 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 516
Cdd:cd18603 67 LGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 517 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 596
Cdd:cd18603 147 IIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRW 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 597 FALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 665
Cdd:cd18603 227 LAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
690-916 |
7.40e-70 |
|
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: 231.35 E-value: 7.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 690 GEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 769
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDPVLFVGTVRYNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 847
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIR-LGRPnaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 848 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEK 916
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
416-917 |
1.50e-68 |
|
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: 238.90 E-value: 1.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 416 VYIASmVSVLMFGIIKGFT------FT-NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD-----V 483
Cdd:COG4987 54 LFVPI-VGVRAFAIGRTVFrylerlVShDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylrV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 484 RLPFHAenflqqFFMVVFILVIMAAVF--PVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLG 561
Cdd:COG4987 133 LLPLLV------ALLVILAAVAFLAFFspALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 562 VIHAYDKKDDCISKFKTLNDENSSHLLyfncALRWFALRMDILMNIVTFVVALLVtLSFSSISASSKGLSLSYII----- 636
Cdd:COG4987 207 ELAAYGALDRALARLDAAEARLAAAQR----RLARLSALAQALLQLAAGLAVVAV-LWLAAPLVAAGALSGPLLAllvla 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 637 ------QLSGLLQVCVRTGtETQAkftSAELLREyILTCVPEHTHPfkvgTCPKDWPSRGEITFKDYRMRYRDNTPLVLD 710
Cdd:COG4987 282 alalfeALAPLPAAAQHLG-RVRA---AARRLNE-LLDAPPAVTEP----AEPAPAPGGPSLELEDVSFRYPGAGRPVLD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 711 GLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL--- 787
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrla 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 788 DPlgSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLV 867
Cdd:COG4987 433 RP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 568956771 868 QSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 917
Cdd:COG4987 511 LADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
358-665 |
1.93e-68 |
|
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: 229.67 E-value: 1.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 358 FLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVvcaSQNNktacnvdqtlqdtkhhmYQLVYIASMVSVLMFGIIKGFTFTN 437
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDFFGL---SQGF-----------------YIGIYAGLGVLQAIFLFLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 438 TTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVL 517
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 518 AGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISK-FKTLNDENSSHLLYFNCAlRW 596
Cdd:cd18606 142 PPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKnEKLIDNMNRAYFLTIANQ-RW 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 597 FALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 665
Cdd:cd18606 221 LAIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
358-666 |
1.85e-64 |
|
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: 218.88 E-value: 1.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 358 FLVLCLFFLMMGSSAFSTWWLGIWldrgsqvvcASQNNKTAcnvdqTLQDTKHHM--YQLVYIASMVSVLMFGIIKGFTF 435
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIW---------ASAYETSS-----ALPPSEVSVlyYLGIYALISLLSVLLGTLRYLLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 436 TNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLV 515
Cdd:cd18604 68 FFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 516 VLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALR 595
Cdd:cd18604 148 PAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 596 WFALRMDILMNIVTFVVALLVTLSFSSISASSkGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 666
Cdd:cd18604 228 WLSVRIDLLGALFSFATAALLVYGPGIDAGLA-GFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
353-665 |
3.07e-64 |
|
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: 219.11 E-value: 3.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 353 GYLVSFLVLCLFFLMMGSSAFSTWWLGIW--LDRGSQVVCASQNNKTACNVDQTLQDTKHHMYqlVYIASMVSVLMFGII 430
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLG--IYAGLTAATFVFGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 431 KGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVF 510
Cdd:cd18601 79 RSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 511 PVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYF 590
Cdd:cd18601 159 PWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 591 NCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 665
Cdd:cd18601 239 LATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
692-903 |
3.26e-62 |
|
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: 208.01 E-value: 3.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVGTVRYNLdplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIIL 851
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568956771 852 LDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGK 903
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
692-906 |
7.23e-62 |
|
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: 209.70 E-value: 7.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRY--RDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 769
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDPVLFVGTVRYNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 847
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIR-YGKPdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 848 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 906
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
692-916 |
1.02e-61 |
|
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: 209.39 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVGTVRYNL---DPlgSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSK 848
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 849 IILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEK 916
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
401-906 |
7.04e-60 |
|
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: 214.58 E-value: 7.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 401 VDQTLQDTKHHMyqLVYIASMVSVLMfgIIKGFT-FTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNR 473
Cdd:TIGR02203 41 LDDGFGGRDRSV--LWWVPLVVIGLA--VLRGICsFVSTYLLSWVSnkvvrdIRVRMFEKLLGLPVSFFDRQPTGTLLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 474 FSKDMDELDVRLPFHAENFLQQFFMVVFILVIM-------AAVFPVVLVVLAGLAVIFLILLRIFHRGVQELK-QVENIs 545
Cdd:TIGR02203 117 ITFDSEQVASAATDAFIVLVRETLTVIGLFIVLlyyswqlTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMgQVTTV- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 546 rspwfshITSSIQGLGVIHAYDKKDDCISKFKTLNDENsshllyfncalRWFALRMD----ILMNIVTFVVA------LL 615
Cdd:TIGR02203 196 -------AEETLQGYRVVKLFGGQAYETRRFDAVSNRN-----------RRLAMKMTsagsISSPITQLIASlalavvLF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 616 VTLSFSSISASSKGLSLSYIIQLsGLLQVCVRTGTETQAKFTSAELLREYILTCVPEHTHPFKvGTCPKDwPSRGEITFK 695
Cdd:TIGR02203 258 IALFQAQAGSLTAGDFTAFITAM-IALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT-GTRAIE-RARGDVEFR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 696 DYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQD 775
Cdd:TIGR02203 335 NVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 776 PVLFVGTVRYNL--DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLD 853
Cdd:TIGR02203 415 VVLFNDTIANNIayGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 854 EATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 906
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
53-243 |
2.65e-58 |
|
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: 199.09 E-value: 2.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVN-----------------GPLAYVSQQ 115
Cdd:cd03290 10 WGSGLA--TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 116 AWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:cd03290 88 PWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568956771 196 LSAVDAHVGKHVFEECIKKTLKG--KTVVLVTHQLQFLESCDEVILLEDG 243
Cdd:cd03290 168 FSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
61-275 |
1.23e-57 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 208.48 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PL-------AYVSQQAWIFHGNVRENI 127
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdlTLeslrrqiGVVPQDTFLFSGTIRENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 206
Cdd:COG1132 435 RYGrPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 207 VFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHnlrgLQFKD 275
Cdd:COG1132 515 IQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR----LQFGE 578
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
692-906 |
2.91e-57 |
|
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: 196.68 E-value: 2.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVGTVRYNLdPLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 849
Cdd:cd03251 81 VSQDVFLFNDTVAENI-AYGRPgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 850 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 906
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
688-906 |
5.73e-57 |
|
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: 207.37 E-value: 5.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 688 SRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRT 767
Cdd:COG5265 354 GGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 768 KLTMIPQDPVLFVGTVRYNL---DPlgSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 844
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIaygRP--DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 845 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 906
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
61-259 |
7.14e-57 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 205.76 E-value: 7.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHGNVRENI 127
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRENL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 206
Cdd:COG4988 432 RLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 207 VFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 259
Cdd:COG4988 512 ILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
55-267 |
1.70e-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: 208.15 E-value: 1.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 55 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHG 121
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGiDLrqidpaslrrqiGVVLQDVFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:COG2274 564 TIRENITLGdPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 201 AHVGKHVFeECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 267
Cdd:COG2274 644 AETEAIIL-ENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
357-666 |
4.70e-55 |
|
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: 193.13 E-value: 4.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 357 SFLVLCLFFLMMGSSAFSTWWLGIWLdrgsqvvcasqnNKTACNVDQTLQDTKHhMYQLVYIASMVSVLMFGIIKGFTFT 436
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWV------------SHSNNSFFNFINDSFN-FFLTVYGFLAGLNSLFTLLRAFLFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 437 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 516
Cdd:cd18605 68 YGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 517 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDdcisKFktlNDENSSHLLYFNCAL-- 594
Cdd:cd18605 148 LLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQE----RF---LKEYLEKLENNQRAQla 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 595 -----RWFALRMDILMNIVTFVVALLVTLSFSSISASSK---GLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 666
Cdd:cd18605 221 sqaasQWLSIRLQLLGVLIVTFVALTAVVQHFFGLSIDAgliGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
56-264 |
9.77e-54 |
|
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: 196.91 E-value: 9.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGN 122
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvDLrdldeddlrrriAVVPQRPHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILFGekynhqRYQHT----VHVC---GLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:COG4987 425 LRENLRLA------RPDATdeelWAALervGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEP 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 196 LSAVDAHVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 264
Cdd:COG4987 499 TEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
56-265 |
1.33e-53 |
|
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: 188.14 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIFHGNVRENILFGEKYNH 135
Cdd:cd03291 49 GAP--VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 136 QRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKT 215
Cdd:cd03291 127 YRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKL 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568956771 216 LKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 265
Cdd:cd03291 207 MANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
451-927 |
1.55e-51 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 190.94 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 451 FNKIVRSPMSFFDTTPTGRLMNRFSKDMDEL-DVRLPFHAENFLQqfFMVVFILVIMAAVFPVVL-VVLAGLAVIFLILL 528
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTLLRGTDALfGLWLEFMREHLAT--LVALVVLLPLALFMNWRLsLVLVVLGIVYTLIT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 529 RIFHRGVQELK-QVENiSRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLndenSSHLLYF-NCALRWFAL-----RM 601
Cdd:PRK13657 174 TLVMRKTKDGQaAVEE-HYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDI----ADNLLAAqMPVLSWWALasvlnRA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 602 D--ILMNIVTFVVALLVTlsfssisassKG-LSLSYIIQLSGLLQVCVR-----TGTETQAkFTSAELLREY--ILTCVP 671
Cdd:PRK13657 249 AstITMLAILVLGAALVQ----------KGqLRVGEVVAFVGFATLLIGrldqvVAFINQV-FMAAPKLEEFfeVEDAVP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 672 EHTHPFKVGTCPKdwpSRGEITFKDYRMRYrDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTII 751
Cdd:PRK13657 318 DVRDPPGAIDLGR---VKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 752 IDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLDpLG--SHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENF 829
Cdd:PRK13657 394 IDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR-VGrpDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 830 SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE--- 906
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgs 552
|
490 500
....*....|....*....|.
gi 568956771 907 FDkpEVLAEkpDSAFAMLLAA 927
Cdd:PRK13657 553 FD--ELVAR--GGRFAALLRA 569
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
690-913 |
2.67e-51 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 181.59 E-value: 2.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 690 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEpASGTIIIDEVDICTVGLEDLRTKL 769
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKI 849
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 850 ILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVL 913
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
358-665 |
6.19e-51 |
|
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: 181.65 E-value: 6.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 358 FLVLCLFFLMMGSSAFSTWWLGIWLDRGSQVVCASQNNKtacnvDQTLQDTKHHMYQLVYIA-SMVSVLMFGIIKGFTFT 436
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNIT-----SSSLEDDEVSYYISVYAGlSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 437 nTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 516
Cdd:cd18602 77 -AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 517 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 596
Cdd:cd18602 156 LIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRW 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 597 FALRMDILMNIVTFVVAL--LVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREY 665
Cdd:cd18602 236 LGIRLDYLGAVIVFLAALssLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
692-906 |
9.01e-51 |
|
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: 178.83 E-value: 9.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVGTVRYNLdplgSHTDEM--LWHVLERTFM---RDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRN 846
Cdd:cd03252 81 VLQENVLFNRSIRDNI----ALADPGmsMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 847 SKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 906
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
416-924 |
1.69e-49 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 187.24 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 416 VYIASMVSVL--MFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFL 493
Cdd:TIGR00958 204 IFFMCLLSIAssVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 494 QQFFMVVFILVIMAAVFP-VVLVVLAGLAVIFLI--LLRIFHRGVQELKQvENISRSPWFS-HITSSIQ--------GLG 561
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPrLTMVTLINLPLVFLAekVFGKRYQLLSEELQ-EAVAKANQVAeEALSGMRtvrsfaaeEGE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 562 VIHAYDKKDDCISKFKTlndENSSHLLYFncalrWFALRMDILMnivtFVVALLVTLSFSSISASSKGLSLSYII---QL 638
Cdd:TIGR00958 363 ASRFKEALEETLQLNKR---KALAYAGYL-----WTTSVLGMLI----QVLVLYYGGQLVLTGKVSSGNLVSFLLyqeQL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 639 SGLLQVCVRTGTETQAKFTSAELLREYIlTCVPEHTHPfkVGTCPKdwPSRGEITFKDYRMRY--RDNTPlVLDGLNLNI 716
Cdd:TIGR00958 431 GEAVRVLSYVYSGMMQAVGASEKVFEYL-DRKPNIPLT--GTLAPL--NLEGLIEFQDVSFSYpnRPDVP-VLKGLTFTL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 717 QSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLD-PLGSHTD 795
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPD 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 796 EMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKeaF 875
Cdd:TIGR00958 585 EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--R 662
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 568956771 876 KSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAML 924
Cdd:TIGR00958 663 ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
690-905 |
1.18e-47 |
|
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: 169.31 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 690 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKL 769
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDPVLFVGTVRYNLDpLG--SHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNS 847
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNIT-LGapLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 848 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVI 905
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
56-264 |
2.72e-46 |
|
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: 165.87 E-value: 2.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGN 122
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLVSQDVFLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:cd03251 92 VAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 202 hVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 264
Cdd:cd03251 172 -ESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
59-259 |
1.42e-43 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 157.77 E-value: 1.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRE 125
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYNHQ-RYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:cd03254 96 NIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 205 KHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 259
Cdd:cd03254 176 KLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
446-906 |
3.45e-43 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 166.43 E-value: 3.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 446 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMD---ELDVRLpfhAENFLQQFFMVVFILVIM-----------AAVFP 511
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEvirDLYVTV---VATVLRSAALIGAMLVAMfsldwrmalvaIMIFP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 512 VVLVVLAglaviflillrIFHRGVQELkqVENIsRSpWFSHITS----SIQGLGVIHAYDKKddciSKF-KTLNDENSSH 586
Cdd:PRK10790 177 AVLVVMV-----------IYQRYSTPI--VRRV-RA-YLADINDgfneVINGMSVIQQFRQQ----ARFgERMGEASRSH 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 587 LLyfncaLRWFALRMD--ILMNIVTFVVALLVTlsfssisasskGLSLSYIIQLSGLLQVCVRTG--------------- 649
Cdd:PRK10790 238 YM-----ARMQTLRLDgfLLRPLLSLFSALILC-----------GLLMLFGFSASGTIEVGVLYAfisylgrlnepliel 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 650 TETQAKFTSAELLREYILTCVPEHTHPFKVGTCPKdwpSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTG 729
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPL---QSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 730 SGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLdPLGSH-TDEMLWHVLERTFMR 808
Cdd:PRK10790 378 SGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANV-TLGRDiSEEQVWQALETVQLA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 809 DTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLN 888
Cdd:PRK10790 457 ELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLS 536
|
490
....*....|....*...
gi 568956771 889 TVLNCDLVLVMENGKVIE 906
Cdd:PRK10790 537 TIVEADTILVLHRGQAVE 554
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
55-244 |
3.60e-43 |
|
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: 154.46 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 55 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHG 121
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvDLrdldleslrkniAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENILfgekynhqryqhtvhvcglqkdlnslpygdlteigergvnlSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:cd03228 91 TIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568956771 202 HvGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGE 244
Cdd:cd03228 130 E-TEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
61-267 |
7.31e-43 |
|
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: 156.16 E-value: 7.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHGNVRENI 127
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFGEKYNHQryQHTVHVCGL---QKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:cd03249 98 RYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 205 KHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 267
Cdd:cd03249 176 KLV-QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
61-240 |
1.18e-42 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 163.61 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRENI 127
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvPLadadadswrdqiAWVPQHPFLFAGTIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFGEKY-NHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 206
Cdd:TIGR02857 417 RLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAE 496
|
170 180 190
....*....|....*....|....*....|....
gi 568956771 207 VFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILL 240
Cdd:TIGR02857 497 VLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
415-887 |
1.24e-42 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 163.69 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 415 LVYIASMVSVLMFGIIKGF-------TFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD---VR 484
Cdd:TIGR02868 50 LYLSVAAVAVRAFGIGRAVfrylerlVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQdlyVR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 485 --LPfhaenflqqffMVVFILVIMAAV-------FPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITS 555
Cdd:TIGR02868 130 viVP-----------AGVALVVGAAAVaaiavlsVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 556 SIQGLGVIHAYDKKDDCISKFKtlnDENSSHLLYFNCALRWFALR--MDILMNIVTfVVALLVTLSFSSISASSKGLSLS 633
Cdd:TIGR02868 199 ALDGAAELVASGALPAALAQVE---EADRELTRAERRAAAATALGaaLTLLAAGLA-VLGALWAGGPAVADGRLAPVTLA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 634 YIIqlsgLLQVCVrtgTETQAKFTSA-ELLREYI-----LTCVPEHTHPFKVGTCPKDWPSRGE---ITFKDYRMRYRDN 704
Cdd:TIGR02868 275 VLV----LLPLAA---FEAFAALPAAaQQLTRVRaaaerIVEVLDAAGPVAEGSAPAAGAVGLGkptLELRDLSAGYPGA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 705 TPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVR 784
Cdd:TIGR02868 348 PP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 YNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 862
Cdd:TIGR02868 427 ENLR-LARPdaTDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
490 500
....*....|....*....|....*
gi 568956771 863 TDTLVQSTIKEAFKSCTVLTIAHRL 887
Cdd:TIGR02868 506 TADELLEDLLAALSGRTVVLITHHL 530
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
442-899 |
2.17e-42 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 162.84 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 442 ASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVrlpfHAENFLQQFFMVVFI-LVIMAAVFP------VVL 514
Cdd:TIGR02857 75 VKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDG----YFARYLPQLVLAVIVpLAILAAVFPqdwisgLIL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 515 VVLAGLAVIFLILLrifhrgvqeLKQVENISRSPWFS------HITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLL 588
Cdd:TIGR02857 151 LLTAPLIPIFMILI---------GWAAQAAARKQWAAlsrlsgHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTM 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 589 YfncalrwfALRMDILMnivTFVVALLVTLSFSSISASSkGLSLSY--IIQLSGLL-------------QVCVRTGTETQ 653
Cdd:TIGR02857 222 R--------VLRIAFLS---SAVLELFATLSVALVAVYI-GFRLLAgdLDLATGLFvlllapefylplrQLGAQYHARAD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 654 AKFTSAELLREYILTCVPEHthpfkvGTCPKDWPSRGEITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKS 733
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPLA------GKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKS 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 734 SLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL---DPLGShtDEMLWHVLERTFMRDT 810
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDAS--DAEIREALERAGLDEF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 811 IMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTV 890
Cdd:TIGR02857 441 VAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALA 520
|
....*....
gi 568956771 891 LNCDLVLVM 899
Cdd:TIGR02857 521 ALADRIVVL 529
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
340-666 |
4.21e-42 |
|
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: 156.89 E-value: 4.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 340 TWKTYHTYIKASGGYLVsFLVLCLFFLMMGSSAFSTWwlgIW-LDRGSQVVCASQNNKTACNVDQTLQDTKHHMYQLVYI 418
Cdd:cd18600 2 TWNTYLRYITSHKSLIF-VLILCLVIFAIEVAASLVG---LWlLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 419 ASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFM 498
Cdd:cd18600 78 GVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 499 VVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKF-K 577
Cdd:cd18600 158 VIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFhK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 578 TLNDENSSHLLYFNcALRWFALRMDILMnIVTFVVALLVTLSFSSISASSKGLSLSYIIQLSGLLQVCVRTGTETQAKFT 657
Cdd:cd18600 238 ALNLHTANWFLYLS-TLRWFQMRIEMIF-VIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMR 315
|
....*....
gi 568956771 658 SAELLREYI 666
Cdd:cd18600 316 SVSRIFKFI 324
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
687-924 |
8.15e-42 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 162.11 E-value: 8.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 687 PSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR 766
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 TKLTMIPQDPVLFVGTVRYNL--DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 844
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 845 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKpDSAFAML 924
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NGVYAQL 575
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
56-245 |
2.74e-41 |
|
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: 150.82 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P------LAYVSQQAWIFHGN 122
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldPadlrrnIGYVPQDVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILFGEKY-NHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:cd03245 94 LRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 202 HVGKHVFEEcIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:cd03245 174 NSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
59-264 |
2.81e-41 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 151.61 E-value: 2.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRE 125
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:cd03253 94 NIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 205 KHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 264
Cdd:cd03253 174 REIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
61-264 |
3.36e-41 |
|
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: 151.48 E-value: 3.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRENI 127
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDaHVGKH 206
Cdd:cd03252 97 ALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-YESEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 207 VFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 264
Cdd:cd03252 176 AIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
689-904 |
2.42e-39 |
|
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: 145.69 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 689 RGEITFKDYRMRYRdNTP--LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR 766
Cdd:cd03248 9 KGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 TKLTMIPQDPVLFVGTVRYNLD-PLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLR 845
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 846 NSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKV 904
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
56-275 |
2.88e-39 |
|
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: 154.49 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGN 122
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlaslrrQVALVSQDVVLFNDT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILFGE--KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:TIGR02203 422 IANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 201 AHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLiHNlrgLQFKD 275
Cdd:TIGR02203 502 NESERLV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL-HN---MQFRE 571
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
712-930 |
2.97e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.62 E-value: 2.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 712 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNLdPLG 791
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNV-LLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 792 SH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQS 869
Cdd:PRK11174 447 NPdaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 870 TIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPdSAFAMLLAAEVG 930
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATLLAHRQE 586
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
59-267 |
1.07e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 153.08 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQkGVVAVNG-------------PLAYVSQQAWIFHGNVRE 125
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGielreldpeswrkHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEK-YNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:PRK11174 442 NVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 205 KHVFeECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 267
Cdd:PRK11174 522 QLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
700-904 |
2.04e-38 |
|
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: 141.20 E-value: 2.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLF 779
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 780 VGTVRYNLdplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDEATASM 859
Cdd:cd03246 89 SGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568956771 860 DSKTDTLVQSTIKEA-FKSCTVLTIAHRLNTVLNCDLVLVMENGKV 904
Cdd:cd03246 128 DVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
56-266 |
8.51e-38 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 149.86 E-value: 8.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV-------------AVNGPLAYVSQQAWIFHGN 122
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:PRK10789 405 VANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 202 HVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 266
Cdd:PRK10789 485 RT-----EHQILHNLrqwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
687-906 |
8.26e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 146.89 E-value: 8.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 687 PSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR 766
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 TKLTMIPQDPVLFVGTVRYNLdPLGSH--TDEMLWHVLERTFMrDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALL 844
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNL-LLAAPnaSDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 845 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 906
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
692-906 |
9.73e-37 |
|
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: 136.29 E-value: 9.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTM 771
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVGTVRYNLdplgshtdemlwhvlertfmrdtimklpeklqaevtenGENFSVGERQLLCMARALLRNSKIIL 851
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 852 LDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIE 906
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
61-264 |
2.29e-36 |
|
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: 147.20 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRENI 127
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGvdlaiadpawlrrQMGVVLQENVLFSRSIRDNI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFGE-KYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKH 206
Cdd:TIGR01846 552 ALCNpGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE-SEA 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 207 VFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 264
Cdd:TIGR01846 631 LIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
30-267 |
5.19e-36 |
|
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: 146.04 E-value: 5.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 30 FKKQRPELYSEQSRSDQGVASPEWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-P 108
Cdd:TIGR01193 458 FINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGfS 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 109 LA------------YVSQQAWIFHGNVRENILFGEKYN--HQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQR 174
Cdd:TIGR01193 538 LKdidrhtlrqfinYLPQEPYIFSGSILENLLLGAKENvsQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQK 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 175 QRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKktLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL 254
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
250
....*....|...
gi 568956771 255 MEERGRYAKLIHN 267
Cdd:TIGR01193 696 LDRNGFYASLIHN 708
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
59-265 |
1.27e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 144.86 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRE 125
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvPLvqydhhylhrqvALVGQEPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:TIGR00958 574 NIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 205 KHVFEEcikKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 265
Cdd:TIGR00958 654 QLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
700-904 |
2.20e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.79 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLF 779
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 780 VGTVRYNLD-PLGSHTDEMLWHVLERTFMRdtiMKLPEK-LQAEVtengENFSVGERQLLCMARALLRNSKIILLDEATA 857
Cdd:COG4619 87 GGTVRDNLPfPFQLRERKFDRERALELLER---LGLPPDiLDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 858 SMDSKTDTLVQSTIKEAFKSC--TVLTIAH------RLntvlnCDLVLVMENGKV 904
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
61-273 |
2.57e-35 |
|
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: 142.53 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRENI 127
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGvdlrqldpaelraRMALVPQDPVLFAASVMENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFG-------EKYNHQRYQHTvhvcglQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:TIGR02204 435 RYGrpdatdeEVEAAARAAHA------HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALD 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 201 AHVGKHVfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHnlrgLQF 273
Cdd:TIGR02204 509 AESEQLV-QQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLAR----LQF 576
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
61-250 |
4.98e-35 |
|
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: 133.00 E-value: 4.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PL-------AYVSQQAWIFHGNVRENI 127
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiGLhdlrsriSIIPQDPVLFSGTIRSNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 -LFGEKYNHQRYQhTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 206
Cdd:cd03244 99 dPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 207 VfEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 250
Cdd:cd03244 178 I-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
692-907 |
3.48e-34 |
|
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: 130.70 E-value: 3.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRdntplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 768
Cdd:cd03257 9 VSFPTGGGSVK-----ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 769 LTMIPQDPVLfvgtvryNLDPL---GSHTDEMLWHVleRTFMRDTIMKLPEKLQAEVTENGEN--------FSVGERQLL 837
Cdd:cd03257 84 IQMVFQDPMS-------SLNPRmtiGEQIAEPLRIH--GKLSKKEARKEAVLLLLVGVGLPEEvlnrypheLSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 838 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEF 907
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
708-915 |
9.46e-34 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 137.57 E-value: 9.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL 787
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 788 DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLV 867
Cdd:COG4618 427 ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568956771 868 QSTIKEAfKS--CTVLTIAHRLNTVLNCDLVLVMENGKVIEF-DKPEVLAE 915
Cdd:COG4618 507 AAAIRAL-KArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
56-273 |
2.47e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 136.69 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGN 122
Cdd:PRK11176 353 GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILF--GEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:PRK11176 433 IANNIAYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 201 AHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLiHNlrgLQF 273
Cdd:PRK11176 513 TES-----ERAIQAALdelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL-HK---MQF 580
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
695-927 |
3.90e-33 |
|
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: 135.03 E-value: 3.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 695 KDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTKLTM 771
Cdd:COG1123 268 KRYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPV--LF-VGTVRYNL-DPLGSHtdemlwHVLERTFMRDTIMKLPEK--LQAEVTEN--GEnFSVGERQLLCMARAL 843
Cdd:COG1123 347 VFQDPYssLNpRMTVGDIIaEPLRLH------GLLSRAERRERVAELLERvgLPPDLADRypHE-LSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 844 LRNSKIILLDEATASMdsktDTLVQSTIKEAFKS------CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEK 916
Cdd:COG1123 420 ALEPKLLILDEPTSAL----DVSVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
250
....*....|..
gi 568956771 917 PDSAFA-MLLAA 927
Cdd:COG1123 496 PQHPYTrALLAA 507
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
693-903 |
4.46e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 125.05 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 693 TFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMI 772
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 773 PQdpvlfvgtvrynldplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILL 852
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 853 DEATASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGK 903
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
61-240 |
1.73e-32 |
|
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: 125.34 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL-------AYVSQQA---WIFHGNVRENILF 129
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkPLekerkriGYVPQRRsidRDFPISVRDVVLM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 130 GekynhqRYQHTVHVCGLQKD-----LNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHV 203
Cdd:cd03235 94 G------LYGHKGLFRRLSKAdkakvDEALERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 568956771 204 GKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILL 240
Cdd:cd03235 168 QEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLLL 205
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
56-268 |
2.19e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 133.41 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA------------YVSQQAWIFHGN 122
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqPIAdyseaalrqaisVVSQRVHLFSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTeIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:PRK11160 430 LRDNLLLAaPNASDEALIEVLQQVGLEKLLEDDKGLNAW-LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 202 HVGKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNL 268
Cdd:PRK11160 509 ETERQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-901 |
2.68e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 136.31 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 151 LNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgkhvfEECIKKT---LKG---KTVVLV 224
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-----EYLVQKTinnLKGnenRITIII 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 225 THQLQFLESCDEVILLEDGE-----------------------------------------------ICEKGTHKELMEE 257
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKN 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 258 R-GRYAKLIHNLRglqfkdpehiynvamVETLKESPAQRDEDAVLASGDEKDE--GKEPE-----------------TEE 317
Cdd:PTZ00265 717 KnGIYYTMINNQK---------------VSSKKSSNNDNDKDSDMKSSAYKDSerGYDPDemngnskhenesasnkkSCK 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 318 FVDTNAPAHQL------------IQTESPQEGIVTWKTYHTYIKASGGYLVSFLV---LCLFFLMMGSSAFSTWWLGIWL 382
Cdd:PTZ00265 782 MSDENASENNAggklpflrnlfkRKPKAPNNLRIVYREIFSYKKDVTIIALSILVaggLYPVFALLYAKYVSTLFDFANL 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 383 DRGSQvvcasqnnktacnvdqtlqdtKHHMYQLVyiasmVSVLMF--GIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMS 460
Cdd:PTZ00265 862 EANSN---------------------KYSLYILV-----IAIAMFisETLKNYYNNVIGEKVEKTMKRRLFENILYQEIS 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 461 FFDT---TPtGRLMNRFSKDMDELDVRLPFHAENFlQQFFMVVFILVIMAAVF-PVVLVVLAGLAVIFLILLRIFHRgVQ 536
Cdd:PTZ00265 916 FFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIF-THFIVLFLVSMVMSFYFcPIVAAVLTGTYFIFMRVFAIRAR-LT 992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 537 ELKQVEN-----------------ISRSPWFShITSSIQGLGVIHAYDKKD---DCISKFKTLNDENSSHLLYFNCALRW 596
Cdd:PTZ00265 993 ANKDVEKkeinqpgtvfaynsddeIFKDPSFL-IQEAFYNMNTVIIYGLEDyfcNLIEKAIDYSNKGQKRKTLVNSMLWG 1071
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 597 FALRMDILMNIVTFVV-ALLVTLSFSSISASSKGLsLSYIIQLSGLLQVCVRTGTETQAKFTsaeLLREYILTCVPEHTH 675
Cdd:PTZ00265 1072 FSQSAQLFINSFAYWFgSFLIRRGTILVDDFMKSL-FTFLFTGSYAGKLMSLKGDSENAKLS---FEKYYPLIIRKSNID 1147
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 676 PFKVG--TCPKDWPSRGEITFKDYRMRY--RDNTPLVLDgLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL--------- 742
Cdd:PTZ00265 1148 VRDNGgiRIKNKNDIKGKIEIMDVNFRYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhi 1226
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 743 ---------------------------------------------VEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPV 777
Cdd:PTZ00265 1227 vfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPM 1306
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 778 LFVGTVRYNLDpLGSH--TDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEA 855
Cdd:PTZ00265 1307 LFNMSIYENIK-FGKEdaTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEA 1385
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 568956771 856 TASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTVLNCDLVLVMEN 901
Cdd:PTZ00265 1386 TSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
56-257 |
3.24e-32 |
|
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: 132.47 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHGN 122
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAdlkqwdretfgkhIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENIL-FGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:TIGR01842 408 VAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 202 hVGKHVFEECIKKT-LKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:TIGR01842 488 -EGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
709-857 |
4.10e-32 |
|
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: 121.99 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVG-TVRYNL 787
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 788 -------DPLGSHTDEMLWHVLERtfmrdtiMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATA 857
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
56-245 |
5.14e-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: 132.18 E-value: 5.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV------------AVNGP-LAYVSQQAWIFHGN 122
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELGRhIGYLPQDVELFDGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENI-LFGEkynhqryqHT------------VHvcglqkDL-NSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQ 188
Cdd:COG4618 422 IAENIaRFGD--------ADpekvvaaaklagVH------EMiLRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 189 LYLLDDPLSAVDAhVGKHVFEECIKKtLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:COG4618 488 LVVLDEPNSNLDD-EGEAALAAAIRA-LKarGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
61-278 |
1.31e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.05 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICG-NvGSGKSSLISALLGQMQLQKGVVAVNGP--------LAYVSQQA---WIFHGNVRENIL 128
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGpN-GAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FGekynhqRYQHTVHVCGLQKD--------LNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAV 199
Cdd:COG1121 100 MG------RYGRRGLFRRPSRAdreavdeaLERV---GLEDLADRPIGeLSGGQQQRVLLARALAQDPDLLLLDEPFAGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 200 DAHvGKHVFEECIKKtLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEkGTHKELMEErgryaKLIHNLRGLQFKDP 276
Cdd:COG1121 171 DAA-TEEALYELLRE-LRreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTP-----ENLSRAYGGPVALL 242
|
..
gi 568956771 277 EH 278
Cdd:COG1121 243 AH 244
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
695-927 |
2.40e-31 |
|
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: 123.37 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 695 KDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQ 774
Cdd:COG1124 9 VSYGQGGRRVP--VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 775 DPVLFV---GTVRYNLD-PLGSH----TDEMLWHVLERTFMRDTIM-KLPEKLqaevtengenfSVGERQLLCMARALLR 845
Cdd:COG1124 87 DPYASLhprHTVDRILAePLRIHglpdREERIAELLEQVGLPPSFLdRYPHQL-----------SGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 846 NSKIILLDEATASMdsktDTLVQSTI-------KEAFKScTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKP 917
Cdd:COG1124 156 EPELLLLDEPTSAL----DVSVQAEIlnllkdlREERGL-TYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGP 230
|
250
....*....|.
gi 568956771 918 DSAFA-MLLAA 927
Cdd:COG1124 231 KHPYTrELLAA 241
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
692-913 |
2.48e-31 |
|
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: 122.67 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIIIDEVDICT--VGLED 764
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 765 LRTKLTMIPQDPVLFVGTVRYNLDpLGshtdemLWHVLERTfmRDTIMKLPEK------LQAEVTE--NGENFSVGERQL 836
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA-YG------LRLHGIKL--KEELDERVEEalrkaaLWDEVKDrlHALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 837 LCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVL 913
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
694-903 |
4.70e-31 |
|
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: 121.42 E-value: 4.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 694 FKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIP 773
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 774 QDP--VLFVGTVR----YNLDPLGSHTDEMlwhvLERTFMRDTIMKLPEKLQAEVtengENFSVGERQLLCMARALLRNS 847
Cdd:cd03225 82 QNPddQFFGPTVEeevaFGLENLGLPEEEI----EERVEEALELVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 848 KIILLDEATASMDSKTDTLVQSTIKEaFKSC--TVLTIAHRLNTVLN-CDLVLVMENGK 903
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
59-245 |
6.48e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.69 E-value: 6.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRE 125
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkPLsampppewrrqvAYVPQEPALWGGTVRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYNHQRYQHTvHVCGLQKDLNsLPYGDLteigERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvG 204
Cdd:COG4619 93 NLPFPFQLRERKFDRE-RALELLERLG-LPPDIL----DKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-N 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 205 KHVFEECIKKTL--KGKTVVLVTH-QLQFLESCDEVILLEDGEI 245
Cdd:COG4619 166 TRRVEELLREYLaeEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
61-257 |
7.03e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 118.63 E-value: 7.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAwIFHGN--VREN 126
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEP-ALYPDltVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILF-------GEKYNHQRYQHTVHVCGLQKDLNSLpygdlteIGergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 199
Cdd:COG1131 94 LRFfarlyglPRKEARERIDELLELFGLTDAADRK-------VG----TLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 200 DAhVGKHVFEECIKKtLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 257
Cdd:COG1131 163 DP-EARRELWELLRE-LAaeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
689-917 |
7.39e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 125.60 E-value: 7.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 689 RGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTK 768
Cdd:PRK10789 311 RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 769 LTMIPQDPVLFVGTVRYNLdPLG--SHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRN 846
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNI-ALGrpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 847 SKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 917
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
692-929 |
8.11e-30 |
|
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: 125.02 E-value: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIIIDEVDICTVGLEDLRTK 768
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 769 LTMIPQDPvlfvgtvRYNLDPL--GSHTDEMLW-HVLERTFMRDTIMKLPEK--LQAEVTENGENFSVGERQLLCMARAL 843
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVtvGDQIAEALEnLGLSRAEARARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 844 LRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIE-------FDKPEVL 913
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEdgppeeiLAAPQAL 237
|
250
....*....|....*.
