|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
43-1344 |
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: 816.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 43 PNPVDDAGLLSFATFSWLTPVMVKGYRQRLTVDTLPPLSTYDSSDTNAKRFRVLWDEEVARVG----------------- 105
Cdd:TIGR00957 201 PCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRkqpvsavygkkdpskpk 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 106 ---------------------PEKASLSHVVWKFQRTRVLMDIVANILCIIMAAIGPVILiHQILQQTERTSGKVWVGIG 164
Cdd:TIGR00957 281 gssqldaneevealivksphkPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQIL-SLLIRFVNDPMAPDWQGYF 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 165 LCIALFATEFTKVFFWALAWAINYRTAIRLKVALSTLVFEN--LVSFKTLTHISVGEVLNILSSDSYSLFEAALFCPLPA 242
Cdd:TIGR00957 360 YTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKalVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIW 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 243 TIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMFMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFT 322
Cdd:TIGR00957 440 SAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 323 NTIQDIRRRERKLLEKAGFVQSGNS---ALAPIVSTIaIVLTLSCHILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIK 399
Cdd:TIGR00957 520 DKVEGIRQEELKVLKKSAYLHAVGTftwVCTPFLVAL-ITFAVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVIS 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 400 AMAEANVSLRRMKKILidksppsyiTQPE-DPDTV------------LLLANATLTWeheasrkstpkklqnqkrhlckk 466
Cdd:TIGR00957 599 SIVQASVSLKRLRIFL---------SHEElEPDSIerrtikpgegnsITVHNATFTW----------------------- 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 467 QRSEaysersPPAkgatgpeeqsdslksvLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYV 546
Cdd:TIGR00957 647 ARDL------PPT----------------LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYV 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 547 SQQAWIFHGNVRENILFGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:TIGR00957 705 PQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLF 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 627 DDPLSAVDAHVGKHVFEECI--KKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNLRG 704
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAP 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 705 LQfkDPEHLY-NAAMVEAFKESPAEREEDAGIIVLAPGNE------------KDEGKESETGSEFVDTKVPEH--QLIQT 769
Cdd:TIGR00957 865 DE--QQGHLEdSWTALVSGEGKEAKLIENGMLVTDVVGKQlqrqlsasssdsGDQSRHHGSSAELQKAEAKEEtwKLMEA 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 770 ESPQEGTVTWKTYHTYIKASgGYLLSLFTVFLFLLMIGSAAFSNWWLGLWLDKGsrMTCGPQGNRTMceVGAVLADIGqh 849
Cdd:TIGR00957 943 DKAQTGQVELSVYWDYMKAI-GLFITFLSIFLFVCNHVSALASNYWLSLWTDDP--MVNGTQNNTSL--RLSVYGALG-- 1015
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 850 vyqwVYTASMVFMLVFGVTKGFVFtkttlmASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAEN 929
Cdd:TIGR00957 1016 ----ILQGFAVFGYSMAVSIGGIQ------ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKM 1085
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 930 FLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKES 1009
Cdd:TIGR00957 1086 FMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQER 1165
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1010 CITYHLLYFN----------CALRWFALRMDVLMNILTFTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTE 1079
Cdd:TIGR00957 1166 FIHQSDLKVDenqkayypsiVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSE 1245
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1080 TQAKFTSVELLREYISTcvpECTHPLKV-GTCPKD-WPSRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTG 1157
Cdd:TIGR00957 1246 METNIVAVERLKEYSET---EKEAPWQIqETAPPSgWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTG 1322
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1158 SGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGTVRYNLDPFESHTDEMLWQVLERTFMRD 1237
Cdd:TIGR00957 1323 AGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKT 1402
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1238 TIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNT 1317
Cdd:TIGR00957 1403 FVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT 1482
|
1370 1380
....*....|....*....|....*...
gi 89111135 1318 VLNCDHVLVMENGKVIEFDKP-EVLAEK 1344
Cdd:TIGR00957 1483 IMDYTRVIVLDKGEVAEFGAPsNLLQQR 1510
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
45-1350 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 802.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 45 PVDDAGLLSFATFSWLTPVMVKGYRQRLTVDTLPPLSTYDSSDTNAKRFRVLWDEEVARVGPEK-ASLSHVVWKfqrtRV 123
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKPKPWLlRALNNSLGG----RF 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 124 LMDIVANILCIIMAAIGPVILIHqiLQQTERTSGKVWVGIGLCIALFATEFTKVFFWALAWAINYRTAIRLKVALSTLVF 203
Cdd:PLN03130 304 WLGGFFKIGNDLSQFVGPLLLNL--LLESMQNGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVF 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 204 ENlvSFKtLTHIS-----VGEVLNILSSDSYSLFEaalFC-------PLPATIPILMVFCaayaFFILGPTALIGISVYV 271
Cdd:PLN03130 382 RK--SLR-LTHEGrkkftSGKITNLMTTDAEALQQ---ICqqlhtlwSAPFRIIIAMVLL----YQQLGVASLIGSLMLV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 272 IFIPVQMFMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAP 351
Cdd:PLN03130 452 LMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILN 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 352 IVSTIAIVLTLSCHILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRMKKILIDK------SPPsyiT 425
Cdd:PLN03130 532 SIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEervllpNPP---L 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 426 QPEDPdtVLLLANATLTWEHEASRkstpkklqnqkrhlckkqrseaysersppakgatgpeeqsdslkSVLHSISFVVRK 505
Cdd:PLN03130 609 EPGLP--AISIKNGYFSWDSKAER--------------------------------------------PTLSNINLDVPV 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 506 GKILGICGNVGSGKSSLLAALLGQM-QLQKGVVAVNGTLAYVSQQAWIFHGNVRENILFGEKYDHQRYQHTVRVCGLQKD 584
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHD 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 585 LSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQF 664
Cdd:PLN03130 723 LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHF 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 665 LESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNlrglqfkdpehlynAAMVEAFKESPAEREEDAGIIVLAPGNEK 744
Cdd:PLN03130 803 LSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMEN--------------AGKMEEYVEENGEEEDDQTSSKPVANGNA 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 745 DEGKESetGSEFVDTKVPEHQLIQTESPQEGTVTWKTYHTYIKASGGYLLslfTVFLFLLMIGSAAF---SNWWLGLWLD 821
Cdd:PLN03130 869 NNLKKD--SSSKKKSKEGKSVLIKQEERETGVVSWKVLERYKNALGGAWV---VMILFLCYVLTEVFrvsSSTWLSEWTD 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 822 KGSRMTCGPQgnrtmcevgavladigqhVYQWVYTasmvfMLVFG---VTKG--FVFTKTTLMASSSLHDTVFDKILKSP 896
Cdd:PLN03130 944 QGTPKTHGPL------------------FYNLIYA-----LLSFGqvlVTLLnsYWLIMSSLYAAKRLHDAMLGSILRAP 1000
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 897 MSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQEL 976
Cdd:PLN03130 1001 MSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREV 1080
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 977 KKVENVSRSPWFTHITSSMQGLGIIHAY----------GKK-ESCITYHLLYFNcALRWFALRMDVLMNILTFTVALLVT 1045
Cdd:PLN03130 1081 KRLDSITRSPVYAQFGEALNGLSTIRAYkaydrmaeinGRSmDNNIRFTLVNMS-SNRWLAIRLETLGGLMIWLTASFAV 1159
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1046 LSFSSISTSSK-----GLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREYI-----STCVPECTHPlkvgtcPKDWP 1115
Cdd:PLN03130 1160 MQNGRAENQAAfastmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIdlpseAPLVIENNRP------PPGWP 1233
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1116 SRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT 1195
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 KLTVIPQDPVLFVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNS 1275
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1276 KIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFA 1350
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
45-1353 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 758.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 45 PVDDAGLLSFATFSWLTPVMVKGYRQRLTVDTLPPLSTYDSSDTNAKRFRVLWDEEVARVGP-----EKASLSHVVWKFQ 119
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRPKPwllraLNNSLGGRFWLGG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 120 RTRVLMDIvanilciiMAAIGPVILIHqILQQTERtSGKVWVGIGLCIALFatefTKVFFWALAWAINYRTAIRLKVAL- 198
Cdd:PLN03232 308 IFKIGHDL--------SQFVGPVILSH-LLQSMQE-GDPAWVGYVYAFLIF----FGVTFGVLCESQYFQNVGRVGFRLr 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 199 STLVFENLVSFKTLTH-----ISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPTALIGISVYVIF 273
Cdd:PLN03232 374 STLVAAIFHKSLRLTHearknFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 274 IPVQMFMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIV 353
Cdd:PLN03232 454 IPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSI 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 354 STIAIVLTLSCHILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRMKKILIDK------SPPsyiTQP 427
Cdd:PLN03232 534 PVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEerilaqNPP---LQP 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 428 EDPdtVLLLANATLTWEHEASrkstpkklqnqkrhlckkqrseaysersppakgatgpeeqsdslKSVLHSISFVVRKGK 507
Cdd:PLN03232 611 GAP--AISIKNGYFSWDSKTS--------------------------------------------KPTLSDINLEIPVGS 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 508 ILGICGNVGSGKSSLLAALLGQM-QLQKGVVAVNGTLAYVSQQAWIFHGNVRENILFGEKYDHQRYQHTVRVCGLQKDLS 586
Cdd:PLN03232 645 LVAIVGGTGEGKTSLISAMLGELsHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLD 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 587 NLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLE 666
Cdd:PLN03232 725 LLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLP 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 667 SCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNlrglqfkdpehlynAAMVEAFKEspaEREEDAGIIVLAPGNEKDE 746
Cdd:PLN03232 805 LMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMEN--------------AGKMDATQE---VNTNDENILKLGPTVTIDV 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 747 gKESETGSeFVDTKVPEHQLIQTESPQEGTVTWKTYHTYIKASGGYLLSLFTVFLFLLMIGSAAFSNWWLGLWLDKGSRM 826
Cdd:PLN03232 868 -SERNLGS-TKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPK 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 827 TCGPQgnrtmcevgavladigqhVYQWVYTasmvfMLVFG-----VTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFD 901
Cdd:PLN03232 946 SYSPG------------------FYIVVYA-----LLGFGqvavtFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFH 1002
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 902 TTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVEN 981
Cdd:PLN03232 1003 TNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDS 1082
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 982 VSRSPWFTHITSSMQGLGIIHAY----------GKKESCITYHLLYFNCALRWFALRMDVLMNILTFTVALLVTLSF--- 1048
Cdd:PLN03232 1083 VTRSPIYAQFGEALNGLSSIRAYkaydrmakinGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNgna 1162
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1049 --SSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREYIStcVP-ECTHPLKVGTCPKDWPSRGEITFRDY 1125
Cdd:PLN03232 1163 enQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYID--LPsEATAIIENNRPVSGWPSRGSIKFEDV 1240
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1126 QMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPV 1205
Cdd:PLN03232 1241 HLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPV 1320
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 LFVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATA 1285
Cdd:PLN03232 1321 LFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1286 SMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFAMLL 1353
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
106-1355 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 698.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 106 PEKASLSHVVWKFQRTRVLMDIVANILCIIMAAIGPVILIHQILQQTERTSGKVWvGIGLCIALFATEFTKVFFWALAWA 185
Cdd:PTZ00243 229 PKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGR-GLGLVLTLFLTQLIQSVCLHRFYY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 186 INYRTAIRLKVALSTLVFEN--LVSFKTLTH--ISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGP 261
Cdd:PTZ00243 308 ISIRCGLQYRSALNALIFEKcfTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGW 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 262 TALIGISVYVIFIPVQMFMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKagf 341
Cdd:PTZ00243 388 CALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRD--- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 342 VQSGNSAL------APIVsTIAIVLTLscHILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRMKKIL 415
Cdd:PTZ00243 465 VQLARVATsfvnnaTPTL-MIAVVFTV--YYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFL 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 416 -IDKSPPSYI--------TQPEDPDT-----VL----------------------LLANATLTWEHEA----SRKSTPKK 455
Cdd:PTZ00243 542 eCDNATCSTVqdmeeywrEQREHSTAcqlaaVLenvdvtafvpvklprapkvktsLLSRALRMLCCEQcrptKRHPSPSV 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 456 L---------QNQKRHLCKKQRSEAYSERSPPAKGATGPEEQSDSL-----KSVLHSISFVVRKGKILGICGNVGSGKSS 521
Cdd:PTZ00243 622 VvedtdygspSSASRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFfelepKVLLRDVSVSVPRGKLTVVLGATGSGKST 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 522 LLAALLGQMQLQKGVVAVNGTLAYVSQQAWIFHGNVRENILFGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGL 601
Cdd:PTZ00243 702 LLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGV 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 602 NLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICE 681
Cdd:PTZ00243 782 NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEF 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 682 KGTHKELMEergryAKLIHNLRGLQFKDPEHlynaamveafKESPAEREEDAGIIvlAPGNEKDEGKESET------GSE 755
Cdd:PTZ00243 862 SGSSADFMR-----TSLYATLAAELKENKDS----------KEGDADAEVAEVDA--APGGAVDHEPPVAKqegnaeGGD 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 756 FVDTKVPEHQLIQTESPQEGTVTWKTYHTYIKASGGYLLSLFTVFLFLLMIGSAAFSNWWLGLWLDKGsrmtcgpqgnrt 835
Cdd:PTZ00243 925 GAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMWSTRS------------ 992
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 836 mcevgavlADIGQHVYQWVYTAsMVFMLVFGVTKGFVFTKTTL-MASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSK 914
Cdd:PTZ00243 993 --------FKLSAATYLYVYLG-IVLLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSR 1063
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 915 DMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSS 994
Cdd:PTZ00243 1064 DIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEA 1143
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 995 MQGLGIIHAYGKKESCITYHLLYF----------NCALRWFALRMDVLMNILTFTVALLVTLSFSSISTSSK----GLSL 1060
Cdd:PTZ00243 1144 LQGSATITAYGKAHLVMQEALRRLdvvyscsyleNVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSQEiglvSLSL 1223
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1061 SYIIQLSGLLQVCVRTGTETQAKFTSVELLREYI-----------------------------STCVPECTHPlkVGTCP 1111
Cdd:PTZ00243 1224 TMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdevphedmpeldeevdalerrtgmaadvtGTVVIEPASP--TSAAP 1301
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1112 KDWPSrGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLE 1191
Cdd:PTZ00243 1302 HPVQA-GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLR 1380
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1192 DLRTKLTVIPQDPVLFVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARAL 1271
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1272 L-RNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFA 1350
Cdd:PTZ00243 1461 LkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
....*
gi 89111135 1351 MLLAA 1355
Cdd:PTZ00243 1541 SMVEA 1545
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-1336 |
2.73e-165 |
|
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: 534.49 E-value: 2.73e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 44 NPVDDAGLLSFATFSWLTPVMVKGYRQRLTVDTLPPLSTYDSSDTNAKRFRVLWDEEVARVGPEKASLSHV----VWKFQ 119
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKLLNALrrcfFWRFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 120 RTRVLMDIVANILCIIMAAIGPVILIHQILQQTERTSGkVWVGIGLCIaLFATEFtkVFFWALAWAINYrTAIRLKVALS 199
Cdd:TIGR01271 84 FYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIA-YYLALGLCL-LFIVRT--LLLHPAIFGLHH-LGMQMRIALF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 200 TLVFENLV--SFKTLTHISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQ 277
Cdd:TIGR01271 159 SLIYKKTLklSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 278 MFMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTIA 357
Cdd:TIGR01271 239 ACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 358 IVLTLSCH-----ILLRRKLTApVAFSVIAMFNVMKfsiaILPFSIKAMAEANVSLRRMKKILID---KSPPSYITQPEd 429
Cdd:TIGR01271 319 VFLSVVPYalikgIILRRIFTT-ISYCIVLRMTVTR----QFPGAIQTWYDSLGAITKIQDFLCKeeyKTLEYNLTTTE- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 430 pdtvLLLANATLTWEHEASRKSTPKKLQNQKRHLCKKQRSEAYSERSPpakgatgpeeqsdSLKSVLHSISFVVRKGKIL 509
Cdd:TIGR01271 393 ----VEMVNVTASWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNFSL-------------YVTPVLKNISFKLEKGQLL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 510 GICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWIFHGNVRENILFGEKYDHQRYQHTVRVCGLQKDLSNLP 589
Cdd:TIGR01271 456 AVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFP 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 590 YGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLESCD 669
Cdd:TIGR01271 536 EKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKAD 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 670 EVILLEDGEICEKGTHKELMEERG-------------------RYAKLIHNLR--GLQFKDPEHLYNAAMVEAFKESPAE 728
Cdd:TIGR01271 616 KILLLHEGVCYFYGTFSELQAKRPdfsslllgleafdnfsaerRNSILTETLRrvSIDGDSTVFSGPETIKQSFKQPPPE 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 729 -REEDAGIIVLAP------------GNEKDEGKESETGS--------------EFVDTKVPEHQLIQTESPQEG------ 775
Cdd:TIGR01271 696 fAEKRKQSIILNPiasarkfsfvqmGPQKAQATTIEDAVrepserkfslvpedEQGEESLPRGNQYHHGLQHQAqrrqsv 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 776 --------------------------------------------------------------------------TVTWKT 781
Cdd:TIGR01271 776 lqlmthsnrgenrreqlqtsfrkkssitqqnelaseldiysrrlskdsvyeiseeineedlkecfaderenvfeTTTWNT 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 782 YHTYIKASGgyllSLFTVFLFLLMIGSAAFSNWWLGLWLDKGSRMTCGPQGN-----RTMCEVGAVLADIGQHVYQ-WVY 855
Cdd:TIGR01271 856 YLRYITTNR----NLVFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNYVDQqhanaSSPDVQKPVIITPTSAYYIfYIY 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 856 TASMVFMLVFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFF 935
Cdd:TIGR01271 932 VGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTL 1011
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 936 MVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCIT-YH 1014
Cdd:TIGR01271 1012 IVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETlFH 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1015 ----------LLYFNcALRWFALRMDVLMnILTFTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAKF 1084
Cdd:TIGR01271 1092 kalnlhtanwFLYLS-TLRWFQMRIDIIF-VFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLM 1169
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1085 TSVELLREYISTcVPECTHPLKVGT--------------CPKDWPSRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTV 1150
Cdd:TIGR01271 1170 RSVSRVFKFIDL-PQEEPRPSGGGGkyqlstvlvienphAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRV 1248
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1151 GIVGRTGSGKSSLGMALFRLVEpASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGTVRYNLDPFESHTDEMLWQVL 1230
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVA 1327
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1231 ERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLT 1310
Cdd:TIGR01271 1328 EEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL 1407
|
1450 1460
....*....|....*....|....*.