gi 568956771 914 AEKPDSAFAMLLAAEV 929
Cdd:COG1123 238 AAVPRLGAARGRAAPA 253
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
59-245 |
9.46e-30 |
|
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: 116.34 E-value: 9.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGplayvsQQAWIFHGNVRENI--LFGEKYnhq 136
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIgyLPEEPS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 137 ryqhtvhvcglqkdlnslPYGDLTeiGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKK-T 215
Cdd:cd03230 84 ------------------LYENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRElK 142
|
170 180 190
....*....|....*....|....*....|.
gi 568956771 216 LKGKTVVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:cd03230 143 KEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
359-642 |
9.50e-30 |
|
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: 119.67 E-value: 9.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 359 LVLCLFFLMMGS--SAFSTWWLGIWLDrgsqvvcasqnnktACNVDQTLQDTKHHMYQLVYIASMVSVLMFGIIKGFTFT 436
Cdd:pfam00664 1 LILAILLAILSGaiSPAFPLVLGRILD--------------VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 437 NTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVV 516
Cdd:pfam00664 67 HTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 517 LAGLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRW 596
Cdd:pfam00664 147 LLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568956771 597 FALRMDILMNIVTFVVALLVTLSFSSISASSKGL--SLSYIIQLSGLL 642
Cdd:pfam00664 227 SFGITQFIGYLSYALALWFGAYLVISGELSVGDLvaFLSLFAQLFGPL 274
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
692-930 |
1.05e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.33 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDP-VLFVG-TVR---------YNLDPlgSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMA 840
Cdd:PRK13632 88 IFQNPdNQFIGaTVEddiafglenKKVPP--KKMKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 841 RALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP-EVLAEKP 917
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPkEILNNKE 234
|
250 260
....*....|....*....|
gi 568956771 918 -------DSAFAMLLAAEVG 930
Cdd:PRK13632 235 ilekakiDSPFIYKLSKKLK 254
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
59-257 |
1.61e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 118.22 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWI-FHGNVR 124
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrDLaslsrrelarriAYVPQEPPApFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFGekynhqRYQHTVHVCGLQKD--------LNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:COG1120 94 ELVALG------RYPHLGLFGRPSAEdreaveeaLERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 196 LSAVDAHvgkHVFE--ECIKK--TLKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:COG1120 165 TSHLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
61-245 |
1.65e-29 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 117.19 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRENI 127
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkPIsqyehkylhskvSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKH 206
Cdd:cd03248 109 AYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQ 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 568956771 207 VFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:cd03248 188 QVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
56-242 |
2.31e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 113.72 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------PLAYVSQQAWIF-HGNVREN 126
Cdd:cd03293 14 GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQQDALLpWLTVLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFGEKYNH-------QRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 199
Cdd:cd03293 94 VALGLELQGvpkaearERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568956771 200 DAHVGKHVFEEcIKKTLK--GKTVVLVTHQLqflescDEVILLED 242
Cdd:cd03293 163 DALTREQLQEE-LLDIWRetGKTVLLVTHDI------DEAVFLAD 200
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
61-266 |
2.33e-28 |
|
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: 122.36 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSS---LISALL----GQM--------QLQKGVVAvnGPLAYVSQQAWIFHGNVRE 125
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTiakLVAGLYqpwsGEIlfdgipreEIPREVLA--NSVAMVDQDIFLFEGTVRD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NI-LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:TIGR03796 572 NLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 205 KHVFEEcIKKtlKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 266
Cdd:TIGR03796 652 KIIDDN-LRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
61-260 |
4.30e-28 |
|
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: 113.80 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQQAWIFHGN-------VRENI 127
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkePREARRQIGVLPDERglydrltVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 -LFGEKY------NHQRYQHTVHVCGLQKDLNSLpygdlteIGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:COG4555 96 rYFAELYglfdeeLKKRIEELIELLGLEEFLDRR-------VGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 201 AhVGKHVFEECIKKTLK-GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGR 260
Cdd:COG4555 165 V-MARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
61-245 |
6.66e-28 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 110.77 E-value: 6.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHGNVRENI 127
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LfgekynhqryqhtvhvcglqkdlnslpygdlteigergvnlSGGQRQRISLARAVYANRQLYLLDDPLSAVDaHVGKHV 207
Cdd:cd03246 97 L-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERA 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 568956771 208 FEECIKKT-LKGKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:cd03246 135 LNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
61-266 |
7.96e-28 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 120.45 E-value: 7.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV-------------AVNGPLAYVSQQAWIFHGNVRENI 127
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqdlagldvqAVRRQLGVVLQNGRLMSGSIFENI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV 207
Cdd:TIGR03797 548 AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIV 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 208 FEECikKTLKGkTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 266
Cdd:TIGR03797 628 SESL--ERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
59-254 |
1.01e-27 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 112.60 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PL----AYVSQQAWIFHG- 121
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyRLrrrmGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENILFGEKYNHQRYQHTV--------HVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLD 193
Cdd:cd03261 93 TVFENVAFPLREHTRLSEEEIreivleklEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 194 DPLSAVDAhVGKHVFEECI---KKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 254
Cdd:cd03261 162 EPTAGLDP-IASGVIDDLIrslKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
59-244 |
1.16e-27 |
|
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: 109.64 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWifhgnvRENILfgekYNHQr 137
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEEL------RRRIG----YVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 138 yqhtvhvcglqkdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLK 217
Cdd:cd00267 81 -------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE 129
|
170 180
....*....|....*....|....*...
gi 568956771 218 GKTVVLVTHQLQFLE-SCDEVILLEDGE 244
Cdd:cd00267 130 GRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
692-913 |
1.29e-27 |
|
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: 112.83 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVG-TV-------RYN-LDPLGSHTDE---MLWHVLERTfmrdtimKLPEKLQAEVTEngenFSVGERQLLCM 839
Cdd:COG1120 80 VPQEPPAPFGlTVrelvalgRYPhLGLFGRPSAEdreAVEEALERT-------GLEHLADRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 840 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVL 913
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPeEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
56-244 |
2.41e-27 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 110.63 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW--------------IFH 120
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkDLTKLSLKELrrkvglvfqnpddqFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 121 GNVRENILFGEKyNHQRYQHTVhvcgLQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLArAVYANR-QLYLLDDPLSA 198
Cdd:cd03225 91 PTVEEEVAFGLE-NLGLPEEEI----EERVEEALELVGLEGLRDRSPfTLSGGQKQRVAIA-GVLAMDpDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568956771 199 VDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQFL-ESCDEVILLEDGE 244
Cdd:cd03225 165 LDPAGRRELLE--LLKKLKaeGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
708-903 |
3.17e-27 |
|
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: 109.20 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG--LEDLRTKLTMIPQDPVLFVG-TVR 784
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 YNLdplgshtdemlwhvlertfmrdtimklpeklqaevtenGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTD 864
Cdd:cd03229 95 ENI--------------------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568956771 865 TLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGK 903
Cdd:cd03229 137 REVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
59-245 |
3.19e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.06 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQqawifhgnvre 125
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 nilfgekynhqryqhtvhvcglqkdlnSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:cd03214 81 ---------------------------ALELLGLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568956771 205 KHVFEECIK-KTLKGKTVVLVTHQL-QFLESCDEVILLEDGEI 245
Cdd:cd03214 134 IELLELLRRlARERGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
61-242 |
1.19e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 108.34 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQQAWIFHGN-------VRENI 127
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHADglkpeltVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LF-----GEKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH 202
Cdd:COG4133 97 RFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568956771 203 vGKHVFEECIKKTL-KGKTVVLVTHQLQFLESCdEVILLED 242
Cdd:COG4133 166 -GVALLAELIAAHLaRGGAVLLTTHQPLELAAA-RVLDLGD 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
61-264 |
1.38e-26 |
|
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: 116.07 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQ---AWI---------FHGNVRENI 127
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqDIRDVTQAslrAAIgivpqdtvlFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFG-------EKYNHQRYQHtVHvcglqkDL-NSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 199
Cdd:COG5265 453 AYGrpdaseeEVEAAARAAQ-IH------DFiESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 200 DAHVgkhvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 264
Cdd:COG5265 526 DSRT-----ERAIQAALrevaRGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
692-918 |
4.39e-26 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 107.59 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 768
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 769 LTMIPQDPVLFVG-TVRYNLD-PLGSHTDEMLWHVLERTFM-------RDTIMKLPEKLqaevtengenfSVGERQLLCM 839
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTRLSEEEIREIVLEkleavglRGAEDLYPAEL-----------SGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 840 ARALLRNSKIILLDEATASMDSKTDTLVQSTI---KEAFKsCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAE 915
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIrslKKELG-LTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
...
gi 568956771 916 KPD 918
Cdd:cd03261 227 SDD 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
61-258 |
5.77e-26 |
|
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: 107.03 E-value: 5.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQ-----------QawIFHGNV 123
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRkvglvfqnpddQ--LFAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLArAVYANR-QLYLLDDP 195
Cdd:COG1122 94 EEDVAFGpenlglpREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIA-GVLAMEpEVLVLDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 196 LSAVDAHvGKHVFEECIKK-TLKGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:COG1122 162 TAGLDPR-GRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
705-903 |
8.14e-26 |
|
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: 106.01 E-value: 8.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 705 TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIdevdICTVGLedlrtkltmIPQDPVLFVGTVR 784
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV----PGSIAY---------VSQEPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 YNLdpLGSHT--DEMLWHVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 862
Cdd:cd03250 84 ENI--LFGKPfdEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568956771 863 T-DTLVQSTIKEAFKSC-TVLTIAHRLNTVLNCDLVLVMENGK 903
Cdd:cd03250 162 VgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
53-228 |
9.16e-26 |
|
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: 112.84 E-value: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIF 119
Cdd:TIGR02868 344 YPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 HGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSA 198
Cdd:TIGR02868 422 DTTVRENLRLArPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|
gi 568956771 199 VDAHVGKHVFEEcIKKTLKGKTVVLVTHQL 228
Cdd:TIGR02868 502 LDAETADELLED-LLAALSGRTVVLITHHL 530
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
64-245 |
9.72e-26 |
|
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: 106.23 E-value: 9.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVrKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL-----------------AYVSQQAWIF-HGNVRE 125
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYnHQRYQHTVHVcglQKDLNSLpygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:cd03297 95 NLAFGLKR-KRNREDRISV---DELLDLL---GLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 205 KHVFEEC--IKKTLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:cd03297 168 LQLLPELkqIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
684-917 |
1.71e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 113.97 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 684 KDWPSRGEITFKDYRMRY--RDNTPLVLDgLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII-DEVDICTV 760
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYdtRKDVEIYKD-LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 761 GLEDLRTKLTMIPQDPVLFVGTVRYNL-------------------------------------------DPLGSHTDEM 797
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyynedgndsqenknkrnscrakcagdlnDMSNTTDSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 798 LWH---------------VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 862
Cdd:PTZ00265 534 LIEmrknyqtikdsevvdVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 863 TDTLVQSTIK--EAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 917
Cdd:PTZ00265 614 SEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
52-245 |
4.03e-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: 104.49 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 52 EWQSGSPKS-VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW----------IF 119
Cdd:cd03255 9 TYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtDISKLSEKELaafrrrhigfVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 -------HGNVRENILFGEKY-------NHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYA 185
Cdd:cd03255 89 qsfnllpDLTALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYP-----------SELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 186 NRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMEL-LRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
56-249 |
4.19e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 103.16 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP------------LAYVSQQAWIFHGNV 123
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENIlfgekynhqryqhtvhvcglqkdlnslpygdlteigerGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHV 203
Cdd:cd03247 92 RNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568956771 204 GKHVFEeCIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKG 249
Cdd:cd03247 134 ERQLLS-LIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
695-905 |
4.46e-25 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 102.90 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 695 KDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQ 774
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 775 dpvlfvgtvryNLDPLGshtdemLWHVLERTFMRdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDE 854
Cdd:cd03214 81 -----------ALELLG------LAHLADRPFNE--------------------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568956771 855 ATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVI 905
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
692-918 |
9.24e-25 |
|
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: 103.91 E-value: 9.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 768
Cdd:COG1127 6 IEVRNLTKSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 769 LTMIPQDPVLFVG-TVRYNLD-PLGSHTD-------EMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGerqllcM 839
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAfPLREHTDlseaeirELVLEKLELVGLPGAADKMPSEL-----------SGG------M 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 840 ------ARALLRNSKIILLDEATASMD----SKTDTLVQsTIKEAFKsCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFD 908
Cdd:COG1127 147 rkrvalARALALDPEILLYDEPTAGLDpitsAVIDELIR-ELRDELG-LTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
250
....*....|
gi 568956771 909 KPEVLAEKPD 918
Cdd:COG1127 225 TPEELLASDD 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
56-243 |
9.91e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.40 E-value: 9.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------PLAYVSQQA----WIfhgNV 123
Cdd:COG1116 21 GGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQEPallpWL---TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPL 196
Cdd:COG1116 98 LDNVALGlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 197 SAVDAHVGKHVFEECIK---KTlkGKTVVLVTHQLQ---FLesCDEVILLEDG 243
Cdd:COG1116 167 GALDALTRERLQDELLRlwqET--GKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
60-250 |
1.16e-24 |
|
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: 102.88 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 60 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVREN 126
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 IlfgEKYNHQRyqhtvhvcglQKDLnslpYGDLtEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgKH 206
Cdd:cd03369 102 L---DPFDEYS----------DEEI----YGAL-RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 207 VFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 250
Cdd:cd03369 163 LIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
62-265 |
1.25e-24 |
|
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: 109.59 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRENIL 128
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGidintvtreslrkSIATVFQDAGLFNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV 207
Cdd:TIGR01192 431 LGrEGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARV 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 208 fEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 265
Cdd:TIGR01192 511 -KNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
692-911 |
1.26e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.71 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDP-VLFVGT-----VRYNLDPLGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARA 842
Cdd:PRK13635 86 VFQNPdNQFVGAtvqddVAFGLENIGVPREEMVERVdqaLRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 843 LLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPE 911
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
61-245 |
1.76e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 102.21 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENIL 128
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDYALFpHLTVAENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FGEKYNHQRYQHTVhvcglQKDLNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV 207
Cdd:cd03259 95 FGLKLRGVPKAEIR-----ARVRELLELVGLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568956771 208 FEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 245
Cdd:cd03259 170 REE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
692-906 |
2.38e-24 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 102.66 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLV--LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVE-PASGTIIIDEVDICTV---GLEDL 765
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLsgkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 766 RTKLTMIPQDPVLFVG-TVRYNLD-PL------GSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLL 837
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlPLeiagvpKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 838 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRElgLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
62-197 |
4.67e-24 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 98.87 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIF-HGNVRENI 127
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 128 LFGEkyNHQRYQHTVHVCGLQKDLNSLPYGDL--TEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLS 197
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
62-266 |
4.80e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 107.74 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRENIL 128
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhvgkhV 207
Cdd:PRK13657 431 VGrPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV-----E 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 208 FEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 266
Cdd:PRK13657 506 TEAKVKAALdelmKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
692-908 |
5.69e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 101.06 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEdlRTKLTM 771
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLF-----VGTVRYNLDPLGSHTDEMLWHVLERTFMrdtiMKLPEKLQAEVTEngenFSVGERQLLCMARALLRN 846
Cdd:cd03259 77 VFQDYALFphltvAENIAFGLKLRGVPKAEIRARVRELLEL----VGLEGLLNRYPHE----LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 847 SKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFD 908
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
692-910 |
7.17e-24 |
|
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: 101.49 E-value: 7.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTK 768
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 769 LTMIPQDpvlfvgtvrYNLDP------------LGSHTdemLWHVLERTFMRDTIMK---------LPEKLQAEVTEnge 827
Cdd:cd03256 80 IGMIFQQ---------FNLIErlsvlenvlsgrLGRRS---TWRSLFGLFPKEEKQRalaalervgLLDKAYQRADQ--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 828 nFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVL-NCDLVLVMENGKV 904
Cdd:cd03256 145 -LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAReYADRIVGLKDGRI 223
|
....*.
gi 568956771 905 IeFDKP 910
Cdd:cd03256 224 V-FDGP 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
61-256 |
1.07e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 103.69 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAWIF-HGNVRENI 127
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlftnlpprerRVGFVFQHYALFpHMTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFG-------EKYNHQRYQH---TVHvcglqkdlnslpygdLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPL 196
Cdd:COG1118 97 AFGlrvrppsKAEIRARVEElleLVQ---------------LEGLADRYPSqLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 197 SAVDAHVGKHVfEECIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELME 256
Cdd:COG1118 162 GALDAKVRKEL-RRWLRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
59-244 |
1.17e-23 |
|
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: 98.80 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG---------------PLAYVSQQAWIF-HGN 122
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRIGMVFQDFALFpHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILFGekynhqryqhtvhvcglqkdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH 202
Cdd:cd03229 93 VLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568956771 203 VGKHVFEECikKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGE 244
Cdd:cd03229 135 TRREVRALL--KSLQaqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
59-261 |
1.20e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 106.73 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWIFHGNVRE 125
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrPLsslshsvlrqgvAMVQQDPVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgk 205
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-- 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 206 hvfEECIKKTL----KGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRY 261
Cdd:PRK10790 512 ---EQAIQQALaavrEHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
692-905 |
1.21e-23 |
|
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: 100.27 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTvGLEDLRTKLTM 771
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVG-TVRYNLD---PLGSHTDEMLWHVLERTFmrdTIMKLPEKLQAEVTengeNFSVGERQLLCMARALLRNS 847
Cdd:cd03263 80 CPQFDALFDElTVREHLRfyaRLKGLPKSEIKEEVELLL---RVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 848 KIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 905
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
61-245 |
4.36e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.58 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA----------------YVSQqawiFHG-- 121
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqDISslserelarlrrrhigFVFQ----FFNll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 ---NVRENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYL 191
Cdd:COG1136 99 pelTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 192 LDDPLSAVDAHVGKHVFE---ECIKKTlkGKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLEllrELNREL--GTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
708-906 |
9.12e-23 |
|
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: 100.13 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIIIDEVDICTVGLEDLRT----KLTMIPQD----- 775
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 776 -PVLfvgTVRYNL-DPLGSHTD-----------EMlwhvLERTFMRDtimklPEKL------QaevtengenFSVGERQL 836
Cdd:COG0444 100 nPVM---TVGDQIaEPLRIHGGlskaeareraiEL----LERVGLPD-----PERRldryphE---------LSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 837 LCMARALLRNSKIILLDEATASMdsktDTLVQSTI-------KEAFKsCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTAL----DVTIQAQIlnllkdlQRELG-LAILFITHDLGVVAEiADRVAVMYAGRIVE 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
692-915 |
1.06e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 98.24 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvglEDLRTKLTM 771
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQD-------PVL---FVGTVRYN----LDPLGSHTDEMLWHVLERT----FMRDTIMKLpeklqaevtengenfSVGE 833
Cdd:COG1121 80 VPQRaevdwdfPITvrdVVLMGRYGrrglFRRPSRADREAVDEALERVgledLADRPIGEL---------------SGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 834 RQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVL-NCDLVLVMeNGKVIEFDKP- 910
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPe 223
|
....*
gi 568956771 911 EVLAE 915
Cdd:COG1121 224 EVLTP 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
61-257 |
1.39e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 100.17 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENIL 128
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvtglppekrNVGMVFQDYALFpHLTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FG---EKYN----HQRYQHTVHVCGLqkdlnslpygdlTEIGERGVN-LSGGQRQRISLARAVyANR-QLYLLDDPLSAV 199
Cdd:COG3842 100 FGlrmRGVPkaeiRARVAELLELVGL------------EGLADRYPHqLSGGQQQRVALARAL-APEpRVLLLDEPLSAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 200 DAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:COG3842 167 DAKLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
708-915 |
1.41e-22 |
|
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: 97.12 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQDPVLFVG-TVRY 785
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 786 NLDpLGSHT------DEMLWHVLERtFMRdtimkLPEKLQAEvtenGENFSVGERQLLCMARALLRNSKIILLDEATASM 859
Cdd:cd03224 95 NLL-LGAYArrrakrKARLERVYEL-FPR-----LKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 860 DSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAE 915
Cdd:cd03224 164 APKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
61-256 |
1.57e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 97.57 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWiFHGNVRenILFGEKYN--HQRy 138
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA-FRRRVQ--MVFQDPYAslHPR- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 139 qHTV--------HVCGLqkdlnslpygdlTEIGERGVN------------------LSGGQRQRISLARAVYANRQLYLL 192
Cdd:COG1124 96 -HTVdrilaeplRIHGL------------PDREERIAElleqvglppsfldryphqLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 193 DDPLSAVDAHVGKHV---FEEcIKKTlKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 256
Cdd:COG1124 163 DEPTSALDVSVQAEIlnlLKD-LREE-RGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
56-249 |
1.96e-22 |
|
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: 96.81 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQ---------AWIF------ 119
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkDLLKLSRRlrkirrkeiQMVFqdpmss 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 -----------------HGNVRENilfgEKYNHQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARA 182
Cdd:cd03257 95 lnprmtigeqiaeplriHGKLSKK----EARKEAVLLLLVGVGLPEEVLNRYPHE-----------LSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 183 VYANRQLYLLDDPLSAVDAHVgkhvfEECIKKTLK------GKTVVLVTHQLQFL-ESCDEVILLEDGEICEKG 249
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSV-----QAQILDLLKklqeelGLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
692-904 |
2.11e-22 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 96.40 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYR--DNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVE-PASGTIIIDEVDICTVGLEDL--- 765
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 766 -RTKLTMIPQD----PVLfvgTVRYNLD-PL------GSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGE 833
Cdd:cd03255 80 rRRHIGFVFQSfnllPDL---TALENVElPLllagvpKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 834 RQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKV 904
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
690-886 |
2.72e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.19 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 690 GEITFKDYRMRYRDNTPLVlDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIIIDEVDictvgledl 765
Cdd:COG4178 361 GALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGKSTL----LRaiagLWPYGSGRIARPAGA--------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 766 rtKLTMIPQDPVLFVGTVR----YNLDPlGSHTDEMLWHVLERTFMRDtimkLPEKLQAEvtENGEN-FSVGERQLLCMA 840
Cdd:COG4178 427 --RVLFLPQRPYLPLGTLReallYPATA-EAFSDAELREALEAVGLGH----LAERLDEE--ADWDQvLSLGEQQRLAFA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568956771 841 RALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR 886
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
357-666 |
3.47e-22 |
|
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: 98.06 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 357 SFLVLCLFFLMMGSSAFSTWWLGIWLDRgsqvvcasqnnktacNVDQTLQDTkhHMYQLVYIASMVS--VLMFGIikGFT 434
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDD---------------PVNGPQEHG--QVYLSVLGALAILqgITVFQY--SMA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 435 FTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVL 514
Cdd:cd18559 62 VSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 515 VVLAgLAVIFLILLRIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFnCAL 594
Cdd:cd18559 142 VGIP-LGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSI-VYL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 595 RWFALRMDILMNIVTFVVALLVTLSFSSISASSkGLSLSYIIQLSGLLQVCVRTGTETQAKFTSAELLREYI 666
Cdd:cd18559 220 RALAVRLWCVGPCIVLFASFFAYVSRHSLAGLV-ALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
59-256 |
4.04e-22 |
|
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: 96.20 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWI---------FHG------- 121
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrrigmlFQGgalfdsl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENILFGEKynhqryQHT----------VHVC----GLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANR 187
Cdd:COG1127 98 TVFENVAFPLR------EHTdlseaeirelVLEKlelvGLPGAADKMP-------SE----LSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 188 QLYLLDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 256
Cdd:COG1127 161 EILLYDEPTAGLDP-ITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
692-919 |
4.35e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.13 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPV-LFVG-TVRYN----LDPLGSHTDEM---LWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARA 842
Cdd:PRK13648 88 VFQNPDnQFVGsIVKYDvafgLENHAVPYDEMhrrVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 843 LLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDS 919
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
58-254 |
5.10e-22 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 95.71 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 58 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQK-----GVVAVNG---------PLAY------VSQQAW 117
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGkdiydldvdVLELrrrvgmVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 118 IFHGNVRENILFGEKynhqryqhtVHVCGLQKDLNSLPYGDLTEIG--------ERGVNLSGGQRQRISLARAVYANRQL 189
Cdd:cd03260 92 PFPGSIYDNVAYGLR---------LHGIKLKEELDERVEEALRKAAlwdevkdrLHALGLSGGQQQRLCLARALANEPEV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 190 YLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKEL 254
Cdd:cd03260 163 LLLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
61-257 |
1.32e-21 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 94.42 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVSQQAWIFHG-NVRE 125
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglpPheraragIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYNHQRyqhtvhvcGLQKDLNSLpYGDLTEIGER----GVNLSGGQRQRISLARAVYANRQLYLLDDP---LSA 198
Cdd:cd03224 95 NLLLGAYARRRA--------KRKARLERV-YELFPRLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 199 VdahVGKHVFeECIKKtLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:cd03224 166 K---IVEEIF-EAIRE-LRdeGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
48-245 |
1.73e-21 |
|
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: 93.00 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 48 VASPEWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ--KGVVAVNGP----------LAYVSQQ 115
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRpldkrsfrkiIGYVPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 116 AwIFHGN--VRENILFGEKYnhqryqhtvhvcglqkdlnslpygdlteigeRGvnLSGGQRQRISLARAVYANRQLYLLD 193
Cdd:cd03213 91 D-ILHPTltVRETLMFAAKL-------------------------------RG--LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 194 DPLSAVDAHVGKHVFeecikKTLK-----GKTVVLVTHQL--QFLESCDEVILLEDGEI 245
Cdd:cd03213 137 EPTSGLDSSSALQVM-----SLLRrladtGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
708-929 |
2.70e-21 |
|
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: 93.94 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEdlRTKLTMIPQDPVLFVG-TVRYN 786
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 787 LDplgshtdemlWHVLERTFMRDTI----MKLPEKLQAE--VTENGENFSVGERQLLCMARALLRNSKIILLDEATASMD 860
Cdd:cd03299 92 IA----------YGLKKRKVDKKEIerkvLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 861 SKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSAF-AMLLAAEV 929
Cdd:cd03299 162 VRTKEKLREELKKIRKEfgVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFvAEFLGFNN 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
61-254 |
3.87e-21 |
|
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: 93.41 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG----------------PLAYVSQQAWIFHG-NV 123
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkarrRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPL 196
Cdd:cd03258 100 FENVALpleiagvPKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 197 SAVDAHVGKHVFE--ECIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 254
Cdd:cd03258 169 SALDPETTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
53-245 |
3.98e-21 |
|
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: 92.70 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P----LAYVSQQAWIF-H 120
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlpPkdrdIAMVFQNYALYpH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 121 GNVRENILFGEKYNH-------QRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLD 193
Cdd:cd03301 87 MTVYDNIAFGLKLRKvpkdeidERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 194 DPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 245
Cdd:cd03301 156 EPLSNLDAKLRVQMRAE-LKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
62-256 |
4.27e-21 |
|
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: 93.17 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLA-----------YVSQQAWIF-HGNVRENILF 129
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHYALFrHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 130 G-------EKYNHQRYQHTVHvcglqkdlNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:cd03296 98 GlrvkprsERPPEAEIRAKVH--------ELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 202 HVGKHvfeecIKKTLK------GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELME 256
Cdd:cd03296 170 KVRKE-----LRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
58-245 |
4.82e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 92.59 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 58 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG---------------PLAYVSQQAWIF-HG 121
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQQFNLFpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENILFGEKYNHQR---------YQHTVHVcGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLL 192
Cdd:cd03262 92 TVLENITLAPIKVKGMskaeaeeraLELLEKV-GLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568956771 193 DDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQF-LESCDEVILLEDGEI 245
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
62-257 |
7.35e-21 |
|
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: 93.48 E-value: 7.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA----------WIF-------HGNV 123
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqDIAAMSRKElrelrrkkisMVFqsfallpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANRQLYLLDDPL 196
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 197 SAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
61-280 |
7.61e-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: 97.28 E-value: 7.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW---------IF---------HG 121
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkDLTKLSRRSLrelrrrvqmVFqdpysslnpRM 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENI-----LFGEKYNHQRYQHTVHV---CGLQKD-LNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLL 192
Cdd:COG1123 360 TVGDIIaeplrLHGLLSRAERRERVAELlerVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLIL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 193 DDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELmeergryaklihnl 268
Cdd:COG1123 429 DEPTSALDVSVQAQIlnlLRD-LQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV-------------- 492
|
250
....*....|..
gi 568956771 269 rglqFKDPEHIY 280
Cdd:COG1123 493 ----FANPQHPY 500
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
56-255 |
2.03e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 91.59 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIF-HG 121
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENI-----LfgEKYNHQRYQHTVhvcglqKDLNSLPYGDLTEIGER-GVNLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:cd03295 91 TVEENIalvpkL--LKWPKEKIRERA------DELLALVGLDPAEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 196 LSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 255
Cdd:cd03295 163 FGALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
64-245 |
2.05e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 94.01 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------------PLAYVSQQAWIF-HGNVRE 125
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargiflpphrrRIGYVFQEARLFpHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYN--HQRYQHTVHVCglqkdlnslpygDLTEIG---ERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAV 199
Cdd:COG4148 97 NLLYGRKRAprAERRISFDEVV------------ELLGIGhllDRRPaTLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568956771 200 DAHVgKHvfeECIK--KTLKGKT---VVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:COG4148 165 DLAR-KA---EILPylERLRDELdipILYVSHSLDEVARlADHVVLLEQGRV 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
55-254 |
2.09e-20 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 90.64 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 55 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAWIFHG- 121
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENI-LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDlTEIGergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:cd03263 91 TVREHLrFYARLKGLPKSEIKEEVELLLRVLGLTDKAN-KRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 201 aHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 254
Cdd:cd03263 166 -PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
708-905 |
2.51e-20 |
|
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: 88.64 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQdpvlfvgtvryn 786
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 787 ldplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDEATASMDSK-TDT 865
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568956771 866 LVQsTIKEaFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVI 905
Cdd:cd03216 121 LFK-VIRR-LRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
694-905 |
2.59e-20 |
|
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: 90.29 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 694 FKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdicTVGLEDLRTKLTMIP 773
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-----GKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 774 QD-------PVL---FVGTVRYN----LDPLGSHTDEMLWHVLERTFMRDtimklpeKLQAEVTEngenFSVGERQLLCM 839
Cdd:cd03235 75 QRrsidrdfPISvrdVVLMGLYGhkglFRRLSKADKAKVDEALERVGLSE-------LADRQIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 840 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMeNGKVI 905
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-266 |
2.73e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 27 RHVFKKQRpeLYSEQSRSDQGVASPEWQSGSP-KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV 105
Cdd:COG1134 8 ENVSKSYR--LYHEPSRSLKELLLRRRRTRREeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 106 NG----PLAYvsqqAWIFHGN--VRENILFG-------EKYNHQRYQHTVhvcglqkdlnslpygDLTEIGE------Rg 166
Cdd:COG1134 86 NGrvsaLLEL----GAGFHPEltGRENIYLNgrllglsRKEIDEKFDEIV---------------EFAELGDfidqpvK- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 167 vNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvgkhvF-EECIKK----TLKGKTVVLVTHQLQFLES-CDEVILL 240
Cdd:COG1134 146 -TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA-----FqKKCLARirelRESGRTVIFVSHSMGAVRRlCDRAIWL 219
|
250 260
....*....|....*....|....*.
gi 568956771 241 EDGEICEKGTHKELMEergRYAKLIH 266
Cdd:COG1134 220 EKGRLVMDGDPEEVIA---AYEALLA 242
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
61-256 |
2.86e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.92 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSL---ISAL--LGQMQLQKGVVAVNGPLA----------YVSQQAWIF-HGNVR 124
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLeeITSGDLIVDGLKVNDPKVderlirqeagMVFQQFYLFpHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFGekynhqryqhTVHVCGLQK-DLNSLPYGDLTEIG--ERG----VNLSGGQRQRISLARAVYANRQLYLLDDPLS 197
Cdd:PRK09493 96 ENVMFG----------PLRVRGASKeEAEKQARELLAKVGlaERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 198 AVDAHVGKHVFEecIKKTL--KGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELME 256
Cdd:PRK09493 166 ALDPELRHEVLK--VMQDLaeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
36-245 |
3.30e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 90.28 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 36 ELYSEQSRSDQGVASPEWQ-SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGplayvsQ 114
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 115 QAWI------FHGN--VRENILFG-------EKYNHQRYQHTVHVCGLQKDLNsLPYGdlteigergvNLSGGQRQRISL 179
Cdd:cd03220 85 VSSLlglgggFNPEltGRENIYLNgrllglsRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 180 ARAVYANRQLYLLDDPLSAVDAHvgkhvF-EECIKK----TLKGKTVVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAA-----FqEKCQRRlrelLKQGKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
56-256 |
4.37e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 94.97 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLG---QMQLQKGVVAVNGP-------------LAYVSQQAW-- 117
Cdd:COG1123 16 GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMtq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 118 IFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLY 190
Cdd:COG1123 96 LNPVTVGDQIAEAlenlglsRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 191 LLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELME 256
Cdd:COG1123 165 IADEPTTALDVTTQAEILDL-LRELQRerGTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
692-913 |
4.67e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.33 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDN-TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLT 770
Cdd:PRK13650 5 IEVKNLTFKYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 771 MIPQDP-VLFVGT-----VRYNLDPLGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMAR 841
Cdd:PRK13650 85 MVFQNPdNQFVGAtveddVAFGLENKGIPHEEMKERVneaLELVGMQDFKEREPARL-----------SGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 842 ALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVL 913
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
709-902 |
6.29e-20 |
|
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: 89.31 E-value: 6.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTK----LTMIPQDPVLFVGTVR 784
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 YNLdPLGSHTDEMLWH-VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK- 862
Cdd:cd03290 97 ENI-TFGSPFNKQRYKaVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHl 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568956771 863 TDTLVQSTIKEAFK--SCTVLTIAHRLNTVLNCDLVLVMENG 902
Cdd:cd03290 176 SDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
709-911 |
7.41e-20 |
|
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: 94.37 E-value: 7.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVG---LEDLRTKLTMIPQDPvlfvgtvrY 785
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--------F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 786 N-LDP-----------LGSH--------TDEMLWHVLERTFM-RDTIMKLP-EklqaevtengenFSVGERQLLCMARAL 843
Cdd:COG4172 373 GsLSPrmtvgqiiaegLRVHgpglsaaeRRARVAEALEEVGLdPAARHRYPhE------------FSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 844 LRNSKIILLDEATASMD-SktdtlVQSTIKEAFKSC------TVLTIAHRLNTV--LnCDLVLVMENGKVIE-------F 907
Cdd:COG4172 441 ILEPKLLVLDEPTSALDvS-----VQAQILDLLRDLqrehglAYLFISHDLAVVraL-AHRVMVMKDGKVVEqgpteqvF 514
|
....