gi 89111135 1311 IAHRLNTVLNCDHVLVMENGKVIEFD 1336
Cdd:TIGR01271 1408 SEHRVEALLECQQFLVIEGSSVKQYD 1433
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
125-411 |
1.08e-131 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 406.56 E-value: 1.08e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 125 MDIVANILCIIMAAIGPVILIHQILQQTERTSGKVWVGIGLCIALFATEFTKVFFWALAWAINYRTAIRLKVALSTLVFE 204
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 205 NLVSFKTLTHISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMFMAKLN 284
Cdd:cd18592 81 KILRLRSLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 285 SAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTIAIVLTLSC 364
Cdd:cd18592 161 GKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 89111135 365 HILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRM 411
Cdd:cd18592 241 HVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
791-1094 |
1.50e-125 |
|
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: 391.16 E-value: 1.50e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 791 GYLLSLFTVFLFLLMIGSAAFSNWWLGLWLDKGSRMTCGPQGNrTMCEVGAVLADIGQHVYQWVYTASMVFMLVFGVTKG 870
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDN-STVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 871 FVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPA 950
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 951 VLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCI----------TYHLLYFNC 1020
Cdd:cd18599 160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLskfkklldqnSSAFFLFNC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1021 ALRWFALRMDVLMNILTFTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREYI 1094
Cdd:cd18599 240 AMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1118-1338 |
3.43e-123 |
|
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: 381.07 E-value: 3.43e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1118 GEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKL 1197
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDPVLFVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKI 1277
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1278 ILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKP 1338
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
486-678 |
4.98e-105 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 331.36 E-value: 4.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 486 EEQSDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWIFHGNVRENILFGE 565
Cdd:cd03250 11 DSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 566 KYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEEC 645
Cdd:cd03250 91 PFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC 170
|
170 180 190
....*....|....*....|....*....|....
gi 89111135 646 IKKTLR-GKTVVLVTHQLQFLESCDEVILLEDGE 678
Cdd:cd03250 171 ILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
778-1358 |
1.22e-97 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 325.20 E-value: 1.22e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 778 TWKTYHTYIKASGGYLLSLFTVFLFLLMIGSAAFSN-WWLGLWLDKGSrmtcgpqgnrtmceVGAVLADIGQHVyqWVYT 856
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLpLLLGRIIDALL--------------AGGDLSALLLLL--LLLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 857 ASMVFMLVFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFM 936
Cdd:COG1132 69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 937 VVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKE------SC 1010
Cdd:COG1132 149 LIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREErelerfRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1011 ITYHLLYFNCALRWFALRMDVLMNILtFTVALLVTLSFSSISTSSKGLS-------LSYIIQLSGLLQVCVRTGTETQAK 1083
Cdd:COG1132 229 ANEELRRANLRAARLSALFFPLMELL-GNLGLALVLLVGGLLVLSGSLTvgdlvafILYLLRLFGPLRQLANVLNQLQRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1084 FTSVELLREYISTC--VPECTHPLKVGtcpkdwPSRGEITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKS 1161
Cdd:COG1132 308 LASAERIFELLDEPpeIPDPPGAVPLP------PVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1162 SLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGTVRYNL---DPfeSHTDEMLWQVLERTFMRDT 1238
Cdd:COG1132 381 TLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1239 IMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTV 1318
Cdd:COG1132 459 IEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTI 538
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 89111135 1319 LNCDHVLVMENGKVIEFDKPEVLAEKpDSAFAMLLAAEVR 1358
Cdd:COG1132 539 RNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQFG 577
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1114-1338 |
1.58e-86 |
|
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: 280.07 E-value: 1.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1114 WPSRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL 1193
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1194 RTKLTVIPQDPVLFVGTVRYNLDPFESHTDEMLWQVLertfmrdtimklpeklqaEVTENGENFSVGERQLLCVARALLR 1273
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1274 NSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKP 1338
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
853-1344 |
1.86e-81 |
|
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: 283.26 E-value: 1.86e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 853 WVYTASMVFMLVF----GVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSkDMDELDVRLPFHAE 928
Cdd:COG2274 196 WVLAIGLLLALLFegllRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 929 NFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGkKE 1008
Cdd:COG2274 275 TALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALG-AE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1009 SC-------ITYHLLYFNCALRWFALRMDVLMNILT--FTVALLV-----------TLSFSSISTSSKGLSLSYIIQLSG 1068
Cdd:COG2274 354 SRfrrrwenLLAKYLNARFKLRRLSNLLSTLSGLLQqlATVALLWlgaylvidgqlTLGQLIAFNILSGRFLAPVAQLIG 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1069 LLQvcvrtgtETQAKFTSVELLREYISTcVPECTHPLKVGTCPKDwpsRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQ 1148
Cdd:COG2274 434 LLQ-------RFQDAKIALERLDDILDL-PPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPVLDNISLTIKPGE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1149 TVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGTVRYNL---DPfeSHTDEM 1225
Cdd:COG2274 503 RVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1226 LWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKG 1305
Cdd:COG2274 581 IIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG 660
|
490 500 510
....*....|....*....|....*....|....*....
gi 89111135 1306 CTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEK 1344
Cdd:COG2274 661 RTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1118-1356 |
1.36e-75 |
|
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: 251.37 E-value: 1.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1118 GEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKL 1197
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDPVLFVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKI 1277
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1278 ILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAE 1356
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTD 256
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
115-709 |
2.45e-74 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 259.33 E-value: 2.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 115 VWKF---QRTRVLMDIVANILCIIMAAIGPVIL---IHQILQQTERTSGKVWVGIGLCIALFateftKVFFWALAWAINY 188
Cdd:COG1132 12 LLRYlrpYRGLLILALLLLLLSALLELLLPLLLgriIDALLAGGDLSALLLLLLLLLGLALL-----RALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 189 RTAIRLKVALSTLVFENL--VSFKTLTHISVGEVLNILSSDSYSLFEAALFCPLPA-TIPILMVFCAAYAFFI---LGPT 262
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLlrLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLvRSVVTLIGALVVLFVIdwrLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 263 ALIGISVYVIFIPVqmFMAKLNSAFRRSAILVtDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFV 342
Cdd:COG1132 167 VLLVLPLLLLVLRL--FGRRLRKLFRRVQEAL-AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 343 QSGNSALAPIVSTIAIVLTL--SCHILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRMKKILiDksp 420
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLlvGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL-D--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 421 psyiTQPEDPDtvlllanatltweheasrKSTPKKLQNQKRHLCKKQRSEAYSERSPpakgatgpeeqsdslksVLHSIS 500
Cdd:COG1132 320 ----EPPEIPD------------------PPGAVPLPPVRGEIEFENVSFSYPGDRP-----------------VLKDIS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 501 FVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRENILFG-EK 566
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGrPD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 567 YDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEEcI 646
Cdd:COG1132 441 ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-L 519
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 647 KKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHnlrgLQFKD 709
Cdd:COG1132 520 ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR----LQFGE 578
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
795-1094 |
7.20e-71 |
|
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: 239.33 E-value: 7.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 795 SLFTVFLFLLMIGSAAFSNWWLGLWLDKGSRMTcgpqgnrtmcevgavlaDIGQHVYQWVYTA-SMVFMLVFGVTKGFVF 873
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSP-----------------NSSSGYYLGVYAAlLVLASVLLVLLRWLLF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 874 TKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLL 953
Cdd:cd18580 64 VLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 954 VVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCIT--YHLL--------YFNCALR 1023
Cdd:cd18580 144 VLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEenLRLLdasqrafyLLLAVQR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1024 WFALRMDVLMNILTFTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREYI 1094
Cdd:cd18580 224 WLGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1118-1344 |
2.52e-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: 235.20 E-value: 2.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1118 GEITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKL 1197
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDPVLFVGTVRYNLDPF-ESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSK 1276
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGrPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1277 IILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEK 1344
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
127-411 |
2.88e-70 |
|
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: 237.38 E-value: 2.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 127 IVANILCIIMAAIGPvILIHQILQQTERTSGK-VWVGIGLCIALFATEFTKVFFWALAWAINYRTAIRLKVALSTLVFE- 204
Cdd:cd18579 3 GLLKLLEDLLSLAQP-LLLGLLISYLSSYPDEpLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 205 -NLVSFKTLTHISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMFMAKL 283
Cdd:cd18579 82 aLRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 284 NSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTIAIVLTLS 363
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 89111135 364 CHILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRM 411
Cdd:cd18579 242 TYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
882-1344 |
8.36e-70 |
|
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: 245.44 E-value: 8.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 882 SSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDvrlPFHAeNFLQQFFMVVFI-LVILAAVFPA------VLLV 954
Cdd:COG4988 91 RRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALD---GYFA-RYLPQLFLAALVpLLILVAVFPLdwlsglILLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 955 VASLAVGFFIL--------------------------------LRIFHRGVQELKKVENVSRSpwFTHITssMQGLGIih 1002
Cdd:COG4988 167 TAPLIPLFMILvgkgaakasrrqwralarlsghfldrlrglttLKLFGRAKAEAERIAEASED--FRKRT--MKVLRV-- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1003 aygkkescityhllyfncalrwfALR----MDVLMNILTFTVALLVtlsfssistsskGLSLSYI-IQLSGLLQVCV--- 1074
Cdd:COG4988 241 -----------------------AFLssavLEFFASLSIALVAVYI------------GFRLLGGsLTLFAALFVLLlap 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1075 ------RT-GTETQAKFTSV---ELLREYISTCVPEcthpLKVGTCPKDWPSRGEITFRDYQMRYRDNTPlVLDSLNLNI 1144
Cdd:COG4988 286 efflplRDlGSFYHARANGIaaaEKIFALLDAPEPA----APAGTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1145 QSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGTVRYNLDPFESH-TD 1223
Cdd:COG4988 361 PPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDaSD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1224 EMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAF 1303
Cdd:COG4988 441 EELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA 520
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 89111135 1304 KGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEK 1344
Cdd:COG4988 521 KGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1120-1331 |
2.07e-63 |
|
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: 213.01 E-value: 2.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVGTVRYNLdpfeshtdemlwqvlertfmrdtimklpeklqaevtengenFSVGERQLLCVARALLRNSKIIL 1279
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 89111135 1280 LDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGK 1331
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
77-701 |
3.98e-62 |
|
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: 226.64 E-value: 3.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 77 LPPLSTYDSSDTNAKRFRVLWdeevARVGPEKASLSHVvwkfqrtrvlmdIVANILCIIMAAIGPV---ILIHQILQQTE 153
Cdd:COG2274 128 LEPTPEFDKRGEKPFGLRWFL----RLLRRYRRLLLQV------------LLASLLINLLALATPLftqVVIDRVLPNQD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 154 RTSgkVWV-GIGLCIALfateftkVFFWALAWAINY---RTAIRLKVALSTLVFENLVSFKT--LTHISVGEVLN----- 222
Cdd:COG2274 192 LST--LWVlAIGLLLAL-------LFEGLLRLLRSYlllRLGQRIDLRLSSRFFRHLLRLPLsfFESRSVGDLASrfrdv 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 223 -----ILSSDSYSLFEAALFcplpatIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMFMAKLNS-AFRRSAilvtd 296
Cdd:COG2274 263 esireFLTGSLLTALLDLLF------VLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSReESEASA----- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 297 KRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTI--AIVLTLSCHILLRRKLTA 374
Cdd:COG2274 332 KRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLatVALLWLGAYLVIDGQLTL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 375 P--VAFSVIA-MFNVmkfSIAILPFSIKAMAEANVSLRRMKKILidKSPPsyitqpedpdtvlllanatltwehEASRKS 451
Cdd:COG2274 412 GqlIAFNILSgRFLA---PVAQLIGLLQRFQDAKIALERLDDIL--DLPP------------------------EREEGR 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 452 TPKKLQNQKRHLCKKQRSEAYSERSPPakgatgpeeqsdslksVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQ 531
Cdd:COG2274 463 SKLSLPRLKGDIELENVSFRYPGDSPP----------------VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 532 LQKGVVAVNGT-------------LAYVSQQAWIFHGNVRENILFG-EKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIG 597
Cdd:COG2274 527 PTSGRILIDGIdlrqidpaslrrqIGVVLQDVFLFSGTIRENITLGdPDATDEEIIEAARLAGLHDFIEALPMGYDTVVG 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 598 ERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFeECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDG 677
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL-ENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKG 685
|
650 660
....*....|....*....|....
gi 89111135 678 EICEKGTHKELMEERGRYAKLIHN 701
Cdd:COG2274 686 RIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
795-1093 |
4.39e-62 |
|
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: 214.26 E-value: 4.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 795 SLFTVFLFLLMIGSAAFSNWWLGLWLDKGSRMTCGPQGNRtmcevgavladigqHVYQWVYTASMVFMLVFGVTKGFVFT 874
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQR--------------DYRLGVYGALGLGQAIFVFLGSLALA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 875 KTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLV 954
Cdd:cd18603 67 LGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 955 VASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCIT--------YHLLYFN--CALRW 1024
Cdd:cd18603 147 IIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIResdrrvdeNQRAYYPsiVSNRW 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1025 FALRMDVLMNILTFTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREY 1093
Cdd:cd18603 227 LAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1120-1334 |
2.59e-61 |
|
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: 2.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRY--RDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKL 1197
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDPVLFVGTVRYNL---DPfeSHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRN 1274
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygKP--DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1275 SKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 1334
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1120-1344 |
6.01e-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: 208.62 E-value: 6.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVGTVRYNL---DPfeSHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSK 1276
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRP--DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1277 IILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEK 1344
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
887-1345 |
1.22e-60 |
|
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: 218.87 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 887 TVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELD-----VRLPfhaenflqqffMVVFILVILAAVF-------PAVLLV 954
Cdd:COG4987 93 RLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylrVLLP-----------LLVALLVILAAVAflaffspALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 955 VASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKEScityHLLYFNCA-LRWFAL--RMDV 1031
Cdd:COG4987 162 ALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDR----ALARLDAAeARLAAAqrRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1032 L------MNILTFTVALLVTLSFSSISTSSKGLSLSYII-----------QLSGLLQVCVRTGtETQAkftSVELLREyI 1094
Cdd:COG4987 238 LsalaqaLLQLAAGLAVVAVLWLAAPLVAAGALSGPLLAllvlaalalfeALAPLPAAAQHLG-RVRA---AARRLNE-L 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1095 STCVPECTHPlkvgTCPKDWPSRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA 1174
Cdd:COG4987 313 LDAPPAVTEP----AEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1175 SGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGTVRYNL---DPfeSHTDEMLWQVLERTFMRDTIMKLPEKLQAEVT 1251
Cdd:COG4987 389 SGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLG 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1252 ENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGK 1331
Cdd:COG4987 467 EGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGR 546
|
490
....*....|....
gi 89111135 1332 VIEFDKPEVLAEKP 1345
Cdd:COG4987 547 IVEQGTHEELLAQN 560
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
849-1334 |
6.80e-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: 216.89 E-value: 6.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 849 HVYQWVYTASMVFMLVFGVTKgfvFTKTTLMASSS---LHD---TVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVR 922
Cdd:TIGR02203 51 SVLWWVPLVVIGLAVLRGICS---FVSTYLLSWVSnkvVRDirvRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 923 LPFHAENFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIH 1002
Cdd:TIGR02203 128 ATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1003 AYGKKEscitYHLLYFNCA---LRWFALRMDVLMNILT----------FTVALLVTLSFSSISTSSKGLSLSYIIQLsGL 1069
Cdd:TIGR02203 208 LFGGQA----YETRRFDAVsnrNRRLAMKMTSAGSISSpitqliaslaLAVVLFIALFQAQAGSLTAGDFTAFITAM-IA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1070 LQVCVRTGTETQAKFTSVELLREYISTCVPEcTHPLKVGTCPKDwPSRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQT 1149
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDS-PPEKDTGTRAIE-RARGDVEFRNVTFRYPGRDRPALDSISLVIEPGET 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1150 VGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGTVRYNL---DPfESHTDEML 1226
Cdd:TIGR02203 361 VALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEI 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1227 WQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGC 1306
Cdd:TIGR02203 440 ERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR 519
|
490 500
....*....|....*....|....*...
gi 89111135 1307 TVLTIAHRLNTVLNCDHVLVMENGKVIE 1334
Cdd:TIGR02203 520 TTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
799-1093 |
8.82e-60 |
|
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: 207.33 E-value: 8.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 799 VFLFLLMIGSAAFSNWWLGLWldkgsrmtcgpQGNRtmcevgavlADIGQHVYQWVY----TASMVFMLVFGvtkgFVFT 874
Cdd:cd18606 5 LLLLILSQFAQVFTNLWLSFW-----------TEDF---------FGLSQGFYIGIYaglgVLQAIFLFLFG----LLLA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 875 KTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLV 954
Cdd:cd18606 61 YLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 955 VASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCI--TYHLL------YF--NCALRW 1024
Cdd:cd18606 141 LPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIkkNEKLIdnmnraYFltIANQRW 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1025 FALRMDVLMNILTFTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREY 1093
Cdd:cd18606 221 LAIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1120-1334 |
4.80e-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: 197.45 E-value: 4.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVGTVRYNL---DPFEshTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSK 1276
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1277 IILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 1334
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
128-693 |
1.41e-56 |
|
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: 206.92 E-value: 1.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 128 VANILCIIMAAIGPVILIHQILQQtERTSGKVWVGIGLCIALFateftkVFFWALAWA---INYRTAIRLKVALSTLVFE 204
Cdd:COG4988 27 LLSGLLIIAQAWLLASLLAGLIIG-GAPLSALLPLLGLLLAVL------LLRALLAWLrerAAFRAAARVKRRLRRRLLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 205 NLVSF--KTLTHISVGEVLNILSS-----DSY-SLFEAALFcpLPATIPILMVfcaAYAFFILGPTALIgISVYVIFIPV 276
Cdd:COG4988 100 KLLALgpAWLRGKSTGELATLLTEgvealDGYfARYLPQLF--LAALVPLLIL---VAVFPLDWLSGLI-LLVTAPLIPL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 277 qmFMAKLNSAFRRsailVTDKRVQTM----NEFLTCIR---LIKMYAWEKSFTNTI----QDIRRRERKLLEKAgFVQSG 345
Cdd:COG4988 174 --FMILVGKGAAK----ASRRQWRALarlsGHFLDRLRgltTLKLFGRAKAEAERIaeasEDFRKRTMKVLRVA-FLSSA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 346 NSALAPIVStIAIVLTLSCHILLRRKLTAPVAFSVIAM----FnvmkfsiaiLP-------FSIKAMAEAnvSLRRMKKI 414
Cdd:COG4988 247 VLEFFASLS-IALVAVYIGFRLLGGSLTLFAALFVLLLapefF---------LPlrdlgsfYHARANGIA--AAEKIFAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 415 LidksppsyitqpEDPDTVLLLANATLTWEHEASrkstpkklqnqkrhLCKKQRSEAYSERSPpakgatgpeeqsdslks 494
Cdd:COG4988 315 L------------DAPEPAAPAGTAPLPAAGPPS--------------IELEDVSFSYPGGRP----------------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRENI 561
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRENL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFGE-KYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKH 640
Cdd:COG4988 432 RLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 641 VFEEcIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 693
Cdd:COG4988 512 ILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
495-699 |
8.86e-56 |
|
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: 195.46 E-value: 8.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWIFHGNVRENILFGEKYDHQRYQH 574
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 575 TVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKT 654
Cdd:cd03291 132 VVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKT 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 89111135 655 VVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 699
Cdd:cd03291 212 RILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
791-1093 |
3.11e-55 |
|
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: 195.23 E-value: 3.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 791 GYLLSLFTVFLFLLMIGSAAFSNWWLGLWLDKGSRMTCGPQGNRTMCEVGAVLADIGQHVYQWVYTASMVFMLVFGVTKG 870
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 871 FVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPA 950
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 951 VLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCI------------TYHLlyF 1018
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQeefdahqdlhseAWFL--F 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1019 NCALRWFALRMDVLMNILTFTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREY 1093
Cdd:cd18601 239 LATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
190-698 |
3.81e-55 |
|
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: 202.69 E-value: 3.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 190 TAIRLKV--ALSTLVFENLVSFKTlthisvGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPTA---- 263
Cdd:COG4987 88 ADLRVRLyrRLEPLAPAGLARLRS------GDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALalvl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 264 LIGISVYVIFIPVqmFMAKLNSAF-RRSAILVTDKRVQTMnEFLTCIRLIKMY----AWEKSFTNTIQDIRRRERKLLEK 338
Cdd:COG4987 162 ALGLLLAGLLLPL--LAARLGRRAgRRLAAARAALRARLT-DLLQGAAELAAYgaldRALARLDAAEARLAAAQRRLARL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 339 AGFVQSGNSALAPIvsTIAIVLTLSCHILLRRKLTAP----VAFSVIAMFNVmkfsIAILPFSIKAMAEANVSLRRMKKI 414
Cdd:COG4987 239 SALAQALLQLAAGL--AVVAVLWLAAPLVAAGALSGPllalLVLAALALFEA----LAPLPAAAQHLGRVRAAARRLNEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 415 LiDKSPPsyITQPEDP-----DTVLLLANATLTWEheasrkstpkklqnqkrhlckkqrseaysersppakGATGPeeqs 489
Cdd:COG4987 313 L-DAPPA--VTEPAEPapapgGPSLELEDVSFRYP------------------------------------GAGRP---- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 490 dslksVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGN 556
Cdd:COG4987 350 -----VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFG--EKYDHQRYQHTVRVcGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD 634
Cdd:COG4987 425 LRENLRLArpDATDEELWAALERV-GLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 635 AHVGKHVFEEcIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 698
Cdd:COG4987 504 AATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
796-1094 |
4.07e-55 |
|
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: 194.22 E-value: 4.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 796 LFTVFLFLLMIGSAAFSNWWLGLWLDKGSRMTCGPQGNRtmcevgavladigqHV--YQWVYTASMVFMLVFGVTKGFVF 873
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEV--------------SVlyYLGIYALISLLSVLLGTLRYLLF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 874 TKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLL 953
Cdd:cd18604 68 FFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 954 VVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCI-------------TYHLLYFNc 1020
Cdd:cd18604 148 PAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIeemlrridrysraFRYLWNLN- 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1021 alRWFALRMDVLMNILTFTVALLVTLSFSSISTSSkGLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREYI 1094
Cdd:cd18604 227 --RWLSVRIDLLGALFSFATAALLVYGPGIDAGLA-GFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
494-677 |
6.00e-55 |
|
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: 190.62 E-value: 6.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 494 SVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVN-----------------GTLAYVSQQAWIFHGN 556
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAH 636
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 89111135 637 VGKHVFEECIKKTLRG--KTVVLVTHQLQFLESCDEVILLEDG 677
Cdd:cd03290 175 LSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1104-1334 |
9.03e-55 |
|
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: 202.36 E-value: 9.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1104 PLKVGtcpkdwpsRGEITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEV 1183
Cdd:COG5265 350 PLVVG--------GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1184 DICILSLEDLRTKLTVIPQDPVLFVGTVRYNL---DPfeSHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVG 1260
Cdd:COG5265 421 DIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRP--DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGG 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1261 ERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 1334
Cdd:COG5265 499 EKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
131-411 |
3.36e-53 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 189.24 E-value: 3.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 131 ILCIIMAAI--GPVILIHQILQ----QTERTSGKVWVgigLCIALFATEFTKVFFWALAWAINYRTAIRLKVALSTLVFE 204
Cdd:cd18596 4 LLAVLSSVLsfAPPFFLNRLLRyledPGEDATVRPWV---WVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 205 nlvsfKTL--------------------------THISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFI 258
Cdd:cd18596 81 -----KALrrrdksgssksseskkkdkeededekSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 259 LGPTALIGISVYVIFIPVQMFMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEK 338
Cdd:cd18596 156 LGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRK 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 339 AGFVQSGNSALAPIVSTIAIVLTLSCHILL-RRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRM 411
Cdd:cd18596 236 RFLLDLLLSLLWFLIPILVTVVTFATYTLVmGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1120-1334 |
2.67e-52 |
|
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: 183.84 E-value: 2.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVGTVRYNLdpfeSHTDEM--LWQVLERTFM---RDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRN 1274
Cdd:cd03252 81 VLQENVLFNRSIRDNI----ALADPGmsMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1275 SKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 1334
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1118-1341 |
6.94e-52 |
|
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: 184.29 E-value: 6.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1118 GEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEpASGTIFIDEVDICILSLEDLRTKL 1197
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDPVLFVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKI 1277
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1278 ILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVL 1341
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
127-411 |
8.61e-51 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 181.50 E-value: 8.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 127 IVANILCIIMAAIGPVILIHQILQQTERTSGK----VWVGIGLCIALFATEFTKVFFWALAWAINYRTAIRLKVALSTLV 202
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEDAYLGGpppsIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 203 FE---NLvSFKTLTHISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMF 279
Cdd:cd18597 83 YRkslRL-SGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 280 MAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTIAIV 359
Cdd:cd18597 162 LMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 89111135 360 LTLSCHILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRM 411
Cdd:cd18597 242 LSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
795-1094 |
5.30e-50 |
|
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: 179.65 E-value: 5.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 795 SLFTVFLFLLMIGSAAFSNWWLGLWLDKGSrmtcgpqgnrtmcEVGAVLADIGQHVYQWVYTASMVFMLVFGVTKGFVFT 874
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSN-------------NSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 875 KTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLV 954
Cdd:cd18605 68 YGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 955 VASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCITYHLLYFNCALR----------W 1024
Cdd:cd18605 148 LLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRaqlasqaasqW 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1025 FALRMDVLMNILTFTVALLVTLSFSSISTSSK---GLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREYI 1094
Cdd:cd18605 228 LSIRLQLLGVLIVTFVALTAVVQHFFGLSIDAgliGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
131-411 |
1.04e-48 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 175.35 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 131 ILCIIMAAIGPVILiHQILQQTERTSGKVWVGIGLCIALFATEFTKVFFWALAWAINYRTAIRLKVALSTLVFEnlvsfK 210
Cdd:cd18595 7 LLSDILLFASPQLL-KLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYR-----K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 211 TLThIS--------VGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMFMAK 282
Cdd:cd18595 81 ALR-LSnsarkkstVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 283 LNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTIAIVLTL 362
Cdd:cd18595 160 KIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 89111135 363 SCHILL--RRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRM 411
Cdd:cd18595 240 ATYVLSdpDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1118-1333 |
4.36e-48 |
|
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: 171.23 E-value: 4.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1118 GEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKL 1197
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDPVLFVGTVRYNL---DPFesHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRN 1274
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1275 SKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVI 1333
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
887-1355 |
1.10e-47 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 180.93 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 887 TVFDKILKSPMSFFDTTPTGRLMNRFSKDMDEL-DVRLPFHAENFLQQFFMVVFILVILAAVFP-AVLLVVasLAVGFFI 964
Cdd:PRK13657 94 EYFERIIQLPLAWHSQRGSGRALHTLLRGTDALfGLWLEFMREHLATLVALVVLLPLALFMNWRlSLVLVV--LGIVYTL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 965 LLRIFHRGVQELK-KVENvSRSPWFTHITSSMQGLGIIHAYGKKES------CITYHLLYF-NCALRWFALRmdVLMNIL 1036
Cdd:PRK13657 172 ITTLVMRKTKDGQaAVEE-HYHDLFAHVSDAIGNVSVVQSYNRIEAetqalrDIADNLLAAqMPVLSWWALA--SVLNRA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1037 TFTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSVEL----LREYIST--CVPECTHPLKVGTC 1110
Cdd:PRK13657 249 ASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMaapkLEEFFEVedAVPDVRDPPGAIDL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1111 PKdwpSRGEITFRDYQMRYrDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSL 1190
Cdd:PRK13657 329 GR---VKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1191 EDLRTKLTVIPQDPVLFVGTVRYNLD-PFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVAR 1269
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRvGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1270 ALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE---FDkpEVLAEkpD 1346
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFD--ELVAR--G 560
|
....*....