gi 568956771 908 DKPE 911
Cdd:COG4172 515 DAPQ 518
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
56-258 |
1.15e-19 |
|
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: 89.16 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL----------AYVSQQAWIFHG---- 121
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrQLRRQIGMIFQQfnli 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 ---NVRENILFGekynhqR--YQHTVHVCglqkdLNSLPYGD-------LTEIG------ERGVNLSGGQRQRISLARAV 183
Cdd:cd03256 91 erlSVLENVLSG------RlgRRSTWRSL-----FGLFPKEEkqralaaLERVGlldkayQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 184 YANRQLYLLDDPLSAVD---AHVGKHVFEEcIKKTlKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:cd03256 160 MQQPKLILADEPVASLDpasSRQVMDLLKR-INRE-EGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
692-906 |
1.21e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.57 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLRTK 768
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 769 LTMIPQD-PVLFVGTVRYNLD-PL---GSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMA 840
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENVAlPLrvtGKSRKEIRRRVrevLDLVGLSDKAKALPHEL-----------SGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 841 RALLRNSKIILLDEATASMDSKTdtlvqST-IKEAFKS-----CTVLtIA-HRLNTVLNCDL-VLVMENGKVIE 906
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPET-----SWeIMELLEEinrrgTTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
61-254 |
1.21e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P----LAYVSQQAWIF-HGNVRENIL 128
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdlpPkdrnIAMVFQSYALYpHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FGEKYN-------HQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:COG3839 98 FPLKLRkvpkaeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 202 HVgKHVFEECIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 254
Cdd:COG3839 167 KL-RVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
701-915 |
1.41e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.11 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 701 YRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC--TVGLEDLRTKLTMIPQD 775
Cdd:PRK13637 12 YMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 776 P--VLFVGTVR----YNLDPLGSHTDEMLWHVLERtfmrdtiMKLPeKLQAEVTENGENF--SVGERQLLCMARALLRNS 847
Cdd:PRK13637 92 PeyQLFEETIEkdiaFGPINLGLSEEEIENRVKRA-------MNIV-GLDYEDYKDKSPFelSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 848 KIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAE 915
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPrEVFKE 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
692-905 |
1.88e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.38 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNT----PLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG-LEDLR 766
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 TKLTMIPQDP-VLFVGT-----VRYNLDPLGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLL 837
Cdd:PRK13633 85 NKAGMVFQNPdNQIVATiveedVAFGPENLGIPPEEIRERVdesLKKVGMYEYRRHAPHLL-----------SGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 838 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLNCDLVLVMENGKVI 905
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
692-916 |
2.19e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGLEDLRTKL 769
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDP--VLFVGTV----RYNLDPLGSHTDEM---LWHVLERTFMrdtimklpEKLQAEVTengENFSVGERQLLCMA 840
Cdd:PRK13636 85 GMVFQDPdnQLFSASVyqdvSFGAVNLKLPEDEVrkrVDNALKRTGI--------EHLKDKPT---HCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 841 RALLRNSKIILLDEATASMD----SKTDTLVQSTIKEAfkSCTVLTIAHRLNTV-LNCDLVLVMENGKVI-EFDKPEVLA 914
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVpLYCDNVFVMKEGRVIlQGNPKEVFA 231
|
..
gi 568956771 915 EK 916
Cdd:PRK13636 232 EK 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
59-245 |
3.76e-19 |
|
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: 85.95 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG---------------- 121
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkPVTRRSPRDAIRAGiayvpedrkreglvld 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 -NVRENILfgekynhqryqhtvhvcglqkdLNSLpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:cd03215 93 lSVAENIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568956771 201 ahVG--KHVFEECIKKTLKGKTVVLVTHQLQ-FLESCDEVILLEDGEI 245
Cdd:cd03215 137 --VGakAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
708-905 |
5.04e-19 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 87.11 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIIDEVDICTVGlEDLRTKLTMIP--QDPVLFVG 781
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 782 -TVRYNLD----PLGSHTDEMLWHVLERTFMRDTIMKLPE--KLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDE 854
Cdd:cd03219 90 lTVLENVMvaaqARTGSGLLLARARREEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 855 ATASMDSK-TDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 905
Cdd:cd03219 170 PAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
692-886 |
5.89e-19 |
|
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: 84.90 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDgLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdictvgledlRTKLTM 771
Cdd:cd03223 1 IELENLSLATPDGRVLLKD-LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVGTVRynldplgshtdEML---WhvlertfmrdtimklpeklqaevtenGENFSVGERQLLCMARALLRNSK 848
Cdd:cd03223 69 LPQRPYLPLGTLR-----------EQLiypW--------------------------DDVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 568956771 849 IILLDEATASMDSKTDTLVQSTIKEAFksCTVLTIAHR 886
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
61-245 |
6.60e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 84.79 E-value: 6.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHGnVRenilfgekynhqryq 139
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkEVSFASPRDARRAG-IA--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 140 hTVHvcglQkdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK-- 217
Cdd:cd03216 79 -MVY----Q--------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRaq 131
|
170 180
....*....|....*....|....*....
gi 568956771 218 GKTVVLVTHQLQ-FLESCDEVILLEDGEI 245
Cdd:cd03216 132 GVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
64-258 |
7.47e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 86.73 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFG- 130
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppaerPVSMLFQENNLFpHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 131 ---EKYN---HQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD---- 200
Cdd:COG3840 97 rpgLKLTaeqRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 201 ---AHVGKHVFEEcikktlKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:COG3840 166 qemLDLVDELCRE------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
692-906 |
8.77e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.70 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLV--LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRT-- 767
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 768 -KLTMIPQdpvlfvgtvRYNLdpLGSHTdemlwhVLERTFMRDTIMKLP-EKLQAEVTENGE-------------NFSVG 832
Cdd:PRK11153 82 rQIGMIFQ---------HFNL--LSSRT------VFDNVALPLELAGTPkAEIKARVTELLElvglsdkadrypaQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 833 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
701-931 |
9.30e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 9.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 701 YRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG-LEDLRTKLTMIPQDP-VL 778
Cdd:PRK13644 11 YPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 779 FVG-TVRYNLdplgSHTDEMLwhVLERTFMRDTI-MKLPE-KLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEA 855
Cdd:PRK13644 90 FVGrTVEEDL----AFGPENL--CLPPIEIRKRVdRALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 856 TASMDSKTDTLVQSTIKEAF-KSCTVLTIAHRLNTVLNCDLVLVMENGKViefdkpeVLAEKPDSAFAMLLAAEVGL 931
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKI-------VLEGEPENVLSDVSLQTLGL 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
692-921 |
9.32e-19 |
|
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: 86.59 E-value: 9.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVlDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFvgtvrynldPlgsHtdemlWHVLERTFMRDTIMKLP-EKLQAEVTE-------NGENF--------SVGERQ 835
Cdd:cd03295 80 VIQQIGLF---------P---H-----MTVEENIALVPKLLKWPkEKIRERADEllalvglDPAEFadryphelSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 836 LLCMARALLRNSKIILLDEATASMDSKTDTLVQS---TIKEAFKScTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 911
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEefkRLQQELGK-TIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPD 221
|
250
....*....|
gi 568956771 912 VLAEKPDSAF 921
Cdd:cd03295 222 EILRSPANDF 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
61-256 |
9.44e-19 |
|
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: 86.24 E-value: 9.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P----LAYVSQQAWIF-HGNVRENIL 128
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlpPekrdISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FGEKYN-------HQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:cd03299 94 YGLKKRkvdkkeiERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 202 HVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 256
Cdd:cd03299 163 RTKEKLREE-LKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
61-247 |
1.02e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.87 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA---------------YVSQQAW-IFHGNV 123
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqDLSrlkrreipylrrrigVVFQDFRlLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENILFG---EKYNHQRYQHTVH-----VcGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVyANR-QLYLLDD 194
Cdd:COG2884 97 YENVALPlrvTGKSRKEIRRRVRevldlV-GLSDKAKALPH-----------ELSGGEQQRVAIARAL-VNRpELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 195 PLSAVDAHVGK---HVFEEcIKKTlkGKTVVLVTHQLQFLESCDE-VILLEDGEICE 247
Cdd:COG2884 164 PTGNLDPETSWeimELLEE-INRR--GTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
692-905 |
1.10e-18 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 85.88 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDN--TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEdLRTKL 769
Cdd:cd03266 2 ITADALTKRFRDVkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDPVLFVG-TVRYNLDPLGShtdemlWHVLERTFMRDTIMKLPEKLQAEVTEN--GENFSVGERQLLCMARALLRN 846
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAG------LYGLKGDELTARLEELADRLGMEELLDrrVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 847 SKIILLDEATASMdsktDTLVQSTIKEAFKS-----CTVLTIAHRLNTVLN-CDLVLVMENGKVI 905
Cdd:cd03266 155 PPVLLLDEPTTGL----DVMATRALREFIRQlralgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
61-257 |
1.19e-18 |
|
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: 86.14 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENIL 128
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnlpphkrPVNTVFQNYALFpHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FG---EKYNHQRYQHTVHvcglqkdlNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:cd03300 95 FGlrlKKLPKAEIKERVA--------EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 205 KHVFEEC--IKKTLkGKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:cd03300 167 KDMQLELkrLQKEL-GITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
413-615 |
1.29e-18 |
|
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: 87.22 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 413 YQLVYIASMVSVLMFGIIKGFTFTNTTLMASSSLH------NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLP 486
Cdd:cd07346 35 LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRvvfdlrRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 487 FHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQEL-----KQVENISrspwfSHITSSIQGLG 561
Cdd:cd07346 115 SGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKAsrevrESLAELS-----AFLQESLSGIR 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 562 VIHAYDKKDDCISKFKTLNDENSSHLLYfncALRWFAL---RMDILMNIVTFVVALL 615
Cdd:cd07346 190 VVKAFAAEEREIERFREANRDLRDANLR---AARLSALfspLIGLLTALGTALVLLY 243
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
60-265 |
1.91e-18 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 86.45 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 60 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLgQMQLQKGVVAVNG------PL-------AYVSQQAWIFHGNVREN 126
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvPLqkwrkafGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFGEKYNHQRYQHTVHVCGLQKDLNSLPyGDLT-EIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhvgk 205
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEEVGLKSVIEQFP-GQLDfVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP---- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 206 hVFEECIKKTLK----GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 265
Cdd:cd03289 172 -ITYQVIRKTLKqafaDCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
61-260 |
2.33e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 85.43 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL--------------AYVSQQAWIF-HGNVR 124
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGeDLtdskkdinklrrkvGMVFQQFNLFpHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFGekynhqryqhTVHVCGLQKDlnslpygDLTEIGER-----GV---------NLSGGQRQRISLARAVYANRQLY 190
Cdd:COG1126 96 ENVTLA----------PIKVKKMSKA-------EAEERAMEllervGLadkadaypaQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 191 LLDDPLSAVDAhvgkhvfeECIKKTLK--------GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELME----E 257
Cdd:COG1126 159 LFDEPTSALDP--------ELVGEVLDvmrdlakeGMTMVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFFEnpqhE 230
|
...
gi 568956771 258 RGR 260
Cdd:COG1126 231 RTR 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
62-242 |
2.38e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 84.46 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ---KGVVAVNG------P-----LAYVSQQAWIF-HGNVREN 126
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGrrltalPaeqrrIGILFQDDLLFpHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFG--EKYNHQRYQHTVhvcglQKDLNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH- 202
Cdd:COG4136 97 LAFAlpPTIGRAQRRARV-----EQALEEA---GLAGFADRDPAtLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAl 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568956771 203 ---VGKHVFEECIKKTLkgkTVVLVTHQLQFLESCDEVILLED 242
Cdd:COG4136 169 raqFREFVFEQIRQRGI---PALLVTHDEEDAPAAGRVLDLGN 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
61-240 |
2.50e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--PLAYVSQQ---AWIFHGNVRENILFGekynh 135
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMG----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 136 qRYQHTvhvcGLQKDLN---------SLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGK 205
Cdd:NF040873 82 -RWARR----GLWRRLTrddraavddALERVGLADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 568956771 206 HVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILL 240
Cdd:NF040873 157 RIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
692-917 |
2.68e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIIIDEVDICTVGLEDLRTK 768
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 769 LTMIPQDP-VLFVGT-----VRYNLDPLGSHTDEML---WHVLERTFMRDTIMKLPeklqaevtengENFSVGERQLLCM 839
Cdd:PRK13640 86 VGIVFQNPdNQFVGAtvgddVAFGLENRAVPRPEMIkivRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 840 ARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKP 917
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
692-904 |
2.87e-18 |
|
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: 84.38 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICtvGLED-----LR 766
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 TKLTMIPQDPVLFVG-TVRYNL-------DPLGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLC 838
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVafalevtGVPPREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 839 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNC--DLVLVMENGKV 904
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
415-616 |
3.16e-18 |
|
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: 86.29 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 415 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhAE---- 490
Cdd:cd18544 45 LLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL-------NElfts 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 491 ---NFLQQFFMVVFILVIM-------AAVFPVVLVVLAGLAVIFLILLRIFHRGVQElkQVENISrspwfSHITSSIQGL 560
Cdd:cd18544 118 glvTLIGDLLLLIGILIAMfllnwrlALISLLVLPLLLLATYLFRKKSRKAYREVRE--KLSRLN-----AFLQESISGM 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 561 GVIHAYDKKDDCISKFKTLNDEnssHLLYFNCALRWFALRMDILMNIVTFVVALLV 616
Cdd:cd18544 191 SVIQLFNREKREFEEFDEINQE---YRKANLKSIKLFALFRPLVELLSSLALALVL 243
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
65-255 |
3.27e-18 |
|
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: 87.47 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 65 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------------PLAYVSQQAWIF-HGNVREN 126
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFGEK-----YNHQRYQHTVHVCGLQKDLnslpygdlteigERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:TIGR02142 96 LRYGMKrarpsERRISFERVIELLGIGHLL------------GRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 201 AHVGKHV--FEECIKKTLkGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 255
Cdd:TIGR02142 164 DPRKYEIlpYLERLHAEF-GIPILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
58-245 |
3.44e-18 |
|
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: 84.25 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 58 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIF----HG-----NVRENI 127
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkPLDIAARNRIGYlpeeRGlypkmKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 L-FGE--KYNHQRYQHTVhvcglQKDLNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhV 203
Cdd:cd03269 92 VyLAQlkGLKKEEARRRI-----DEWLERL---ELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-V 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 204 GKHVFEECIKKTL-KGKTVVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:cd03269 163 NVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
59-265 |
4.57e-18 |
|
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: 84.96 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRE 125
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgK 205
Cdd:cd03288 114 NLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-E 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 206 HVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM-EERGRYAKLI 265
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
59-257 |
4.98e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVREN 126
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvpaenrHVNTVFQSYALFpHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFG---EKYNHQRYQHTVhvcglqkdLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH 202
Cdd:PRK09452 107 VAFGlrmQKTPAAEITPRV--------MEALRMVQLEEFAQRKPhQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 203 VGKHVFEEcIK---KTLkGKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:PRK09452 179 LRKQMQNE-LKalqRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
50-257 |
8.09e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 50 SPEWQSGSPksVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------PLAYVSQQAWIFHGN 122
Cdd:PRK13644 8 SYSYPDGTP--ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsKLQGIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 ---------VRENILFGEKynhqryqhtvHVCGLQKDLNSLPYGDLTEIG------ERGVNLSGGQRQRISLARAVYANR 187
Cdd:PRK13644 86 petqfvgrtVEEDLAFGPE----------NLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 188 QLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
708-911 |
1.04e-17 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 83.93 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIIDEVDIctVGLE-DLRTKLTM-----IPQdpv 777
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDI--TGLPpHRIARLGIartfqNPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 778 LFVG-TVRYNLD-PLGSHTDEMLWHVLERTF--------MRDTIMKLPE--KLQAEVTENGENFSVGERQLLCMARALLR 845
Cdd:COG0411 90 LFPElTVLENVLvAAHARLGRGLLAALLRLPrarreereARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 846 NSKIILLDEATASMDSK-TDTLVQsTIKE--AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 911
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEeTEELAE-LIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
59-255 |
1.10e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 83.63 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWI-FHGNVR 124
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrPLaawspwelarrrAVLPQHSSLaFPFTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFGeKYNHQR-YQHTVHVCG--LQKdlnslpyGDLTEIGERGVN-LSGGQRQRISLARA-------VYANRQLYLLD 193
Cdd:COG4559 94 EVVALG-RAPHGSsAAQDRQIVReaLAL-------VGLAHLAGRSYQtLSGGEQQRVQLARVlaqlwepVDGGPRWLFLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 194 DPLSAVD-AHVgKHVFEecIKKTL--KGKTVVLVTHQL----QFlesCDEVILLEDGEICEKGTHKELM 255
Cdd:COG4559 166 EPTSALDlAHQ-HAVLR--LARQLarRGGGVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
708-918 |
1.86e-17 |
|
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: 82.72 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL-RTKLTMIPQDPVLFVG-TVRY 785
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 786 NLDpLGSHT-------DEMLWHVLERtFMRdtimkLPEKLQAEvtenGENFSVGERQLLCMARALLRNSKIILLDEATAS 858
Cdd:COG0410 98 NLL-LGAYArrdraevRADLERVYEL-FPR-----LKERRRQR----AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 859 mdsktdtLVQSTIKEafksctVLTIAHRLN----TVL----N-------CDLVLVMENGKVIEFDKPEVLAEKPD 918
Cdd:COG0410 167 -------LAPLIVEE------IFEIIRRLNregvTILlveqNarfaleiADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
61-227 |
2.87e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP----LAYVSQQAWIFHGN-------VRENILF 129
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYLGHRNamkpaltVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 130 GEKYNHQRyQHTVHVC----GLQkDLNSLPYGdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGK 205
Cdd:PRK13539 97 WAAFLGGE-ELDIAAAleavGLA-PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AV 163
|
170 180
....*....|....*....|...
gi 568956771 206 HVFEECIKKTLK-GKTVVLVTHQ 227
Cdd:PRK13539 164 ALFAELIRAHLAqGGIVIAATHI 186
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
692-904 |
3.30e-17 |
|
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: 81.42 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGLEDLRTKL 769
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDpvlfvgtvrYNLDPlgsHTDemlwhVLErtfmrdTIMKLPEKLQ----AEVTENGENF---------------- 829
Cdd:cd03262 79 GMVFQQ---------FNLFP---HLT-----VLE------NITLAPIKVKgmskAEAEERALELlekvgladkadaypaq 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 830 -SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKV 904
Cdd:cd03262 136 lSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
692-906 |
3.52e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.97 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLV--LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLR 766
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 TKLTMIPQDpvlfvgtvrYNLdpLGSHTdemlwhV-------LErtfmrdtIMKLP-EKLQAEVTE---------NGENF 829
Cdd:COG1135 82 RKIGMIFQH---------FNL--LSSRT------VaenvalpLE-------IAGVPkAEIRKRVAEllelvglsdKADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 830 ----SVGERQLLCMARALLRNSKIILLDEATASMDSKT-----DTLVQstIKEAFKScTVLTIAHRLNTVLN-CDLVLVM 899
Cdd:COG1135 138 psqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsilDLLKD--INRELGL-TIVLITHEMDVVRRiCDRVAVL 214
|
....*..
gi 568956771 900 ENGKVIE 906
Cdd:COG1135 215 ENGRIVE 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
59-247 |
3.81e-17 |
|
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: 82.55 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYV---SQQAW------IFHG-----NV 123
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqDLYQLdrkQRRAFrrdvqlVFQDspsavNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENI--LFGEKYNH----------QRYQHTVHVCGLQ-KDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLY 190
Cdd:TIGR02769 104 RMTVrqIIGEPLRHltsldeseqkARIAELLDMVGLRsEDADKLP-----------RQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 191 LLDDPLSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICE 247
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKlQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
55-240 |
5.32e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.83 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 55 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL-------AYVSQQ----AWIfhgN 122
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvPVtgpgadrGVVFQKdallPWL---N 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILFGEKYN-------HQRYQHTVHVCGLQkdlnslpygdltEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDD 194
Cdd:COG4525 93 VLDNVAFGLRLRgvpkaerRARAEELLALVGLA------------DFARRRIwQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568956771 195 PLSAVDAHVGKHVFE---ECIKKTlkGKTVVLVTHQLQ---FLEScdEVILL 240
Cdd:COG4525 161 PFGALDALTREQMQElllDVWQRT--GKGVFLITHSVEealFLAT--RLVVM 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
61-273 |
6.26e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.59 E-value: 6.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-----------LAYVSQQAWIF-HGNVRENIL 128
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHYALFrHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FGEKYNHQRYQHTVHVCGlQKDLNSLPYGDLTEIGER-GVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGK-- 205
Cdd:PRK10851 97 FGLTVLPRRERPNAAAIK-AKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKel 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 206 -----HVFEEcikktLKgKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL---------MEERGRYAKLIHNLRG 270
Cdd:PRK10851 176 rrwlrQLHEE-----LK-FTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepatrfvLEFMGEVNRLQGTIRG 249
|
...
gi 568956771 271 LQF 273
Cdd:PRK10851 250 GQF 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
59-265 |
8.54e-17 |
|
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: 85.73 E-value: 8.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLgQMQLQKGVVAVNG-------------PLAYVSQQAWIFHGNVRE 125
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIFSGTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGK 205
Cdd:TIGR01271 1311 NLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTL 1389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 206 HVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 265
Cdd:TIGR01271 1390 QIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
708-905 |
1.19e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.13 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIIIDEVDIctvGLEDLRTKLTMIPQDPVLFVG-TVR 784
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 ynldplgshtdEMLWHVLErtfMRdtimklpeklqaevtengeNFSVGERQLLCMARALLRNSKIILLDEATASMDSKTD 864
Cdd:cd03213 101 -----------ETLMFAAK---LR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 865 TLVQSTIKE-AFKSCTVLTIAHRLNTVL--NCDLVLVMENGKVI 905
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
692-911 |
1.47e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:PRK09536 4 IDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVL-FVGTVRY-----------NLDPLGShTDEMlwhVLERTFMRDTIMKLPEKlqaEVTEngenFSVGERQLLCM 839
Cdd:PRK09536 82 VPQDTSLsFEFDVRQvvemgrtphrsRFDTWTE-TDRA---AVERAMERTGVAQFADR---PVTS----LSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 840 ARALLRNSKIILLDEATASMD----SKTDTLVQSTIKEAFkscTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 911
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDinhqVRTLELVRRLVDDGK---TAVAAIHDLDLAARyCDELVLLADGRVRAAGPPA 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
691-931 |
1.77e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.83 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 691 EITFKDYRMRYRDNTPLVLDGL---NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIcTVG-----L 762
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFERRALydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI-TAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 763 EDLRTKLTMIPQDP--VLFVGTVRYNL--DPLG---------SHTDEMLWHVlertfmrdtimKLPEKLqaeVTENGENF 829
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEKDIcfGPMNfgvseedakQKAREMIELV-----------GLPEEL---LARSPFEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 830 SVGERQLLCMARALLRNSKIILLDEATASMDSKTdtlvQSTIKEAF------KSCTVLTIAHRLNTVLN-CDLVLVMENG 902
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568956771 903 KVIE-------FDKPEVLAEK----PDSA-FAMLLAAEVGL 931
Cdd:PRK13634 223 TVFLqgtpreiFADPDELEAIgldlPETVkFKRALEEKFGI 263
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
61-254 |
1.78e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.44 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV----NGPLAYVSQQAW------------------- 117
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITnpyskkiknfkelrrrvsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 118 --------IFHGNVRENILFG------EKYN-HQRYQHTVHVCGLQKD-LNSLPYGdlteigergvnLSGGQRQRISLAR 181
Cdd:PRK13631 121 vfqfpeyqLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 182 AVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKEL 254
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKAnNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
708-916 |
1.89e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.06 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVG-TVR-- 784
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 --YNLDPLGSH------TDEMLwhvLERTFMRDTIMKLPEKLqaeVTEngenFSVGERQLLCMARALLRNSKIILLDEAT 856
Cdd:PRK11231 97 vaYGRSPWLSLwgrlsaEDNAR---VNQAMEQTRINHLADRR---LTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 857 ASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAEK 916
Cdd:PRK11231 167 TYLDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPeEVMTPG 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
708-906 |
2.54e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLRTKLTMIPQDPVLFVG--- 781
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSISAVNprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 782 TVRY----------NLDPLG--SHTDEMLWHVlertFMRDTIM-KLPEKLqaevtengenfSVGERQLLCMARALLRNSK 848
Cdd:PRK10419 107 TVREiireplrhllSLDKAErlARASEMLRAV----DLDDSVLdKRPPQL-----------SGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 849 IILLDEATASMDSKTDTLVQSTIKE-------AFksctvLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKlqqqfgtAC-----LFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
415-582 |
2.85e-16 |
|
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: 80.53 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 415 LVYIASMVsvlmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvrlpfhaeNFLQ 494
Cdd:cd18547 53 GLYLLSAL----FSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNIS--------QALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 495 Q--------FFMVVFILVIMAAV-FPVVLVVLAGLAVIFLILLRIFHRgVQEL--KQVENISRspWFSHITSSIQGLGVI 563
Cdd:cd18547 121 QsltqlissILTIVGTLIMMLYIsPLLTLIVLVTVPLSLLVTKFIAKR-SQKYfrKQQKALGE--LNGYIEEMISGQKVV 197
|
170
....*....|....*....
gi 568956771 564 HAYDKKDDCISKFKTLNDE 582
Cdd:cd18547 198 KAFNREEEAIEEFDEINEE 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
708-906 |
2.96e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVgLEDLRTKLTMIPQDPVLFVG-TVR 784
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRFRSP-RDAQAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 YNLdplgshtdeML------WHVLERTFMRDTIMKLPEKLQAEV--TENGENFSVGERQLLCMARALLRNSKIILLDEAT 856
Cdd:COG1129 98 ENI---------FLgreprrGGLIDWRAMRRRARELLARLGLDIdpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568956771 857 ASMDSK-TDTLVQsTIKEaFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:COG1129 169 ASLTEReVERLFR-IIRR-LKAqgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
59-256 |
4.46e-16 |
|
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: 78.35 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------P--------LAYVSQQAWIFHG-NV 123
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklPmhkrarlgIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENIL-------FGEKYNHQRYQHTVHVCGLQKDLNSLpygdlteigerGVNLSGGQRQRISLARAVYANRQLYLLDDPL 196
Cdd:cd03218 93 EENILavleirgLSKKEREEKLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 197 SAVDAhvgKHVFE-ECIKKTLKGKTV-VLVT-HQL-QFLESCDEVILLEDGEICEKGTHKELME 256
Cdd:cd03218 162 AGVDP---IAVQDiQKIIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
77-257 |
4.68e-16 |
|
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: 80.23 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 77 ICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFGEKYNHQ-RYQHTVH 143
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGedvtnvpphlrHINMVFQSYALFpHMTVEENVAFGLKMRKVpRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 144 VcglqkdLNSLPYGDLTEIGERG-VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECikKTLK---GK 219
Cdd:TIGR01187 81 V------LEALRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL--KTIQeqlGI 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 568956771 220 TVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:TIGR01187 153 TFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
57-249 |
5.26e-16 |
|
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: 77.79 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 57 SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAyVSQQAWIFHGN-------- 122
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkePAE-ARRRLGFVSDStglydrlt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENIL-FGEKYNHQRYQHTVHVCGLQKDLNSLPYGDlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:cd03266 95 ARENLEyFAGLYGLKGDELTARLEELADRLGMEELLD-----RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568956771 202 HVGKHVFEecIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 249
Cdd:cd03266 170 MATRALRE--FIRQLRalGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
53-245 |
5.60e-16 |
|
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: 78.24 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA----------WIF-- 119
Cdd:COG4181 19 GTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqDLFALDEDArarlrarhvgFVFqs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 -----HGNVRENI-----LFGEKYNHQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQL 189
Cdd:COG4181 99 fqllpTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 190 YLLDDPLSAVDAHVGKHV----FEecIKKTlKGKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:COG4181 168 LFADEPTGNLDAATGEQIidllFE--LNRE-RGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
702-873 |
6.11e-16 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 77.52 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 702 RDNTPLvLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTMIPQDPVLFVG 781
Cdd:COG4133 12 RGERLL-FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 782 -TVRYNLDPL-----GSHTDEMLWHVLERtfmrdtiMKLPEKLQAEVtengENFSVGERQLLCMARALLRNSKIILLDEA 855
Cdd:COG4133 90 lTVRENLRFWaalygLRADREAIDEALEA-------VGLAGLADLPV----RQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170
....*....|....*...
gi 568956771 856 TASMDSKTDTLVQSTIKE 873
Cdd:COG4133 159 FTALDAAGVALLAELIAA 176
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
59-257 |
6.53e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.59 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------PLAYVSQQawifhgN--- 122
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQE------Nhin 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 ----VRENILFGekynhqRYQHT---------VHVcglqkDlNSLPYGDLTEIGERGVN-LSGGQRQRISLArAVYANRQ 188
Cdd:COG4604 88 srltVRELVAFG------RFPYSkgrltaedrEII-----D-EAIAYLDLEDLADRYLDeLSGGQRQRAFIA-MVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 189 LY-LLDDPLSAVDAhvgKHVFEecIKKTLK------GKTVVLVTHQLQFlESC--DEVILLEDGEICEKGTHKELMEE 257
Cdd:COG4604 155 DYvLLDEPLNNLDM---KHSVQ--MMKLLRrladelGKTVVIVLHDINF-ASCyaDHIVAMKDGRVVAQGTPEEIITP 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
700-907 |
6.77e-16 |
|
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: 77.62 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNtpLVLDGLNLNIQSGQTvGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIcTVGLEDLRTKLTMIPQDPVLF 779
Cdd:cd03264 9 RYGKK--RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 780 VG-TVRYNLDPLG-------SHTDEMLWHVLERTFMRDtimKLPEKLQAevtengenFSVGERQLLCMARALLRNSKIIL 851
Cdd:cd03264 85 PNfTVREFLDYIAwlkgipsKEVKARVDEVLELVNLGD---RAKKKIGS--------LSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 852 LDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTV-LNCDLVLVMENGKVIEF 907
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
59-243 |
8.51e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.20 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGV-----VAVNGPLA---YVSQQ----AWIfhgNVREN 126
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgKPVEGPGAergVVFQNegllPWR---NVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFGEKY----NHQRyqhtvhvcgLQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:PRK11248 91 VAFGLQLagveKMQR---------LEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568956771 202 HVGKHVFEECIK---KTlkGKTVVLVTHQLQ---FLEScdEVILLEDG 243
Cdd:PRK11248 162 FTREQMQTLLLKlwqET--GKQVLLITHDIEeavFMAT--ELVLLSPG 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
692-906 |
9.11e-16 |
|
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: 77.13 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTP--LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGledlrTKL 769
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDPVLFvgtvrynldPlgshtdemlWhvleRTfMRDTIMkLPEKLQ----AEVTENGENF---------------- 829
Cdd:cd03293 76 GYVFQQDALL---------P---------W----LT-VLDNVA-LGLELQgvpkAEARERAEELlelvglsgfenayphq 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 830 -SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLN-TVLNCDLVLVMEN--GK 903
Cdd:cd03293 132 lSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGR 211
|
...
gi 568956771 904 VIE 906
Cdd:cd03293 212 IVA 214
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
449-854 |
9.73e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 81.38 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 449 RVFNKIVRSPMSFFDTTPTGRLMNRFSKDMD---ELDVRLPFhaenFLQQFFMVVFILVIMA----AVFPVVLVVLAGLA 521
Cdd:COG4615 86 RLSRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE----LLQSVALVLGCLAYLAwlspPLFLLTLVLLGLGV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 522 VIFLILLRIFHRGVQELKQVENIsrspWFSHITSSIQG---LGvIHAyDKKDD--------CISKFKtlnDENSSHLLYF 590
Cdd:COG4615 162 AGYRLLVRRARRHLRRAREAEDR----LFKHFRALLEGfkeLK-LNR-RRRRAffdedlqpTAERYR---DLRIRADTIF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 591 NCALRWFALRMDILMNIVTFVVALLVTLSFSSISASSkgLSLSYIIQ-LSGLL---------QVCVRTGTETQAKFTSAE 660
Cdd:COG4615 233 ALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFV--LVLLFLRGpLSQLVgalptlsraNVALRKIEELELALAAAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 661 llreyiltcvpEHTHPFKVGTCPKDWpsrGEITFKDYRMRYR---DNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGM 737
Cdd:COG4615 311 -----------PAAADAAAPPAPADF---QTLELRGVTYRYPgedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 738 ALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFvgtvRYNLDPLGSHTDEMLWHVLERtfmrdtiMKLPEK 817
Cdd:COG4615 377 LLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLER-------LELDHK 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 568956771 818 LQAevtENGE----NFSVGERQLLCMARALLRNSKIILLDE 854
Cdd:COG4615 446 VSV---EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
59-258 |
1.25e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWIFHG-NVR 124
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFGEK-YNH------QRYQHTVHVcGLQKDlnslpygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPL 196
Cdd:PRK11231 95 ELVAYGRSpWLSlwgrlsAEDNARVNQ-AMEQT-------RINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 197 SAVDAHvgkHVFEecIKKTL-----KGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:PRK11231 167 TYLDIN---HQVE--LMRLMrelntQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
61-255 |
1.32e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP--------------------------LAYVSQ 114
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgqlkvadknqlrllrtrLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 115 QAWIF-HGNVRENILfgekynhqryQHTVHVCGLQKDL---NSLPYGDLTEIGERG-----VNLSGGQRQRISLARAVYA 185
Cdd:PRK10619 100 HFNLWsHMTVLENVM----------EAPIQVLGLSKQEareRAVKYLAKVGIDERAqgkypVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 186 NRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 255
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLF 240
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
61-256 |
1.36e-15 |
|
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: 77.33 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVSQQAWIFHG-NVRE 125
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpPhriarlgIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGekynhqryqhtvhvCGLQKDLNSLPyGDLTEI-------GER----GVNLSGGQRQRISLARAVYANRQLYLLDD 194
Cdd:COG0410 98 NLLLG--------------AYARRDRAEVR-ADLERVyelfprlKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 195 P---LSAVdahVGKHVFeECIKKtLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELME 256
Cdd:COG0410 163 PslgLAPL---IVEEIF-EIIRR-LNreGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
709-915 |
1.43e-15 |
|
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: 80.62 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII----DEVDICTVGLeDLRTKLT----MIPQDPVLFv 780
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigILHQEYDLY- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 781 gTVRYNLDPLgshTDEMLWHVLERTFMRDTIMKL-----PEKLQAEVTEN-GENFSVGERQLLCMARALLRNSKIILLDE 854
Cdd:TIGR03269 378 -PHRTVLDNL---TEAIGLELPDELARMKAVITLkmvgfDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 855 ATASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAE 915
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPeEIVEE 518
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
53-241 |
1.57e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.00 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGspKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP----------LAYVSQQA---WIF 119
Cdd:PRK15056 16 WRNG--HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 HGNVRENILFGeKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSA 198
Cdd:PRK15056 94 PVLVEDVVMMG-RYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 199 VDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLE 241
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTVMVK 216
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
402-582 |
1.81e-15 |
|
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: 77.94 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 402 DQTLQDTKHHMYQLVYI------ASMVSVLMFGIIKGFTftNTTLMA--SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNR 473
Cdd:cd18563 28 DVLIQLGPGGNTSLLLLlvlglaGAYVLSALLGILRGRL--LARLGEriTADLRRDLYEHLQRLSLSFFDKRQTGSLMSR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 474 FSKDMDELDVRLPFHAENFLQQFFMVVFILVIM---------AAVFPVVLVVLaGLAVIFLILLRIFHRgvqelkqvenI 544
Cdd:cd18563 106 VTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLfslnwklalLVLIPVPLVVW-GSYFFWKKIRRLFHR----------Q 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568956771 545 SRSpWF---SHITSSIQGLGVIHAYDKKDDCISKFKTLNDE 582
Cdd:cd18563 175 WRR-WSrlnSVLNDTLPGIRVVKAFGQEKREIKRFDEANQE 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
53-240 |
1.98e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.29 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPKsVLHNISFVVRKGKVLGICGNVGSGKS-------SLISALLGQMQLQKGVVAVNGPLAY---VS---QQAWIF 119
Cdd:PRK10247 15 YLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKStllkivaSLISPTSGTLLFEGEDISTLKPEIYrqqVSycaQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 HGNVRENILFGEKYNHQRYQHTVHVCGLQKdlnslpYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSA 198
Cdd:PRK10247 94 GDTVYDNLIFPWQIRNQQPDPAIFLDDLER------FALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 199 VDAHvGKHVFEECIKK--TLKGKTVVLVTHQLQFLESCDEVILL 240
Cdd:PRK10247 168 LDES-NKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
61-227 |
1.99e-15 |
|
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: 75.86 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA-----YVSQQAWIFHGN-------VRENI 127
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtPLAeqrdePHENILYLGHLPglkpelsALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFgekYN--HQRYQHTVHvcglqkdlNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvG 204
Cdd:TIGR01189 95 HF---WAaiHGGAQRTIE--------DALAAVGLTGFEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-G 162
|
170 180
....*....|....*....|....
gi 568956771 205 KHVFEECIKKTL-KGKTVVLVTHQ 227
Cdd:TIGR01189 163 VALLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
62-256 |
2.13e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.36 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGpLAYVSQQAW--------IFHG--------NVRE 125
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmVFQNpdnqfvgaTVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKyNHQ--------RYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLS 197
Cdd:PRK13635 102 DVAFGLE-NIGvpreemveRVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 198 AVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 256
Cdd:PRK13635 170 MLDPRGRREVLE--TVRQLKeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
695-902 |
2.32e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 76.32 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 695 KDYRMRYRDNTPL-VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID----EVDICTVG---LEDLR 766
Cdd:COG4778 12 KTFTLHLQGGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 TK--------LTMIPQdpvlfVGTVRYNLDPLgshtdemlwhvLERTFMRD----------TIMKLPEKL--QAEVTeng 826
Cdd:COG4778 92 RRtigyvsqfLRVIPR-----VSALDVVAEPL-----------LERGVDREearararellARLNLPERLwdLPPAT--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 827 enFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAfKS--CTVLTIAHRLNTVLN-CDLVLVMENG 902
Cdd:COG4778 153 --FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KArgTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
709-918 |
2.52e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.44 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDP-VLFVGT----- 782
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGAtvedd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 783 VRYNLDPLGSHTDEMLWHVLERTF---MRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASM 859
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLavnMLDFKTREPARL-----------SGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 860 DSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKP-EVLAEKPD 918
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPsELFATSED 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
692-905 |
2.70e-15 |
|
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: 75.61 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDnTPLVLDglnLNIQSGQTVGIVGRTGSGKSSLG--MALFRLvePASGTIIIDEVDICTvgLEDLRTKL 769
Cdd:cd03298 1 VRLDKIRFSYGE-QPMHFD---LTFAQGEITAIVGPSGSGKSTLLnlIAGFET--PQSGRVLINGVDVTA--APPADRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQDPVLFVG-TVRYNLD----P---LGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMAR 841
Cdd:cd03298 73 SMLFQENNLFAHlTVEQNVGlglsPglkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 842 ALLRNSKIILLDEATASMD----SKTDTLVQSTIKEafKSCTVLTIAHRLNTVLNC-DLVLVMENGKVI 905
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
695-918 |
3.48e-15 |
|
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: 76.04 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 695 KDYRMRYrdntplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvgledlrTKLTM--- 771
Cdd:cd03218 8 KRYGKRK------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---------TKLPMhkr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 -------IPQDPVLFVG-TVRYNLDPlgshtdemlwhVLErtfmrdtIMKLPEKLQAEVTE--------------NGENF 829
Cdd:cd03218 73 arlgigyLPQEASIFRKlTVEENILA-----------VLE-------IRGLSKKEREEKLEelleefhithlrksKASSL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 830 SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEF 907
Cdd:cd03218 135 SGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAE 214
|
250
....*....|.
gi 568956771 908 DKPEVLAEKPD 918
Cdd:cd03218 215 GTPEEIAANEL 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
59-247 |
3.54e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.65 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW-IFHGNVRenILFGEKYNHQ 136
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGePLAKLNRAQRkAFRRDIQ--MVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 137 RYQHTV---------HVCGLQK-----------DLNSLPYGDLTEigeRGVNLSGGQRQRISLARAVYANRQLYLLDDPL 196
Cdd:PRK10419 103 NPRKTVreiireplrHLLSLDKaerlarasemlRAVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 197 SAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGEICE 247
Cdd:PRK10419 180 SNLDLVLQAGVIR--LLKKLQqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
690-921 |
3.64e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.19 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 690 GEITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSL-----GmalfrLVEPASGTIIIDEVDIctvglED 764
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDV-----TD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 765 LRTK---LTMIPQDPVLFVG-TVRYNLD-PL------GSHTDEMLWHVLErtfmrdtIMKLPEKLQAEVTEngenFSVGE 833
Cdd:COG3839 70 LPPKdrnIAMVFQSYALYPHmTVYENIAfPLklrkvpKAEIDRRVREAAE-------LLGLEDLLDRKPKQ----LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 834 RQLLCMARALLRNSKIILLDEATASMDSKtdtL-VQ--STIKE---AFKSCTV---------LTIAHRlntvlncdlVLV 898
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAK---LrVEmrAEIKRlhrRLGTTTIyvthdqveaMTLADR---------IAV 206
|
250 260
....*....|....*....|...
gi 568956771 899 MENGKVIEFDKPEVLAEKPDSAF 921
Cdd:COG3839 207 MNDGRIQQVGTPEELYDRPANLF 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
59-260 |
3.98e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.33 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL------------LGQMQL--------QKGVV-AVNGPLAYVSQQAW 117
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIdtarslsqQKGLIrQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 118 IF-HGNVRENILFG--------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQ 188
Cdd:PRK11264 96 LFpHRTVLENIIEGpvivkgepKEEATARARELLAKVGLAGKETSYPR-----------RLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 189 LYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELM----EERGR 260
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFadpqQPRTR 241
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
358-618 |
4.95e-15 |
|
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: 76.69 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 358 FLVLCLFFLMMGSSAFSTWWLGIWLDRGSQvvcasqnnktacnvdqtlqdtKHHMYQLVYIASMVsVLMFgIIKG-FTFT 436
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDIFV---------------------EKDLEALLLVPLAI-IGLF-LLRGlASYL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 437 NTTLMASSSLH------NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVF 510
Cdd:cd18552 59 QTYLMAYVGQRvvrdlrNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 511 PV-VLVVLAGLAVIFLILLRI------FHRGVQElkQVENISrspwfSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEN 583
Cdd:cd18552 139 WKlTLIALVVLPLAALPIRRIgkrlrkISRRSQE--SMGDLT-----SVLQETLSGIRVVKAFGAEDYEIKRFRKANERL 211
|
250 260 270
....*....|....*....|....*....|....*
gi 568956771 584 sshllyfncalRWFALRMDILMNIVTFVVALLVTL 618
Cdd:cd18552 212 -----------RRLSMKIARARALSSPLMELLGAI 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
59-257 |
5.60e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG------------NVRE 125
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvPVPARARLARARIGvvpqfdnldlefTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NIL-FGekynhqRY--QHTVHVCGLQKDLnsLPYGDL-TEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:PRK13536 134 NLLvFG------RYfgMSTREIEAVIPSL--LEFARLeSKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 202 HvGKHVFEECIKKTL-KGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 257
Cdd:PRK13536 206 H-ARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
708-918 |
5.87e-15 |
|
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: 76.43 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTMIPQDPVLFVGTVRYNL 787
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 788 dPLGSHTDEMLW-HVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDtl 866
Cdd:cd03291 119 -IFGVSYDEYRYkSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE-- 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 867 vqstiKEAFKSC--------TVLTIAHRLNTVLNCDLVLVMENGKVIEFDK-PEVLAEKPD 918
Cdd:cd03291 196 -----KEIFESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTfSELQSLRPD 251
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
689-906 |
6.87e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.33 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 689 RGEITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIIIDEVDICTVGLE 763
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 764 DLRTKLTMIPQDPvlfvgtvrynlDPLGSHTdemLWHVLERTFMRDTIMKLPEKLQAEVTENGE---------------- 827
Cdd:PRK14247 79 ELRRRVQMVFQIP-----------NPIPNLS---IFENVALGLKLNRLVKSKKELQERVRWALEkaqlwdevkdrldapa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 828 -NFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAH------RLNtvlncDLVLVME 900
Cdd:PRK14247 145 gKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLY 219
|
....*.
gi 568956771 901 NGKVIE 906
Cdd:PRK14247 220 KGQIVE 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
59-244 |
7.23e-15 |
|
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: 72.48 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV--NGPLAYVSQqawifhgnvrenilfgekynhq 136
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 137 ryqhtvhvcglqkdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHvGKHVFEECIKKtL 216
Cdd:cd03221 71 --------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALEEALKE-Y 116
|
170 180
....*....|....*....|....*....
gi 568956771 217 KGkTVVLVTHQLQFLES-CDEVILLEDGE 244
Cdd:cd03221 117 PG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
69-249 |
7.68e-15 |
|
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: 74.45 E-value: 7.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 69 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFGE----K 132
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadrPVSMLFQENNLFaHLTVEQNVGLGLspglK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 133 YNHQRyQHTVHVC----GLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD----AHVG 204
Cdd:cd03298 101 LTAED-RQAIEVAlarvGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568956771 205 KHVFEECIKktlKGKTVVLVTHQLQFLESCDE-VILLEDGEICEKG 249
Cdd:cd03298 169 DLVLDLHAE---TKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
701-899 |
7.99e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 7.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 701 YRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFV 780
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 781 GTVRYNLdplgshtdEMLWHV----LERTFMRDTIMK--LPEKLqaeVTENGENFSVGERQLLCMARALLRNSKIILLDE 854
Cdd:PRK10247 95 DTVYDNL--------IFPWQIrnqqPDPAIFLDDLERfaLPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568956771 855 ATASMDSKTDTLVQSTIKEAF--KSCTVLTIAHRLNTVLNCDLVLVM 899
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
45-245 |
8.45e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 74.61 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 45 DQGVASPEWqsGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQK---GVVAVNG-PL---------AY 111
Cdd:cd03234 8 DVGLKAKNW--NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGqPRkpdqfqkcvAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 112 VSQQ-AWIFHGNVRENILF------GEKYNHQRYQHTVHVCGLqKDLNSLPYGdlteiGERGVNLSGGQRQRISLARAVY 184
Cdd:cd03234 86 VRQDdILLPGLTVRETLTYtailrlPRKSSDAIRKKRVEDVLL-RDLALTRIG-----GNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 185 ANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ-----LQFLescDEVILLEDGEI 245
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQprsdlFRLF---DRILLLSSGEI 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
692-925 |
8.75e-15 |
|
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: 79.22 E-value: 8.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTM 771
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVGTVRYNLdPLGSHTDEMLWH-VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKII 850
Cdd:TIGR00957 704 VPQQAWIQNDSLRENI-LFGKALNEKYYQqVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 851 LLDEATASMDSKTDTLVQSTI---KEAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDK-PEVLAEkpDSAFAMLL 925
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSyQELLQR--DGAFAEFL 859
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
695-911 |
9.11e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 76.69 E-value: 9.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 695 KDYRMRYR--DNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIIIDEVDICTV---GLEDLR 766
Cdd:PRK09473 16 KDLRVTFStpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLpekELNKLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 T-KLTMIPQDPVLfvgtvryNLDPLgSHTDEMLWHVL-------------ERTFMRDTImKLPEKLQaEVTENGENFSVG 832
Cdd:PRK09473 96 AeQISMIFQDPMT-------SLNPY-MRVGEQLMEVLmlhkgmskaeafeESVRMLDAV-KMPEARK-RMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 833 ERQLLCMARALLRNSKIILLDEATASMdsktDTLVQSTI-------KEAFKScTVLTIAHRLNTVLN-CDLVLVMENGKV 904
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTAL----DVTVQAQImtllnelKREFNT-AIIMITHDLGVVAGiCDKVLVMYAGRT 240
|
....*..
gi 568956771 905 IEFDKPE 911
Cdd:PRK09473 241 MEYGNAR 247
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
708-905 |
9.52e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.12 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvgledlrTKLT------MIP---QDPVL 778
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---------TKLPeykrakYIGrvfQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 779 fvGT-----VRYNL---------DPLGshtdemlWHVL--ERTFMRDTI----MKLPEKLQAEVtengENFSVGERQLLC 838
Cdd:COG1101 92 --GTapsmtIEENLalayrrgkrRGLR-------RGLTkkRRELFRELLatlgLGLENRLDTKV----GLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 839 MARALLRNSKIILLDEATASMDSKTDTLV----QSTIKEafKSCTVLTIAHRLNTVLNC-DLVLVMENGKVI 905
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEE--NNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
705-918 |
9.87e-15 |
|
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: 79.18 E-value: 9.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 705 TPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTMIPQDPVLFVGTVR 784
Cdd:TIGR01271 439 TP-VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 YNLdPLGSHTDEMLW-HVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKT 863
Cdd:TIGR01271 505 DNI-IFGLSYDEYRYtSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 864 DtlvqstiKEAFKSC--------TVLTIAHRLNTVLNCDLVLVMENGKVIEFDK-PEVLAEKPD 918
Cdd:TIGR01271 584 E-------KEIFESClcklmsnkTRILVTSKLEHLKKADKILLLHEGVCYFYGTfSELQAKRPD 640
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
64-254 |
1.14e-14 |
|
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: 73.94 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAWIFHG-NVRENI-LF 129
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLyIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 130 GEKYNHQRYQHTvhvcglQKDLNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVF 208
Cdd:cd03265 98 ARLYGVPGAERR------ERIDELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568956771 209 EEcIKKTLK--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 254
Cdd:cd03265 172 EY-IEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
53-282 |
1.20e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.59 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------------PLAYVS 113
Cdd:PRK13646 12 YQKGTPyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 114 Q--QAWIFHGNVRENILFGEKynhqRYQHTVhvcglqKDLNSLPYGDLTEIG-ERGV------NLSGGQRQRISLARAVY 184
Cdd:PRK13646 92 QfpESQLFEDTVEREIIFGPK----NFKMNL------DEVKNYAHRLLMDLGfSRDVmsqspfQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 185 ANRQLYLLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERGRY 261
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSlqTDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
250 260
....*....|....*....|....
gi 568956771 262 AKL---IHNLRGLQfKDPEHIYNV 282
Cdd:PRK13646 241 ADWhigLPEIVQLQ-YDFEQKYQT 263
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
59-250 |
1.22e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.81 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL------------AYVSQQAWI-FHGNVR 124
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrPLadwspaelarrrAVLPQHSSLsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFGekynhqRYQHTvhvcGLQKDLNSLPYG-----DLTEIGERGV-NLSGGQRQRISLARA------VYANRQLYLL 192
Cdd:PRK13548 95 EVVAMG------RAPHG----LSRAEDDALVAAalaqvDLAHLAGRDYpQLSGGEQQRVQLARVlaqlwePDGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 193 DDPLSAVD-AHvGKHVFEecIKKTL---KGKTVVLVTHQL----QFlesCDEVILLEDGEICEKGT 250
Cdd:PRK13548 165 DEPTSALDlAH-QHHVLR--LARQLaheRGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
713-917 |
1.42e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.61 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 713 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLR----TKLTMIPQDPVLF-----VGTV 783
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMphmtvLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 784 RYNLDPLG---SHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASMD 860
Cdd:PRK10070 128 AFGMELAGinaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 861 SKTDTLVQSTIK--EAFKSCTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKP 917
Cdd:PRK10070 197 PLIRTEMQDELVklQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
61-250 |
1.51e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.88 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGqmqLQK---GVVAVNG-PLAYVSQQAW---------IF-HGN---- 122
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LERptsGSVLVDGvDLTALSERELraarrkigmIFqHFNllss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 --VRENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLD 193
Cdd:COG1135 97 rtVAENVALpleiagvPKAEIRKRVAELLELVGLSDKADAYP-----------SQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 194 DPLSAVDAHVGKHVFE---EcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 250
Cdd:COG1135 166 EATSALDPETTRSILDllkD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
713-921 |
1.62e-14 |
|
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: 74.60 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 713 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL----RTKLTMIPQDPVLF-----VGTV 783
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLphrtvLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 784 RYNLDPLG---SHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASMD 860
Cdd:cd03294 124 AFGLEVQGvprAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 861 SKTDTLVQSTI----KEAFKscTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKPDSAF 921
Cdd:cd03294 193 PLIRREMQDELlrlqAELQK--TIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
692-918 |
1.96e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.87 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLV---LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC----TVGLED 764
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 765 LRTKLTMIPQDP--VLFVGTV----RYNLDPLGSHTDE-----MLWhvLERTFMRDTIM-KLPEKLqaevtengenfSVG 832
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVlkdvEFGPKNFGFSEDEakekaLKW--LKKVGLSEDLIsKSPFEL-----------SGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 833 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP 910
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGhTVILVTHNMDDVAEyADDVLVLEHGKLIKHASP 229
|
....*...
gi 568956771 911 EVLAEKPD 918
Cdd:PRK13641 230 KEIFSDKE 237
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
66-245 |
2.22e-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: 72.97 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 66 SFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFG--- 130
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqshtglapyqrPVSMLFQENNLFaHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 131 -EKYNHQRYQHTVHVC---GLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 206
Cdd:TIGR01277 98 gLKLNAEQQEKVVDAAqqvGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568956771 207 VFeeCIKKTL---KGKTVVLVTHQLQFL-ESCDEVILLEDGEI 245
Cdd:TIGR01277 167 ML--ALVKQLcseRQRTLLMVTHHLSDArAIASQIAVVSQGKI 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
60-249 |
2.30e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 60 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------LAYVSQQAWI-FHGNVRE 125
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLsFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGekynhqRYQHTVHVCGLQKD-----LNSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAV 199
Cdd:PRK09536 97 VVEMG------RTPHRSRFDTWTETdraavERAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568956771 200 DAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 249
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
692-913 |
3.04e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG----LED 764
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 765 LRTKLTMIPQDP--VLFVGTV-----------RYNLDPLGSHTDEMLwhvLERTFMRDTIMKLPEKLqaevtengenfSV 831
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVereiifgpknfKMNLDEVKNYAHRLL---MDLGFSRDVMSQSPFQM-----------SG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 832 GERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFD 908
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQT 228
|
....*
gi 568956771 909 KPEVL 913
Cdd:PRK13646 229 SPKEL 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
61-250 |
3.22e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 73.24 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVSQQAWIFHG-NVRE 125
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglpPheiarlgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGV------NLSGGQRQRISLARAVYANRQLYLLDDP---L 196
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLadrpagELSYGQQRRLEIARALATDPKLLLLDEPaagL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 197 SAVDAHVGKHVFEEcIKKtlKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 250
Cdd:cd03219 175 NPEETEELAELIRE-LRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
719-929 |
3.53e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.82 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 719 GQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG---LEDLRTKLTMIPQDPVLFVG---TVRYN-LDPLG 791
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYASLDprqTVGDSiMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 792 SH--------TDEMLWhVLERTFMRdtimklPEKLQAEVTEngenFSVGERQLLCMARALLRNSKIILLDEATASMDSKT 863
Cdd:PRK10261 430 VHgllpgkaaAARVAW-LLERVGLL------PEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 864 ---------DTLVQSTIKEAFKS---CTVLTIAHRlntvlncdlVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAEV 929
Cdd:PRK10261 499 rgqiinlllDLQRDFGIAYLFIShdmAVVERISHR---------VAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
62-245 |
4.83e-14 |
|
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: 72.06 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA----------------WIFHGNVR 124
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAipylrrkigvvfqdfrLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILF-------GEKYNHQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLS 197
Cdd:cd03292 97 ENVAFalevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568956771 198 AVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDE-VILLEDGEI 245
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
112-265 |
4.86e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 112 VSQQAWIFHGNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDLTEIGERGVNLSGGQRQRISLARAVYANRQLY 190
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 191 LLDDPLSAVDAHVgkhvfEECIKKTL------KGKTVVLVTHQLQFLESCDEVILLEDGE-----ICEKGTHKELME-ER 258
Cdd:PTZ00265 1381 LLDEATSSLDSNS-----EKLIEKTIvdikdkADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQD 1455
|
....*..
gi 568956771 259 GRYAKLI 265
Cdd:PTZ00265 1456 GVYKKYV 1462
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
59-245 |
5.87e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.79 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKG-VVAVNGPLAYVS-------QQA----WifhGNVREN 126
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGeLLAGTAPLAEARedtrlmfQDArllpW---KKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFGEKYN-HQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGK 205
Cdd:PRK11247 102 VGLGLKGQwRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568956771 206 HVFEECIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEI 245
Cdd:PRK11247 170 IEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
710-906 |
6.13e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.97 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 710 DGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII---DEVDICTVGLEDLRTKLTMIPQDPVLfvgtvryN 786
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDPLA-------S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 787 LDP---LGSHTDEMLwhvleRTFM----RDTIMklpEKLQAEVTENG----------ENFSVGERQLLCMARALLRNSKI 849
Cdd:PRK15079 111 LNPrmtIGEIIAEPL-----RTYHpklsRQEVK---DRVKAMMLKVGllpnlinrypHEFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 850 ILLDEATASMD----SKTDTLVQSTIKEAFKSctVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:PRK15079 183 IICDEPVSALDvsiqAQVVNLLQQLQREMGLS--LIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
696-914 |
6.46e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 696 DYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII--DEVDICTVGLEDLRTKLTMIP 773
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 774 QDP---VLFV---GTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAevtengenFSVGERQLLCMARALLRNS 847
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQC--------LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 848 KIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLA 914
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPgEVFA 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
59-256 |
6.72e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG------------NVRE 125
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGePVPSRARHARQRVGvvpqfdnldpdfTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NIL-FGEKYNHQRYQHTVHVCGLqkdlnsLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHv 203
Cdd:PRK13537 100 NLLvFGRYFGLSAAAARALVPPL------LEFAKLENKADAKVgELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 204 GKHVFEECIKKTL-KGKTVVLVTHqlqFLES----CDEVILLEDGEICEKGTHKELME 256
Cdd:PRK13537 173 ARHLMWERLRSLLaRGKTILLTTH---FMEEaerlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
59-304 |
7.01e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.47 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL----LGQMQLQkGVVAVNG-PL---------AYVsQQAWIFHGN-- 122
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGS-GSVLLNGmPIdakemraisAYV-QQDDLFIPTlt 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILF----------GEKYNHQRYQHTVHVCGLQKDLNslpygdlTEIGERGV--NLSGGQRQRISLARAVYANRQLY 190
Cdd:TIGR00955 116 VREHLMFqahlrmprrvTKKEKRERVDEVLQALGLRKCAN-------TRIGVPGRvkGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 191 LLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVILLEDGEICEKGTHKELMEergRYAKLIHNL 268
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAVP---FFSDLGHPC 265
|
250 260 270
....*....|....*....|....*....|....*...
gi 568956771 269 rglqfkdPEHiYNVA--MVETLKESPAQRDEDAVLASG 304
Cdd:TIGR00955 266 -------PEN-YNPAdfYVQVLAVIPGSENESRERIEK 295
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
691-923 |
7.69e-14 |
|
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: 71.99 E-value: 7.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 691 EITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLT 770
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 771 MipQDPVLFVG-TVRYNL------DPLGSHTDEMLwhvlertfMRDTIMKLPEKLQAEVTENG--ENFSVGERQLLCMAR 841
Cdd:cd03296 80 F--QHYALFRHmTVFDNVafglrvKPRSERPPEAE--------IRAKVHELLKLVQLDWLADRypAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 842 ALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTI--AHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPD 918
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
....*
gi 568956771 919 SAFAM 923
Cdd:cd03296 230 SPFVY 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
64-280 |
7.80e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.10 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFGE 131
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlshvppyqrPINMMFQSYALFpHMTVEQNIAFGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 132 KYNH-------QRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDahvg 204
Cdd:PRK11607 117 KQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 205 khvfeecikKTLKGKTvvlvthQLQFLEscdevILLEDGEICEKGTH--KELMEERGRYAklIHNlRG--LQFKDPEHIY 280
Cdd:PRK11607 182 ---------KKLRDRM------QLEVVD-----ILERVGVTCVMVTHdqEEAMTMAGRIA--IMN-RGkfVQIGEPEEIY 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
58-249 |
9.39e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 58 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAW---------IFHG------- 121
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLlpvrhriqvVFQDpnsslnp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 --NVRENILFGEKYNH------QRYQHTVHVcglqkdlnslpygdLTEIG-------ERGVNLSGGQRQRISLARAVYAN 186
Cdd:PRK15134 378 rlNVLQIIEEGLRVHQptlsaaQREQQVIAV--------------MEEVGldpetrhRYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 187 RQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGK---TVVLVTHQLQFLES-CDEVILLEDGEICEKG 249
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILA--LLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
53-245 |
1.18e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.15 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSG-SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG---------PLAYVSQQ--AWIFH 120
Cdd:PRK10535 14 YPSGeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvatldadALAQLRREhfGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 121 gnvRENILfgekyNHQRYQHTVHV----CGLQKD---------LNSLPYGDltEIGERGVNLSGGQRQRISLARAVYANR 187
Cdd:PRK10535 94 ---RYHLL-----SHLTAAQNVEVpavyAGLERKqrllraqelLQRLGLED--RVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 188 QLYLLDDPLSAVDAHVGKHVFeeCIKKTL--KGKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVM--AILHQLrdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
692-915 |
1.23e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.92 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTM 771
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQ----DPVLfvgTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVTEngenFSVGERQLLCMARALLRNS 847
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 848 KIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAH------RLntvlnCDLVLVMENGKVIEFDKPEVLAE 915
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
672-906 |
1.27e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.62 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 672 EHTHPFKVGTCPKDWPsrgEITFKDYRMRYRDNTpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTII 751
Cdd:PRK10522 306 PYKAEFPRPQAFPDWQ---TLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 752 IDEVDICTVGLEDLRTKLTMIPQDPVLFvgtvRYNLDPLGSHTDEML---WhvLERtfmrdtiMKLPEKLQaevTENGE- 827
Cdd:PRK10522 382 LDGKPVTAEQPEDYRKLFSAVFTDFHLF----DQLLGPEGKPANPALvekW--LER-------LKMAHKLE---LEDGRi 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 828 ---NFSVGERQLLCMARALLRNSKIILLDEATASMDSK------TDTLVQstIKEAFKscTVLTIAHRLNTVLNCDLVLV 898
Cdd:PRK10522 446 snlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLPL--LQEMGK--TIFAISHDDHYFIHADRLLE 521
|
....*...
gi 568956771 899 MENGKVIE 906
Cdd:PRK10522 522 MRNGQLSE 529
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
59-227 |
1.30e-13 |
|
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: 70.60 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLA-----YVSQQAWIFHGN-------VRE 125
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgPLDfqrdsIARGLLYLGHAPgikttlsVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NIlfgekynhqRYQHTVHvcGLQKDLNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:cd03231 93 NL---------RFWHADH--SDEQVEEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|...
gi 568956771 205 KHVFEECIKKTLKGKTVVLVTHQ 227
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
57-257 |
1.35e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.14 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 57 SPKSVLHNISFVVRKGKVLGICGNVGSGKSS---LISALLGQMQLQKGVVAVNGpLAYVSQQAW--------IFH----- 120
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWdirekvgiVFQnpdnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 121 ---GNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDPL 196
Cdd:PRK13640 97 fvgATVGDDVAFGlENRAVPRPEMIKIVRDVLADVGMLDYID-----SEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 197 SAVDAHvGKHVFEECIKKTLKGK--TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:PRK13640 172 SMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
59-256 |
1.69e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.74 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISaLLGQMQ-LQKGVVAVNG-PL------------AYVSQQAWIFHG-NV 123
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQpPSEGEILLDAqPLeswsskafarkvAYLPQQLPAAEGmTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENILFGeKY------------NHQRYQHTVHVCGLqkdlnslpygdlTEIGERGVN-LSGGQRQRISLARAVYANRQLY 190
Cdd:PRK10575 103 RELVAIG-RYpwhgalgrfgaaDREKVEEAISLVGL------------KPLAHRLVDsLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 191 LLDDPLSAVD-AHvgkHVFEECIKKTL---KGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 256
Cdd:PRK10575 170 LLDEPTSALDiAH---QVDVLALVHRLsqeRGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
66-255 |
1.93e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 66 SFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------PLAYVSQQAWIF-HGNVRENILFG--- 130
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtttppsrrPVSMLFQENNLFsHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 131 ----EKYNHQRYQHTVHVCGLQKDLNSLPygdlteiGErgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD----AH 202
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568956771 203 VGKHVFEECIKKTLkgkTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 255
Cdd:PRK10771 168 MLTLVSQVCQERQL---TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
56-268 |
1.95e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.78 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------------------PLAYVSQ 114
Cdd:PRK13641 15 GTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 115 QAWIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDL-NSLPYgdlteigergvNLSGGQRQRISLARAVYAN 186
Cdd:PRK13641 95 EAQLFENTVLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSEDLiSKSPF-----------ELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 187 RQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERGRYAKli 265
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKK-- 241
|
...
gi 568956771 266 HNL 268
Cdd:PRK13641 242 HYL 244
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
401-615 |
2.79e-13 |
|
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: 71.31 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 401 VDQTLQDTKHHMyqLVYIASMVsvLMFGIIKG-FTFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNR 473
Cdd:cd18542 26 IDSVIGGGLREL--LWLLALLI--LGVALLRGvFRYLQGYLAEKASqkvaydLRNDLYDHLQRLSFSFHDKARTGDLMSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 474 FSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAV-FPVVLVVLAGLAVIFLILLrIFHRGVQelKQVENISRSpwFSH 552
Cdd:cd18542 102 CTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSInWKLTLISLAIIPFIALFSY-VFFKKVR--PAFEEIREQ--EGE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 553 ITSSIQ----GLGVIHAYDKKDDCISKFKTLNDEnsshllYFNCALR-------WFALrMDILMNIVTFVVALL 615
Cdd:cd18542 177 LNTVLQenltGVRVVKAFAREDYEIEKFDKENEE------YRDLNIKlakllakYWPL-MDFLSGLQIVLVLWV 243
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
61-245 |
2.84e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.23 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA------------WIFHG------ 121
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqPMSKLSSAAkaelrnqklgfiYQFHHllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 ---NVRENILFGEKYN---HQRYQHTVHVCGLQKDLNslpygdlteigERGVNLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:PRK11629 104 aleNVAMPLLIGKKKPaeiNSRALEMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568956771 196 LSAVDAHVGKHVFEECIK-KTLKGKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
692-922 |
3.83e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 71.67 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKltM 771
Cdd:COG3842 6 LELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVG--M 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLF-----VGTVRYNLDPLG---SHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARAL 843
Cdd:COG3842 82 VFQDYALFphltvAENVAFGLRMRGvpkAEIRARVAELLELVGLEGLADRYPHQL-----------SGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 844 LRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC---TV---------LTIAHRlntvlncdlVLVMENGKVIEFDKPE 911
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELgitFIyvthdqeeaLALADR---------IAVMNDGRIEQVGTPE 221
|
250
....*....|.
gi 568956771 912 VLAEKPDSAFA 922
Cdd:COG3842 222 EIYERPATRFV 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
708-913 |
4.11e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.19 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVL-FVGTVR-- 784
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 --YNLDPLGS---HTDEMLWHVLERTfmrdtimklpeklqaEVTENGENF----SVGERQLLCMARALLRNS------KI 849
Cdd:PRK13548 97 vaMGRAPHGLsraEDDALVAAALAQV---------------DLAHLAGRDypqlSGGEQQRVQLARVLAQLWepdgppRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 850 ILLDEATASMDSKTdtlvQSTIKEAFKSCT------VLTIAHRLN-TVLNCDLVLVMENGKVIEFDKP-EVL 913
Cdd:PRK13548 162 LLLDEPTSALDLAH----QHHVLRLARQLAherglaVIVVLHDLNlAARYADRIVLLHQGRLVADGTPaEVL 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
708-916 |
4.19e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGL-EDLRTKLTMIPQDPVLFVGTVRYN 786
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 787 ldplgshtdeMLWHVLErtfMRDTIMKLPEKLQA-EVTEN----------GENFSVGERQLLCMARALLRNSKIILLDEA 855
Cdd:PRK10895 98 ----------NLMAVLQ---IRDDLSAEQREDRAnELMEEfhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 856 TASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAEK 916
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPtEILQDE 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
709-915 |
5.07e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLgM-ALFRLVEPASGTIIID--EVDI--------CTVGledlrtkltMIPQDPV 777
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDgkPVRIrsprdaiaLGIG---------MVHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 778 LF-VGTVRYNLDpLGshTDEMLWHVLERTFMRDTIMKLPEK------LQAEVtengENFSVGERQLLCMARALLRNSKII 850
Cdd:COG3845 91 LVpNLTVAENIV-LG--LEPTKGGRLDRKAARARIRELSERygldvdPDAKV----EDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 851 LLDEATASM-DSKTDTLVQsTIKEaFKS--CTVLTIAHRLNTVL-NCDLVLVMENGKVI-EFDKPEV----LAE 915
Cdd:COG3845 164 ILDEPTAVLtPQEADELFE-ILRR-LAAegKSIIFITHKLREVMaIADRVTVLRRGKVVgTVDTAETseeeLAE 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
692-909 |
5.07e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.80 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYrdNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL--VEP---ASGTIIIDEVDIC-----TVg 761
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYsprtdTV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 762 leDLRTKLTMIPQDPVLFVGT----VRYNLDPLGSHTDEMLWHVLERTFMRDTIMklpEKLQAEVTENGENFSVGERQLL 837
Cdd:PRK14239 83 --DLRKEIGMVFQQPNPFPMSiyenVVYGLRLKGIKDKQVLDEAVEKSLKGASIW---DEVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 838 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDK 909
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
401-616 |
5.12e-13 |
|
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: 70.52 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 401 VDqTLQDTKHHMYQLVYIASMVSVLMFGIIKGFTFTNTTLMASS-----SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFS 475
Cdd:cd18541 26 ID-ALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASrrieyDLRNDLFAHLLTLSPSFYQKNRTGDLMARAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 476 KDMDEldVR--LPFHAENFLQQFFMVVFILVIMAAVFP----VVLVVLAGLAVIFLILLRIFHRG---VQELkqvenisr 546
Cdd:cd18541 105 NDLNA--VRmaLGPGILYLVDALFLGVLVLVMMFTISPkltlIALLPLPLLALLVYRLGKKIHKRfrkVQEA-------- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 547 spwFSHITSSIQ----GLGVIHAYDKKDDCISKFKTLNDENSSHllyfNCAL-RWFALrMDILMNIVTFVVALLV 616
Cdd:cd18541 175 ---FSDLSDRVQesfsGIRVIKAFVQEEAEIERFDKLNEEYVEK----NLRLaRVDAL-FFPLIGLLIGLSFLIV 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
700-928 |
5.34e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL-----VEPASGTIIIDEVDICTVGLEDLR----TKLT 770
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 771 MIPQDPVLfvgtvryNLDPLgsHTDE-MLWHVL------ERTFMRDTIMKLPEKL---QA--EVTENGENFSVGERQLLC 838
Cdd:PRK15134 96 MIFQEPMV-------SLNPL--HTLEkQLYEVLslhrgmRREAARGEILNCLDRVgirQAakRLTDYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 839 MARALLRNSKIILLDEATASMdsktDTLVQSTIKEAFK------SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPE 911
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTAL----DVSVQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAA 242
|
250
....*....|....*...