gi 89111135 1347 SAFAMLLAA 1355
Cdd:PRK13657 561 GRFAALLRA 569
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
162-411 |
1.59e-47 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 172.02 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 162 GIGLCIALFATEFTKVFFWALawainyRTAIRLKVALSTLVFENL--VSFKTLTHISVGEVLNILSSDSYSLFEAALFCP 239
Cdd:cd18593 45 GVSLCSFLFIITHHPYFFGMQ------RIGMRLRVACSSLIYRKAlrLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 240 LPATIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMFMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEK 319
Cdd:cd18593 119 YLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 320 SFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTIAIVLTLSCHILLRRKLTAPVAFSVIAMFNVMKFSIAI-LPFSI 398
Cdd:cd18593 199 AFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMTLfFPFAI 278
|
250
....*....|...
gi 89111135 399 KAMAEANVSLRRM 411
Cdd:cd18593 279 QFGSELSVSIRRI 291
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
840-1352 |
1.08e-46 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 180.30 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 840 GAVLADIGQHVYQWVYTASMVFMLVFGVT-------KGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRF 912
Cdd:TIGR00958 185 GRVIDTLGGDKGPPALASAIFFMCLLSIAssvsaglRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 913 SKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAvLLVVASLAVGFFILL-RIFHRGVQEL-KKVEN-------VS 983
Cdd:TIGR00958 265 SSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPR-LTMVTLINLPLVFLAeKVFGKRYQLLsEELQEavakanqVA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 984 RspwftHITSSMQ--------GLGIIHAYGKKESC--------ITYHLLYFNCALrwfaLRMDVLMNILTFTVALLVTls 1047
Cdd:TIGR00958 344 E-----EALSGMRtvrsfaaeEGEASRFKEALEETlqlnkrkaLAYAGYLWTTSV----LGMLIQVLVLYYGGQLVLT-- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1048 fssiSTSSKGLSLSYII---QLSGLLQVCVRTGTETQAKFTSVELLREYISTcVPECTHPlkVGTCPKdwPSRGEITFRD 1124
Cdd:TIGR00958 413 ----GKVSSGNLVSFLLyqeQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDR-KPNIPLT--GTLAPL--NLEGLIEFQD 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1125 YQMRY--RDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQ 1202
Cdd:TIGR00958 484 VSFSYpnRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1203 DPVLFVGTVRYNLD-PFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLD 1281
Cdd:TIGR00958 563 EPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1282 EATASMDSKTDTLVQNTIKdaFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDSAFAML 1352
Cdd:TIGR00958 643 EATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
131-410 |
2.36e-46 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 168.58 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 131 ILCIIMAAIGPV--ILIHQIL------QQTERTSGKVWvGIGLCIALFATeftkVFFWALAWAINYRTAIRLKVALSTLV 202
Cdd:cd18594 4 ILLFLEESLKIVqpLLLGRLVayfvpdSTVTKTEAYLY-ALGLSLCAFLR----VLLHHPYFFGLHRYGMQLRIALSSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 203 FENLVSFKT--LTHISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMFM 280
Cdd:cd18594 79 YKKTLKLSSsaLSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 281 AKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTIAIVL 360
Cdd:cd18594 159 GKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 89111135 361 TLSCHILLRRKLTAPVAFSVIAMFNVMKFSIAI-LPFSIKAMAEANVSLRR 410
Cdd:cd18594 239 TFVPYVLTGNTLTARKVFTVISLLNALRMTITRfFPESIQTLSESRVSLKR 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
493-698 |
6.33e-45 |
|
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: 162.40 E-value: 6.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRE 559
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFG-EKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVG 638
Cdd:cd03251 95 NIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ES 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 639 KHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 698
Cdd:cd03251 174 ERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1108-1354 |
7.53e-43 |
|
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: 168.20 E-value: 7.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1108 GTCPKDWPSRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICI 1187
Cdd:TIGR03796 466 ATSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREE 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1188 LSLEDLRTKLTVIPQDPVLFVGTVRYNL---DPfeSHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQL 1264
Cdd:TIGR03796 546 IPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQR 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1265 LCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDafKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEK 1344
Cdd:TIGR03796 624 LEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAV 701
|
250
....*....|
gi 89111135 1345 PdSAFAMLLA 1354
Cdd:TIGR03796 702 G-GAYARLIR 710
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
485-679 |
1.31e-42 |
|
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: 155.44 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 485 PEEQSDSLKSVlhsiSFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAW 551
Cdd:cd03245 13 PNQEIPALDNV----SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 552 IFHGNVRENILFGEKY-DHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:cd03245 89 LFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 89111135 631 SAVDAHVGKHVFEEcIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEI 679
Cdd:cd03245 169 SAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
796-1093 |
2.19e-42 |
|
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: 157.77 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 796 LFTVFLFLLMIGSAAFSNWWLGLWLDKGSRmtcgPQGNRTMCEVGAVLADIGQHvYQWVYTASMVFMLVFGVTKGFVFTK 875
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHD----VASVVFNITSSSLEDDEVSY-YISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 876 TTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLVV 955
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 956 ASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYG--KKESCITYH--------LLYFNCALRWF 1025
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRqqARFTQQMLElidrnntaFLFLNTANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1026 ALRMDVLMNILTFTVALLVTLSFSSISTSSK--GLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREY 1093
Cdd:cd18602 237 GIRLDYLGAVIVFLAALSSLTAALAGYISPSlvGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1108-1327 |
3.81e-42 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 163.23 E-value: 3.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1108 GTCPKDWPSRGEITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICI 1187
Cdd:TIGR02857 310 GKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1188 LSLEDLRTKLTVIPQDPVLFVGTVRYNLDPFESH-TDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLC 1266
Cdd:TIGR02857 389 ADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1267 VARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVM 1327
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
489-678 |
5.80e-42 |
|
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: 151.77 E-value: 5.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 489 SDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHG 555
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAYVPQDPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENILfgekydhqryqhtvrvcglqkdlsnlpygdlteigerglnlSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:cd03228 91 TIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 89111135 636 HvGKHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGE 678
Cdd:cd03228 130 E-TEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
495-674 |
6.71e-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: 162.46 E-value: 6.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIFHGNVRENI 561
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFGEKY-DHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKH 640
Cdd:TIGR02857 417 RLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAE 496
|
170 180 190
....*....|....*....|....*....|....
gi 89111135 641 VFEEcIKKTLRGKTVVLVTHQLQFLESCDEVILL 674
Cdd:TIGR02857 497 VLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
493-698 |
3.66e-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: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIFHGNVRE 559
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFG--EKYDHQRYQhTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHV 637
Cdd:cd03253 94 NIRYGrpDATDEEVIE-AAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 638 GKHVFEeCIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 698
Cdd:cd03253 173 EREIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
495-701 |
3.79e-41 |
|
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: 151.92 E-value: 3.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRENI 561
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFGEKYDHQR-YQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKH 640
Cdd:cd03249 98 RYGKPDATDEeVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 641 VfEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 701
Cdd:cd03249 178 V-QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1115-1352 |
4.39e-41 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 160.95 E-value: 4.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1115 PSRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLR 1194
Cdd:PRK11176 337 RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1195 TKLTVIPQDPVLFVGTVRYNLD--PFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALL 1272
Cdd:PRK11176 417 NQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1273 RNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKpDSAFAML 1352
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ-NGVYAQL 575
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
490-693 |
1.26e-40 |
|
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: 150.07 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 490 DSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGN 556
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmIGVVLQDTFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFGEKY-DHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:cd03254 93 IMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 636 HVGKHVfEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 693
Cdd:cd03254 173 ETEKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
93-709 |
1.45e-40 |
|
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: 159.11 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 93 FRVLWdeevARVGPEKASLshvvwkfqrtrvlmdIVANILCIIMAAIGPVI--LIHQILQQT--ERTSGKVW----VGIG 164
Cdd:TIGR02203 2 FRRLW----SYVRPYKAGL---------------VLAGVAMILVAATESTLaaLLKPLLDDGfgGRDRSVLWwvplVVIG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 165 LCIALFATEFTKVFFwaLAWAINyRTAIRLKVALSTLVFENLVSFKTLThiSVGEVLNILSSDSYSLFEAAlfcplpATI 244
Cdd:TIGR02203 63 LAVLRGICSFVSTYL--LSWVSN-KVVRDIRVRMFEKLLGLPVSFFDRQ--PTGTLLSRITFDSEQVASAA------TDA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 245 PILMV-------FCAAYAFFILGPTALIgisVYVIFIPVQMFMAKLNSAFRRsailVTDKRVQTMNEFLTCI-------R 310
Cdd:TIGR02203 132 FIVLVretltviGLFIVLLYYSWQLTLI---VVVMLPVLSILMRRVSKRLRR----ISKEIQNSMGQVTTVAeetlqgyR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 311 LIKMYAWEKSFTNTIQDIRRRERKLLEKagfVQSGNSALAPIVSTI-----AIVLTLSCHILLRRKLTAPVAFSVIAmfn 385
Cdd:TIGR02203 205 VVKLFGGQAYETRRFDAVSNRNRRLAMK---MTSAGSISSPITQLIaslalAVVLFIALFQAQAGSLTAGDFTAFIT--- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 386 vmkfSIAILPFSIKAMAEANVSLRRMkkILIDKSPPSYITQPEDPDTvlllanatltweheasrkstpkklqnQKRHLCK 465
Cdd:TIGR02203 279 ----AMIALIRPLKSLTNVNAPMQRG--LAAAESLFTLLDSPPEKDT--------------------------GTRAIER 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 466 ---KQRSEAYSERSPPAKgatgpeeqsdslKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT 542
Cdd:TIGR02203 327 argDVEFRNVTFRYPGRD------------RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 543 -------------LAYVSQQAWIFHGNVRENILFGE--KYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQ 607
Cdd:TIGR02203 395 dladytlaslrrqVALVSQDVVLFNDTIANNIAYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQ 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 608 RQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVfEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKE 687
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNE 553
|
650 660
....*....|....*....|..
gi 89111135 688 LMEERGRYAKLiHNlrgLQFKD 709
Cdd:TIGR02203 554 LLARNGLYAQL-HN---MQFRE 571
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1116-1334 |
1.56e-40 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 159.50 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1116 SRGEITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT 1195
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 KLTVIPQDPVLFVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNS 1275
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1276 KIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 1334
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
495-698 |
2.29e-40 |
|
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: 149.56 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIFHGNVRENI 561
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFG-EKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDaHVGKH 640
Cdd:cd03252 97 ALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-YESEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 641 VFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 698
Cdd:cd03252 176 AIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1131-1357 |
3.69e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 158.47 E-value: 3.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1131 DNTPLvLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGT 1210
Cdd:PRK11174 361 DGKTL-AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1211 VRYNLDPFESH-TDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDS 1289
Cdd:PRK11174 439 LRDNVLLGNPDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1290 KTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPdSAFAMLLAAEV 1357
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATLLAHRQ 585
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
476-701 |
5.79e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.62 E-value: 5.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 476 SPPAKGATGPeeqsdslksvlhsISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQkGVVAVNGT------------- 542
Cdd:PRK11174 359 SPDGKTLAGP-------------LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIelreldpeswrkh 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 543 LAYVSQQAWIFHGNVRENILFGEK-YDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDR 621
Cdd:PRK11174 425 LSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 622 QLYLLDDPLSAVDAHVGKHVFeECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 701
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVM-QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1120-1334 |
1.74e-38 |
|
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: 142.07 E-value: 1.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSlEDLRTKLTV 1199
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVGTVRYNLdpfeshtdemlwqvlertfmrdtimklpeklqaevtenGENFSVGERQLLCVARALLRNSKIIL 1279
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1280 LDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 1334
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
490-700 |
2.84e-38 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 152.17 E-value: 2.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 490 DSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVV-------------AVNGTLAYVSQQAWIFHGN 556
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFGE-KYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:PRK10789 405 VANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 636 HVgkhvfEECIKKTLR----GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 700
Cdd:PRK10789 485 RT-----EHQILHNLRqwgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1117-1332 |
3.94e-38 |
|
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: 142.61 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1117 RGEITFRDYQMRYRdNTP--LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLR 1194
Cdd:cd03248 9 KGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1195 TKLTVIPQDPVLFVGTVRYNLD-PFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLR 1273
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1274 NSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKV 1332
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
905-1315 |
5.39e-38 |
|
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: 150.59 E-value: 5.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 905 TGRLMNRFSKDMDELD---VR--LPFHAEnflqqfFMVVFILVILAAVF--PAVLLVVASLAVGFFILLRIFHRGVQELK 977
Cdd:TIGR02868 109 RGDLLGRLGADVDALQdlyVRviVPAGVA------LVVGAAAVAAIAVLsvPAALILAAGLLLAGFVAPLVSLRAARAAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 978 KVENVSRSPWFTHITSSMQGLGIIHAYGKKESCITYhllYFNCALRWFAL--RMDVL------MNILTFTVALLVTLSFS 1049
Cdd:TIGR02868 183 QALARLRGELAAQLTDALDGAAELVASGALPAALAQ---VEEADRELTRAerRAAAAtalgaaLTLLAAGLAVLGALWAG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1050 SISTSSKGLSLSYIiqlsGLLQVCVRTGTETQAKFT--SVELLREYISTC----VPECTHPLKVGTCPKDWPSRGE---I 1120
Cdd:TIGR02868 260 GPAVADGRLAPVTL----AVLVLLPLAAFEAFAALPaaAQQLTRVRAAAEriveVLDAAGPVAEGSAPAAGAVGLGkptL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1121 TFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVI 1200
Cdd:TIGR02868 336 ELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1201 PQDPVLFVGTVRYNLD-PFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIIL 1279
Cdd:TIGR02868 415 AQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILL 494
|
410 420 430
....*....|....*....|....*....|....*.