gi 568956771 912 VLAEKPDSAFA-MLLAAE 928
Cdd:PRK15134 243 TLFSAPTHPYTqKLLNSE 260
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
62-258 |
5.59e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLG----------QMQLQKGVVAVNGPLA-----YVSQQAWIFHG----- 121
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirkSRANTGYIFQQfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 --NVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPYgdLTEIG------ERGVNLSGGQRQRISLARAVYANRQLYLLD 193
Cdd:PRK09984 100 rlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 194 DPLSAVDAHVGKHVFEEC--IKKTlKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:PRK09984 178 EPIASLDPESARIVMDTLrdINQN-DGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
63-234 |
6.17e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 63 HNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL-----AYVSQQAWIFHGN-------VRENILF 129
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGePIrrqrdEYHQDLLYLGHQPgikteltALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 130 gekynhqrYQHtVHVCGLQKDLNSLpygdLTEIGERGV------NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHv 203
Cdd:PRK13538 98 --------YQR-LHGPGDDEALWEA----LAQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ- 163
|
170 180 190
....*....|....*....|....*....|..
gi 568956771 204 GKHVFEECIKKTL-KGKTVVLVTHQLQFLESC 234
Cdd:PRK13538 164 GVARLEALLAQHAeQGGMVILTTHQDLPVASD 195
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
409-616 |
6.31e-13 |
|
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: 70.57 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 409 KHHMYQLVYIASMVSVLMFgIIKGFTFTNTTLMAS------SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD 482
Cdd:cd18545 33 NGDLSGLLIIALLFLALNL-VNWVASRLRIYLMAKvgqrilYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 483 VRLPFHAENFLQQFFMVVFILVIMAAVFPVV-LVVLAGLAVIFLILLRI---FHRGVQEL-KQVENISrspwfSHITSSI 557
Cdd:cd18545 112 DLLSNGLINLIPDLLTLVGIVIIMFSLNVRLaLVTLAVLPLLVLVVFLLrrrARKAWQRVrKKISNLN-----AYLHESI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 558 QGLGVIHAYDKKDDCISKFKTLNDEN-SSHLLyfncALRWFALRMDILMNIVTFVVALLV 616
Cdd:cd18545 187 SGIRVIQSFAREDENEEIFDELNRENrKANMR----AVRLNALFWPLVELISALGTALVY 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
61-251 |
7.95e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISAL-------LGQMQL------------QKGVVAVNGPLAYVSQQ--AWIf 119
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIagnhfdfsktpsDKAIRELRRNVGMVFQQynLWP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 HGNVRENILfgekynhqryQHTVHVCGLQKD---------LNSLpygDLTEIGER-GVNLSGGQRQRISLARAVYANRQL 189
Cdd:PRK11124 96 HLTVQQNLI----------EAPCRVLGLSKDqalaraeklLERL---RLKPYADRfPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 190 YLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTH 251
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVS--IIRELAetGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDA 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-254 |
1.17e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAY-------------------VSQQAWIF 119
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiklrkevgmVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 -HGNVRENILFGEKYNHQRYQHTVHVCgLQKDLNSLpyGDLTEIGER----GVNLSGGQRQRISLARAVYANRQLYLLDD 194
Cdd:PRK14246 103 pHLSIYDNIAYPLKSHGIKEKREIKKI-VEECLRKV--GLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 195 PLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQ-LQFLESCDEVILLEDGEICEKGTHKEL 254
Cdd:PRK14246 180 PTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
74-245 |
1.30e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.29 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 74 VLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL-----------------AYVSQQAWIF-HGNVRENILFG-EKYN 134
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLFpHYKVRGNLRYGmAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 135 HQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV--FEECI 212
Cdd:PRK11144 106 VAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELlpYLERL 174
|
170 180 190
....*....|....*....|....*....|....
gi 568956771 213 KKTLKgKTVVLVTHQLQ-FLESCDEVILLEDGEI 245
Cdd:PRK11144 175 AREIN-IPILYVSHSLDeILRLADRVVVLEQGKV 207
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
60-247 |
1.39e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.27 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 60 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA----------WIFHG------- 121
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqPLHQMDEEAraklrakhvgFVFQSfmliptl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENI-----LFGEKYNHQRYQ--HTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDD 194
Cdd:PRK10584 104 NALENVelpalLRGESSRQSRNGakALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568956771 195 PLSAVDAHVGKHVFEECIKKTLK-GKTVVLVTHQLQFLESCDEVILLEDGEICE 247
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
413-616 |
1.40e-12 |
|
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: 69.13 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 413 YQLVYIASMVSVLMFgiIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENF 492
Cdd:cd18557 40 LILLAIYLLQSVFTF--VRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 493 LQQFFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLRIFHRGVQEL-KQV-ENISRSPwfSHITSSIQGLGVIHAYDKKD 570
Cdd:cd18557 118 LRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLsKEVqDALAKAG--QVAEESLSNIRTVRSFSAEE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568956771 571 DCISKFKTLNDEnsSHLLYFNCAlRWFALRMDIlMNIVTFVVALLV 616
Cdd:cd18557 196 KEIRRYSEALDR--SYRLARKKA-LANALFQGI-TSLLIYLSLLLV 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
708-906 |
1.61e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVG---LEDLRTKLTMIPQDPvlfvgtvR 784
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 YNLDP-----------LGSHTDEMlwHVLERTFMRDTIMKL----PEKLQAEVTEngenFSVGERQLLCMARALLRNSKI 849
Cdd:PRK15134 373 SSLNPrlnvlqiieegLRVHQPTL--SAAQREQQVIAVMEEvgldPETRHRYPAE----FSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 850 ILLDEATASMDsKTdtlVQSTIKEAFKS------CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:PRK15134 447 IILDEPTSSLD-KT---VQAQILALLKSlqqkhqLAYLFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
709-902 |
1.93e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDictvgLEDLRTKLT------MIPQD-PVLFVG 781
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-----YNKLDHKLAaqlgigIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 782 TVRYNLdPLGSHTDEMLW--HVLERTFMRD--TIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATA 857
Cdd:PRK09700 96 TVLENL-YIGRHLTKKVCgvNIIDWREMRVraAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568956771 858 SM-DSKTDTL--VQSTIKEAFKSctVLTIAHRLNTVLN-CDLVLVMENG 902
Cdd:PRK09700 175 SLtNKEVDYLflIMNQLRKEGTA--IVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
708-906 |
2.02e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.17 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQDPVLFVGtvr 784
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIPG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 ynldplgshtdemlwhVLERTFMRDTimklpeklqaevtenGENFSVGERQLLCMARALLRNSKIILLDEatasMDSKTD 864
Cdd:cd03217 92 ----------------VKNADFLRYV---------------NEGFSGGEKKRNEILQLLLLEPDLAILDE----PDSGLD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568956771 865 TLVQSTIKEAFKS-----CTVLTIAH--RLNTVLNCDLVLVMENGKVIE 906
Cdd:cd03217 137 IDALRLVAEVINKlreegKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
61-227 |
2.10e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV--NGPLAYVSQQAWIFHGNVRENILF---GEKYNH 135
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSD 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 136 QRYQHTVHVCGLQkDLNslpyGDLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKT 215
Cdd:COG4178 458 AELREALEAVGLG-HLA----ERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREE 531
|
170
....*....|..
gi 568956771 216 LKGKTVVLVTHQ 227
Cdd:COG4178 532 LPGTTVISVGHR 543
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
692-906 |
2.36e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.85 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDI-CTVGLEDLRTKLT 770
Cdd:PRK11264 4 IEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 771 MIPQDpvlfVGTV--RYNLDPLGShtdeMLWHVLE-----RTFMRDTIMKLPEKLQAEVTENGEN------FSVGERQLL 837
Cdd:PRK11264 82 QLRQH----VGFVfqNFNLFPHRT----VLENIIEgpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 838 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
708-908 |
2.38e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIIDEvdictvgledlRTKLTMIPQDPVLFVG-- 781
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILagelEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 782 ---TVRYNLDPLGSHTDEMLwHVLERTFMRDTIMKLPEKLQAEVTENGE--------------------------NFSVG 832
Cdd:COG0488 78 vldTVLDGDAELRALEAELE-ELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 833 ERQLLCMARALLRNSKIILLDEATASMDSKT-----DTLVQSTikeafksCTVLTIAH-R--LNTVlnCDLVLVMENGKV 904
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNYP-------GTVLVVSHdRyfLDRV--ATRILELDRGKL 227
|
....
gi 568956771 905 IEFD 908
Cdd:COG0488 228 TLYP 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
692-921 |
2.55e-12 |
|
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: 67.80 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGtiiiDEVDIC-----TVGLEDLR 766
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFgerrgGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 TKL---------TMIPQDPVL------FVGTV-RYNldplgSHTDEM------------LWHVLERTFmrdtimklpekl 818
Cdd:COG1119 78 KRIglvspalqlRFPRDETVLdvvlsgFFDSIgLYR-----EPTDEQrerarellellgLAHLADRPF------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 819 qaevtengENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE--AFKSCTVLTIAHRLNTVLNC-DL 895
Cdd:COG1119 141 --------GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTH 212
|
250 260
....*....|....*....|....*..
gi 568956771 896 VLVMENGKVIEF-DKPEVLAEKPDSAF 921
Cdd:COG1119 213 VLLLKDGRVVAAgPKEEVLTSENLSEA 239
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
62-249 |
2.98e-12 |
|
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: 66.83 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVL------------GICGNVGSGKSSLISALLGQMQLQKGVVAVNGP------------LAYVSQQaw 117
Cdd:cd03264 3 LENLTKRYGKKRALdgvsltlgpgmyGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 118 iFhgNVRENILFGEKYNHQRYQHTVH-------VCGLQKDLNslpygdLTEIGERGVN-LSGGQRQRISLARAVYANRQL 189
Cdd:cd03264 81 -F--GVYPNFTVREFLDYIAWLKGIPskevkarVDEVLELVN------LGDRAKKKIGsLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 190 YLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 249
Cdd:cd03264 152 LIVDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
53-276 |
3.07e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.12 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV----------NGPLAYVSQQAWI-- 118
Cdd:PRK13634 12 YQYKTPfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkkNKKLKPLRKKVGIvf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 -------FHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKD-LNSLPYgdlteigergvNLSGGQRQRISLARAV 183
Cdd:PRK13634 92 qfpehqlFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEElLARSPF-----------ELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 184 YANRQLYLLDDPLSAVDAHvGKH----VFEECIKKtlKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKEL---- 254
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPK-GRKemmeMFYKLHKE--KGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPREIfadp 237
|
250 260 270
....*....|....*....|....*....|.
gi 568956771 255 --MEERG-------RYAKLIHNLRGLQFKDP 276
Cdd:PRK13634 238 deLEAIGldlpetvKFKRALEEKFGISFPKP 268
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
54-250 |
3.98e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.67 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 54 QSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG---------PLAYVSQQ-AWIF-HGN 122
Cdd:PRK11153 13 QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalsekELRKARRQiGMIFqHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 ------VRENILF-----GEKYNH--QRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQL 189
Cdd:PRK11153 93 llssrtVFDNVALplelaGTPKAEikARVTELLELVGLSDKADRYP-----------AQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 190 YLLDDPLSAVDAHVGKHVFE--ECIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 250
Cdd:PRK11153 162 LLCDEATSALDPATTRSILEllKDINREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
59-258 |
4.11e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.66 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVS----QQAWIFH 120
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvrirsPrdairagIAYVPedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 121 GNVRENILFGekyNHQRYQH---------TVHVCGLQKDLNSLPYGDLTEIGergvNLSGGQRQRISLARAVYANRQLYL 191
Cdd:COG1129 345 LSIRENITLA---SLDRLSRgglldrrreRALAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 192 LDDPLSAVDahVG-KHVFEECIKK-TLKGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:COG1129 418 LDEPTRGID--VGaKAEIYRLIRElAAEGKAVIVISSELPeLLGLSDRILVMREGRIVGELDREEATEEA 485
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
59-245 |
4.15e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.71 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVnGP---LAYVSQQAWIFHGN--VRENIlfgeky 133
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQHQEELDPDktVLDEL------ 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 134 nhQRY---QHTVHVCGLQKDLNsLPYGD-LTEIGergvNLSGGQRQRISLARAVYANRQLYLLDDP-----LSAVDAhvg 204
Cdd:COG0488 401 --RDGapgGTEQEVRGYLGRFL-FSGDDaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA--- 470
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568956771 205 khvFEECIKkTLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:COG0488 471 ---LEEALD-DFPG-TVLLVSHDRYFLDRvATRILEFEDGGV 507
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
53-257 |
4.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVnGPLAYVSQ---------------- 114
Cdd:PRK13643 11 YQPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTskqkeikpvrkkvgvv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 115 ----QAWIFHGNVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPygdlTEIGERG-VNLSGGQRQRISLARAVYANRQL 189
Cdd:PRK13643 90 fqfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLA----DEFWEKSpFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 190 YLLDDPLSAVD--AHVGKHVFEECIKKTlkGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:PRK13643 166 LVLDEPTAGLDpkARIEMMQLFESIHQS--GQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
692-916 |
4.24e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDP--VLFVGTV-------RYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARA 842
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 843 LLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIA-HRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEK 916
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
695-911 |
4.51e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.41 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 695 KDYRMRYRDNTpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGLEDLRTKLTMI 772
Cdd:PRK13639 5 RDLKYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgePIKYDKKSLLEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 773 PQDP--VLFVGTVRYNL--DP--LGSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARAL 843
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVafGPlnLGLSKEEVEKRVkeaLKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 844 LRNSKIILLDEATASMD----SKTDTLVQSTIKEAFkscTVLTIAHRLNTV-LNCDLVLVMENGKVIEFDKPE 911
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKEGI---TIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPK 222
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
61-255 |
4.54e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 67.17 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQA------WIFHG-----NVRENIl 128
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhKLEYGDYKYrckhirMIFQDpntslNPRLNI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 fGE------KYN--------HQRYQHTVHVCGLqkdlnslpYGDLTEIGERgvNLSGGQRQRISLARAVYANRQLYLLDD 194
Cdd:COG4167 107 -GQileeplRLNtdltaeerEERIFATLRLVGL--------LPEHANFYPH--MLSSGQKQRVALARALILQPKIIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 195 PLSAVDAHVGKhvfeECIKKTLK-----GKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 255
Cdd:COG4167 176 ALAALDMSVRS----QIINLMLElqeklGISYIYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEVF 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
690-906 |
4.62e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.38 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 690 GEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEV------DICTVGLE 763
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 764 DLRTKLTMIPQDPVLF-----VGTVRYNLDPLGSHTDEMLWHVLERTFMRdtiMKLPEKLQAEVTENGENFSVGERQLLC 838
Cdd:PRK14246 87 KLRKEVGMVFQQPNPFphlsiYDNIAYPLKSHGIKEKREIKKIVEECLRK---VGLWKEVYDRLNSPASQLSGGQQQRLT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 839 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
59-256 |
4.75e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.45 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ--KGVVAVN----------GPLAYVSQQA---------- 116
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIYHvalcekcgyvERPSKVGEPCpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 117 ----WIFHGNVRENIlfgEKYNHQRYQHTVHVCG----LQKDLNSLP---YG------------DLTEIGER----GVNL 169
Cdd:TIGR03269 93 evdfWNLSDKLRRRI---RKRIAIMLQRTFALYGddtvLDNVLEALEeigYEgkeavgravdliEMVQLSHRithiARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 170 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEECIKKtlKGKTVVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhnaLEEAVKA--SGISMVLTSHWPEVIEDlSDKAIWLENGEI 247
|
250
....*....|.
gi 568956771 246 CEKGTHKELME 256
Cdd:TIGR03269 248 KEEGTPDEVVA 258
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
61-245 |
5.83e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICG-NvGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG--------------NVR 124
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGeN-GAGKSTLMKILSGVYQPDSGEILLDGePVRFRSPRDAQAAGiaiihqelnlvpnlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFGE------KYNHQR-YQHTVHVC---GLQKDLNslpygdlTEIGErgvnLSGGQRQRISLARAVYANRQLYLLDD 194
Cdd:COG1129 98 ENIFLGReprrggLIDWRAmRRRARELLarlGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568956771 195 PLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEI 245
Cdd:COG1129 167 PTASLTEREVERLFR--IIRRLKaqGVAIIYISHRLdEVFEIADRVTVLRDGRL 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
709-906 |
6.74e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC---TVGLEDLRTKLTMIPQDPvlfVG---- 781
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP---YGslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 782 --TVRYNL-DPLGSHTDemlwhvLERTFMRDTIMKLPEK--LQAEVTENGEN-FSVGERQLLCMARALLRNSKIILLDEA 855
Cdd:PRK11308 108 rkKVGQILeEPLLINTS------LSAAERREKALAMMAKvgLRPEHYDRYPHmFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 856 TasmdSKTDTLVQSTI-------KEAFKSCTVLtIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:PRK11308 182 V----SALDVSVQAQVlnlmmdlQQELGLSYVF-ISHDLSVVEHiADEVMVMYLGRCVE 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
59-227 |
8.10e-12 |
|
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: 64.48 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVV--AVNGPLAYVSQQAWIFHGNVRENILFgekynhq 136
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmPEGEDLLFLPQRPYLPLGTLREQLIY------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 137 ryqhtvhvcglqkdlnslPYGDlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECikkTL 216
Cdd:cd03223 87 ------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KE 136
|
170
....*....|.
gi 568956771 217 KGKTVVLVTHQ 227
Cdd:cd03223 137 LGITVISVGHR 147
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
700-854 |
8.21e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.21 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIIIDEVDIctvgledlrTKLTM---- 771
Cdd:COG1137 12 SYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDI---------THLPMhkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 ------IPQDPVLFVG-TVRYNLdplgshtdeMLwhVLERTFM-RDTIMKLPEKLQAE-----VTEN-GENFSVGERQLL 837
Cdd:COG1137 77 rlgigyLPQEASIFRKlTVEDNI---------LA--VLELRKLsKKEREERLEELLEEfgithLRKSkAYSLSGGERRRV 145
|
170
....*....|....*..
gi 568956771 838 CMARALLRNSKIILLDE 854
Cdd:COG1137 146 EIARALATNPKFILLDE 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
62-243 |
8.48e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG--------------NVREN 126
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFGekynhqryqHTVHVCGL--QKDLNSLPYGDLTEIGE------RGVNLSGGQRQRISLARAVYANRQLYLLDDPLSA 198
Cdd:PRK11288 100 LYLG---------QLPHKGGIvnRRLLNYEAREQLEHLGVdidpdtPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568956771 199 VDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDG 243
Cdd:PRK11288 171 LSAREIEQLFR--VIRELRaeGRVILYVSHRMeEIFALCDAITVFKDG 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
692-904 |
9.92e-12 |
|
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: 65.35 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDlrTKLTM 771
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDpvlfvgtvrYNLDPLGSHTDEMLWHVLERTFMRDTI----------MKLPEKLQAEVTEngenFSVGERQLLCMAR 841
Cdd:cd03301 77 VFQN---------YALYPHMTVYDNIAFGLKLRKVPKDEIdervrevaelLQIEHLLDRKPKQ----LSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 842 ALLRNSKIILLDEATASMDSKTDTLVQSTIK---EAFKSCTV---------LTIAHRlntvlncdlVLVMENGKV 904
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKrlqQRLGTTTIyvthdqveaMTMADR---------IAVMNDGQI 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
50-255 |
1.02e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.75 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 50 SPEWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQ---LQKGVVAVNGPLA--------YVSQQAWI 118
Cdd:PLN03211 72 SDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKPTkqilkrtgFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 F-HGNVRENILFgekynhqryqhtvhvCGLQKDLNSLPYGDLTEIGE---------------------RGVnlSGGQRQR 176
Cdd:PLN03211 152 YpHLTVRETLVF---------------CSLLRLPKSLTKQEKILVAEsviselgltkcentiignsfiRGI--SGGERKR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 177 ISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVILLEDGEICEKGTHKEL 254
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGRCLFFGKGSDA 294
|
.
gi 568956771 255 M 255
Cdd:PLN03211 295 M 295
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
692-904 |
1.10e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.24 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdicTVGLEDLRTKLTM 771
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLF--------VGtvrynLDPLGSHTDEMLwHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARAL 843
Cdd:PRK11247 86 MFQDARLLpwkkvidnVG-----LGLKGQWRDAAL-QALAAVGLADRANEWPAAL-----------SGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 844 LRNSKIILLDEATASMDSKTDTLVQSTI-----KEAFkscTVLTIAHRLN-TVLNCDLVLVMENGKV 904
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
700-921 |
1.15e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.44 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIIID--EV--------DICtvgledl 765
Cdd:PRK11432 15 RFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDgeDVthrsiqqrDIC------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 766 rtkltMIPQDPVLF----VG-TVRYNLDPLGSHTDEMLWHVLERTFMRDtimklpekLQAEVTENGENFSVGERQLLCMA 840
Cdd:PRK11432 82 -----MVFQSYALFphmsLGeNVGYGLKMLGVPKEERKQRVKEALELVD--------LAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 841 RALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKP 917
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfnITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQP 228
|
....
gi 568956771 918 DSAF 921
Cdd:PRK11432 229 ASRF 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
709-905 |
1.20e-11 |
|
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: 65.01 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQ---SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDictvgLEDLRTKLTMIPQD---------P 776
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV-----LFDSRKKINLPPQQrkiglvfqqY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 777 VLFVG-TVRYNLdplgshtdEMLWHVLERTFMRDTIMKLPEKLQAEVTENG--ENFSVGERQLLCMARALLRNSKIILLD 853
Cdd:cd03297 85 ALFPHlNVRENL--------AFGLKRKRNREDRISVDELLDLLGLDHLLNRypAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 854 EATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTV-LNCDLVLVMENGKVI 905
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
709-928 |
1.20e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIIIDEVDICTVGLEDLRTK--------LTMIPQDPV 777
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHgtyEGEIIFEGEELQASNIRDTERAgiaiihqeLALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 778 L---FVGTV-----RYNLDPLGSHTDEMLWHVlertfmrdtimklpeKLQAEVTENGENFSVGERQLLCMARALLRNSKI 849
Cdd:PRK13549 100 LeniFLGNEitpggIMDYDAMYLRAQKLLAQL---------------KLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 850 ILLDEATASM-DSKTDTLVqsTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEkpDSAFAMLL 925
Cdd:PRK13549 165 LILDEPTASLtESETAVLL--DIIRDLKAhgIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTE--DDIITMMV 240
|
...
gi 568956771 926 AAE 928
Cdd:PRK13549 241 GRE 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
692-916 |
1.20e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlEDLRTKLTM 771
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQ-DPVLFVGTVRYNLDPLGSH-------TDEMLWHVLErtFMRdtimkLPEKLQAEVTEngenFSVGERQLLCMARAL 843
Cdd:PRK13536 119 VPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLE--FAR-----LESKADARVSD----LSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 844 LRNSKIILLDEATASMDSKTDTLVQSTIKEAF-KSCTVLTIAH------RLntvlnCDLVLVMENGKVIEFDKPEVLAEK 916
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
708-906 |
1.30e-11 |
|
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: 65.53 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGlED----LRTKLtmipqdpvlfVGTV 783
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDararLRARH----------VGFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 784 RYNLDPLGSHTdeMLWHV---LERTFMRDtimklPEKLQAEVTEN---GENF-------SVGERQLLCMARALLRNSKII 850
Cdd:COG4181 96 FQSFQLLPTLT--ALENVmlpLELAGRRD-----ARARARALLERvglGHRLdhypaqlSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 851 LLDEATASMDSKTDTLVQS---TIKEAFKSCTVLT-----IAHRlntvlnCDLVLVMENGKVIE 906
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDllfELNRERGTTLVLVthdpaLAAR------CDRVLRLRAGRLVE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
708-928 |
1.32e-11 |
|
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: 68.17 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP----ASGTIIIDEVDICTVGLEDLRT----KLTMIPQDPVlf 779
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 780 vgTvryNLDPLgsHTDE------MLWH--------------VLERTFMRDtimklPEK-LQAEVTEngenFSVGERQLLC 838
Cdd:COG4172 103 --T---SLNPL--HTIGkqiaevLRLHrglsgaaararaleLLERVGIPD-----PERrLDAYPHQ----LSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 839 MARALLRNSKIILLDEATasmdskT--DTLVQSTIKEAFKSCT------VLTIAHRLNTVLN-CDLVLVMENGKVIEFDK 909
Cdd:COG4172 167 IAMALANEPDLLIADEPT------TalDVTVQAQILDLLKDLQrelgmaLLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
250 260
....*....|....*....|
gi 568956771 910 PEVLAEKPDSAFA-MLLAAE 928
Cdd:COG4172 241 TAELFAAPQHPYTrKLLAAE 260
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
677-905 |
1.38e-11 |
|
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: 65.37 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 677 FKVGTCPKDWpsrgeitfkdyrmryrDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIIID 753
Cdd:cd03234 7 WDVGLKAKNW----------------NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 754 EVDictvgledlRTKLTM------IPQDPVLFVG-TVR-----YNLDPLGSHTDEmlwhvlERTFMRDTIMKLpekLQAE 821
Cdd:cd03234 71 GQP---------RKPDQFqkcvayVRQDDILLPGlTVRetltyTAILRLPRKSSD------AIRKKRVEDVLL---RDLA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 822 VTENG----ENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAH--RLNTVLNCD 894
Cdd:cd03234 133 LTRIGgnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFD 212
|
250
....*....|.
gi 568956771 895 LVLVMENGKVI 905
Cdd:cd03234 213 RILLLSSGEIV 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
62-256 |
1.47e-11 |
|
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: 67.79 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGqMQLQKGVVAVNG-PLAYVSQQAW---------IF---HG------N 122
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrmqvVFqdpFGslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRE------NILFGEKYNHQRYQHTVHVcglqkdlnslpygdLTEIG-----------ErgvnLSGGQRQRISLARAVYA 185
Cdd:COG4172 381 VGQiiaeglRVHGPGLSAAERRARVAEA--------------LEEVGldpaarhryphE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 186 NRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGK---TVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 256
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILD--LLRDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
692-921 |
1.61e-11 |
|
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: 64.95 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctVGLEDLRTKLTM 771
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFvgtvrynldplgSHTDemlwhVLERTFMRDTIMKLPEK-LQAEVTE-----NGENF--------SVGERQLL 837
Cdd:cd03300 77 VFQNYALF------------PHLT-----VFENIAFGLRLKKLPKAeIKERVAEaldlvQLEGYanrkpsqlSGGQQQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 838 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLA 914
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIY 219
|
....*..
gi 568956771 915 EKPDSAF 921
Cdd:cd03300 220 EEPANRF 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
55-264 |
1.87e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.78 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 55 SGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQQAWIFHGN------ 122
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKKIGIIFQNpdnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 ---VRENILFG---EKYNHQRYQ----HTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLL 192
Cdd:PRK13632 98 gatVEDDIAFGlenKKVPPKKMKdiidDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 193 DDPLSAVDAHvGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM--EERGRYAKL 264
Cdd:PRK13632 167 DESTSMLDPK-GKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILnnKEILEKAKI 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
59-256 |
2.02e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.05 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------P--------LAYVSQQAWIFHG-NV 123
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithlPmhkrarlgIGYLPQEASIFRKlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENIL----FGEKYNHQRyqhtvhvcglQKDLNSLpygdLTEIG------ERGVNLSGGQRQRISLARAVYANRQLYLLD 193
Cdd:COG1137 96 EDNILavleLRKLSKKER----------EERLEEL----LEEFGithlrkSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 194 DPLSAVD--AhvgkhVFEecIKK---TLKGKTV-VLVT-HQLQ-FLESCDEVILLEDGEICEKGTHKELME 256
Cdd:COG1137 162 EPFAGVDpiA-----VAD--IQKiirHLKERGIgVLITdHNVReTLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
692-919 |
2.03e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.11 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC--TVGLEDLRTKL 769
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 770 TMIPQdpvlfvgtvRYNLDP-LGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEV--TENGENF----SVGERQLLCMARA 842
Cdd:PRK09493 80 GMVFQ---------QFYLFPhLTALENVMFGPLRVRGASKEEAEKQARELLAKVglAERAHHYpselSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 843 LLRNSKIILLDEATASMDSKTD----TLVQSTIKEAFKSCTV---LTIAHRLNTVLncdlvLVMENGKVIEFDKPEVLAE 915
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGMTMVIVtheIGFAEKVASRL-----IFIDKGRIAEDGDPQVLIK 225
|
....
gi 568956771 916 KPDS 919
Cdd:PRK09493 226 NPPS 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
61-260 |
2.31e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.90 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWifhG------------NVRENI 127
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGePLDPEDRRRI---GylpeerglypkmKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 L-FGE-KynhqryqhtvhvcGLQKD---------LNSLpygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:COG4152 93 VyLARlK-------------GLSKAeakrradewLERL---GLGDRANKKVeELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 196 LSAVDAhVGKHVFEECIK-KTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGR 260
Cdd:COG4152 157 FSGLDP-VNVELLKDVIReLAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
708-906 |
2.54e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 64.65 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII-----------DEVDICtvgleDLRTKLTMIPQD- 775
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIR-----ELRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 776 ---PVLfvgTVRYNL--DP---LGshtdemlwhvLERTFMRDTIMKLPEKLQaeVTENGENF----SVGERQLLCMARAL 843
Cdd:PRK11124 92 nlwPHL---TVQQNLieAPcrvLG----------LSKDQALARAEKLLERLR--LKPYADRFplhlSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 844 LRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
61-254 |
2.57e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.28 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-----------LAYVSQQAWIF-HGNVRENIL 128
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFpHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 129 FGEKynhqryqhtvhVCGLQKD------LNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDA 201
Cdd:PRK11432 101 YGLK-----------MLGVPKEerkqrvKEALELVDLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 202 HVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 254
Cdd:PRK11432 170 NLRRSMREK-IRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
59-229 |
3.21e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.67 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL-----L-------GQMQL------QKGV--VAVNGPLAYVSQQAWI 118
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLipgarveGEILLdgediyDPDVdvVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 FHGNVRENILFGEKYNHQRyqhtvhvcglqkdlnslPYGDLTEIGER------------------GVNLSGGQRQRISLA 180
Cdd:COG1117 104 FPKSIYDNVAYGLRLHGIK-----------------SKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568956771 181 RAVYANRQLYLLDDPLSAVD----AHVgkhvfEECIKKtLKGK-TVVLVTHQLQ 229
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDpistAKI-----EELILE-LKKDyTIVIVTHNMQ 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
62-275 |
3.39e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.25 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAY--------------VSQQA--WIFHGNVR 124
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkPIDYsrkglmklresvgmVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLS 197
Cdd:PRK13636 102 QDVSFGavnlklpEDEVRKRVDNALKRTGIEHLKDKPTHC-----------LSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 198 AVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQFLE-SCDEVILLEDGEICEKGTHKELMEERG-------RYAKLIHN 267
Cdd:PRK13636 171 GLDP-MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEmlrkvnlRLPRIGHL 249
|
....*...
gi 568956771 268 LRGLQFKD 275
Cdd:PRK13636 250 MEILKEKD 257
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
677-908 |
4.07e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 63.71 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 677 FKVGTCPKDWPSRGEITFKDYRMRYRdntpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDE-- 754
Cdd:cd03220 10 YPTYKGGSSSLKKLGILGRKGEVGEF----WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 755 ---VDIcTVGLEDlrtKLTMIpqDPVLFVGTVrYNLDPlgshtDEMlwhvleRTFMRDTIM--KLPEKLQAEVtengENF 829
Cdd:cd03220 86 sslLGL-GGGFNP---ELTGR--ENIYLNGRL-LGLSR-----KEI------DEKIDEIIEfsELGDFIDLPV----KTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 830 SVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEF 907
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFD 223
|
.
gi 568956771 908 D 908
Cdd:cd03220 224 G 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
692-890 |
4.08e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYrdNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICT-------VGLED 764
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNqniyerrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 765 LRTKLTMIPQDPVLF----VGTVRYNLDPLGSHTDEMLWHVLERTfMRDTimKLPEKLQAEVTENGENFSVGERQLLCMA 840
Cdd:PRK14258 86 LRRQVSMVHPKPNLFpmsvYDNVAYGVKIVGWRPKLEIDDIVESA-LKDA--DLWDEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568956771 841 RALLRNSKIILLDEATASMDSKTDTLVQSTIKEAF--KSCTVLTIAHRLNTV 890
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
62-256 |
4.24e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.39 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLayVSQQAWifhGNVREN--ILFGEKYNhQRYQ 139
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA--ITDDNF---EKLRKHigIVFQNPDN-QFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 140 HTVH---VCGLQKdlNSLPYGDLTEIGERGVN--------------LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH 202
Cdd:PRK13648 99 SIVKydvAFGLEN--HAVPYDEMHRRVSEALKqvdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 203 VGKHVFEECIK-KTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 256
Cdd:PRK13648 177 ARQNLLDLVRKvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
708-914 |
4.54e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVdictvgledLRTKLT----------MIPQDPV 777
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN---------PCARLTpakahqlgiyLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 778 LFVG-TVRYN-LDPLGSHTDEMlwhvlertfmrdtimklpEKLQAEVTENGENFS---------VGERQLLCMARALLRN 846
Cdd:PRK15439 97 LFPNlSVKENiLFGLPKRQASM------------------QKMKQLLAALGCQLDldssagsleVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 847 SKIILLDEATASMD-SKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI------EFDKPEVLA 914
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIAlsgktaDLSTDDIIQ 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
62-254 |
5.08e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.64 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------------------PLAYVSQQAWIFHG 121
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkikevkrlrkeiGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENILFGEKYNHQRYQHTVHVCGLQKDLNSLPygdlTEIGERG-VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP----EDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 201 AHvGKHVFEECIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKEL 254
Cdd:PRK13645 183 PK-GEEDFINLFERLNKeyKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
707-873 |
5.82e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 707 LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIctvGLEDLRTKLTMI-PQD---PVLfvgT 782
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNamkPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 783 VRYNL----DPLGSHtDEMLWHVLERTFMRDtIMKLPEKlqaevtengeNFSVGERQLLCMARALLRNSKIILLDEATAS 858
Cdd:PRK13539 90 VAENLefwaAFLGGE-ELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....*
gi 568956771 859 MDSKTDTLVQSTIKE 873
Cdd:PRK13539 158 LDAAAVALFAELIRA 172
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
56-289 |
6.37e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.30 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------PLAYVSQQAWI------- 118
Cdd:PRK13637 15 GTPfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvKLSDIRKKVGLvfqypey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 --FHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDlnslPYGDLTEIgergvNLSGGQRQRISLARAVYANRQL 189
Cdd:PRK13637 95 qlFEETIEKDIAFGpinlglsEEEIENRVKRAMNIVGLDYE----DYKDKSPF-----ELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 190 YLLDDPLSAVDAHVGKHVFEEcIKKTLKGK--TVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGRYAK--- 263
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNK-IKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKEVETLESigl 244
|
250 260 270
....*....|....*....|....*....|....*
gi 568956771 264 -------LIHNLRGLQFKDPEHIYNV--AMVETLK 289
Cdd:PRK13637 245 avpqvtyLVRKLRKKGFNIPDDIFTIeeAKEEILK 279
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
66-255 |
6.86e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.44 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 66 SFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-----------------PLAYVSQQ-AWIFHGNVRENI 127
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFGEKY-------NHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD 200
Cdd:PRK10070 128 AFGMELaginaeeRREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 201 AHVGKHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELM 255
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
59-257 |
8.32e-11 |
|
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: 62.16 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQM--QLQKGVVAVNGplayvsqqawifhgnvrENILFGEKYNHQ 136
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-----------------EDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 137 R------YQHTVHVCGLqKDLNSLpygdlteigeRGVN--LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVF 208
Cdd:cd03217 76 RlgiflaFQYPPEIPGV-KNADFL----------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568956771 209 EEcIKKTL-KGKTVVLVTHQLQFLESC--DEVILLEDGEICEKGThKELMEE 257
Cdd:cd03217 145 EV-INKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGD-KELALE 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
708-922 |
8.60e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVglEDLRTKLTMIPQDPVLFVG-TVRYN 786
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 787 L-----------DPLGSHTDEMLWHVlertFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEA 855
Cdd:PRK11607 112 IafglkqdklpkAEIASRVNEMLGLV----HMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 856 TASMDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSAFA 922
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
692-916 |
8.74e-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: 65.59 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLV---EPASGTIIIdEVDIC-TVGLEDLRT 767
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRIIY-HVALCeKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 768 KL---------TMIPQDpVLFVG---TVRYNLDplgshtdEMLWHVLERTF-------MRDTIMK-LPE----------- 816
Cdd:TIGR03269 77 KVgepcpvcggTLEPEE-VDFWNlsdKLRRRIR-------KRIAIMLQRTFalygddtVLDNVLEaLEEigyegkeavgr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 817 --------KLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTV-LTIAHRL 887
Cdd:TIGR03269 149 avdliemvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|.
gi 568956771 888 NTVLN--CDLVLVMENGKVIEFDKPEVLAEK 916
Cdd:TIGR03269 229 PEVIEdlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
57-254 |
9.84e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.67 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 57 SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP---------------LAYVSQQAWIFHG 121
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDD 194
Cdd:PRK13652 95 TVEQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 195 PLSAVDAHVGKHV--FEECIKKTLkGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKEL 254
Cdd:PRK13652 164 PTAGLDPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
695-914 |
1.08e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.27 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 695 KDYRMR---YRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTM 771
Cdd:PRK15112 12 KTFRYRtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPV-----------LFVGTVRYNLDPLGSHTDEMLWHVLERTFMR-DTIMKLPEKLqaevtengenfSVGERQLLCM 839
Cdd:PRK15112 92 IFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHML-----------APGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 840 ARALLRNSKIILLDEATASMD-SKTDTLVQSTIK-EAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEF-DKPEVLA 914
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERgSTADVLA 239
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
62-296 |
1.26e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.88 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLI------SALLGQMQLQKGV--------------VAVNGPLAYVSQQAWIFHG 121
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEGKVtfhgknlyapdvdpVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENILFGEKYNhqryqhtvhvcGLQKDLNSLPYGDLTE----------IGERGVNLSGGQRQRISLARAVYANRQLYL 191
Cdd:PRK14243 106 SIYDNIAYGARIN-----------GYKGDMDELVERSLRQaalwdevkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 192 LDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGthkelmeerGRYAKLIhnlrgl 271
Cdd:PRK14243 175 MDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG---------GRYGYLV------ 238
|
250 260
....*....|....*....|....*
gi 568956771 272 QFKDPEHIYNvamvetlkeSPAQRD 296
Cdd:PRK14243 239 EFDRTEKIFN---------SPQQQA 254
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
59-257 |
1.29e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PL--------AYVSQQAWIFHgnvR 124
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllPLhararrgiGYLPQEASIFR---R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENIlfgekynhqrYQHTVHVCGLQKDLNSLPYGD-LTEIGER----------GVNLSGGQRQRISLARAVYANRQLYLLD 193
Cdd:PRK10895 93 LSV----------YDNLMAVLQIRDDLSAEQREDrANELMEEfhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 194 DPLSAVDAhvgKHVFEecIKKTLK-----GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:PRK10895 163 EPFAGVDP---ISVID--IKRIIEhlrdsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
418-526 |
1.32e-10 |
|
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: 63.33 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 418 IASMVSVLmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFF 497
Cdd:cd18572 44 LLSVLSGL-FSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLV 122
|
90 100 110
....*....|....*....|....*....|
gi 568956771 498 MVVFILVIMAAV-FPVVLVVLAGLAVIFLI 526
Cdd:cd18572 123 QLVGGLAFMFSLsWRLTLLAFITVPVIALI 152
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
692-908 |
1.32e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRL----VEPASGTIIIDEvdictvgledlRT 767
Cdd:COG0488 316 LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTVKLGE-----------TV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 768 KLTMIPQDpvlfvgtvRYNLDPlgshtDEMLWHVLERTFMRDTIMKL----------PEKLQAEVtengENFSVGERQLL 837
Cdd:COG0488 379 KIGYFDQH--------QEELDP-----DKTVLDELRDGAPGGTEQEVrgylgrflfsGDDAFKPV----GVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 838 CMARALLRNSKIILLDEAT-----ASMDSKTDTLvqstikEAFKScTVLTIAH-R--LNTVlnCDLVLVMENGKVIEFD 908
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTnhldiETLEALEEAL------DDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
64-257 |
1.33e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------PL-------AYV--SQQAWIFHGN--VRE 125
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprsPLdavkkgmAYIteSRRDNGFFPNfsIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKYNHQRYQHTVhvcGL------------QKDLNSLPYGDLTE-IGErgvnLSGGQRQRISLARAVYANRQLYLL 192
Cdd:PRK09700 361 NMAISRSLKDGGYKGAM---GLfhevdeqrtaenQRELLALKCHSVNQnITE----LSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 193 DDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRDDMSE 499
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
62-244 |
1.50e-10 |
|
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: 64.85 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLG----------------QMQLQ-------KGVVAVNGPLAYVSQQAwi 118
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASnirdterAGIVIIHQELTLVPELS-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 fhgnVRENILFGEKYNHQ----RYQHTVHVC-------GLQKDLNSLPYGDLteigergvnlSGGQRQRISLARAVYANR 187
Cdd:TIGR02633 95 ----VAENIFLGNEITLPggrmAYNAMYLRAknllrelQLDADNVTRPVGDY----------GGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 188 QLYLLDDPLSAVDAHVGKHVFEecIKKTLKGKTV--VLVTHQLQFLES-CDEVILLEDGE 244
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
708-915 |
1.60e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.41 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdiCTVGledlrtkltmipqdPVLFVGTvryNL 787
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN----GRVS--------------ALLELGA---GF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 788 DPlgSHTdemlwhVLERTFMRDTIMKLP-----EKLQ--AEVTENGE-------NFSVGERQLLCMARALLRNSKIILLD 853
Cdd:COG1134 100 HP--ELT------GRENIYLNGRLLGLSrkeidEKFDeiVEFAELGDfidqpvkTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 854 EATASMDS----KTDTLVQSTIKEAfksCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP-EVLAE 915
Cdd:COG1134 172 EVLAVGDAafqkKCLARIRELRESG---RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPeEVIAA 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
62-291 |
1.62e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWI---------------FHGNVREN 126
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAV 199
Cdd:PRK13647 101 VAFGpvnmgldKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 200 DAHVGKHVFEECIKKTLKGKTVVLVTHQLQF-LESCDEVILLEDGEICEKG-----THKELMEERGRYAKLIHNLrglqF 273
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLVAQI----F 245
|
250
....*....|....*...
gi 568956771 274 KDPEHIYNVAMVETLKES 291
Cdd:PRK13647 246 EDLPELGQSKLPLTVKEA 263
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
445-583 |
1.74e-10 |
|
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: 62.89 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 445 SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAV-FPVVLVVLAGLAVI 523
Cdd:cd18546 73 DLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLdPRLALVALAALPPL 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 524 FlILLRIFHRGVQEL--KQVENISRSpwFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEN 583
Cdd:cd18546 153 A-LATRWFRRRSSRAyrRARERIAAV--NADLQETLAGIRVVQAFRRERRNAERFAELSDDY 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
64-257 |
1.87e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.44 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVN-----------GP---------LAYVSQQAWIF-HGN 122
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPdgrgrakryIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENIL------FGEKYNHQRYQHTVHVCGLQKD-----LNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYL 191
Cdd:TIGR03269 382 VLDNLTeaigleLPDELARMKAVITLKMVGFDEEkaeeiLDKYPD-----------ELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 192 LDDPLSAVDAhVGKHVFEECIKKTLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:TIGR03269 451 LDEPTGTMDP-ITKVDVTHSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
706-931 |
2.36e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.02 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 706 PLVlDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA----SGTIIIDEVdicTVGLEDLRTKLT-MIPQDPvlfv 780
Cdd:PRK10418 17 PLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK---PVAPCALRGRKIaTIMQNP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 781 gtvRYNLDPLgsHTdeMLWHVLERTFMR---DTIMKLPEKLQAEVTENGE--------NFSVGERQLLCMARALLRNSKI 849
Cdd:PRK10418 89 ---RSAFNPL--HT--MHTHARETCLALgkpADDATLTAALEAVGLENAArvlklypfEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 850 ILLDEATASMDSktdtLVQSTIKEAFKSCT------VLTIAHRLNTVLNC-DLVLVMENGKVIEFDKPEVLAEKPDSAFA 922
Cdd:PRK10418 162 IIADEPTTDLDV----VAQARILDLLESIVqkralgMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
250
....*....|
gi 568956771 923 -MLLAAEVGL 931
Cdd:PRK10418 238 rSLVSAHLAL 247
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
692-910 |
2.58e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG----LED 764
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 765 LRTKLTMIPQDP--VLFVGTV----RYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKlqaevteNGENFSVGERQLLC 838
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVlkdvAFGPQNFGVSQEEAEALAREKLALVGISESLFEK-------NPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 839 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP 910
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKP 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
688-920 |
2.73e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.91 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 688 SRGEITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV------- 760
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 761 ------GLEDLRTKLTMIPQdpvlfvgtvRYNldpLGSHTdEMLWHVLE---------RTFMRDTIMKLPEKLQAEVTEN 825
Cdd:PRK10619 80 kvadknQLRLLRTRLTMVFQ---------HFN---LWSHM-TVLENVMEapiqvlglsKQEARERAVKYLAKVGIDERAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 826 GE---NFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLNC-DLVLVME 900
Cdd:PRK10619 147 GKypvHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVsSHVIFLH 226
|
250 260
....*....|....*....|
gi 568956771 901 NGKVIEFDKPEVLAEKPDSA 920
Cdd:PRK10619 227 QGKIEEEGAPEQLFGNPQSP 246
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
59-245 |
3.19e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.55 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL--AYVSQQAWIF-HGNVRENIL--FGEKY 133
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLriGYLPQEPPLDdDLTVLDTVLdgDAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 134 NHQRYQHTVHVCGLQKDLNSLPYGDL-TEIGERGV--------------------------NLSGGQRQRISLARAVYAN 186
Cdd:COG0488 91 ALEAELEELEAKLAEPDEDLERLAELqEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 187 RQLYLLDDP-----LSAVDAhvgkhvFEECIKKtLKGkTVVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:COG0488 171 PDLLLLDEPtnhldLESIEW------LEEFLKN-YPG-TVLVVSHDRYFLDRvATRILELDRGKL 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
692-918 |
3.35e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIIIDEVDICTVGLE--D 764
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 765 LRTKLTMIPQDPVLFVGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMK---LPEKLQAEVTENGENFSVGERQLLCMAR 841
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKkaaLWDEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 842 ALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSCTVLTIAHR-LNTVLNCDLVLVMENGKVIEFDKPEVLAEKPD 918
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
59-254 |
3.60e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.33 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISAL--LGQMQLQ---KGVVAVNGPLAY---------------VSQQAWI 118
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYsprtdtvdlrkeigmVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 FHGNVRENILFGEKYNHQRYQHTVHVcGLQKDLNSLPYGDltEIGER----GVNLSGGQRQRISLARAVYANRQLYLLDD 194
Cdd:PRK14239 98 FPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWD--EVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 195 PLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 254
Cdd:PRK14239 175 PTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
709-905 |
3.61e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTvGLEDLRTKLTMIPQDPVLFVG-TVRY 785
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkEIDFKS-SKEALENGISMVHQELNLVLQrSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 786 NLdPLGSHTDEMLWhVLERTFMRDTImKLPEKLQAEV--TENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK- 862
Cdd:PRK10982 93 NM-WLGRYPTKGMF-VDQDKMYRDTK-AIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKe 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 863 TDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 905
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
712-929 |
4.05e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 712 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI-------------IIDEVDICTVGLEDLR-TKLTMIPQDPV 777
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgADMAMIFQEPM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 778 LFVGTVRynldPLGSHTDEMLwhVLERTFMRDTIM----------KLPEKlQAEVTENGENFSVGERQLLCMARALLRNS 847
Cdd:PRK10261 115 TSLNPVF----TVGEQIAESI--RLHQGASREEAMveakrmldqvRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 848 KIILLDEATASMdsktDTLVQSTIKEAFK------SCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSA 920
Cdd:PRK10261 188 AVLIADEPTTAL----DVTIQAQILQLIKvlqkemSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHAPQHP 263
|
....*....
gi 568956771 921 FAMLLAAEV 929
Cdd:PRK10261 264 YTRALLAAV 272
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
692-931 |
4.37e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPLV---LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVG----LED 764
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 765 LRTKLTMIPQDP--VLFVGT----VRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVtengenfSVGERQLLC 838
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETvlkdVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFEL-------SGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 839 MARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEK 916
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
250
....*....|....*
gi 568956771 917 PDsafaMLLAAEVGL 931
Cdd:PRK13643 235 VD----FLKAHELGV 245
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
708-905 |
5.10e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.20 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDL----RTKLTMIPQdpvlfvgtv 783
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQ--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 784 RYNLDP--LGSHTDEM--LWHVLERTFMRDTIMKLPEKLQAE--VTENGENFSVGERQLLCMARALLRNSKIILLDEATA 857
Cdd:PRK10535 94 RYHLLShlTAAQNVEVpaVYAGLERKQRLLRAQELLQRLGLEdrVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568956771 858 SMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLNCDLVLVMENGKVI 905
Cdd:PRK10535 174 ALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-261 |
8.03e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLI-----------------SALLGQMQL--QKGVVAVNGPLAYVSQQAWIF 119
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmndkvsgyrysgDVLLGGRSIfnYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 HGNVRENILFGEKynhqryqhtVHVCGLQKDLNSLPYGDLTEIG----------ERGVNLSGGQRQRISLARAVYANRQL 189
Cdd:PRK14271 114 PMSIMDNVLAGVR---------AHKLVPRKEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 190 YLLDDPLSAVDAHVGKHVfEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELME-----ERGRY 261
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSspkhaETARY 261
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
62-255 |
8.40e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 8.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG-----------------NV 123
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhEVVTRSPQDGLANGivyisedrkrdglvlgmSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENI---------LFGEKYNHQRYQHTVhvcglqKDLNSL-----PYGDLTeIGergvNLSGGQRQRISLARAVYANRQL 189
Cdd:PRK10762 348 KENMsltalryfsRAGGSLKHADEQQAV------SDFIRLfniktPSMEQA-IG----LLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 190 YLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEIC-----EKGTHKELM 255
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMpEVLGMSDRILVMHEGRISgeftrEQATQEKLM 488
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
60-254 |
8.99e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.48 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 60 SVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAY-------VSQQAWI---------FHGN 122
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYdkkslleVRKTVGIvfqnpddqlFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENILFG-------EKYNHQRYQHTVHVCGLQKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:PRK13639 96 VEEDVAFGplnlglsKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 196 LSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 254
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
59-250 |
9.53e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPL--AYVSQQAWI-------------FHGNV 123
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYLdttlpltvnrflrLRPGT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 R-ENILFGEKynhqRYQHT-VHVCGLQKdlnslpygdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVD- 200
Cdd:PRK09544 97 KkEDILPALK----RVQAGhLIDAPMQK-------------------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDv 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568956771 201 -AHVGKHVFEECIKKTLkGKTVVLVTHQLQF-LESCDEVILLeDGEICEKGT 250
Cdd:PRK09544 154 nGQVALYDLIDQLRREL-DCAVLMVSHDLHLvMAKTDEVLCL-NHHICCSGT 203
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
61-245 |
1.12e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 60.05 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICG-NvGSGKSSLISALLGQMQLQKGVVAVNG-------P-------LAYVSQQAWIFHG-NVR 124
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGpN-GAGKTTLFNLITGFYRPTSGRILFDGrditglpPhriarlgIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFGekynhqryQHTVHVCGLQKDLNSLPYG------------------DLTEI-GERGVNLSGGQRQRISLARAVYA 185
Cdd:COG0411 98 ENVLVA--------AHARLGRGLLAALLRLPRArreereareraeellervGLADRaDEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 186 NRQLYLLDDPLSAVdAHVGKHVFEECIKK--TLKGKTVVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:COG0411 170 EPKLLLLDEPAAGL-NPEETEELAELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
713-887 |
1.14e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.60 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 713 NLNIQSGQTVGIVGRTGSGKSSLG--MALFrlVEPASGTIIIDEVDiCTVGLEDLRtKLTMIPQDPVLFVG-TVRYN--- 786
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLnlIAGF--LTPASGSLTLNGQD-HTTTPPSRR-PVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 787 -LDP---LGSHTDEMLWHVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATASMD-- 860
Cdd:PRK10771 95 gLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180
....*....|....*....|....*....
gi 568956771 861 --SKTDTLVQSTIKEafKSCTVLTIAHRL 887
Cdd:PRK10771 164 lrQEMLTLVSQVCQE--RQLTLLMVSHSL 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
62-244 |
1.20e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLG----------------QMQL-------QKGVVAVNGPLAYVSQQAwi 118
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifegeELQAsnirdteRAGIAIIHQELALVKELS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 fhgnVRENILFGEK--------YN--HQRYQHTVHvcGLQKDLNslPYgdlTEIGergvNLSGGQRQRISLARAVYANRQ 188
Cdd:PRK13549 99 ----VLENIFLGNEitpggimdYDamYLRAQKLLA--QLKLDIN--PA---TPVG----NLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 189 LYLLDDPLSAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDGE 244
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLD--IIRDLKahGIACIYISHKLnEVKAISDTICVIRDGR 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
59-255 |
1.21e-09 |
|
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: 59.71 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGK---VLGicGNvGSGKSSLISALLGQM-QLQKGVVAVNG-------------PLAYVS---QQAWI 118
Cdd:COG1119 16 KTILDDISWTVKPGEhwaILG--PN-GAGKSTLLSLITGDLpPTYGNDVRLFGerrggedvwelrkRIGLVSpalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 FHGNVRENIL---FG-----EKYN---HQRYQHTVHVCGLQkDLNSLPYGDLteigergvnlSGGQRQRISLARAVYANR 187
Cdd:COG1119 93 RDETVLDVVLsgfFDsiglyREPTdeqRERARELLELLGLA-HLADRPFGTL----------SQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 188 QLYLLDDPLSAVDAHvGKHVFEECIKK--TLKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 255
Cdd:COG1119 162 ELLILDEPTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
684-913 |
1.37e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 684 KDWPSRGEITFKDYRMRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLE 763
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 764 DLRTKLTMIPQD-PVLFVGTVRyNLDPLGSHTdemlWH-VLERTFMRDTimklpEKLQAEVTENG---------ENFSVG 832
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVR-ELVAIGRYP----WHgALGRFGAADR-----EKVEEAISLVGlkplahrlvDSLSGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 833 ERQLLCMARALLRNSKIILLDEATASMD--SKTDT--LVQSTIKEafKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEF 907
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDiaHQVDVlaLVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229
|
....*.
gi 568956771 908 DKPEVL 913
Cdd:PRK10575 230 GTPAEL 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
44-245 |
1.42e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 59.27 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 44 SDQGVASPEWQSgspKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIfhgnV 123
Cdd:cd03267 22 SLKSLFKRKYRE---VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL----R 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 124 RENILFGekynhQRYQ-----HTVHVCGLQKDLNSLPYG-------------DLTEIGERGV-NLSGGQRQRISLARAVY 184
Cdd:cd03267 95 RIGVVFG-----QKTQlwwdlPVIDSFYLLAAIYDLPPArfkkrldelsellDLEELLDTPVrQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 185 ANRQLYLLDDPLSAVDAhVGKHVFEECIKK--TLKGKTVVLVTHQLQFLES-CDEVILLEDGEI 245
Cdd:cd03267 170 HEPEILFLDEPTIGLDV-VAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
54-288 |
1.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.72 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 54 QSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-------PLAYVSQQAWIFHGN---- 122
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeeNLWDIRNKAGMVFQNpdnq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 -----VRENILFG-------------------EKYNHQRYQ-HTVHVcglqkdlnslpygdlteigergvnLSGGQRQRI 177
Cdd:PRK13633 98 ivatiVEEDVAFGpenlgippeeirervdeslKKVGMYEYRrHAPHL------------------------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 178 SLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKE-- 253
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNT-IKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEif 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568956771 254 ----LMEERG----RYAKLIHNLRGLQFKDPEHIYNV-AMVETL 288
Cdd:PRK13633 233 keveMMKKIGldvpQVTELAYELKKEGVDIPSDILTIdEMVNEL 276
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
708-920 |
1.91e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVgtvRYNL 787
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQ---RPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 788 DPLgSHTDEMLWHVLERTFM-----------RDTIMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEAT 856
Cdd:PRK14271 113 FPM-SIMDNVLAGVRAHKLVprkefrgvaqaRLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 857 ASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDSA 920
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
705-904 |
1.97e-09 |
|
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: 57.83 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 705 TPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED-LRTKLTMIPQDPV---LFV 780
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 781 G-TVRYNLDpLGSHtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIILLDEATASM 859
Cdd:cd03215 92 DlSVAENIA-LSSL-----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568956771 860 DSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKV 904
Cdd:cd03215 136 DVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
709-929 |
2.07e-09 |
|
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: 60.99 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIIIDEVDICTVGLEDLRTK--------LTMIPQDPV 777
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHgtwDGEIYWSGSPLKASNIRDTERAgiviihqeLTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 778 L---FVGTvryNLDPLGSHTDEMLWHVLERTFMRDtiMKLPEklqAEVTENGENFSVGERQLLCMARALLRNSKIILLDE 854
Cdd:TIGR02633 96 AeniFLGN---EITLPGGRMAYNAMYLRAKNLLRE--LQLDA---DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 855 ATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEkpDSAFAMLLAAEV 929
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSE--DDIITMMVGREI 242
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
61-257 |
2.38e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 59.68 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLG---QMQLQKGVVAVNG-PLAYVSQQAW----------IFHG----- 121
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGeDLLKLSEKELrkirgreiqmIFQDpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 N--------VRENILFGEKYNH-QRYQHTVHV---CGL---QKDLNSLPYgdlteigergvNLSGGQRQRISLARAVYAN 186
Cdd:COG0444 100 NpvmtvgdqIAEPLRIHGGLSKaEARERAIELlerVGLpdpERRLDRYPH-----------ELSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 187 RQLYLLDDPLSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELMEE 257
Cdd:COG0444 169 PKLLIADEPTTALDVTIQAQIlnlLKD-LQREL-GLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
707-929 |
2.84e-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: 60.11 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 707 LVLDGLNLNIQ-----SGQTVgIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDictvgLEDlRTKLTMIP-------- 773
Cdd:COG4148 9 LRRGGFTLDVDftlpgRGVTA-LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV-----LQD-SARGIFLPphrrrigy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 774 --QDPVLFVG-TVRYNLD------PLGSHTDEM--------LWHVLERTfmrdtimklPEKLqaevtengenfSVGERQL 836
Cdd:COG4148 82 vfQEARLFPHlSVRGNLLygrkraPRAERRISFdevvellgIGHLLDRR---------PATL-----------SGGERQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 837 LCMARALLRNSKIILLDEATASMD--SKTDTL--VQSTIKEAfkSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP- 910
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDlaRKAEILpyLERLRDEL--DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLa 219
|
250
....*....|....*....
gi 568956771 911 EVLAEKPDSAFAMLLAAEV 929
Cdd:COG4148 220 EVLSRPDLLPLAGGEEAGS 238
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
715-872 |
3.15e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.57 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 715 NIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDevdictvgLEDLRTKLTMIPQDpvlFVGTVRynlDPLGSHT 794
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE--------LDTVSYKPQYIKAD---YEGTVR---DLLSSIT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 795 DEMLWHvlerTFMRDTIMKlPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIK 872
Cdd:cd03237 87 KDFYTH----PYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
708-913 |
3.20e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIC---TVGLedLRTKLTMIPQDPVLFVG-TV 783
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqTAKI--MREAVAIVPEGRRVFSRmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 784 RYNLDPLGSHTDEMLWHV-LERTFmrdtimKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 862
Cdd:PRK11614 98 EENLAMGGFFAERDQFQErIKWVY------ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 863 TDTLVQSTIKEAF-KSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVL 913
Cdd:PRK11614 172 IIQQIFDTIEQLReQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
709-904 |
4.07e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALfrlvepaSGTIIIDEVDICTVGL------------EDLRTKLT----MI 772
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAGSHIELlgrtvqregrlaRDIRKSRAntgyIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 773 PQDPVLFVGTVRYNLdPLGSHTDEMLWHVLERTFMRdtiMKLPEKLQAeVTENG---------ENFSVGERQLLCMARAL 843
Cdd:PRK09984 93 QQFNLVNRLSVLENV-LIGALGSTPFWRTCFSWFTR---EQKQRALQA-LTRVGmvhfahqrvSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 844 LRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKV 904
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
120-254 |
4.11e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.66 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 120 HGNVRENILFGEKYN-------HQRYQHTVHVCGLQKDLNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLL 192
Cdd:PRK11000 89 HLSVAENMSFGLKLAgakkeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLL 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 193 DDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 254
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIE-ISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
61-227 |
4.32e-09 |
|
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: 60.15 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV--NGPLAYVSQQAWIFHGNVRENILFGEKYNHQRY 138
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 139 QhtvhvcGL-QKDLNS-LPYGDLTEIGERGVN----------LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKH 206
Cdd:TIGR00954 547 R------GLsDKDLEQiLDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY 620
|
170 180
....*....|....*....|.
gi 568956771 207 VFEECIKktlKGKTVVLVTHQ 227
Cdd:TIGR00954 621 MYRLCRE---FGITLFSVSHR 638
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
690-910 |
4.48e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.87 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 690 GEITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDIcTVGL---- 762
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI-PANLkkik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 763 --EDLRTKLTMIPQDP--VLFVGTVRYNL--DP--LGSHTDEMLWHVLERTfmrdTIMKLPEKLqaeVTENGENFSVGER 834
Cdd:PRK13645 84 evKRLRKEIGLVFQFPeyQLFQETIEKDIafGPvnLGENKQEAYKKVPELL----KLVQLPEDY---VKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 835 QLLCMARALLRNSKIILLDEATASMDSKTD----TLVQSTIKEAFKSctVLTIAHRLNTVLN-CDLVLVMENGKVIEFDK 909
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfiNLFERLNKEYKKR--IIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
.
gi 568956771 910 P 910
Cdd:PRK13645 235 P 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
709-905 |
4.58e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII--DEV------DICTVGLEDLRTKLTMIPQDPV--- 777
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVtfngpkSSQEAGIGIIHQELNLIPQLTIaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 778 LFVGtvRYNLDPLGShtdeMLWHVlertfMRDTIMKLPEKLQAEVTEN---GEnFSVGERQLLCMARALLRNSKIILLDE 854
Cdd:PRK10762 100 IFLG--REFVNRFGR----IDWKK-----MYAEADKLLARLNLRFSSDklvGE-LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 855 ATasmDSKTDTLVQS---TIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKVI 905
Cdd:PRK10762 168 PT---DALTDTETESlfrVIRElKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
62-254 |
6.87e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.20 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLaYVSQQAW--------IFH--------GNVRE 125
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVWdirhkigmVFQnpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFG---EKYNHQ----RYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSA 198
Cdd:PRK13650 102 DVAFGlenKGIPHEemkeRVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 199 VDAHvGKHVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL 254
Cdd:PRK13650 171 LDPE-GRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
59-245 |
7.05e-09 |
|
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: 56.89 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMqlqKGVVAVNGPLAYVSQQAWIFHGNVRENILF-GEKYNHQR 137
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYNGIPYKEFAEKYPGEIIYvSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 138 Y---QHTVH-VCGLQKDLNSlpygdlteigeRGVnlSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHvFEECIK 213
Cdd:cd03233 97 TltvRETLDfALRCKGNEFV-----------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE-ILKCIR 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 568956771 214 ---KTLKGKTVVLVTHQLQFLESC-DEVILLEDGEI 245
Cdd:cd03233 163 tmaDVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQ 198
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
168-256 |
7.69e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.54 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 168 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTHQ-LQFLESCDEVILLEDGEIC 246
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
90
....*....|
gi 568956771 247 EKGTHKELME 256
Cdd:PRK14267 228 EVGPTRKVFE 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
61-258 |
8.58e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.17 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLI---SALL----GQMQ-----------------------LQ-------KGVV 103
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtGTIEwifkdeknkkktkekekvleklvIQktrfkkiKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 104 AVNGPLAYVSQQA--WIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKD-LNSLPYgdlteigergvNLSGGQ 173
Cdd:PRK13651 102 EIRRRVGVVFQFAeyQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGLDESyLQRSPF-----------ELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 174 RQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKG-TH 251
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTY 250
|
....*..
gi 568956771 252 KELMEER 258
Cdd:PRK13651 251 DILSDNK 257
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
61-255 |
1.13e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.81 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------------PLAYVSQQAWIF-HGNVRE 125
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVFsRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 NILFGEKY-NHQRYQHTV-HVCGLQKDLnslpygdLTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHV 203
Cdd:PRK11614 100 NLAMGGFFaERDQFQERIkWVYELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 204 GKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELM 255
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
445-547 |
1.15e-08 |
|
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: 57.44 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 445 SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPV-VLVVLAGLAVI 523
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVlTLVTLAVVPLA 149
|
90 100
....*....|....*....|....
gi 568956771 524 FLILLRIfhrgvqeLKQVENISRS 547
Cdd:cd18551 150 FLIILPL-------GRRIRKASKR 166
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
61-227 |
1.19e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP------LAYVSQQAWIFHGN-------VRENI 127
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVGHRSginpyltLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 LFGEKYNHQRYQHTvHVCGLQK--DLNSLPYGdlteigergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGK 205
Cdd:PRK13540 96 LYDIHFSPGAVGIT-ELCRLFSleHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 568956771 206 HVFEECIKKTLKGKTVVLVTHQ 227
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
709-906 |
1.40e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEV--------DICTVGLEDLRTKLTMIPQdpvlfv 780
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttAALAAGVAIIYQELHLVPE------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 781 GTVRYNLdplgshtdeMLWH-------VLERTFMRDTIMKLpEKLQAEVTENG--ENFSVGERQLLCMARALLRNSKIIL 851
Cdd:PRK11288 94 MTVAENL---------YLGQlphkggiVNRRLLNYEAREQL-EHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 852 LDEATASMDSKTDTLVQSTIKEAFKSCTV-LTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRViLYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
707-918 |
1.81e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 707 LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFR---LVEP--ASGTIIIDEVDICTVGLE--DLRTKLTMIPQDPVLF 779
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 780 VGTVRYNL------DPLGSHTDEMLWHVLERTFMRDTImklPEKLQaevtENGENFSVGERQLLCMARALLRNSKIILLD 853
Cdd:PRK14243 104 PKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEV---KDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 854 EATASMDSKTDTLVQSTIKEAFKSCTVLTIAHRLNTV---------LNCDLVLV-MENGKVIEFDKPEVLAEKPD 918
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAarvsdmtafFNVELTEGgGRYGYLVEFDRTEKIFNSPQ 251
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
701-910 |
1.81e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 701 YRDNTP---LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEV----DICTVG------------ 761
Cdd:PRK13631 31 FDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdKKNNHElitnpyskkikn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 762 LEDLRTKLTMIPQDP--VLFVGTVRYNL--DP--LGSHTDE---MLWHVLERTFMRDTIMKlpeklqaevtENGENFSVG 832
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDImfGPvaLGVKKSEakkLAKFYLNKMGLDDSYLE----------RSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 833 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKP 910
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
687-886 |
2.00e-08 |
|
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: 58.22 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 687 PSRGEITFKDYRMRYrDNTPLV-------LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdict 759
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 760 vgledlRTKLTMIPQDPVLFVGTVR----YnldPLGShtDEMLwhvlERTFMRDTIMKLPEKLQAE--VTENG------- 826
Cdd:TIGR00954 514 ------KGKLFYVPQRPYMTLGTLRdqiiY---PDSS--EDMK----RRGLSDKDLEQILDNVQLThiLEREGgwsavqd 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 827 --ENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAfkSCTVLTIAHR 886
Cdd:TIGR00954 579 wmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
692-903 |
2.22e-08 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 53.99 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEvdictvgledlRTKLTM 771
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQdpvlfvgtvrynldplgshtdemlwhvlertfmrdtimklpeklqaevtengenFSVGERQLLCMARALLRNSKIIL 851
Cdd:cd03221 68 FEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 852 LDEATASMDSKTDTLVQSTIKEaFKsCTVLTIAH-R--LNTVlnCDLVLVMENGK 903
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE-YP-GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
59-272 |
2.27e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.15 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP--LAYVSQQAWIFHGNVREN------ILFG 130
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLLAQNattpgdITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 131 EKYNHQRYQHTVHVCGLQKD-----LNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVG 204
Cdd:PRK10253 100 ELVARGRYPHQPLFTRWRKEdeeavTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 205 KHVFE--ECIKKTlKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEergryAKLIHNLRGLQ 272
Cdd:PRK10253 180 IDLLEllSELNRE-KGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT-----AELIERIYGLR 244
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
52-290 |
2.70e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 56.25 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 52 EWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPlAYVSQQAW--------IFH--- 120
Cdd:PRK13642 13 KYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrkigmVFQnpd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 121 -----GNVRENILFG-EKYNHQRYQHTVHVCGLQKDLNSLPYGDlteigERGVNLSGGQRQRISLARAVYANRQLYLLDD 194
Cdd:PRK13642 92 nqfvgATVEDDVAFGmENQGIPREEMIKRVDEALLAVNMLDFKT-----REPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 195 PLSAVDAhVGKHVFEECIKKtLKGK---TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL------MEERGR----Y 261
Cdd:PRK13642 167 STSMLDP-TGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELfatsedMVEIGLdvpfS 244
|
250 260 270
....*....|....*....|....*....|
gi 568956771 262 AKLIHNLRGLQFKDPE-HIYNVAMVETLKE 290
Cdd:PRK13642 245 SNLMKDLRKNGFDLPEkYLSEDELVELLAD 274
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
411-566 |
3.10e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 56.42 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 411 HMYQLVYIASMVsVLMFGIIKGFTFTNTTLM---ASSSLHN-RV--FNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVR 484
Cdd:cd18565 49 PRGQLWLLGGLT-VAAFLLESLFQYLSGVLWrrfAQRVQHDlRTdtYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 485 LPFHAENFLQQFFMVVFILVIMA------AVFPVVLV-VLAGLAVIFLILLRIFHRGVQElkQVENISrspwfSHITSSI 557
Cdd:cd18565 128 LDDGANSIIRVVVTVLGIGAILFylnwqlALVALLPVpLIIAGTYWFQRRIEPRYRAVRE--AVGDLN-----ARLENNL 200
|
....*....