gi 89111135 1280 LDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRL 1315
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1115-1334 |
8.04e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 151.13 E-value: 8.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1115 PSRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLR 1194
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1195 TKLTVIPQDPVLFVGTVRYNL---DPfeSHTDEMLWQVLERTFMrDTIMKLPEKLQAEVTENGENFSVGERQLLCVARAL 1271
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1272 LRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 1334
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
162-410 |
1.19e-37 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 143.91 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 162 GIGLCIALFATEFTKVFFWALAWAINYRTAIRLKVALSTLVFENLVSFKTLT----HISVGEVLNILSSDSYSLFEAALF 237
Cdd:cd18591 55 GYVLAVILFLALLLQATFSQASYHIVIREGIRLKTALQAMIYEKALRLSSWNlssgSMTIGQITNHMSEDANNIMFFFWL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 238 CPLPATIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMFMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAW 317
Cdd:cd18591 135 IHYLWAIPLKIIVGLILLYLKLGVSALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 318 EKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTIAIVLTLSCHILLRRK-LTAPVAFSVIAMFNVMKFSIAILPF 396
Cdd:cd18591 215 ENIFLDKIQEARRKELKLLLKDAVYWSLMTFLTQASPILVTLVTFGLYPYLEGEpLTAAKAFSSLALFNQLTVPLFIFPV 294
|
250
....*....|....
gi 89111135 397 SIKAMAEANVSLRR 410
Cdd:cd18591 295 VIPILINAVVSTRR 308
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1128-1332 |
3.67e-37 |
|
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: 138.12 E-value: 3.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLF 1207
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 VGTVRYNLdpfeshtdemlwqvlertfmrdtimklpeklqaevtengenFSVGERQLLCVARALLRNSKIILLDEATASM 1287
Cdd:cd03246 89 SGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 89111135 1288 DSKTDTLVQNTIKDA-FKGCTVLTIAHRLNTVLNCDHVLVMENGKV 1332
Cdd:cd03246 128 DVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
489-684 |
2.26e-36 |
|
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: 137.62 E-value: 2.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 489 SDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIFHG 555
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENI-LFGEKYDHQRYQhTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD 634
Cdd:cd03244 93 TIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 89111135 635 AHVgkhvfEECIKKTLR----GKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 684
Cdd:cd03244 172 PET-----DALIQKTIReafkDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1126-1332 |
8.39e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.33 E-value: 8.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1126 QMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPV 1205
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 LFVGTVRYNLD-PFESHTDEMLWQVLERTFMRdtiMKLPEK-LQAEVtengENFSVGERQLLCVARALLRNSKIILLDEA 1283
Cdd:COG4619 85 LWGGTVRDNLPfPFQLRERKFDRERALELLER---LGLPPDiLDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1284 TASMDSKTDTLVQNTIKDAF--KGCTVLTIAH------RLntvlnCDHVLVMENGKV 1332
Cdd:COG4619 158 TSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
778-1094 |
1.01e-35 |
|
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: 138.78 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 778 TWKTYHTYIKASGGYLLSL-FTVFLFLLMIGSAAFSNWWLG--LWLDKGSRMTCGPQGnrtmceVGAVLADIGQHVYQWV 854
Cdd:cd18600 2 TWNTYLRYITSHKSLIFVLiLCLVIFAIEVAASLVGLWLLRsqADRVNTTRPESSSNT------YAVIVTFTSSYYVFYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 855 YTASMVFMLVFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQF 934
Cdd:cd18600 76 YVGVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 935 FMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCIT-Y 1013
Cdd:cd18600 156 LIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETlF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1014 H----------LLYFNcALRWFALRMDVLMnILTFTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAK 1083
Cdd:cd18600 236 HkalnlhtanwFLYLS-TLRWFQMRIEMIF-VIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSL 313
|
330
....*....|.
gi 89111135 1084 FTSVELLREYI 1094
Cdd:cd18600 314 MRSVSRIFKFI 324
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
495-698 |
1.36e-35 |
|
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: 145.66 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLlAALLGQMQL-QKGVVAVNG-------------TLAYVSQQAWIFHGNVREN 560
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTL-TKLLQRLYTpQHGQVLVDGvdlaiadpawlrrQMGVVLQENVLFSRSIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGE-KYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHvGK 639
Cdd:TIGR01846 551 IALCNpGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE-SE 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 640 HVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 698
Cdd:TIGR01846 630 ALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1120-1335 |
1.83e-35 |
|
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: 134.94 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRdntplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTK 1196
Cdd:cd03257 9 VSFPTGGGSVK-----ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1197 LTVIPQDPVLfvgtvryNLDPfeSHTdemLWQVLERTFMRDTIMKLPEKLQAEVTENGEN--------------FSVGER 1262
Cdd:cd03257 84 IQMVFQDPMS-------SLNP--RMT---IGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeevlnrypheLSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1263 QLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEF 1335
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1136-1343 |
2.33e-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: 140.27 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGTVRYNL 1215
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1216 DPFESHTDEmlwQVLE---RTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 1292
Cdd:COG4618 427 ARFGDADPE---KVVAaakLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGE 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1293 TLVQNTIKDAFK-GCTVLTIAHRLNTVLNCDHVLVMENGKVIEF-DKPEVLAE 1343
Cdd:COG4618 504 AALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFgPRDEVLAR 556
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
495-701 |
4.12e-34 |
|
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: 141.42 E-value: 4.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL-------------AYVSQQAWIFHGNVRENI 561
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqfiNYLPQEPYIFSGSILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFG--EKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGK 639
Cdd:TIGR01193 569 LLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEK 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 640 HVFEECIKktLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHN 701
Cdd:TIGR01193 649 KIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
495-707 |
4.93e-34 |
|
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: 139.45 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRENI 561
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVdlrqldpaelrarMALVPQDPVLFAASVMENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFG--EKYDHQRYQhTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGK 639
Cdd:TIGR02204 435 RYGrpDATDEEVEA-AARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQ 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 640 HVfEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHnlrgLQF 707
Cdd:TIGR02204 514 LV-QQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLAR----LQF 576
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1128-1331 |
1.81e-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: 126.59 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQdpvlf 1207
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 vgtvrynldpfeshtdemlwqvlertfmrdtimklpeklqaevtengenFSVGERQLLCVARALLRNSKIILLDEATASM 1287
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 89111135 1288 DSKTDTLVQNTIKDAF-KGCTVLTIAHRLNTVLN-CDHVLVMENGK 1331
Cdd:cd00267 112 DPASRERLLELLRELAeEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
493-699 |
2.22e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 139.09 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRE 559
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFG-EKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVG 638
Cdd:TIGR00958 574 NIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 639 KHVFEEcikKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 699
Cdd:TIGR00958 654 QLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
493-691 |
2.51e-33 |
|
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: 136.71 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIFHGNVRE 559
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGTVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NIL-FGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVG 638
Cdd:TIGR01842 411 NIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE-EG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 89111135 639 KHVFEECIKKT-LRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:TIGR01842 490 EQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
495-691 |
1.84e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICG-NvGSGKSSLLAALLGQMQLQKGVVAVNGT--------LAYVSQQA---WIFHGNVRENIL 562
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGpN-GAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FG-----------EKYDHQRYQHTVRVCGLQkDLSNLPygdlteIGErglnLSGGQRQRISLARAVYSDRQLYLLDDPLS 631
Cdd:COG1121 100 MGrygrrglfrrpSRADREAVDEALERVGLE-DLADRP------IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 632 AVDAHvGKHVFEECIKKtLR--GKTVVLVTHQLQFLES-CDEVILLEDGEICEkGTHKELMEE 691
Cdd:COG1121 169 GVDAA-TEEALYELLRE-LRreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTP 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1123-1355 |
2.62e-32 |
|
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: 133.10 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1123 RDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTKLTV 1199
Cdd:COG1123 268 KRYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPV--LF-VGTVRYNL-DPFESH-----------TDEMLWQV-LERTFMRdtimKLPeklqaevtenGEnFSVGERQ 1263
Cdd:COG1123 347 VFQDPYssLNpRMTVGDIIaEPLRLHgllsraerrerVAELLERVgLPPDLAD----RYP----------HE-LSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1264 LLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEV 1340
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEE 491
|
250
....*....|....*.
gi 89111135 1341 LAEKPDSAFA-MLLAA 1355
Cdd:COG1123 492 VFANPQHPYTrALLAA 507
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1137-1285 |
3.20e-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: 122.76 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVG-TVRYNL 1215
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1216 -------DPFESHTDEMLWQVLERtfmrdtiMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATA 1285
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
495-674 |
3.60e-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: 124.95 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------LAYVSQQA---WIFHGNVRENILF 563
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsidRDFPISVRDVVLM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 564 GekydhqRYQHtvrvCGLQKDLSN---------LPYGDLTEIGERGL-NLSGGQRQRISLARAVYSDRQLYLLDDPLSAV 633
Cdd:cd03235 94 G------LYGH----KGLFRRLSKadkakvdeaLERVGLSELADRQIgELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 89111135 634 DAHVGKHVFEecIKKTLR--GKTVVLVTHQL-QFLESCDEVILL 674
Cdd:cd03235 164 DPKTQEDIYE--LLRELRreGMTILVVTHDLgLVLEYFDRVLLL 205
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
494-702 |
5.73e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 133.03 E-value: 5.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 494 SVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVREN 560
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFG--EKYDHQRYQHTVRVcGLQKDLSNLPYGDLTeIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVG 638
Cdd:PRK11160 434 LLLAapNASDEALIEVLQQV-GLEKLLEDDKGLNAW-LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 639 KHVFEeCIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNL 702
Cdd:PRK11160 512 RQILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
496-707 |
1.88e-31 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 131.68 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLlAALLGQM-QLQKGVVAVNG------TL-------AYVSQQAWIFHGNVRENI 561
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTI-ANLLTRFyDIDEGEILLDGhdlrdyTLaslrnqvALVSQNVHLFNDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LF--GEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVgk 639
Cdd:PRK11176 438 AYarTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES-- 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 640 hvfEECIKKTL----RGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLiHNlrgLQF 707
Cdd:PRK11176 516 ---ERAIQAALdelqKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL-HK---MQF 580
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1128-1331 |
2.42e-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: 122.58 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP--V 1205
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 LFVGTVR---------YNLDPFEShtDEMLWQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNSK 1276
Cdd:cd03225 88 FFGPTVEeevafglenLGLPEEEI--EERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1277 IILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGK 1331
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1120-1358 |
6.24e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.56 E-value: 6.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDP-VLFVG-TVR---------YNLDPFEshtdemlwqvlertfMRDTIMKLPEKLQAE--VTENGENFSVGERQLLC 1266
Cdd:PRK13632 88 IFQNPdNQFIGaTVEddiafglenKKVPPKK---------------MKDIIDDLAKKVGMEdyLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1267 VARALLRNSKIILLDEATASMDSKTDTLVQNTI----KDAFKgcTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKP-EVL 1341
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMvdlrKTRKK--TLISITHDMDEAILADKVIVFSEGKLIAQGKPkEIL 230
|
250 260
....*....|....*....|....
gi 89111135 1342 AEKP-------DSAFAMLLAAEVR 1358
Cdd:PRK13632 231 NNKEilekakiDSPFIYKLSKKLK 254
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
493-679 |
7.86e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.08 E-value: 7.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRE 559
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVPQEPALWGGTVRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKYDHQRYQHTvRVCGLQKDLsNLPYGDL-TEIGErglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHvG 638
Cdd:COG4619 93 NLPFPFQLRERKFDRE-RALELLERL-GLPPDILdKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPE-N 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 89111135 639 KHVFEECIKKTLR--GKTVVLVTH-QLQFLESCDEVILLEDGEI 679
Cdd:COG4619 166 TRRVEELLREYLAeeGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1125-1355 |
1.00e-30 |
|
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: 122.22 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1125 YQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP 1204
Cdd:COG1124 11 YGQGGRRVP--VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1205 VLFV---GTVRYNLD-PFESH----TDEMLWQVLERTFMRDTIM-KLPEKLqaevtengenfSVGERQLLCVARALLRNS 1275
Cdd:COG1124 89 YASLhprHTVDRILAePLRIHglpdREERIAELLEQVGLPPSFLdRYPHQL-----------SGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1276 KIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFA-M 1351
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDlrEERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGPKHPYTrE 237
|
....
gi 89111135 1352 LLAA 1355
Cdd:COG1124 238 LLAA 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
493-691 |
1.52e-30 |
|
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: 121.69 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWI-FHGNVR 558
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVPQEPPApFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGekydhqRYQHTVRVCGLQKD--------LSNLpygDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:COG1120 94 ELVALG------RYPHLGLFGRPSAEdreaveeaLERT---GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 630 LSAVDAHvgkHVFE--ECIKK--TLRGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:COG1120 165 TSHLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1120-1341 |
1.89e-30 |
|
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: 121.30 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVG-TV-------RYN-LDPFESHTDE---MLWQVLERTfmrdtimKLPEKLQAEVTEngenFSVGERQLLCV 1267
Cdd:COG1120 80 VPQEPPAPFGlTVrelvalgRYPhLGLFGRPSAEdreAVEEALERT-------GLEHLADRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1268 ARALLRNSKIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVL 1341
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPeEVL 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
495-679 |
2.80e-30 |
|
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: 127.94 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRENI 561
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 -LFGEKyDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVGKH 640
Cdd:COG4618 427 aRFGDA-DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEA 504
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 89111135 641 VFEECI---KKtlRGKTVVLVTHQLQFLESCDEVILLEDGEI 679
Cdd:COG4618 505 ALAAAIralKA--RGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1117-1345 |
2.81e-30 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 127.91 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1117 RGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTK 1196
Cdd:PRK10789 311 RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1197 LTVIPQDPVLFVGTVRYNL---DPfeSHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLR 1273
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 1274 NSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKP 1345
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
585-1329 |
1.20e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 128.61 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 585 LSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVgkhvfEECIKKT---LRG---KTVVLV 658
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-----EYLVQKTinnLKGnenRITIII 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 659 THQLQFLESCDEVILLEDGE-----------------------------------------------ICEKGTHKELMEE 691
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKN 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 692 R-GRYAKLIHN------------------LRGLQFKDPEHLYNAAmvEAFKESPAEREEdagiivlAPGNEKDEGKESET 752
Cdd:PTZ00265 717 KnGIYYTMINNqkvsskkssnndndkdsdMKSSAYKDSERGYDPD--EMNGNSKHENES-------ASNKKSCKMSDENA 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 753 GSEFVDTKVPEHQLI---QTESPQEGTVTWKTYHTYIKAsggyllslFTVFLFLLMIGSAAFSNWWLgLWLDKGSrmtcg 829
Cdd:PTZ00265 788 SENNAGGKLPFLRNLfkrKPKAPNNLRIVYREIFSYKKD--------VTIIALSILVAGGLYPVFAL-LYAKYVS----- 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 830 pqgnrTMCEVGAVLADIGQHVYQWVYTAsmVFMLVFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDT---TPtG 906
Cdd:PTZ00265 854 -----TLFDFANLEANSNKYSLYILVIA--IAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-G 925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 907 RLMNRFSKDMDELDVRLpfhAENFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIF-------------HRGV 973
Cdd:PTZ00265 926 LLSAHINRDVHLLKTGL---VNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFairarltankdveKKEI 1002
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 974 QELKKV------ENVSRSPWFThITSSMQGLGIIHAYGKK-------ESCITY------HLLYFNCALRWFALRMDVLMN 1034
Cdd:PTZ00265 1003 NQPGTVfaynsdDEIFKDPSFL-IQEAFYNMNTVIIYGLEdyfcnliEKAIDYsnkgqkRKTLVNSMLWGFSQSAQLFIN 1081
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1035 ILTFTV-ALLVTLSFSSISTSSKGLsLSYIIQLSGLLQVCVRTGTETQAKFTsvelLREYISTCVPECTHPLKVGTCPKD 1113
Cdd:PTZ00265 1082 SFAYWFgSFLIRRGTILVDDFMKSL-FTFLFTGSYAGKLMSLKGDSENAKLS----FEKYYPLIIRKSNIDVRDNGGIRI 1156
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1114 WPS---RGEITFRDYQMRY--RDNTPLVLDsLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL------------------ 1170
Cdd:PTZ00265 1157 KNKndiKGKIEIMDVNFRYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtnd 1235
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1171 ------------------------------------VEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVGTVRYN 1214
Cdd:PTZ00265 1236 mtneqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYEN 1315
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1215 LDpF--ESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 1292
Cdd:PTZ00265 1316 IK-FgkEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1394
|
890 900 910
....*....|....*....|....*....|....*....