gi 568956771 558 QGLGVIHAY 566
Cdd:cd18565 201 SGIAVIKAF 209
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
427-618 |
3.29e-08 |
|
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: 55.95 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 427 FGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIM 506
Cdd:cd18576 52 FSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 507 AAVFP-VVLVVLAGLAVIFLIlLRIFHRGVQEL-KQV-ENISRSpwFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDEn 583
Cdd:cd18576 132 FFISWkLTLLMLATVPVVVLV-AVLFGRRIRKLsKKVqDELAEA--NTIVEETLQGIRVVKAFTREDYEIERYRKALER- 207
|
170 180 190
....*....|....*....|....*....|....*
gi 568956771 584 sshllYFNCALRwFALRMDILMNIVTFVVALLVTL 618
Cdd:cd18576 208 -----VVKLALK-RARIRALFSSFIIFLLFGAIVA 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
64-258 |
3.78e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQ-KGVVAVNG-PLAYVSQQAWIFHG--NVRENilfgekynhQRYQ 139
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkPVDIRNPAQAIRAGiaMVPED---------RKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 140 HTVHVCGLQKD-----LNSLPY-GDLTEIGERGV--------------------NLSGGQRQRISLARAVYANRQLYLLD 193
Cdd:TIGR02633 349 GIVPILGVGKNitlsvLKSFCFkMRIDAAAELQIigsaiqrlkvktaspflpigRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 194 DPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
54-243 |
3.79e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 54 QSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--------PLAY------VSQQ-AWI 118
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhKLAAqlgigiIYQElSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 FHGNVRENILFGE--------------KYNHQRYQHTVHVCGLQKDLNslpygdlteigERGVNLSGGQRQRISLARAVY 184
Cdd:PRK09700 93 DELTVLENLYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 185 ANRQLYLLDDPLSAVDAHVGKHVFeeCIKKTLK--GKTVVLVTHQL-QFLESCDEVILLEDG 243
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLF--LIMNQLRkeGTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
57-249 |
3.98e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.48 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 57 SPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQmqLQKGVVAVNGPLAY--VSQQAWIFHGNVRENILFGEK-- 132
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGI--LPAGVRQTAGRVLLdgKPVAPCALRGRKIATIMQNPRsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 133 YN--HQRYQHTVHVC---GLQKDLNSLPYGdLTEIG----ERGVNL-----SGGQRQRISLARAVYANRQLYLLDDPLSA 198
Cdd:PRK10418 92 FNplHTMHTHARETClalGKPADDATLTAA-LEAVGlenaARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568956771 199 VDAHVGKHVFE--ECIKKTlKGKTVVLVTHQLQFLESC-DEVILLEDGEICEKG 249
Cdd:PRK10418 171 LDVVAQARILDllESIVQK-RALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
708-918 |
4.15e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.12 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIidevdictvgledlrtkltmipQDPVLFVGTVrynl 787
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------------------RNGKLRIGYV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 788 dPLGSHTDEMLWHVLERtFMR-------DTIMKLPEKLQAE--VTENGENFSVGERQLLCMARALLRNSKIILLDEATAS 858
Cdd:PRK09544 73 -PQKLYLDTTLPLTVNR-FLRlrpgtkkEDILPALKRVQAGhlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 859 MDSKTDTLVQSTIKEAFK--SCTVLTIAHRLNTVL-NCDLVLVMeNGKVIEFDKPEVLAEKPD 918
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
59-228 |
5.21e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALlGQMQLQKGVVAVNGPLAYVSQQAW--------------------- 117
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYerrvnlnrlrrqvsmvhpkpn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 118 IFHGNVRENILFGEKYNHQRYQhtVHVCGLQKdlNSLPYGDL-----TEIGERGVNLSGGQRQRISLARAVYANRQLYLL 192
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVGWRPK--LEIDDIVE--SALKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 568956771 193 DDPLSAVDAHVGKHVFEECIKKTLKGK-TVVLVTHQL 228
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
708-912 |
5.42e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGlEDLRTKLTMIPQD-------PVL 778
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkPVRIRSPR-DAIRAGIAYVPEDrkgeglvLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 779 fvgTVRYN-----LDPLGSHTdeMLWHVLERTFMRDTIMKL---PEKLQAEVTengeNFSVGERQLLCMARALLRNSKII 850
Cdd:COG1129 346 ---SIRENitlasLDRLSRGG--LLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 851 LLDEATASMD--SKTDtlVQSTIKE-AFKSCTVLTIAHRLNTVL-NCDLVLVMENGKVI-EFDKPEV 912
Cdd:COG1129 417 ILDEPTRGIDvgAKAE--IYRLIRElAAEGKAVIVISSELPELLgLSDRILVMREGRIVgELDREEA 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
65-259 |
6.00e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 65 ISFVVRKGKVLGICGNVGSGKSSLISALLGqMQLQKGVVAVNG-PL------------AYVSQQAwifhgnvreNILFGE 131
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGqPLeawsaaelarhrAYLSQQQ---------TPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 132 KYNH--QRYQHT-VHVCGLQKDLN----SLPYGDLTEigeRGVN-LSGGQRQRISLA-------RAVYANRQLYLLDDPL 196
Cdd:PRK03695 85 PVFQylTLHQPDkTRTEAVASALNevaeALGLDDKLG---RSVNqLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 197 SAVDahVGKHVFEECIKKTL--KGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERG 259
Cdd:PRK03695 162 NSLD--VAQQAALDRLLSELcqQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
64-255 |
6.25e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.80 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PL-----AYVSQQA-WIFHG-----NVRENI---- 127
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhPLhfgdySYRSQRIrMIFQDpstslNPRQRIsqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 128 ---------LFGEKYNHQRYQhTVHVCGLQKD-LNSLPYGdlteigergvnLSGGQRQRISLARAVYANRQLYLLDDPLS 197
Cdd:PRK15112 111 dfplrlntdLEPEQREKQIIE-TLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 198 AVDAHVGKHVFEECIKKTLK-GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELM 255
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
62-263 |
6.51e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.44 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAWIfHGNVR--ENI-LFGekynhqry 138
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGL-NGQLTgiENIeLKG-------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 139 qhtvHVCGLQKDL------NSLPYGDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSavdahVGKHVF-EE 210
Cdd:PRK13545 111 ----LMMGLTKEKikeiipEIIEFADIGKFIYQPVkTYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQTFtKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 211 CIKK----TLKGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGRYAK 263
Cdd:PRK13545 182 CLDKmnefKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
65-245 |
6.75e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 56.34 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 65 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWifhgnvRENI--------LFGEKYNH 135
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqPVTADNREAY------RQLFsavfsdfhLFDRLLGL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 136 QRYQHTVHVcglQKDLNSLPYGDLTEIgERG----VNLSGGQRQRISLARAVYANRQLYLLD------DPlsavdahVGK 205
Cdd:COG4615 425 DGEADPARA---RELLERLELDHKVSV-EDGrfstTDLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568956771 206 HVFEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEI 245
Cdd:COG4615 494 RVFYTELLPELKarGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
53-245 |
7.26e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAY-------------VSQQAWI 118
Cdd:PRK15439 18 SKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnPCARltpakahqlgiylVPQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 119 FHG-NVRENILFG---EKYNHQRYQHTVHVCGLQKDLNSlPYGDLtEIGErgvnlsggqRQRISLARAVYANRQLYLLDD 194
Cdd:PRK15439 98 FPNlSVKENILFGlpkRQASMQKMKQLLAALGCQLDLDS-SAGSL-EVAD---------RQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 195 PLSAVDAHVGKHVFEEcIKKTL-KGKTVVLVTHQL-QFLESCDEVILLEDGEI 245
Cdd:PRK15439 167 PTASLTPAETERLFSR-IRELLaQGVGIVFISHKLpEIRQLADRISVMRDGTI 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
71-231 |
7.92e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.38 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 71 KGKVLGICGNVGSGKSSLISALLGQMQLQ-KGVVAVNGPLAYVSQQAWIFHgnvrenilfgekynhqryqhtvhvcglqk 149
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 150 dlnslpygdlTEIGERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEC------IKKTLKGKTVVL 223
Cdd:smart00382 52 ----------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllLLKSEKNLTVIL 121
|
....*...
gi 568956771 224 VTHQLQFL 231
Cdd:smart00382 122 TTNDEKDL 129
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
56-290 |
8.68e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.13 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 56 GSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVA----VNG-PLAYVSQQ----------AWIFH 120
Cdd:PRK11022 17 SAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAekleFNGqDLQRISEKerrnlvgaevAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 121 G---------NVRENILFGEKYnHQ------RYQHTVHVCGL------QKDLNSLPYgdlteigergvNLSGGQRQRISL 179
Cdd:PRK11022 97 DpmtslnpcyTVGFQIMEAIKV-HQggnkktRRQRAIDLLNQvgipdpASRLDVYPH-----------QLSGGMSQRVMI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 180 ARAVYANRQLYLLDDPLSAVDAHVGKHVFE---ECIKKtlKGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELm 255
Cdd:PRK11022 165 AMAIACRPKLLIADEPTTALDVTIQAQIIElllELQQK--ENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI- 241
|
250 260 270
....*....|....*....|....*....|....*
gi 568956771 256 eergryaklihnlrglqFKDPEHIYNVAMVETLKE 290
Cdd:PRK11022 242 -----------------FRAPRHPYTQALLRALPE 259
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
55-242 |
8.72e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.56 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 55 SGSPKSVLHNISFVvrKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------------PLAYVSQQAWIFHG- 121
Cdd:TIGR01257 941 SGRPAVDRLNITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 NVRENILFGEKYNHQRYQHTvhvcglQKDLNSLpygdLTEIG------ERGVNLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEA------QLEMEAM----LEDTGlhhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568956771 196 LSAVDAHVGKHVFEECIKKTlKGKTVVLVTHQLqflescDEVILLED 242
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHM------DEADLLGD 1128
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
69-244 |
8.74e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 54.34 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 69 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-LAYVSQQAWI-FHGNVREnILFG---EKYNHQRYQHTVh 143
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYIKAdYEGTVRD-LLSSitkDFYTHPYFKTEI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 144 vcglqkdLNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikkt 215
Cdd:cd03237 100 -------AKPL---QIEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaSKVIRRFAEN----- 164
|
170 180
....*....|....*....|....*....
gi 568956771 216 lKGKTVVLVTHQLQFLESCDEVILLEDGE 244
Cdd:cd03237 165 -NEKTAFVVEHDIIMIDYLADRLIVFEGE 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
59-258 |
9.66e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQK-GVVAVNG-PLAYVSQQAWIFHG--------------- 121
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGkPVKIRNPQQAIAQGiamvpedrkrdgivp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 --NVRENIL--------FGEKYNHQRYQHTVhvcglQKDLNSL----PYGDLtEIGergvNLSGGQRQRISLARAVYANR 187
Cdd:PRK13549 355 vmGVGKNITlaaldrftGGSRIDDAAELKTI-----LESIQRLkvktASPEL-AIA----RLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 188 QLYLLDDPLSAVDahVG-KHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:PRK13549 425 KILILDEPTRGID--VGaKYEIYKLINQLVQqGVAIIVISSELpEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
709-860 |
1.09e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.18 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTvGLEDLRTKLTMIPQDPVLF-----VGTV 783
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFhhltvAEHI 1024
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 784 RYNLDPLGSHTDEMLWHVleRTFMRDTimklpeKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMD 860
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEM--EAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
392-523 |
1.09e-07 |
|
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: 54.40 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 392 SQNNKTACNVDQTLQDTKHHMYQLVYIAsmVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLM 471
Cdd:cd18577 30 TDFGSGESSPDEFLDDVNKYALYFVYLG--IGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELT 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 472 NRFSKDMDELDV----RLPFhaenFLQQFFMVV------FI------LVIMaAVFPVVLVVLAGLAVI 523
Cdd:cd18577 108 SRLTSDTNLIQDgigeKLGL----LIQSLSTFIagfiiaFIyswkltLVLL-ATLPLIAIVGGIMGKL 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
61-255 |
1.15e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQM---QLQKGV-----VAVNG-PLAYV---------------SQQA 116
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGArvtgdVTLNGePLAAIdaprlarlravlpqaAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 117 WIFhgNVRENILFGeKYNH-QRYQHTVHVCGLQKDlNSLPYGDLTEIGERGVN-LSGGQRQRISLARAVyanRQLY---- 190
Cdd:PRK13547 96 FAF--SAREIVLLG-RYPHaRRAGALTHRDGEIAW-QALALAGATALVGRDVTtLSGGELARVQFARVL---AQLWpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 191 --------LLDDPLSAVD-AHvgKHVFEECIKKTLK--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELM 255
Cdd:PRK13547 169 aaqpprylLLDEPTAALDlAH--QHRLLDTVRRLARdwNLGVLAIVHDPNLaARHADRIAMLADGAIVAHGAPADVL 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
62-244 |
1.21e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG--------------NVREN 126
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkPVRIRSPRDAIALGigmvhqhfmlvpnlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFGEKynhqryqhtvHVCGLQKDLNSLpYGDLTEIGER-GVN---------LSGGQRQRISLARAVYANRQLYLLDDPl 196
Cdd:COG3845 101 IVLGLE----------PTKGGRLDRKAA-RARIRELSERyGLDvdpdakvedLSVGEQQRVEILKALYRGARILILDEP- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 568956771 197 SAV--DAHVgKHVFEecIKKTLK--GKTVVLVTHQLQ-FLESCDEVILLEDGE 244
Cdd:COG3845 169 TAVltPQEA-DELFE--ILRRLAaeGKSIIFITHKLReVMAIADRVTVLRRGK 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
692-905 |
1.56e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.73 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRdNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLrtkLTM 771
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQD-------PVLFVGTV---RYN----LDPLGSHTDEMLWHVLERTFMrdtimklpekLQAEVTENGEnFSVGERQLL 837
Cdd:PRK15056 83 VPQSeevdwsfPVLVEDVVmmgRYGhmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQKKRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 838 CMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAF-KSCTVLTIAHRLNTVLN-CDLVlVMENGKVI 905
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYT-VMVKGTVL 220
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
416-565 |
1.74e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 53.67 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 416 VYIASMVSVLMFGIIKGFTFTNTTLMASSS----LHNRVFNKIVRSPMSFFDTTPTGRLMnrfsKDMDELD-VRlpfhae 490
Cdd:cd18783 43 VLTIGVVIALLFEGILGYLRRYLLLVATTRidarLALRTFDRLLSLPIDFFERTPAGVLT----KHMQQIErIR------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 491 NFL-QQFFMVVF----ILVIMAAVF----PVVLVVLAGLAVIFLIL---LRIFHRGVQELKQVEnISRSpwfSHITSSIQ 558
Cdd:cd18783 113 QFLtGQLFGTLLdatsLLVFLPVLFfyspTLALVVLAFSALIALIIlafLPPFRRRLQALYRAE-GERQ---AFLVETVH 188
|
....*..
gi 568956771 559 GLGVIHA 565
Cdd:cd18783 189 GIRTVKS 195
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
62-238 |
1.78e-07 |
|
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: 51.94 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLgqmqlqkgvvAVNGPLAYVSqqawifhgnvrenilFGEKYNHQRyqhT 141
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------YASGKARLIS---------------FLPKFSRNK---L 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 142 VHVCGLQKdLNSLPYGDLTeIGERGVNLSGGQRQRISLARAVYAN--RQLYLLDDPLSAVDaHVGKHVFEECIKKTL-KG 218
Cdd:cd03238 63 IFIDQLQF-LIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLH-QQDINQLLEVIKGLIdLG 139
|
170 180
....*....|....*....|
gi 568956771 219 KTVVLVTHQLQFLESCDEVI 238
Cdd:cd03238 140 NTVILIEHNLDVLSSADWII 159
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
446-614 |
1.95e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 53.69 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 446 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvRLPFHAenfLQQFFMVVFILVIMAAVFPVVLVVLAGLAVI-- 523
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVE-RLIADG---IPQGITNVLTLVGVAIILFSINPKLALLTLIpi 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 524 -FLILL-RIFHRGVQEL-KQVENISrspwfSHITS----SIQGLGVIHAYDKKDDCISKFKTLNDEnsshllYFNCALRw 596
Cdd:cd18778 151 pFLALGaWLYSKKVRPRyRKVREAL-----GELNAllqdNLSGIREIQAFGREEEEAKRFEALSRR------YRKAQLR- 218
|
170 180
....*....|....*....|..
gi 568956771 597 fALRmdiLMNI----VTFVVAL 614
Cdd:cd18778 219 -AMK---LWAIfhplMEFLTSL 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
708-911 |
3.08e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVL--------F 779
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgditvqeL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 780 VGTVRYNLDPLGSHTDEMLWHVLERTFMRDTIMKLpeklqaeVTENGENFSVGERQLLCMARALLRNSKIILLDEATASM 859
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHL-------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 860 D--SKTDTLVQSTIKEAFKSCTVLTIAHRLNTVLNCDLVLV-MENGKVIEFDKPE 911
Cdd:PRK10253 175 DisHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIaLREGKIVAQGAPK 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
69-244 |
3.16e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 69 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQqaWI---FHGNVRENILF-GEKYNHQRYQHTVhv 144
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLLRSiTDDLGSSYYKSEI-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 145 cglqkdLNSLpygDLTEIGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikktl 216
Cdd:PRK13409 438 ------IKPL---QLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE------ 502
|
170 180
....*....|....*....|....*...
gi 568956771 217 KGKTVVLVTHQLQFLESCDEVILLEDGE 244
Cdd:PRK13409 503 REATALVVDHDIYMIDYISDRLMVFEGE 530
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
65-258 |
3.28e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 65 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWIFHG-----------------NVREN 126
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkaegiipvhSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 127 ILFGEKYNHQRYQHTVHvcGLQKDLNSLPYGDLTEIGERG-----VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDa 201
Cdd:PRK11288 352 INISARRHHLRAGCLIN--NRWEAENADRFIRSLNIKTPSreqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID- 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 202 hVG-KHVFEECIKKTLK-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:PRK11288 429 -VGaKHEIYNVIYELAAqGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQATERQ 487
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
424-537 |
3.91e-07 |
|
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: 52.64 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 424 VLMFGIIKGFTFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELD----VRLPFHAENFL 493
Cdd:cd18780 49 LGVVLIGSIATFLRSWLFTLAGervvarLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQnavtVNLSMLLRYLV 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568956771 494 QQFFMVVFILV-------IMAAVFPVVLVVlaglAVIFLILLRIFHRGVQE 537
Cdd:cd18780 129 QIIGGLVFMFTtswkltlVMLSVVPPLSIG----AVIYGKYVRKLSKKFQD 175
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
53-259 |
5.97e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAY-------VSQQA-------- 116
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkPLDYskrgllaLRQQVatvfqdpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 117 -WIFHGNVRENILFgekynhqryqhTVHVCGLQKDLNSLPYGD-LTEIGERGVN------LSGGQRQRISLARAVYANRQ 188
Cdd:PRK13638 88 qQIFYTDIDSDIAF-----------SLRNLGVPEAEITRRVDEaLTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956771 189 LYLLDDPLSAVDAhVGKHVFEECIKKTL-KGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKG------THKELMEERG 259
Cdd:PRK13638 157 YLLLDEPTAGLDP-AGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
61-243 |
6.31e-07 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 51.28 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAV---NGP------------------LAYVSQ----- 114
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvdlaqaspreilalrrrtIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 115 ----------QAWIFHGnvrenilFGEKYNHQRYQHTVHVCGLQKDLNSLPygdlteigerGVNLSGGQRQRISLARAVY 184
Cdd:COG4778 106 prvsaldvvaEPLLERG-------VDREEARARARELLARLNLPERLWDLP----------PATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 185 ANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDEVILLEDG 243
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
401-559 |
7.25e-07 |
|
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: 52.13 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 401 VDQTLQDTKHHMYQLVYIASMVSVLMFGI---IKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRF-SK 476
Cdd:cd18555 29 IDNVIVPGNLNLLNVLGIGILILFLLYGLfsfLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAnSN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 477 DMdeldVRlpfhaeNFLQQ--------FFMVVFILVIMaAVFPVVL--VVLAGLAVIFLILLrIFHRGVQELKQVENISR 546
Cdd:cd18555 109 VY----IR------QILSNqvisliidLLLLVIYLIYM-LYYSPLLtlIVLLLGLLIVLLLL-LTRKKIKKLNQEEIVAQ 176
|
170
....*....|...
gi 568956771 547 SPWFSHITSSIQG 559
Cdd:cd18555 177 TKVQSYLTETLYG 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
709-904 |
7.68e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA-SGTIIID--EVDICTVgLEDLRTKLTMIPQD-------PVL 778
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINgkPVDIRNP-AQAIRAGIAMVPEDrkrhgivPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 779 FVGTvRYNLDPLGSHTDEM-LWHVLERTFMRDTIMKLPEKLQAEVTENGeNFSVGERQLLCMARALLRNSKIILLDEATA 857
Cdd:TIGR02633 355 GVGK-NITLSVLKSFCFKMrIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568956771 858 SMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKV 904
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
415-565 |
7.90e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 51.82 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 415 LVYIASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSkdmdELD-VRlpfhaeNFL 493
Cdd:cd18782 46 VVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS----ELDtIR------GFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 494 QQ---------FFMVVFILVIMAAVFPVVLVVLAGLAVIFLILLrIFHRGVQELKQVENISRSPWFSHITSSIQGLGVIH 564
Cdd:cd18782 116 TGtalttlldvLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF-LFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVK 194
|
.
gi 568956771 565 A 565
Cdd:cd18782 195 A 195
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
410-578 |
8.22e-07 |
|
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: 51.68 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 410 HHMYQLVYIASmVSVLMFGIIK-GFTFTNTTLMA--SSSLHNRV----FNKIVRSPMSFFDTTPTGRLMNRFSkdmDELD 482
Cdd:cd18570 35 SGDINLLNIIS-IGLILLYLFQsLLSYIRSYLLLklSQKLDIRLilgyFKHLLKLPLSFFETRKTGEIISRFN---DANK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 483 VRlpfhaeNFLQQ--------FFMVVFILVIMAA----VFPVVLVVLAGLAVIFLILLRIFHRGVQELKQVENISRspwf 550
Cdd:cd18570 111 IR------EAISSttislfldLLMVIISGIILFFynwkLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELN---- 180
|
170 180
....*....|....*....|....*...
gi 568956771 551 SHITSSIQGLGVIHAYDKKDDCISKFKT 578
Cdd:cd18570 181 SYLIESLKGIETIKSLNAEEQFLKKIEK 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
708-929 |
8.65e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 52.01 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMipQDPVLF-----VGT 782
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVF--QHYALFrhmtvFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 783 VRYNLDPLGSHtdemlwhvlER---TFMRDTIMKLPEKLQAEVTEN--GENFSVGERQLLCMARALLRNSKIILLDEATA 857
Cdd:PRK10851 95 IAFGLTVLPRR---------ERpnaAAIKAKVTQLLEMVQLAHLADryPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 858 SMDSKTDTLVQSTIK---EAFKSCTVLTIAHRLNTVLNCDLVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAEV 929
Cdd:PRK10851 166 ALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEV 240
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
704-906 |
8.98e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 704 NTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALfrLVEPA----SGTIIIDEVDICTVGLEDlRTKLTMIP--QDPV 777
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESILDLEPEE-RAHLGIFLafQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 778 LFVGT-------VRYN----------LDPLgshtdEMLWHVLERtfmrdtiMKLPEKLQAEVTEN-GENFSVGER---QL 836
Cdd:CHL00131 95 EIPGVsnadflrLAYNskrkfqglpeLDPL-----EFLEIINEK-------LKLVGMDPSFLSRNvNEGFSGGEKkrnEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 837 LCMAralLRNSKIILLDEATASMDskTDTL--VQSTIKEAFKSCT-VLTIAH--RLNTVLNCDLVLVMENGKVIE 906
Cdd:CHL00131 163 LQMA---LLDSELAILDETDSGLD--IDALkiIAEGINKLMTSENsIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
71-238 |
9.26e-07 |
|
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: 49.67 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 71 KGKVLGICGNVGSGKSSLISALLgqmqlqkgvvavngplayvsqqawifhgnvrenILFGEKYNHQRYQHTVHvCGLQKd 150
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG---------------------------------LALGGAQSATRRRSGVK-AGCIV- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 151 lnslPYGDLTEIGERgVNLSGGQRQRISLARAV----YANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTH 226
Cdd:cd03227 65 ----AAVSAELIFTR-LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
170
....*....|..
gi 568956771 227 QLQFLESCDEVI 238
Cdd:cd03227 140 LPELAELADKLI 151
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
699-918 |
9.37e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 699 MRYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEVDICTV---GLEDLRTKLTM 771
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggqiAPDHGEILFDGENIPAMsrsRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 772 IPQDPVLFVG-TVRYNLD-PLGSHTDemlwhvLERTFMRDTIMKlpeKLQAEVTENGEN-----FSVGERQLLCMARALL 844
Cdd:PRK11831 89 LFQSGALFTDmNVFDNVAyPLREHTQ------LPAPLLHSTVMM---KLEAVGLRGAAKlmpseLSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 845 RNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPD 918
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
59-245 |
1.00e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG--PLAYVSQQAWIF----HGNVRENILFGEK 132
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQHQLEFlradESPLQHLARLAPQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 133 YNHQRYQHTVHVCGLQKDlnslpygDLTEIGERgvnLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECI 212
Cdd:PRK10636 405 ELEQKLRDYLGGFGFQGD-------KVTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI 474
|
170 180 190
....*....|....*....|....*....|....
gi 568956771 213 KktLKGKTVVlVTHQLQFLES-CDEVILLEDGEI 245
Cdd:PRK10636 475 D--FEGALVV-VSHDRHLLRStTDDLYLVHDGKV 505
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
65-254 |
1.06e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.28 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 65 ISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAWI---------FHgnvreniLF----- 129
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkPVTAEQPEDYRklfsavftdFH-------LFdqllg 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 130 --GEKYNHQRYQHTVHVCGLQKDLnSLPYGDLTEIgergvNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVgKHV 207
Cdd:PRK10522 415 peGKPANPALVEKWLERLKMAHKL-ELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RRE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568956771 208 FEECIKKTLK--GKTVVLVTHQLQFLESCDEVILLEDGEICE-KGTHKEL 254
Cdd:PRK10522 488 FYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
169-254 |
1.10e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 51.07 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 169 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAhVGKHVFEECIKKTLKGKTVVLVTH-QLQFLESCDEVILLEDGEICE 247
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDP-ENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
....*..
gi 568956771 248 KGTHKEL 254
Cdd:PRK14247 226 WGPTREV 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
53-284 |
1.16e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.63 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-LAYVSQQAW---------IFHG- 121
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWravrsdiqmIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 122 ----NVRENI---------LFGEKYNHQRYQHTVHV----CGLQKDL-NSLPYgdlteigergvNLSGGQRQRISLARAV 183
Cdd:PRK15079 108 laslNPRMTIgeiiaeplrTYHPKLSRQEVKDRVKAmmlkVGLLPNLiNRYPH-----------EFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 184 YANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELmeerg 259
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVN--LLQQLQremGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV----- 249
|
250 260
....*....|....*....|....*
gi 568956771 260 ryaklihnlrglqFKDPEHIYNVAM 284
Cdd:PRK15079 250 -------------YHNPLHPYTKAL 261
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
68-228 |
1.37e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 68 VVRKGKVLGICGNVGSGKSSLISALLGQM-----------------------QLQ--------KGVVAVNGPlAYVSQQA 116
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELipnlgdyeeepswdevlkrfrgtELQnyfkklynGEIKVVHKP-QYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 117 WIFHGNVREnILfgEKYNhQRyqhtvhvcGLQKDLNSLPygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:PRK13409 174 KVFKGKVRE-LL--KKVD-ER--------GKLDEVVERL--GLENILDRDIsELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*...
gi 568956771 196 LSAVDahvgkhVFE-----ECIKKTLKGKTVVLVTHQL 228
Cdd:PRK13409 240 TSYLD------IRQrlnvaRLIRELAEGKYVLVVEHDL 271
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
53-274 |
1.41e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.90 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 53 WQSGSP--KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGP-------------------LAY 111
Cdd:PRK13649 12 YQAGTPfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkvgLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 112 VSQQAWIFHGNVRENILFG-------EKYNHQRYQHTVHVCGLQKDL-NSLPYgdlteigergvNLSGGQRQRISLARAV 183
Cdd:PRK13649 92 QFPESQLFEETVLKDVAFGpqnfgvsQEEAEALAREKLALVGISESLfEKNPF-----------ELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 184 YANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHK------ELME 256
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGKPKdifqdvDFLE 240
|
250 260
....*....|....*....|....
gi 568956771 257 ERG----RYAKLIHNL--RGLQFK 274
Cdd:PRK13649 241 EKQlgvpKITKFAQRLadRGISFS 264
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
448-612 |
1.49e-06 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis 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: 349993 [Multi-domain] Cd Length: 295 Bit Score: 50.91 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 448 NRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdVRLPFHA-ENFLQQFFMVVFILVIMAAVFP----VVLVVLAGLAV 522
Cdd:cd18549 79 RDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDI-SELAHHGpEDLFISIITIIGSFIILLTINVpltlIVFALLPLMII 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 523 IFLILLRIFHRGVQELK-QVENISrspwfSHITSSIQGLGVIHAYDKKDDCISKFKTLNDE--NSSHLLYFNCAlrWFAL 599
Cdd:cd18549 158 FTIYFNKKMKKAFRRVReKIGEIN-----AQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRflESKKKAYKAMA--YFFS 230
|
170
....*....|...
gi 568956771 600 RMDILMNIVTFVV 612
Cdd:cd18549 231 GMNFFTNLLNLVV 243
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
61-225 |
1.59e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 61 VLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGplayvsqqawifHGNVRenilfGEKYNHQRYqh 140
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG------------KTATR-----GDRSRFMAY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 141 TVHVCGLQKDLNSL-----------------PYGDLTEIGERGV------NLSGGQRQRISLARAVYANRQLYLLDDPLS 197
Cdd:PRK13543 87 LGHLPGLKADLSTLenlhflcglhgrrakqmPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180
....*....|....*....|....*...
gi 568956771 198 AVDAHvGKHVFEECIKKTLKGKTVVLVT 225
Cdd:PRK13543 167 NLDLE-GITLVNRMISAHLRGGGAALVT 193
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
446-533 |
2.94e-06 |
|
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: 50.17 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 446 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDEldVR-----LPFhaenFLQQFFMVVFILVIMAAVFPVV-LVVLAG 519
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSL--VQrflafGPF----LLGNLLTLVVGLVVMLVLSPPLaLVALAS 147
|
90
....*....|....
gi 568956771 520 LAVIFLILLRIFHR 533
Cdd:cd18543 148 LPPLVLVARRFRRR 161
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
62-244 |
3.11e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQ---------------------LQKGVVAVNGPLAYVSQQawifh 120
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQkdsgsilfqgkeidfksskeaLENGISMVHQELNLVLQR----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 121 gNVRENILFGekynhqRYQHTvhvcGLQKDLNSLpYGDLTEI----------GERGVNLSGGQRQRISLARAVYANRQLY 190
Cdd:PRK10982 89 -SVMDNMWLG------RYPTK----GMFVDQDKM-YRDTKAIfdeldididpRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 191 LLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQL-QFLESCDEVILLEDGE 244
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRDGQ 211
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
446-614 |
3.94e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 49.79 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 446 LHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFP-------VVLVVLA 518
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWklalivlAVVPVLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 519 GLAVIF--LILLRifHRGVQELkqveNisrspwfSHITSS----IQGLGVIHAYDKKDDCISKFKTLNDE--NSS-HLLY 589
Cdd:cd18540 157 VVSIYFqkKILKA--YRKVRKI----N-------SRITGAfnegITGAKTTKTLVREEKNLREFKELTEEmrRASvRAAR 223
|
170 180
....*....|....*....|....*
gi 568956771 590 FNcalrwfALRMDILMNIVTFVVAL 614
Cdd:cd18540 224 LS------ALFLPIVLFLGSIATAL 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
69-258 |
4.08e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 69 VRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQqaWI---FHGNVRENI--LFGEKYNHQRYQHTVh 143
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ--YIspdYDGTVEEFLrsANTDDFGSSYYKTEI- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 144 vcglqkdLNSLpygDLTEIGERGV-NLSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikkt 215
Cdd:COG1245 440 -------IKPL---GLEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAEN----- 504
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 568956771 216 lKGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEER 258
Cdd:COG1245 505 -RGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASGPMDMR 546
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
64-257 |
4.90e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 49.73 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG-PLAYVSQQAW---------IF---HG--N----VR 124
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDITGLSGRELrplrrrmqmVFqdpYAslNprmtVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFGEKYNH--------QRYQHTVHVCGLQKD-LNSLPYgdlteigErgvnLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:COG4608 116 DIIAEPLRIHGlaskaerrERVAELLELVGLRPEhADRYPH-------E----FSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 196 LSAVDAHVGKHV---FEEcIKKTLkGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 257
Cdd:COG4608 185 VSALDVSIQAQVlnlLED-LQDEL-GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
718-911 |
4.97e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.37 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 718 SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIdevdictVGLEDLRTKLTMipqdpvlfvgtvrynldplgshtdem 797
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLD-------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 798 lwhvlertfmrdtimklpEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQS-------T 870
Cdd:smart00382 48 ------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrllL 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568956771 871 IKEAFKSCTVLTIAHRLNTVLncDLVLVMENGKVIEFDKPE 911
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLIL 148
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
401-640 |
5.41e-06 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 49.18 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 401 VDQTLQDTKHHMYQLVYIASMVSVLMfGIIKGFTFTNTTLMAS------SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRF 474
Cdd:cd18556 29 TDLLTSSSSDSYNYIVVLAALYVITI-SATKLLGFLSLYLQSSlrveliISISSSYFRYLYEQPKTFFVKENSGDITQRL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 475 SKDMDELDVRLPFHAENF----LQQFFMVVFIL----VIMAAVFPVvlvvlagLAVIFLILLRIFHRGVQELKQ-VENIS 545
Cdd:cd18556 108 NQASNDLYTLVRNLSTNIlpplLQLIIAIVVILssgdYFVAALFLL-------YAVLFVINNTIFTKKIVSLRNdLMDAG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 546 RSPwFSHITSSIQGLGVIHAYDKKDDCISKFK-TLNDENSSHLLYFNCALRWFALrmDILMNIVTFVVALLVTLSFSSIS 624
Cdd:cd18556 181 RKS-YSLLTDSVKNIVAAKQNNAFDFLFKRYEaTLTNDRNSQKRYWKLTFKMLIL--NSLLNVILFGLSFFYSLYGVVNG 257
|
250
....*....|....*....
gi 568956771 625 ASSKG---LSLSYIIQLSG 640
Cdd:cd18556 258 QVSIGhfvLITSYILLLST 276
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
59-245 |
5.58e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.93 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGplAYVSQQ------AWI---F---------H 120
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG--KDVTKLpeykraKYIgrvFqdpmmgtapS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 121 GNVRENILF----GEKY------NHQRYQH------TVHVcGLQKDLNslpygdlTEIGergvNLSGGQRQRISLARAVY 184
Cdd:COG1101 97 MTIEENLALayrrGKRRglrrglTKKRRELfrellaTLGL-GLENRLD-------TKVG----LLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 185 ANRQLYLLDDPLSAVDAHVGKHVFE---ECIKKtlKGKTVVLVTHQLQF-LESCDEVILLEDGEI 245
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLElteKIVEE--NNLTTLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
54-280 |
5.76e-06 |
|
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: 50.07 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 54 QSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSslISALlGQMQLqkgvvaVNGPLAYVSQQAWiFHGnvrENIL-FGEK 132
Cdd:COG4172 18 QGGGTVEAVKGVSFDIAAGETLALVGESGSGKS--VTAL-SILRL------LPDPAAHPSGSIL-FDG---QDLLgLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 133 Y-NHQR-------YQ---------HTV----------HVcGLQK--------DLnslpygdLTEIG----ERGVN----- 168
Cdd:COG4172 85 ElRRIRgnriamiFQepmtslnplHTIgkqiaevlrlHR-GLSGaaararalEL-------LERVGipdpERRLDayphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 169 LSGGQRQRISLARAVyANR-QLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQL----QFlesCDEVILL 240
Cdd:COG4172 157 LSGGQRQRVMIAMAL-ANEpDLLIADEPTTALDVTVQAQILD--LLKDLQrelGMALLLITHDLgvvrRF---ADRVAVM 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568956771 241 EDGEICEKGTHKELmeergryaklihnlrglqFKDPEHIY 280
Cdd:COG4172 231 RQGEIVEQGPTAEL------------------FAAPQHPY 252
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
62-249 |
6.14e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.77 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG------PLAYVSQQ--------AWIF-HGNVRE- 125
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrDLYALSEAerrrllrtEWGFvHQHPRDg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 126 ---------NIlfGEKYNHQRYQHtvhvcglqkdlnslpYGDLTE---------------IGERGVNLSGGQRQRISLAR 181
Cdd:PRK11701 102 lrmqvsaggNI--GERLMAVGARH---------------YGDIRAtagdwlerveidaarIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 182 AVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTL---KGKTVVLVTHQL---QFLesCDEVILLEDGEICEKG 249
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLD--LLRGLvreLGLAVVIVTHDLavaRLL--AHRLLVMKQGRVVESG 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
170-301 |
6.21e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 170 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVF-------EECikktlkGKTVVLVTHQLQFLES-CDEVILLE 241
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLnlmmdlqQEL------GLSYVFISHDLSVVEHiADEVMVMY 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 242 DGEICEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAMVE-TLKESPAQRDEDAVL 301
Cdd:PRK11308 230 LGRCVEKGTKEQI------------------FNNPRHPYTQALLSaTPRLNPDDRRERIKL 272
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
58-107 |
6.31e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 6.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 568956771 58 PKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG 107
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
62-258 |
7.79e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 62 LHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKG-------VVAVNGPLAyvSQQAW--IFHG--------NVR 124
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkEVTFNGPKS--SQEAGigIIHQelnlipqlTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 125 ENILFG-EKYNH-------QRYQHTVhvcGLQKDLNsLPYGDLTEIGErgvnLSGGQRQRISLARAVYANRQLYLLDDPL 196
Cdd:PRK10762 98 ENIFLGrEFVNRfgridwkKMYAEAD---KLLARLN-LRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 197 SAVDAHVGKHVFEecIKKTLK--GKTVVLVTHQLQ-FLESCDEVILLEDGE-ICEKGThKELMEER 258
Cdd:PRK10762 170 DALTDTETESLFR--VIRELKsqGRGIVYISHRLKeIFEICDDVTVFRDGQfIAEREV-ADLTEDS 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
700-906 |
7.94e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.03 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNTPLVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE--PASGTIIIDEVDIC--TVGLEDLRTKLTmiPQD 775
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGreASLIDAIGRKGD--FKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 776 PVLFVGTVRYNldplgshtDEMLWhvlERTFmrdtimklpeklqaevtengENFSVGERQLLCMARALLRNSKIILLDEA 855
Cdd:COG2401 115 AVELLNAVGLS--------DAVLW---LRRF--------------------KELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 856 TASMDSKTDTLVQSTIKEAFKSC--TVLTIAHRLNTV--LNCDLVLVMENGKVIE 906
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAgiTLVVATHHYDVIddLQPDLLIFVGYGGVPE 218
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
418-615 |
8.38e-06 |
|
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: 48.55 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 418 IASMVSVLmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhaENFLQQFF 497
Cdd:cd18548 47 LLALLGLI-AGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQV--------QNFVMMLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 498 MVVF---ILVI------------MAAVFPVVLVVLAG-LAVIFLILLRIFHRgVQelKQVENISRSpwfshITSSIQGLG 561
Cdd:cd18548 118 RMLVrapIMLIgaiimafrinpkLALILLVAIPILALvVFLIMKKAIPLFKK-VQ--KKLDRLNRV-----VRENLTGIR 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568956771 562 VIHAYDKKDDCISKFKTLNDENSSHLLYfncALRWFALR---MDILMNIVTFVVALL 615
Cdd:cd18548 190 VIRAFNREDYEEERFDKANDDLTDTSLK---AGRLMALLnplMMLIMNLAIVAILWF 243
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
708-906 |
9.68e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDlrtklTMIPQDPVLF-----VGT 782
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLpwrnvQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 783 VRYNLDPLGshtdemlwhvLERTFMRDTIMKLPEKLQAEvtENGENF----SVGERQLLCMARALLRNSKIILLDEATAS 858
Cdd:PRK11248 91 VAFGLQLAG----------VEKMQRLEIAHQMLKKVGLE--GAEKRYiwqlSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 859 MDSKT----DTLVQSTIKEAFKSctVLTIAHRLN--TVLNCDLVLVMEN-GKVIE 906
Cdd:PRK11248 159 LDAFTreqmQTLLLKLWQETGKQ--VLLITHDIEeaVFMATELVLLSPGpGRVVE 211
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
708-909 |
1.07e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.11 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPAS--GTIIIDEVDIctvgledlrTKLTM-----IPQDPVLFV 780
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP---------TKQILkrtgfVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 781 G-TVRynldplgshtdEMLWHV----LERTFMRDTIMKLPEKLQAEV----TEN---GENF----SVGERQLLCMARALL 844
Cdd:PLN03211 154 HlTVR-----------ETLVFCsllrLPKSLTKQEKILVAESVISELgltkCENtiiGNSFirgiSGGERKRVSIAHEML 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 845 RNSKIILLDEATASMDSKTD-TLVQSTIKEAFKSCTVLTIAHRLNTVL--NCDLVLVMENGKVIEFDK 909
Cdd:PLN03211 223 INPSLLILDEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEGRCLFFGK 290
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
364-583 |
1.08e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 48.28 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 364 FFLMMGSSAFST---WWLGIWLDRgsqvVCASQNNKTACNVDQTLQDTKhhmYQLVYIASMVSVLMFGIIKGFTFTNTTL 440
Cdd:cd18564 5 LLALLLETALRLlepWPLKVVIDD----VLGDKPLPGLLGLAPLLGPDP---LALLLLAAAALVGIALLRGLASYAGTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 441 MAS------SSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhaENFLQ----QFFMVVFILVIMAAVF 510
Cdd:cd18564 78 TALvgqrvvLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAI--------QDLLVsgvlPLLTNLLTLVGMLGVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 511 PVV-----LVVLAGLAVIFLILLRI---FHRGVQELKQVEnisrspwfSHITSSIQ-GLG---VIHAYDKKDDCISKFKT 578
Cdd:cd18564 150 FWLdwqlaLIALAVAPLLLLAARRFsrrIKEASREQRRRE--------GALASVAQeSLSairVVQAFGREEHEERRFAR 221
|
....*
gi 568956771 579 LNDEN 583
Cdd:cd18564 222 ENRKS 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-330 |
1.20e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 33 QRPELYSEQSRSDQGVASPEWQSGSPKSVLHNISFVVRKGKVLGICGNVGSGKSSLISALL------------GQMQLQK 100
Cdd:PRK10261 3 HSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMrlleqagglvqcDKMLLRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 101 ---GVVAVNGPLAYVSQQ------AWIFHGNVRE-NILF--GEKYN-----HQRYQHTVHVCGLQKDLNSLPYGDLTEIG 163
Cdd:PRK10261 83 rsrQVIELSEQSAAQMRHvrgadmAMIFQEPMTSlNPVFtvGEQIAesirlHQGASREEAMVEAKRMLDQVRIPEAQTIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 164 ERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLKGKT---VVLVTHQLQFL-ESCDEVI 238
Cdd:PRK10261 163 SRYPHqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMsmgVIFITHDMGVVaEIADRVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 239 LLEDGEICEKGTHKELmeergryaklihnlrglqFKDPEHIYNVAMVETLKESPAQRDEDA----VLASGDEKDEgKEPE 314
Cdd:PRK10261 241 VMYQGEAVETGSVEQI------------------FHAPQHPYTRALLAAVPQLGAMKGLDYprrfPLISLEHPAK-QEPP 301
|
330
....*....|....*.
gi 568956771 315 TEEfvDTNAPAHQLIQ 330
Cdd:PRK10261 302 IEQ--DTVVDGEPILQ 315
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
64-254 |
1.64e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGqmqlqkgVVAVNGplaYVSQQAwIFHG----NVRENILfgekyNHQRYQ 139
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMG-------LLAANG---RIGGSA-TFNGreilNLPEKEL-----NKLRAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 140 HTVHVcgLQKDLNSL-PY---GD-LTEI------------GERGVNL--------------------SGGQRQRISLARA 182
Cdd:PRK09473 98 QISMI--FQDPMTSLnPYmrvGEqLMEVlmlhkgmskaeaFEESVRMldavkmpearkrmkmyphefSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568956771 183 VYANRQLYLLDDPLSAVDAHVGKHVFEecIKKTLK---GKTVVLVTHQLQFLE-SCDEVILLEDGEICEKGTHKEL 254
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMT--LLNELKrefNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
691-905 |
1.68e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.77 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 691 EITFKDYRMRYRDNTPL---VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIII-----------DEVD 756
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 757 ICTVGLEDLRTKLTMIPQDPVLF--VGTV----RYNLdplgshtdemlwhvLERTFMRDTI-----MKLP----EKLQAE 821
Cdd:PRK13651 82 KVLEKLVIQKTRFKKIKKIKEIRrrVGVVfqfaEYQL--------------FEQTIEKDIIfgpvsMGVSkeeaKKRAAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 822 VTE-----------NGENFSVGERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRLNT 889
Cdd:PRK13651 148 YIElvgldesylqrSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDN 227
|
250
....*....|....*..
gi 568956771 890 VLN-CDLVLVMENGKVI 905
Cdd:PRK13651 228 VLEwTKRTIFFKDGKII 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
700-916 |
1.76e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNTPL-VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRtKLTM--IPQDP 776
Cdd:COG3845 264 SVRDDRGVpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR-RLGVayIPEDR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 777 vLFVG-----TVRYNLDpLGSHTDEMLWHvleRTFM-RDTIMKLPEKLQAE---VTENGE----NFSVGERQLLCMARAL 843
Cdd:COG3845 343 -LGRGlvpdmSVAENLI-LGRYRRPPFSR---GGFLdRKAIRAFAEELIEEfdvRTPGPDtparSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 844 LRNSKIIL-------LDEATASMdsktdtlVQSTIKEAFKS-CTVLTIAHRLNTVLN-CDLVLVMENGKVI-EFDKPEVL 913
Cdd:COG3845 418 SRDPKLLIaaqptrgLDVGAIEF-------IHQRLLELRDAgAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEAT 490
|
...
gi 568956771 914 AEK 916
Cdd:COG3845 491 REE 493
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
692-885 |
1.78e-05 |
|
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: 48.39 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEvdicTVGLEdlrt 767
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMItgqeQPDSGTIEIGE----TVKLA---- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 768 kltmipqdpvlFVGTVRYNLDPlgshtDEMLWHVLERTFmrDTIMKLPEKLQAEVTENGENF------------SVGERQ 835
Cdd:TIGR03719 389 -----------YVDQSRDALDP-----NKTVWEEISGGL--DIIKLGKREIPSRAYVGRFNFkgsdqqkkvgqlSGGERN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568956771 836 LLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIkEAFKSCTVLtIAH 885
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAGCAVV-ISH 498
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
708-868 |
2.33e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.73 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTV---GLEDLRT-KLTMIPQDPVLFVG-T 782
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 783 VRYNLD-PL---GSHTDEMLWHVLErtfmrdtiMKLPEKLQAEVTENGENFSVGERQLLCMARALLRNSKIILLDEATAS 858
Cdd:PRK11629 104 ALENVAmPLligKKKPAEINSRALE--------MLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170
....*....|.
gi 568956771 859 MDSKT-DTLVQ 868
Cdd:PRK11629 176 LDARNaDSIFQ 186
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
169-256 |
2.45e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 169 LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLK--GKTVVLVTH-QLQFLESCDEVILLEDGEI 245
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-IQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
90
....*....|.
gi 568956771 246 CEKGTHKELME 256
Cdd:PRK11650 214 EQIGTPVEVYE 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
709-885 |
2.63e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.41 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLED---LRTKLTMIPQDPVLFVG-TVR 784
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDrTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 785 YNLD-PL---GSHTDEMLWHV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCMARALLRNSKIILLDEATA 857
Cdd:PRK10908 98 DNVAiPLiiaGASGDDIRRRVsaaLDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|..
gi 568956771 858 SMDsktDTLVQSTIK--EAFK--SCTVLTIAH 885
Cdd:PRK10908 167 NLD---DALSEGILRlfEEFNrvGVTVLMATH 195
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
401-537 |
3.23e-05 |
|
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: 46.74 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 401 VDQTLQDTKHHMYQLVYIA-SMVSVLMFGIIkgFTFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTPTGRLMNR 473
Cdd:cd18573 26 ASKESGDIEIFGLSLKTFAlALLGVFVVGAA--ANFGRVYLLRIAGerivarLRKRLFKSILRQDAAFFDKNKTGELVSR 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 474 FSKDMDE----LDVRLPFHAENFLQ---QFFMVVFI----LVIMAAVFPVVlvvlAGLAVIFLILLRIFHRGVQE 537
Cdd:cd18573 104 LSSDTSVvgksLTQNLSDGLRSLVSgvgGIGMMLYIspklTLVMLLVVPPI----AVGAVFYGRYVRKLSKQVQD 174
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
415-526 |
4.73e-05 |
|
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: 46.15 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 415 LVYIASMVsvlmFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQ 494
Cdd:cd18784 44 LLAIASSV----AAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110
....*....|....*....|....*....|...
gi 568956771 495 QFFMVVFILVIMAAV-FPVVLVVLAGLAVIFLI 526
Cdd:cd18784 120 SLVKAIGVIVFMFKLsWQLSLVTLIGLPLIAIV 152
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
707-860 |
4.74e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 707 LVLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvGLEDlRTKLTMIPQDPVLFvgtVRYN 786
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI----------GLAK-GIKLGYFAQHQLEF---LRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 787 LDPLgSHtdemlwhvLERTFMRDTIMKLPEKLQA------EVTENGENFSVGERQLLCMARALLRNSKIILLDEATASMD 860
Cdd:PRK10636 392 ESPL-QH--------LARLAPQELEQKLRDYLGGfgfqgdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
64-305 |
4.83e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNG----PLAYVSQQAwifhgnVRENI--LFGEKYNHQR 137
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridTLSPGKLQA------LRRDIqfIFQDPYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 138 YQHTVHVCGLQK-DLNSLPYGD-----LTEIGERgVNL------------SGGQRQRISLARAVYANRQLYLLDDPLSAV 199
Cdd:PRK10261 416 PRQTVGDSIMEPlRVHGLLPGKaaaarVAWLLER-VGLlpehawryphefSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 200 DAHVGKHVFEEC--IKKTLkGKTVVLVTHQLQFLESCD-EVILLEDGEICEKGTHKELmeergryaklihnlrglqFKDP 276
Cdd:PRK10261 495 DVSIRGQIINLLldLQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAV------------------FENP 555
|
250 260 270
....*....|....*....|....*....|
gi 568956771 277 EHIYNVAMVETLK-ESPAQRDEDAVLASGD 305
Cdd:PRK10261 556 QHPYTRKLMAAVPvADPSRQRPQRVLLSDD 585
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
415-526 |
4.84e-05 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); 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: 350033 [Multi-domain] Cd Length: 289 Bit Score: 46.31 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 415 LVYIASMVSVLMFGIIkgftFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQ 494
Cdd:cd18589 44 LLTIASAVSEFVCDLI----YNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMW 119
|
90 100 110
....*....|....*....|....*....|...
gi 568956771 495 QFFMVVFILVIMAAVFP-VVLVVLAGLAVIFLI 526
Cdd:cd18589 120 YLARGLFLFIFMLWLSPkLALLTALGLPLLLLV 152
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
418-531 |
5.09e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. 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). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 46.34 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 418 IASMVSVLMFGIIKGFTFTNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRfskdMDELD-VRlpfhaeNFLQ-Q 495
Cdd:cd18588 49 LVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVAR----VRELEsIR------QFLTgS 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568956771 496 FFMVV----FILVIMAAVF----PVVLVVLAGLAVIFLILLRIF 531
Cdd:cd18588 119 ALTLVldlvFSVVFLAVMFyyspTLTLIVLASLPLYALLSLLVT 162
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
712-923 |
5.40e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 712 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIIIDEVDICTVGLEDL-RTKLTMIPQDPVLFVGTVRYNLD-- 788
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLTlh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 789 -PLGSHTDEmLWHVLERTFMRdtiMKLPEKLQAEVTengeNFSVGERQLLCMARALLR-------NSKIILLDEATASMD 860
Cdd:PRK03695 94 qPDKTRTEA-VASALNEVAEA---LGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 861 SKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVL-NCDLVLVMENGKVI------EFDKPEVLAEkpdsAFAM 923
Cdd:PRK03695 166 VAQQAALDRLLSElCQQGIAVVMSSHDLNHTLrHADRVWLLKQGKLLasgrrdEVLTPENLAQ----VFGV 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
708-918 |
5.48e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.95 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDP--VLFVGTVRY 785
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 786 NL--DPLGSHTD-EMLWHVLERTFMRDTIMKLPEKLQaevtengENFSVGERQLLCMARALLRNSKIILLDEATASMDSK 862
Cdd:PRK13652 99 DIafGPINLGLDeETVAHRVSSALHMLGLEELRDRVP-------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 863 -TDTLVQ--STIKEAFkSCTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPD 918
Cdd:PRK13652 172 gVKELIDflNDLPETY-GMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
708-860 |
5.67e-05 |
|
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: 45.18 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIIDEVDICTVGLEDLRTKLTMIPQDPVLFVGTVRYNL 787
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 788 DPLGS-HTDEMLWHVLertfmrdtimklpeklqAEVTENG------ENFSVGERQLLCMARALLRNSKIILLDEATASMD 860
Cdd:cd03231 95 RFWHAdHSDEQVEEAL-----------------ARVGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
162-244 |
6.53e-05 |
|
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: 45.68 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 162 IGERGVNLSGGQRQRISLARAVyANRQ----LYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEV 237
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWI 241
|
....*....
gi 568956771 238 ILL--EDGE 244
Cdd:cd03271 242 IDLgpEGGD 250
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
424-480 |
8.45e-05 |
|
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: 45.61 E-value: 8.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 424 VLMFGIIKGFTFTNTTLMA------SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDE 480
Cdd:cd18574 49 LGLYLLQSLLTFAYISLLSvvgervAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQE 111
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
162-254 |
8.85e-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: 46.54 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 162 IGERGVNLSGGQRQRISLARAVYA---NRQLYLLDDPLSavdahvGKHvFEEcIKKTL--------KGKTVVLVTHQLQF 230
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTT------GLH-FDD-IKKLLevlqrlvdKGNTVVVIEHNLDV 894
|
90 100 110
....*....|....*....|....*....|
gi 568956771 231 LESCDEVILL------EDGEICEKGTHKEL 254
Cdd:TIGR00630 895 IKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
424-618 |
9.52e-05 |
|
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: 45.17 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 424 VLMFGIIKGFTFTNTTLMA---SSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVV 500
Cdd:cd18575 46 ALVLALASALRFYLVSWLGervVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 501 FILVIMAAVFP-VVLVVLAGLAVIFLILLrIFHRGVQEL-----KQVENISrspwfSHITSSIQGLGVIHAYDKKDDCIS 574
Cdd:cd18575 126 GGLVMLFITSPkLTLLVLLVIPLVVLPII-LFGRRVRRLsrasqDRLADLS-----AFAEETLSAIKTVQAFTREDAERQ 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568956771 575 KFKTLNDEnsshllYFNCALRWFALRmDILMNIVTFVVALLVTL 618
Cdd:cd18575 200 RFATAVEA------AFAAALRRIRAR-ALLTALVIFLVFGAIVF 236
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
692-862 |
9.78e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTPlVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEVDICTvgLEDLRT 767
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVagleRITSGEIWIGGRVVNE--LEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 768 KLTMIPQDpvlfvgtvrYNLDPLGSHTDEMLWHVLERTFMRDTIMKLPEKlQAEVTENGE-------NFSVGERQLLCMA 840
Cdd:PRK11650 77 DIAMVFQN---------YALYPHMSVRENMAYGLKIRGMPKAEIEERVAE-AARILELEPlldrkprELSGGQRQRVAMG 146
|
170 180
....*....|....*....|..
gi 568956771 841 RALLRNSKIILLDEATASMDSK 862
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAK 168
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
692-921 |
1.19e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.32 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEVDICTVGLEDlRT 767
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAEN-RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 768 KLTMIpQDPVLFVG-TVRYN----LDPLGSHTDEMLWHVLERTFMrdtimklpEKLQAEVTENGENFSVGERQLLCMARA 842
Cdd:PRK09452 88 VNTVF-QSYALFPHmTVFENvafgLRMQKTPAAEITPRVMEALRM--------VQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 843 LLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIEFDKPEVLAEKPDS 919
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPREIYEEPKN 238
|
..
gi 568956771 920 AF 921
Cdd:PRK09452 239 LF 240
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
159-310 |
1.28e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 159 LTEI-GERGVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLES-CDE 236
Cdd:NF000106 134 LTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHE 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 237 VILLEDGEICEKGTHKELMEERGRyaklihnlRGLQFKdPEHiynVAMVETLKESPAQRDEDAVLASGDEKDEG 310
Cdd:NF000106 214 LTVIDRGRVIADGKVDELKTKVGG--------RTLQIR-PAH---AAELDRMVGAIAQAGLDGIAGATADHEDG 275
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
68-244 |
1.51e-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: 43.33 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 68 VVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVNGPLAYVSQQAwifhgnvrenilfgekynhqryqhtvhvcgl 147
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 148 qkdlnslpygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDPLSAVD-------AHVGKHVFEEcikktlKGKT 220
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKKT 124
|
170 180
....*....|....*....|....
gi 568956771 221 VVLVTHQLQFLESCDEVILLEDGE 244
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
716-915 |
1.67e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.42 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 716 IQSGQTVGIVGRTGSGKSSLGMAL-FRL---VEpASGTIIIDEVDIctvGLEDLRTKLTMIPQDPvLFVG--TVRYNLD- 788
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALaFRSpkgVK-GSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIPtlTVREHLMf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 789 ----PLGSHTD-----EMLWHVLERTFMR---DTIMKLPEKLQAevtengenFSVGERQLLCMARALLRNSKIILLDEAT 856
Cdd:TIGR00955 123 qahlRMPRRVTkkekrERVDEVLQALGLRkcaNTRIGVPGRVKG--------LSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956771 857 ASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLNC--DLVLVMENGKVIEFDKPEVLAE 915
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
162-243 |
1.98e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 162 IGERGVN-LSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQ--LQFLESCDEVI 238
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELL 1091
|
....*
gi 568956771 239 LLEDG 243
Cdd:PLN03140 1092 LMKRG 1096
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
59-195 |
2.01e-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: 44.93 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 59 KSVLHNISFVVRKGKVLGICGNVGSGKSSLISALLGQMQLQKGVVAVnGP---LAYVSQQAWIFHGN--VRENILFGEky 133
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvkLAYVDQSRDALDPNktVWEEISGGL-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 134 nhqryqhtvhvcglqkdlnslpygDLTEIGERGVN---------------------LSGGQRQRISLARAVYANRQLYLL 192
Cdd:TIGR03719 412 ------------------------DIIKLGKREIPsrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLL 467
|
...
gi 568956771 193 DDP 195
Cdd:TIGR03719 468 DEP 470
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
696-904 |
2.70e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 696 DYRMRYRDNTPLVLDGL---------NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIIID--EVDICTVGlED 764
Cdd:PRK11288 247 GYRPRPLGEVRLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDgkPIDIRSPR-DA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 765 LRTKLTMIPQD----PVLFVGTVRYNLD--------PLGSHTDEMLWHVLERTFMRDTIMKLPEKLQAEVtengeNFSVG 832
Cdd:PRK11288 326 IRAGIMLCPEDrkaeGIIPVHSVADNINisarrhhlRAGCLINNRWEAENADRFIRSLNIKTPSREQLIM-----NLSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 833 ERQLLCMARALLRNSKIILLDEATASMDSKTDTLVQSTIKE-AFKSCTVLTIAHRLNTVLN-CDLVLVMENGKV 904
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
169-240 |
3.36e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 3.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 169 LSGGQRQRISLARAVYA---NRQLYLLDDPLSAVDAHVGKHVFEECIKKTLKGKTVVLVTHQLQFLESCDEVILL 240
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
170-244 |
3.90e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 3.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568956771 170 SGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHVFEECIKKTlkgKTVVLVTHQLQFLESCDEVILLEDGE 244
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNTVVTDILHLHGQ 417
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
169-256 |
4.64e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 169 LSGGQRQRISLARAVYANRQ--LYLLDDPlsavdaHVGKHVFE-ECIKKTLK-----GKTVVLVTHQLQFLESCDEVILL 240
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEP------SIGLHQRDnRRLINTLKrlrdlGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100
....*....|....*....|..
gi 568956771 241 ------EDGEICEKGTHKELME 256
Cdd:TIGR00630 563 gpgageHGGEVVASGTPEEILA 584
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
708-761 |
9.79e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 9.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956771 708 VLDGLNLNIQSGQTVGIVGRTGSGKSSLGMALF-----RLVepaSGTIIID--EVDICTVG 761
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDgkEVDVSTVS 332
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
64-259 |
1.13e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 64 NISFVVRKGKVLGICGNVGSGKSS-------LISA------LLGQ------MQLQKGVvavngplAYVSQqAWIFHG--N 122
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPAsegeawLFGQpvdagdIATRRRV-------GYMSQ-AFSLYGelT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 123 VRENI-----LFG--EKYNHQRYQHTVHVCGLQKDLNSLPygdlteigergVNLSGGQRQRISLARAVYANRQLYLLDDP 195
Cdd:NF033858 356 VRQNLelharLFHlpAAEIAARVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 196 LSAVDAhVGKHVFEEcikkTL------KGKTVVLVTHqlqFL---ESCDEVILLEDGEICEKGTHKELMEERG 259
Cdd:NF033858 425 TSGVDP-VARDMFWR----LLielsreDGVTIFISTH---FMneaERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
709-906 |
1.25e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIIIDEvDICTVGleDLRT-----------KLTMIPQ 774
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKVLSGVYPHgsyEGEILFDG-EVCRFK--DIRDsealgiviihqELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 775 DPV---LFVG--TVRY---NLDPLGSHTDEMLWHVlertfmrdtimKLPEKLQAEVTENGenfsVGERQLLCMARALLRN 846
Cdd:NF040905 93 LSIaenIFLGneRAKRgviDWNETNRRARELLAKV-----------GLDESPDTLVTDIG----VGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568956771 847 SKIILLDEATASM-DSKTDTLVQsTIKEaFKS--CTVLTIAHRLNTVLN-CDLVLVMENGKVIE 906
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLD-LLLE-LKAqgITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
442-528 |
1.43e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 41.63 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 442 ASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDvrlPFHAEnFLQQFFMVVFI-LVIMAAVFP------VVL 514
Cdd:cd18584 68 VKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALD---GYFAR-YLPQLVLAAIVpLLILVAVFPldwvsaLIL 143
|
90
....*....|....
gi 568956771 515 VVLAGLAVIFLILL 528
Cdd:cd18584 144 LVTAPLIPLFMILI 157
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
168-244 |
1.56e-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: 42.23 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 168 NLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAH----VGKHVFEecikktLKGkTVVLVTHQLQFLESCDEVIL-LED 242
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHLQE------YPG-TVVAVTHDRYFLDNVAGWILeLDR 233
|
..
gi 568956771 243 GE 244
Cdd:TIGR03719 234 GR 235
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
721-759 |
2.29e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 41.29 E-value: 2.29e-03
10 20 30
....*....|....*....|....*....|....*....
gi 568956771 721 TVGIVGRTGSGKSSLGMALFRlvepaSGTIIIDEVDICT 759
Cdd:COG3596 41 VIALVGKTGAGKSSLINALFG-----AEVAEVGVGRPCT 74
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
709-885 |
2.46e-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: 41.69 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 709 LDGLNLNIQSGQ-----TVGIVGRTGSGKSSLGMALFRLVEPASGTIiidevdictvgleDLRTKLTMIPQ----DpvlF 779
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyispD---Y 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 780 VGTVRYNL-----DPLGSHtdeMLWH-VLERtfmrdtiMKLPEKLQAEVTEngenFSVGERQLLCMARALLRNSKIILLD 853
Cdd:COG1245 415 DGTVEEFLrsantDDFGSS---YYKTeIIKP-------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190
....*....|....*....|....*....|....*
gi 568956771 854 EATASMDSKTDTLVQSTIK---EAFKScTVLTIAH 885
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRrfaENRGK-TAMVVDH 514
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
424-537 |
2.70e-03 |
|
Six-transmembrane helical domain 2 (TMD2) 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: 350022 [Multi-domain] Cd Length: 317 Bit Score: 40.90 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 424 VLMFGIIKGF-TFTNTTLMASSS------LHNRVFNKIVRSPMSFFDTTP--TGRLMNRFSKDMDEL----DVRLPFhae 490
Cdd:cd18578 58 FLVLAIVAGIaYFLQGYLFGIAGerltrrLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVrglvGDRLGL--- 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568956771 491 nFLQQFFMVVFILVI-----------MAAVFPvvLVVLAGlaVIFLILLRIFHRGVQE 537
Cdd:cd18578 135 -ILQAIVTLVAGLIIafvygwklalvGLATVP--LLLLAG--YLRMRLLSGFEEKNKK 187
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
407-527 |
2.91e-03 |
|
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: 40.55 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 407 DTKHHMYQLVYIASM-VSVLMFGIIKGFTF---TNTTLMASSSLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELd 482
Cdd:cd18579 31 PDEPLSEGYLLALALfLVSLLQSLLLHQYFflsFRLGMRVRSALSSLIYRKALRLSSSARQETSTGEIVNLMSVDVQRI- 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 568956771 483 vrlpfhaENFLQQFFMVVFILVIMAAVFpVVLV------VLAGLAVIFLIL 527
Cdd:cd18579 110 -------EDFFLFLHYLWSAPLQIIVAL-YLLYrllgwaALAGLGVLLLLI 152
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
167-245 |
3.04e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 40.24 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 167 VNLSGGQRQRISLARAVYANRQLYLLDDPLSAVDAHVGKHV---FEECIKktlKGKTVVLVTHQLQFLESCD-EVILLED 242
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIlrlFEEFNR---VGVTVLMATHDIGLISRRSyRMLTLSD 212
|
...
gi 568956771 243 GEI 245
Cdd:PRK10908 213 GHL 215
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
700-739 |
3.69e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 3.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNTplVLDGLNLNIQSGQTVGIVGRTGSGKSSLgMAL 739
Cdd:NF033858 10 RYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSL-LSL 46
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
700-887 |
4.21e-03 |
|
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: 40.04 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 700 RYRDNTpLVLDGLNLnIQSGQTVGIVGRTGSGKSS--------LGMALFRLVEPASGTIIID-----EVDICTVGLEDLR 766
Cdd:cd03236 9 RYGPNS-FKLHRLPV-PREGQVLGLVGPNGIGKSTalkilagkLKPNLGKFDDPPDWDEILDefrgsELQNYFTKLLEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 767 TKLTMIPQD----PVLFVGTVRYNLDplgsHTDEmlwhvlerTFMRDTIMKLPEkLQAEVTENGENFSVGERQLLCMARA 842
Cdd:cd03236 87 VKVIVKPQYvdliPKAVKGKVGELLK----KKDE--------RGKLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568956771 843 LLRNSKIILLDEATASMDSKTDTLVQSTIKEAFKSC-TVLTIAHRL 887
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDnYVLVVEHDL 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
692-885 |
5.92e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 692 ITFKDYRMRYRDNtpLVLDGLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIIIDEvdicTVgledlrt 767
Cdd:PRK11819 325 IEAENLSKSFGDR--LLIDDLSFSLPPGGIVGIIGPNGAGKST----LFKMItgqeQPDSGTIKIGE----TV------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 768 KLTmipqdpvlFVGTVRYNLDPlgshtDEMLWHV----LErtfmrdtIMKLpeklqAEVTENGE------NF-------- 829
Cdd:PRK11819 388 KLA--------YVDQSRDALDP-----NKTVWEEisggLD-------IIKV-----GNREIPSRayvgrfNFkggdqqkk 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568956771 830 ----SVGERQLLCMARALLRNSKIILLDEATASMDskTDTLvqSTIKEA---FKSCTVLtIAH 885
Cdd:PRK11819 443 vgvlSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD--VETL--RALEEAlleFPGCAVV-ISH 500
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
445-612 |
6.07e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 39.77 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 445 SLHNRVFNKIVRSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIMAAVFPVVLVVLAGLAVIF 524
Cdd:cd18550 73 DLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 525 LILLRIFHRGVQEL--KQVENISRSPWFSHITSSIQGLGVIHAYDKKDDCISKFKTLNDENSSHLLYFNCALRWFALRMD 602
Cdd:cd18550 153 VLPTRRVGRRRRKLtrEQQEKLAELNSIMQETLSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALG 232
|
170
....*....|
gi 568956771 603 ILMNIVTFVV 612
Cdd:cd18550 233 LFTAIGPALV 242
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
169-265 |
9.16e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956771 169 LSGGQRQRISLA-----RAvyANRQLYLLDDPLsavdahVGKHvFEEcIKKTL--------KGKTVVLVTHQLQFLESCD 235
Cdd:PRK00349 831 LSGGEAQRVKLAkelskRS--TGKTLYILDEPT------TGLH-FED-IRKLLevlhrlvdKGNTVVVIEHNLDVIKTAD 900
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568956771 236 EVILL------EDGEICEKGTHKELMEER----GRYAKLI 265
Cdd:PRK00349 901 WIIDLgpeggdGGGEIVATGTPEEVAKVEasytGRYLKPV 940
|
|
| |