gi 89111135 1293 TLVQNTIKDAFKGC--TVLTIAHRLNTVLNCDHVLVMEN 1329
Cdd:PTZ00265 1395 KLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
493-679 |
2.65e-29 |
|
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: 115.57 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGtlayvsQQAWIFHGNVRENI--LFGEKYdhq 570
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIgyLPEEPS--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 571 ryqhtvrvcglqkdlsnlPYGDLTeiGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVGKHVFEECIKK-T 649
Cdd:cd03230 84 ------------------LYENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRElK 142
|
170 180 190
....*....|....*....|....*....|.
gi 89111135 650 LRGKTVVLVTHQLQFLES-CDEVILLEDGEI 679
Cdd:cd03230 143 KEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
495-679 |
3.06e-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: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIFHGNVRENI 561
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFG-EKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHvGKH 640
Cdd:cd03248 109 AYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQ 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 89111135 641 VFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEI 679
Cdd:cd03248 188 QVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1133-1331 |
3.79e-29 |
|
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: 116.03 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1133 TPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIdevdicilsledlRTKLTVIPQDPVLFVGTVR 1212
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGSIAYVSQEPWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1213 YNL---DPFEShtdEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDS 1289
Cdd:cd03250 84 ENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 89111135 1290 KT-DTLVQNTIKDAFKGC-TVLTIAHRLNTVLNCDHVLVMENGK 1331
Cdd:cd03250 161 HVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
495-694 |
3.84e-29 |
|
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: 117.27 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT------------LAYVSQQAWIFHGN-VRENI 561
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvrkeprearrqIGVLPDERGLYDRLtVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 -LFGEKYDHQRYQHTVRVCGLQKDLsnlpygDLTEIGERGL-NLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhvgk 639
Cdd:COG4555 96 rYFAELYGLFDEELKKRIEELIELL------GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV---- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 640 hVFEECIKKTLR-----GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGR 694
Cdd:COG4555 166 -MARRLLREILRalkkeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
495-691 |
1.07e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.93 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT------------LAYVSQQAwIFHGN--VREN 560
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEP-ALYPDltVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILF-------GEKYDHQRYQHTVRVCGLQkDLSNLPYGdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAV 633
Cdd:COG1131 94 LRFfarlyglPRKEARERIDELLELFGLT-DAADRKVG----------TLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 634 DAhVGKHVFEECIKK-TLRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 691
Cdd:COG1131 163 DP-EARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
495-676 |
2.43e-28 |
|
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: 113.73 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT------LAYVSQQAWIFHGN-------VRENI 561
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdarEDYRRRLAYLGHADglkpeltVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LF-----GEKYDHQRYQHTVRVCGLQkDLSNLPYGdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAH 636
Cdd:COG4133 97 RFwaalyGLRADREAIDEALEAVGLA-GLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 89111135 637 vGKHVFEECIKKTL-RGKTVVLVTHQLQFLESCdEVILLED 676
Cdd:COG4133 166 -GVALLAELIAAHLaRGGAVLLTTHQPLELAAA-RVLDLGD 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1128-1333 |
2.90e-28 |
|
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: 112.53 E-value: 2.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQdpvlf 1207
Cdd:cd03214 8 GYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 vgtvrynldpfeshtdemlwqVLERTfmrdtimKLPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLDEATASM 1287
Cdd:cd03214 81 ---------------------ALELL-------GLAHLADRPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 89111135 1288 DSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 1333
Cdd:cd03214 129 DIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1120-1358 |
3.16e-28 |
|
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: 120.78 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIFIDEVDICILSLEDLRTK 1196
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1197 LTVIPQDPvlfvgtvRYNLDPF--ESHTDEMLW-QVLERTFMRDTIMKLPEK--LQAEVTENGENFSVGERQLLCVARAL 1271
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVtvGDQIAEALEnLGLSRAEARARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1272 LRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE-------FDKPEVL 1341
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEdgppeeiLAAPQAL 237
|
250
....*....|....*..
gi 89111135 1342 AEKPDSAFAMLLAAEVR 1358
Cdd:COG1123 238 AAVPRLGAARGRAAPAA 254
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
495-700 |
5.20e-28 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 121.99 E-value: 5.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVV-------------AVNGTLAYVSQQAWIFHGNVRENI 561
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqdlagldvqAVRRQLGVVLQNGRLMSGSIFENI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHV 641
Cdd:TIGR03797 548 AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIV 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 642 FEECikKTLRGkTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 700
Cdd:TIGR03797 628 SESL--ERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
493-679 |
5.76e-28 |
|
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: 111.76 E-value: 5.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQawifhgnvre 559
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQA---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 nilfgekydhqryqhtvrvcglqkdLSNLpygDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVG 638
Cdd:cd03214 82 -------------------------LELL---GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 89111135 639 KHVFEECIK-KTLRGKTVVLVTHQL-QFLESCDEVILLEDGEI 679
Cdd:cd03214 134 IELLELLRRlARERGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
132-411 |
7.16e-28 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 114.96 E-value: 7.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 132 LCIIMAAIGPVILIHQILQQTERTSGKVWVGIGLCIALFATEFTKVFFWA-LAWAINyRTAIRLKVALSTLVFENLVSFK 210
Cdd:cd18598 7 LLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSShYNFQMN-KVSLKVRAALVTAVYRKALRVR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 211 T--LTHISVGEVLNILSSDS-------YSLFEAALfcpLPATIPI---LMVFCAAYAFfilgptaLIGISVYVIFIPVQM 278
Cdd:cd18598 86 SssLSKFSTGEIVNLMSTDAdrivnfcPSFHDLWS---LPLQIIValyLLYQQVGVAF-------LAGLVFALVLIPINK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 279 FMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRE------RKLLEkAGFVQSgnSALAPI 352
Cdd:cd18598 156 WIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKElkalkgRKYLD-ALCVYF--WATTPV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 353 VSTIaivLTLSCHILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRM 411
Cdd:cd18598 233 LISI---LTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1120-1346 |
8.84e-28 |
|
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: 112.98 E-value: 8.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTK 1196
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1197 LTVIPQDPVLFVG-TVRYNLD-PFESHTDEMLWQVLERTFM-------RDTIMKLPEKLqaevtengenfSVGERQLLCV 1267
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTRLSEEEIREIVLEkleavglRGAEDLYPAEL-----------SGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1268 ARALLRNSKIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEK 1344
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
..
gi 89111135 1345 PD 1346
Cdd:cd03261 228 DD 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
493-688 |
1.26e-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: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT----------------LAYVSQQAWIFHG- 555
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENILFGEKYDHQRYQHTVRVCGLQKdlsnlpygdLTEIGERGL------NLSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:cd03261 93 TVFENVAFPLREHTRLSEEEIREIVLEK---------LEAVGLRGAedlypaELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 630 LSAVDAhVGKHVFEECI---KKTLrGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 688
Cdd:cd03261 164 TAGLDP-IASGVIDDLIrslKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1120-1331 |
1.35e-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: 110.74 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS--LEDLRTKL 1197
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDPVLFVG-TVRYNLdpfeshtdemlwqvlertfmrdtimklpeklqaevtenGENFSVGERQLLCVARALLRNSK 1276
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI--------------------------------------ALGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1277 IILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGK 1331
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
495-679 |
1.37e-27 |
|
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: 110.38 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRENI 561
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LfgekydhqryqhtvrvcglqkdlsnlpygdlteigerglnlSGGQRQRISLARAVYSDRQLYLLDDPLSAVDaHVGKHV 641
Cdd:cd03246 97 L-----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERA 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 89111135 642 FEECIKKT-LRGKTVVLVTHQLQFLESCDEVILLEDGEI 679
Cdd:cd03246 135 LNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
495-662 |
2.74e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 118.23 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIFHGNVRENI 561
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFG--EKYDHQRYQHTVRVcGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGK 639
Cdd:TIGR02868 430 RLArpDATDEELWAALERV-GLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
170 180
....*....|....*....|...
gi 89111135 640 HVFEEcIKKTLRGKTVVLVTHQL 662
Cdd:TIGR02868 509 ELLED-LLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
500-700 |
5.09e-27 |
|
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: 118.89 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 500 SFVVRKGKILGICGNVGSGKSS---LLAALL----GQM--------QLQKGVVAvnGTLAYVSQQAWIFHGNVRENILFg 564
Cdd:TIGR03796 499 SLTLQPGQRVALVGGSGSGKSTiakLVAGLYqpwsGEIlfdgipreEIPREVLA--NSVAMVDQDIFLFEGTVRDNLTL- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 ekydhqrYQHT------VRVC---GLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:TIGR03796 576 -------WDPTipdadlVRACkdaAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDP 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 636 HVGKHVFEEcIKKtlRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 700
Cdd:TIGR03796 649 ETEKIIDDN-LRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
493-678 |
5.58e-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: 108.10 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTlayvsQQAWIFHGNVRENILfgekYDHQry 572
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIG----YVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 573 qhtvrvcglqkdlsnlpygdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRG 652
Cdd:cd00267 81 ------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEG 130
|
170 180
....*....|....*....|....*..
gi 89111135 653 KTVVLVTHQLQFLE-SCDEVILLEDGE 678
Cdd:cd00267 131 RTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
490-683 |
2.14e-26 |
|
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: 107.40 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 490 DSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT------------LAYVSQQAWIFHGNV 557
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENIlfgekydhqryqhtvrvcglqkdlsnlpygdlteigerGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHV 637
Cdd:cd03247 92 RNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 89111135 638 GKHVFeECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKG 683
Cdd:cd03247 134 ERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
490-678 |
3.21e-26 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 107.94 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 490 DSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL-------------AYVSQ----QawI 552
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrkvGLVFQnpddQ--F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 553 FHGNVRENILFG-------EKYDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYL 625
Cdd:cd03225 89 FGPTVEEEVAFGlenlglpEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 626 LDDPLSAVDAHVGKHVFEecIKKTLR--GKTVVLVTHQLQFL-ESCDEVILLEDGE 678
Cdd:cd03225 158 LDEPTAGLDPAGRRELLE--LLKKLKaeGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1120-1341 |
6.82e-26 |
|
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: 107.27 E-value: 6.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIFIDEVDICILS--LED 1192
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTKLTVIPQDPVLFVGTVRYNLD-PFESHtdemlwQVLERTFMRDTIMKLPEK--LQAEVTE--NGENFSVGERQLLCV 1267
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyGLRLH------GIKLKEELDERVEEALRKaaLWDEVKDrlHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1268 ARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVL 1341
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
495-676 |
7.67e-26 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 107.17 E-value: 7.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------LAYVSQQAWIF-HGNVRENILFGE 565
Cdd:cd03293 19 ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDALLpWLTVLDNVALGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 566 KYDH-------QRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVG 638
Cdd:cd03293 99 ELQGvpkaearERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 89111135 639 KHVFEEcIKKTLR--GKTVVLVTHQLqflescDEVILLED 676
Cdd:cd03293 168 EQLQEE-LLDIWRetGKTVLLVTHDI------DEAVFLAD 200
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
495-698 |
1.08e-25 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 114.15 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-LAYVSQQ---AWI---------FHGNVRENI 561
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdIRDVTQAslrAAIgivpqdtvlFNDTIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFG-EKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVgkh 640
Cdd:COG5265 453 AYGrPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT--- 529
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 641 vfEECIKKTL----RGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 698
Cdd:COG5265 530 --ERAIQAALrevaRGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
495-679 |
1.33e-25 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 106.42 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------------LAYVSQQ-AWIFHGN 556
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSfNLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFGEKY-------DHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:cd03255 99 ALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 89111135 630 LSAVDAHVGKHVFEEcIKKT--LRGKTVVLVTHQLQFLESCDEVILLEDGEI 679
Cdd:cd03255 168 TGNLDSETGKEVMEL-LRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
499-679 |
1.97e-25 |
|
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: 105.84 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVrKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL-----------------AYVSQQAWIF-HGNVREN 560
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrkiGLVFQQYALFpHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGEKYdHQRYQHTVRVCGLqkdlsnLPYGDLTEIGERG-LNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGK 639
Cdd:cd03297 96 LAFGLKR-KRNREDRISVDEL------LDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 89111135 640 HVFEEC--IKKTLRGkTVVLVTHQLQFLES-CDEVILLEDGEI 679
Cdd:cd03297 169 QLLPELkqIKKNLNI-PVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
496-631 |
3.34e-25 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 102.73 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIF-HGNVRENI 561
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 562 LFGEkyDHQRYQHTVRVCGLQKDLSNLPYGDL--TEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLS 631
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
495-690 |
4.11e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.31 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLA------------YVSQQAWIF-HGNVRENI 561
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlpprerrvgFVFQHYALFpHMTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFGekydhqryqhtvrvcglqkdLSNLPYGDlTEIGER-----------GL------NLSGGQRQRISLARAVYSDRQLY 624
Cdd:COG1118 97 AFG--------------------LRVRPPSK-AEIRARveellelvqleGLadrypsQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 625 LLDDPLSAVDAHVgkhvfeeciKKTLR----------GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELME 690
Cdd:COG1118 156 LLDEPFGALDAKV---------RKELRrwlrrlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1112-1345 |
8.68e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 112.82 E-value: 8.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1112 KDWPSRGEITFRDYQMRY--RDNTPLVLDsLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI-DEVDICIL 1188
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYdtRKDVEIYKD-LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1189 SLEDLRTKLTVIPQDPVLFVGTVR-------------------YNLDPFESH-------------------------TDE 1224
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLFSNSIKnnikyslyslkdlealsnyYNEDGNDSQenknkrnscrakcagdlndmsnttdSNE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1225 ML-----WQVLE---------RTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSK 1290
Cdd:PTZ00265 534 LIemrknYQTIKdsevvdvskKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1291 TDTLVQNTIKDaFKGC---TVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKP 1345
Cdd:PTZ00265 614 SEYLVQKTINN-LKGNenrITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
495-690 |
8.80e-25 |
|
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: 104.89 E-value: 8.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWiFHGNVRenILFGEKYD--HQRy 572
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA-FRRRVQ--MVFQDPYAslHPR- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 573 qHTV--------RVCGLqkdlsnlpygdlTEIGER--------GLN----------LSGGQRQRISLARAVYSDRQLYLL 626
Cdd:COG1124 96 -HTVdrilaeplRIHGL------------PDREERiaelleqvGLPpsfldryphqLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 627 DDPLSAVDAHVGKHV---FEEcIKKTlRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 690
Cdd:COG1124 163 DEPTSALDVSVQAEIlnlLKD-LREE-RGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1120-1346 |
9.21e-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: 104.68 E-value: 9.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTK 1196
Cdd:COG1127 6 IEVRNLTKSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1197 LTVIPQDPVLFVG-TVRYNLD-PFESHTD-------EMLWQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCV 1267
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAfPLREHTDlseaeirELVLEKLELVGLPGAADKMPSEL-----------SGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1268 ARALLRNSKIILLDEATASMD----SKTDTLVQnTIKDAFkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLA 1342
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDpitsAVIDELIR-ELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230
|
....
gi 89111135 1343 EKPD 1346
Cdd:COG1127 231 ASDD 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1120-1333 |
1.37e-24 |
|
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: 103.35 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICiLSLEDLRTKLTV 1199
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVG-TVRYNLD---PFESHTDEMLWQVLERTFmrdTIMKLPEKLQAEVTengeNFSVGERQLLCVARALLRNS 1275
Cdd:cd03263 80 CPQFDALFDElTVREHLRfyaRLKGLPKSEIKEEVELLL---RVLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1276 KIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 1333
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
496-700 |
1.79e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.05 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRENIL 562
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrnIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FG--EKYDHQRYQHTVRVCGLQKDLSNlPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhvgkh 640
Cdd:PRK13657 431 VGrpDATDEEMRAAAERAQAHDFIERK-PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV----- 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 641 VFEECIKKTL----RGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIH 700
Cdd:PRK13657 505 ETEAKVKAALdelmKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
492-684 |
1.84e-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: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 492 LKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIFHGNVR 558
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENI-LFGEKYDHQRYqhtvrvcglqkdlsnlpyGDLtEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHV 637
Cdd:cd03369 100 SNLdPFDEYSDEEIY------------------GAL-RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 89111135 638 gKHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGT 684
Cdd:cd03369 161 -DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
495-692 |
2.54e-24 |
|
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: 102.80 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG------TLAYVSQ-----------QawIFHGNV 557
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRkvglvfqnpddQ--LFAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENILFG-------EKYDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:COG1122 94 EEDVAFGpenlglpREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 631 SAVDAHvGKHVFEECIKK-TLRGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELMEER 692
Cdd:COG1122 163 AGLDPR-GRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1120-1347 |
2.97e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.06 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPV-LFVG-TVRYN----LDPFESHTDEM---LWQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARA 1270
Cdd:PRK13648 88 VFQNPDnQFVGsIVKYDvafgLENHAVPYDEMhrrVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1271 LLRNSKIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKPDS 1347
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
495-679 |
3.29e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.43 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------------LAYVSQqawiFHG-- 555
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserelarlrrrhIGFVFQ----FFNll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 ---NVRENILF-------GEKYDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYL 625
Cdd:COG1136 99 pelTALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 626 LDDPLSAVDAHVGKHVFE---ECIKKtlRGKTVVLVTHQLQFLESCDEVILLEDGEI 679
Cdd:COG1136 168 ADEPTGNLDSKTGEEVLEllrELNRE--LGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
495-677 |
5.69e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.86 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------LAYVSQQA----WIfhgNVRENIL 562
Cdd:COG1116 26 ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEPallpWL---TVLDNVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FG-------EKYDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:COG1116 103 LGlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 89111135 636 HVGKHVFEECIK-KTLRGKTVVLVTHQLQ---FLesCDEVILLEDG 677
Cdd:COG1116 172 LTRERLQDELLRlWQETGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
495-679 |
5.71e-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: 101.44 E-value: 5.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENIL 562
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQDYALFpHLTVAENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FG-------EKYDHQRYQHTVRVCGLQKDLSNLPYGdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:cd03259 95 FGlklrgvpKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 89111135 636 HVGKHVFEEcIKKTLR--GKTVVLVTH-QLQFLESCDEVILLEDGEI 679
Cdd:cd03259 164 KLREELREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1120-1334 |
6.04e-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: 101.89 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLV--LDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVE-PASGTIFIDEVDICILS---LEDL 1193
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLErPTSGSVLVDGTDLTLLSgkeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1194 RTKLTVIPQdpvlfvgtvRYNLdpFESHTdemlwqvlertfMRDTIMkLPEKL----QAEVTENGE-------------- 1255
Cdd:cd03258 81 RRRIGMIFQ---------HFNL--LSSRT------------VFENVA-LPLEIagvpKAEIEERVLellelvgledkada 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1256 ---NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMEN 1329
Cdd:cd03258 137 ypaQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEK 216
|
....*
gi 89111135 1330 GKVIE 1334
Cdd:cd03258 217 GEVVE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1120-1343 |
6.71e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 102.09 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIcilslEDLRTKLTV 1199
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQD-------PVL---FVGTVRY---NLDPFESHTD-EMLWQVLERT----FMRDTIMKLpeklqaevtengenfSVGE 1261
Cdd:COG1121 80 VPQRaevdwdfPITvrdVVLMGRYgrrGLFRRPSRADrEAVDEALERVgledLADRPIGEL---------------SGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1262 RQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVL-NCDHVLVMeNGKVIEFDKP- 1338
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPe 223
|
....*
gi 89111135 1339 EVLAE 1343
Cdd:COG1121 224 EVLTP 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1120-1338 |
7.50e-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: 101.88 E-value: 7.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT---- 1195
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 ------------KLTVIpqDPVL-----FVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLqaevtengenfS 1258
Cdd:cd03256 80 igmifqqfnlieRLSVL--ENVLsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQL-----------S 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1259 VGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAF--KGCTVLTIAHRLNTVL-NCDHVLVMENGKVIeF 1335
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVDLAReYADRIVGLKDGRIV-F 225
|
...
gi 89111135 1336 DKP 1338
Cdd:cd03256 226 DGP 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1136-1357 |
1.27e-23 |
|
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: 101.26 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEdlRTKLTVIPQDPVLFVgtvryNL 1215
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFP-----HM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1216 DPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAE--VTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDT 1293
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1294 LVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAF-AMLLAAEV 1357
Cdd:cd03299 167 KLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFvAEFLGFNN 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1120-1339 |
2.22e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 101.63 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDP-VLFVGT-----VRYNLDPFESHTDEMLWQV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARA 1270
Cdd:PRK13635 86 VFQNPdNQFVGAtvqddVAFGLENIGVPREEMVERVdqaLRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1271 LLRNSKIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPE 1339
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1136-1343 |
3.38e-23 |
|
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: 99.43 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQDPVLFVG-TVRY 1213
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1214 NLD-----PFESHTDEMLWQVLERtFMRdtimkLPEKLQAEvtenGENFSVGERQLLCVARALLRNSKIILLDEATASMD 1288
Cdd:cd03224 95 NLLlgayaRRRAKRKARLERVYEL-FPR-----LKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1289 SKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAE 1343
Cdd:cd03224 165 PKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
493-678 |
3.92e-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: 98.03 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT---------------LAYVSQQAWIF-HGN 556
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplrrrIGMVFQDFALFpHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFGekydhqryqhtvrvcglqkdlsnlpygdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAH 636
Cdd:cd03229 93 VLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 89111135 637 VGKHVFEECikKTLR---GKTVVLVTHQLQFLES-CDEVILLEDGE 678
Cdd:cd03229 135 TRREVRALL--KSLQaqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1136-1334 |
7.08e-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: 101.28 E-value: 7.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIFIDEVDICILSLEDLRT----KLTVIPQD----- 1203
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1204 -PVLfvgTVRYNL-DPFESHTD-------EMLWQVLERTFMRDtimklPEKL------QaevtengenFSVGERQLLCVA 1268
Cdd:COG0444 100 nPVM---TVGDQIaEPLRIHGGlskaearERAIELLERVGLPD-----PERRldryphE---------LSGGMRQRVMIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1269 RALLRNSKIILLDEATASMdsktDTLVQ----NTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:COG0444 163 RALALEPKLLIADEPTTAL----DVTIQaqilNLLKDlqRELGLAILFITHDLGVVAEiADRVAVMYAGRIVE 231
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
796-1070 |
8.20e-23 |
|
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: 100.02 E-value: 8.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 796 LFTVFLFLLMIGSAAFSNWWLGLWLDKGSrmtcgpqgnrtmceVGAVLADIGQHVYQWVYTASMVFMLVFGVTKGFVFTK 875
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLL--------------PDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 876 TTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLVV 955
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 956 ASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYGKKESCIT--------YHLLYF--NCALRWF 1025
Cdd:pfam00664 148 LAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEkydkaleeALKAGIkkAVANGLS 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 89111135 1026 ALRMDVLMNILTFTVALLVTLSFSSISTSSKGL--SLSYIIQLSGLL 1070
Cdd:pfam00664 228 FGITQFIGYLSYALALWFGAYLVISGELSVGDLvaFLSLFAQLFGPL 274
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1136-1333 |
9.44e-23 |
|
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: 96.34 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQdpvlfvgtvryn 1214
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1215 ldpfeshtdemlwqvlertfmrdtimklpeklqaevtengenFSVGERQLLCVARALLRNSKIILLDEATASMDSK-TDT 1293
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 89111135 1294 LVqNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 1333
Cdd:cd03216 121 LF-KVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
496-699 |
1.27e-22 |
|
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: 104.20 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRENIL 562
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIdintvtreslrksIATVFQDAGLFNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FGEK--YDHQRYQHTVRVCGLQKDLSNLPyGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKH 640
Cdd:TIGR01192 431 LGREgaTDEEVYEAAKAAAAHDFILKRSN-GYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEAR 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 641 VFE--ECIKKTlrgKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 699
Cdd:TIGR01192 510 VKNaiDALRKN---RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1120-1349 |
1.50e-22 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 98.14 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVlDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLF--------VGTV----RYNLDPFESHTDEMLWQV-LERTFMRDtimKLPEKLqaevtengenfSVGERQLLC 1266
Cdd:cd03295 80 VIQQIGLFphmtveenIALVpkllKWPKEKIRERADELLALVgLDPAEFAD---RYPHEL-----------SGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1267 VARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAE 1343
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
|
....*.
gi 89111135 1344 KPDSAF 1349
Cdd:cd03295 226 SPANDF 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1120-1336 |
1.56e-22 |
|
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: 97.20 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEdlRTKLTV 1199
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLF-----VGTVRYNLDPFESHTDEMLWQVLERTFMrdtiMKLPEKLQAEVTEngenFSVGERQLLCVARALLRN 1274
Cdd:cd03259 77 VFQDYALFphltvAENIAFGLKLRGVPKAEIRARVRELLEL----VGLEGLLNRYPHE----LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1275 SKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFD 1336
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1137-1339 |
1.64e-22 |
|
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: 103.23 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIFIDEVDICILS---LEDLRTKLTVIPQDP--------- 1204
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPfgslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1205 ----------VLFVGtvrynLDPFEshTDEMLWQVLERTFM-RDTIMKLP-EklqaevtengenFSVGERQLLCVARALL 1272
Cdd:COG4172 381 vgqiiaeglrVHGPG-----LSAAE--RRARVAEALEEVGLdPAARHRYPhE------------FSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1273 RNSKIILLDEATASMD-SktdtlVQNTIKDAFK------GCTVLTIAHRLNTV--LnCDHVLVMENGKVIE-------FD 1336
Cdd:COG4172 442 LEPKLLVLDEPTSALDvS-----VQAQILDLLRdlqrehGLAYLFISHDLAVVraL-AHRVMVMKDGKVVEqgpteqvFD 515
|
...
gi 89111135 1337 KPE 1339
Cdd:COG4172 516 APQ 518
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1120-1332 |
1.72e-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: 97.18 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYR--DNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVE-PASGTIFIDEVDICILSLEDL--- 1193
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1194 -RTKLTVIPQD----PVLfvgTVRYNLD-PFE------SHTDEMLWQVLERTFMRDTIMKLPEKLqaevtengenfSVGE 1261
Cdd:cd03255 80 rRRHIGFVFQSfnllPDL---TALENVElPLLlagvpkKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1262 RQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNCDHVLVMENGKV 1332
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
495-691 |
3.11e-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: 96.73 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQQAWIFHG-NVRE 559
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGE-KYDHQRYQHTV-RVCGLqkdlsnLPygDLTEI-GERGLNLSGGQRQRISLARAVYSDRQLYLLDDP---LSAV 633
Cdd:cd03224 95 NLLLGAyARRRAKRKARLeRVYEL------FP--RLKERrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 634 dahVGKHVFeECIKKtLR--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:cd03224 167 ---IVEEIF-EAIRE-LRdeGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1120-1332 |
4.02e-22 |
|
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: 96.32 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIL---SLEDLRTK 1196
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1197 LTVIPQDPVLFvgtvrYNLDPFESHTDEM--------LWQ-----VLERTFMRDTIMKLPEKLqaevtengenfSVGERQ 1263
Cdd:cd03292 80 IGVVFQDFRLL-----PDRNVYENVAFALevtgvpprEIRkrvpaALELVGLSHKHRALPAEL-----------SGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1264 LLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK-GCTVLTIAHRLNTVLNCDH-VLVMENGKV 1332
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1128-1333 |
5.43e-22 |
|
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: 95.68 E-value: 5.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdiciLSLEDLRTKLTVIPQD---- 1203
Cdd:cd03235 8 SYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQRrsid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1204 ---PVL---FVGTVRY---NLDPFESHTD-EMLWQVLERTFMRDtimklpeKLQAEVTEngenFSVGERQLLCVARALLR 1273
Cdd:cd03235 81 rdfPISvrdVVLMGLYghkGLFRRLSKADkAKVDEALERVGLSE-------LADRQIGE----LSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 1274 NSKIILLDEATASMDSKT-DTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMeNGKVI 1333
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTqEDIYELLRELRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVV 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
496-690 |
6.64e-22 |
|
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: 96.25 E-value: 6.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLA-----------YVSQQAWIF-HGNVRENILF 563
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHYALFrHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 564 GEKYDHQRYQH---TVRvcglQKDLSNLPYGDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGK 639
Cdd:cd03296 98 GLRVKPRSERPpeaEIR----AKVHELLKLVQLDWLADRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 640 HvfeecIKKTLR------GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELME 690
Cdd:cd03296 174 E-----LRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
123-387 |
7.51e-22 |
|
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: 96.94 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 123 VLMDIVANILCIIMAAIGPVILIHQI-----LQQTERTSGKVWVG--IGLCIALFATEFTKVFFWalawainYRTAIRLK 195
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILdvllpDGDPETQALNVYSLalLLLGLAQFILSFLQSYLL-------NHTGERLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 196 VALSTLVFENLV--SFKTLTHISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPT-ALIGISVYVI 272
Cdd:pfam00664 74 RRLRRKLFKKILrqPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 273 FIPVQMFMAKLNSAFRRSAILVTDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPI 352
Cdd:pfam00664 154 YILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQF 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 89111135 353 VSTIAIVLTL--SCHILLRRKLTAPVAFSVIAMFNVM 387
Cdd:pfam00664 234 IGYLSYALALwfGAYLVISGELSVGDLVAFLSLFAQL 270
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1118-1330 |
7.74e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.42 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1118 GEITFRDYQMRYRDNTPLVlDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIFIDEVDicilsledl 1193
Cdd:COG4178 361 GALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGKSTL----LRaiagLWPYGSGRIARPAGA--------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1194 rtKLTVIPQDPVLFVGTVR----YNLDPfESHTDEMLWQVLERTFMRDtimkLPEKLQAEvtENGEN-FSVGERQLLCVA 1268
Cdd:COG4178 427 --RVLFLPQRPYLPLGTLReallYPATA-EAFSDAELREALEAVGLGH----LAERLDEE--ADWDQvLSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 1269 RALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLNCDHVLVMENG 1330
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
493-688 |
9.06e-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: 95.33 E-value: 9.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKG--------------------VVAVNGTLAYVSQQAWI 552
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegevlldgkdiydldvdVLELRRRVGMVFQKPNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 553 FHGNVRENILFGEKydhqryqhtVRVCGLQKDLSNLPYGDLTEIG--------ERGLNLSGGQRQRISLARAVYSDRQLY 624
Cdd:cd03260 93 FPGSIYDNVAYGLR---------LHGIKLKEELDERVEEALRKAAlwdevkdrLHALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 625 LLDDPLSAVDAhVGKHVFEECIKKTLRGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKEL 688
Cdd:cd03260 164 LLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
493-690 |
1.01e-21 |
|
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: 95.82 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-LAYVSQQAWI---------FHG------- 555
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdITGLSEKELYelrrrigmlFQGgalfdsl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENILFGEKydhqryQHTvrvcglqkdlsNLPYGDLTEIGERGLN--------------LSGGQRQRISLARAVYSDR 621
Cdd:COG1127 98 TVFENVAFPLR------EHT-----------DLSEAEIRELVLEKLElvglpgaadkmpseLSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 622 QLYLLDDPLSAVDAhVGKHVFEECIKKtLR---GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 690
Cdd:COG1127 161 EILLYDEPTAGLDP-ITSAVIDELIRE-LRdelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
495-679 |
1.17e-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: 94.90 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT---------------LAYVSQQAWIF-HGNVR 558
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkkninelrqkVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGEkydhqryqhtVRVCGLQKDlsnlpygDLTEIGERGL--------------NLSGGQRQRISLARAVYSDRQLY 624
Cdd:cd03262 95 ENITLAP----------IKVKGMSKA-------EAEERALELLekvgladkadaypaQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 625 LLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQF-LESCDEVILLEDGEI 679
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
495-691 |
1.21e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 98.25 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENIL 562
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDYALFpHLTVAENVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FGEKYD-------HQRYQHTVRVCGLQKdlsnlpYGDlTEIGErglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:COG3842 100 FGLRMRgvpkaeiRARVAELLELVGLEG------LAD-RYPHQ----LSGGQQQRVALARALAPEPRVLLLDEPLSALDA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 636 HVGKHVFEEcIKKTLR--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:COG3842 169 KLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
493-695 |
1.96e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.56 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIFHGNVRE 559
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVgk 639
Cdd:PRK10790 434 NVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-- 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 640 hvfEECIKKTLRG----KTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRY 695
Cdd:PRK10790 512 ---EQAIQQALAAvrehTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
493-679 |
2.57e-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: 93.86 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-----------TLAYVSQQAWIF-HGNVREN 560
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNYALYpHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGEKYDH-------QRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAV 633
Cdd:cd03301 93 IAFGLKLRKvpkdeidERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 89111135 634 DAHVGKHVFEEcIKKTLR--GKTVVLVTH-QLQFLESCDEVILLEDGEI 679
Cdd:cd03301 162 DAKLRVQMRAE-LKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
795-1094 |
3.16e-21 |
|
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: 95.74 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 795 SLFTVFLFLLMIGSAAFSNWWLGLWLDKGSRmtcGPQGN----RTMCEVGAVLADIGQHVYqwvytasmvFMLVFgvtkg 870
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVN---GPQEHgqvyLSVLGALAILQGITVFQY---------SMAVS----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 871 fvftKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPA 950
Cdd:cd18559 64 ----IGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 951 VLLVVAsLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLGIIHAYG-------KKESCITYHLLYFN--CA 1021
Cdd:cd18559 140 AAVGIP-LGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEweeafirQVDAKRDNELAYLPsiVY 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1022 LRWFALRMDVLMNILTfTVALLVTLSFSSISTSSKGLSLSYIIQLSGLLQVCVRTGTETQAKFTSVELLREYI 1094
Cdd:cd18559 219 LRALAVRLWCVGPCIV-LFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
493-692 |
3.80e-21 |
|
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: 94.17 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL----------AYVSQQAWIFHG------- 555
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrQLRRQIGMIFQQfnlierl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENILFGekydhqR--YQHTVRVC-GL------QKDLSNLPYGDLTE-IGERGLNLSGGQRQRISLARAVYSDRQLYL 625
Cdd:cd03256 94 SVLENVLSG------RlgRRSTWRSLfGLfpkeekQRALAALERVGLLDkAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 626 LDDPLSAVD---AHVGKHVFEEcIKKTlRGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEER 692
Cdd:cd03256 168 ADEPVASLDpasSRQVMDLLKR-INRE-EGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1137-1330 |
8.58e-21 |
|
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: 92.39 E-value: 8.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTK----LTVIPQDPVLFVGTVR 1212
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1213 YNL---DPFESHTDEMlwqVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDS 1289
Cdd:cd03290 97 ENItfgSPFNKQRYKA---VTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 89111135 1290 K-TDTLVQNTIKDAFKG--CTVLTIAHRLNTVLNCDHVLVMENG 1330
Cdd:cd03290 174 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
461-679 |
1.33e-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: 91.83 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 461 RHLCKKQRSEAYSERSPPAKGATGPEEQSDSlKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVN 540
Cdd:cd03220 4 ENVSKSYPTYKGGSSSLKKLGILGRKGEVGE-FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 541 GTLAYVSQQAWIFHGN--VRENILFG-------EKYDHQRYQHTVRVCGLQKDLsNLPYGdlteigerglNLSGGQRQRI 611
Cdd:cd03220 83 GRVSSLLGLGGGFNPEltGRENIYLNgrllglsRKEIDEKIDEIIEFSELGDFI-DLPVK----------TYSSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 612 SLARAVYSDRQLYLLDDPLSAVDAHVGK---HVFEECIKKtlrGKTVVLVTHQLQFLES-CDEVILLEDGEI 679
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEkcqRRLRELLKQ---GKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
495-688 |
1.98e-20 |
|
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: 91.87 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT----------------LAYVSQQAWIFHG-NV 557
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrkarrrIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENILF-------GEKYDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:cd03258 100 FENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 631 SAVDAHVGKHVFeECIKKTLR--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 688
Cdd:cd03258 169 SALDPETTQSIL-ALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
495-683 |
2.24e-20 |
|
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: 91.41 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-LAYVSQQ---------AWIFHG--------- 555
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdLLKLSRRlrkirrkeiQMVFQDpmsslnprm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENIL--FGEKYDHQRYQHTVRVCGLQKDLSNLPygdlteigERGLN-----LSGGQRQRISLARAVYSDRQLYLLDD 628
Cdd:cd03257 100 TIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLP--------EEVLNrypheLSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 629 PLSAVDAHVGKHVFEEcIK--KTLRGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKG 683
Cdd:cd03257 172 PTSALDVSVQAQILDL-LKklQEELGLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
493-689 |
2.79e-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: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWIF-HGNVR 558
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENI-----LfgEKYDHQRYQHtvRVCGLQKdLSNLPYGdltEIGER-GLNLSGGQRQRISLARAVYSDRQLYLLDDPLSA 632
Cdd:cd03295 94 ENIalvpkL--LKWPKEKIRE--RADELLA-LVGLDPA---EFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 633 VDAHVGKHVFEECIK-KTLRGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 689
Cdd:cd03295 166 LDPITRDQLQEEFKRlQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
495-688 |
3.60e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.60 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENIL 562
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQSYALYpHMTVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FG---EKYD----HQRYQHTVRVCGLQKDLSNLPygdlteigergLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:COG3839 98 FPlklRKVPkaeiDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 636 HVgKHVFEECIKKTLR--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 688
Cdd:COG3839 167 KL-RVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1120-1334 |
3.80e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.50 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTK 1196
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1197 LTVIPQDP-----------VLFVGTVRYnLDPFESHTDEMlwQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLL 1265
Cdd:COG2884 81 IGVVFQDFrllpdrtvyenVALPLRVTG-KSRKEIRRRVR--EVLDLVGLSDKAKALPHEL-----------SGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1266 CVARALLRNSKIILLDEATASMDSKTdtlvQNTIKDAFK-----GCTVLtIA-HRLNTVLNCDH-VLVMENGKVIE 1334
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPET----SWEIMELLEeinrrGTTVL-IAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1136-1344 |
4.91e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.23 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFVG-TVR-- 1212
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1213 --YNLDPFESH------TDEMLWQVLertfMRDT-IMKLPEKLqaeVTEngenFSVGERQLLCVARALLRNSKIILLDEA 1283
Cdd:PRK11231 97 vaYGRSPWLSLwgrlsaEDNARVNQA----MEQTrINHLADRR---LTD----LSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1284 TASMD-SKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAEK 1344
Cdd:PRK11231 166 TTYLDiNHQVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPeEVMTPG 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
461-691 |
7.19e-20 |
|
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: 91.17 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 461 RHLCK---KQRSEAYSERsppAKGATGPE--EQSDSLKSVlHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKG 535
Cdd:cd03294 4 KGLYKifgKNPQKAFKLL---AKGKSKEEilKKTGQTVGV-NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 536 VVAVNGT-----------------LAYVSQQAWIF-HGNVRENILFG-------EKYDHQRYQHTVRVCGLQKDLSNLPy 590
Cdd:cd03294 80 KVLIDGQdiaamsrkelrelrrkkISMVFQSFALLpHRTVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 591 gdlteiGErglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIK-KTLRGKTVVLVTHQL-QFLESC 668
Cdd:cd03294 159 ------DE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlQAELQKTIVFITHDLdEALRLG 228
|
250 260
....*....|....*....|...
gi 89111135 669 DEVILLEDGEICEKGTHKELMEE 691
Cdd:cd03294 229 DRIAIMKDGRLVQVGTPEEILTN 251
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1129-1339 |
9.47e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1129 YRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS-LEDLRTKLTVIPQDP-VL 1206
Cdd:PRK13644 11 YPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1207 FVG-TVRYNLdpfeSHTDEMLwqVLERTFMRDTI-MKLPE-KLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEA 1283
Cdd:PRK13644 90 FVGrTVEEDL----AFGPENL--CLPPIEIRKRVdRALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1284 TASMDSKTDTLVQNTIKDAF-KGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPE 1339
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
485-679 |
9.66e-20 |
|
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: 88.76 E-value: 9.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 485 PEEQSDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQ--KGVVAVNGT----------LAYVSQQAwI 552
Cdd:cd03213 14 KSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRpldkrsfrkiIGYVPQDD-I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 553 FHGN--VRENILFGekydhqryqhtvrvcglqkdlSNLpygdlteigeRGLnlSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:cd03213 93 LHPTltVRETLMFA---------------------AKL----------RGL--SGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 631 SAVDAHVGKHVFeecikKTLR-----GKTVVLVTHQL--QFLESCDEVILLEDGEI 679
Cdd:cd03213 140 SGLDSSSALQVM-----SLLRrladtGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
495-721 |
1.19e-19 |
|
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: 94.20 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-LAYVSQQAW---------IF---------HG 555
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdLTKLSRRSLrelrrrvqmVFqdpysslnpRM 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENI-----LFGEKYDHQRYQHTVRV---CGLQKDLSN-LPYGdlteigerglnLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:COG1123 360 TVGDIIaeplrLHGLLSRAERRERVAELlerVGLPPDLADrYPHE-----------LSGGQRQRVAIARALALEPKLLIL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 627 DDPLSAVDAHVGKHV---FEEcIKKTLrGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELmeergryaklihnl 702
Cdd:COG1123 429 DEPTSALDVSVQAQIlnlLRD-LQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV-------------- 492
|
250
....*....|....*....
gi 89111135 703 rglqFKDPEHLYNAAMVEA 721
Cdd:COG1123 493 ----FANPQHPYTRALLAA 507
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
495-721 |
1.48e-19 |
|
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: 93.81 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLG---QMQLQKGVVAVNGT-------------LAYVSQQAW--IFHGN 556
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMtqLNPVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFG-EKYDHQRYQHTVRVcglqkdLSNLPYGDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVD 634
Cdd:COG1123 101 VGDQIAEAlENLGLSRAEARARV------LELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 635 AHVGKHVFEEcIKKTLR--GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNLRGLQFKDPE 711
Cdd:COG1123 175 VTTQAEILDL-LRELQRerGTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPA 253
|
250
....*....|
gi 89111135 712 HLYNAAMVEA 721
Cdd:COG1123 254 AAAAEPLLEV 263
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
499-679 |
1.75e-19 |
|
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: 91.70 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------------LAYVSQQAWIF-HGNVREN 560
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrrIGYVFQEARLFpHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGEKY-----DHQRYQHTVRVCGLQKDLSNLPygdlteigergLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:COG4148 98 LLYGRKRapraeRRISFDEVVELLGIGHLLDRRP-----------ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 89111135 636 HVgKHvfeECIK--KTLRGKT---VVLVTHQLQFLES-CDEVILLEDGEI 679
Cdd:COG4148 167 AR-KA---EILPylERLRDELdipILYVSHSLDEVARlADHVVLLEQGRV 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
495-700 |
1.97e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLayvsqqAWI------FHGN--VRENILFG-- 564
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SALlelgagFHPEltGRENIYLNgr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 ----------EKYDHqryqhtVRvcglqkdlsnlpygDLTEIGE------RglNLSGGQRQRISLARAVYSDRQLYLLDD 628
Cdd:COG1134 115 llglsrkeidEKFDE------IV--------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 629 PLSAVDAHvgkhvF-EECIKK----TLRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEergRYAKLIH 700
Cdd:COG1134 173 VLAVGDAA-----FqKKCLARirelRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA---AYEALLA 242
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1136-1333 |
2.01e-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: 89.03 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIFIDEVDICILSlEDLRTKLTVIP--QDPVLFVG 1209
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1210 -TVRYNLD----PFESHTDEMLWQVLERTFMRDTIMKLPE--KLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDE 1282
Cdd:cd03219 90 lTVLENVMvaaqARTGSGLLLARARREEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1283 ATASMDSK-TDTLVqNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 1333
Cdd:cd03219 170 PAAGLNPEeTEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
495-674 |
2.68e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.29 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG--TLAYVSQQ---AWIFHGNVRENILFG----- 564
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVAMGrwarr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 ------EKYDHQRYQHTVRVCGLQkDLSNLPYGDLteigerglnlSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVG 638
Cdd:NF040873 87 glwrrlTRDDRAAVDDALERVGLA-DLAGRQLGEL----------SGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 89111135 639 KHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILL 674
Cdd:NF040873 156 ERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
496-676 |
3.00e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.54 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQ---KGVVAVNGT-----------LAYVSQQAWIF-HGNVREN 560
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRrltalpaeqrrIGILFQDDLLFpHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFG--EKYDHQRYQHTVrvcglQKDLSNLpygDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAH- 636
Cdd:COG4136 97 LAFAlpPTIGRAQRRARV-----EQALEEA---GLAGFADRDPAtLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAl 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 89111135 637 ---VGKHVFEEcIKKtlRGKTVVLVTHQLQFLESCDEVILLED 676
Cdd:COG4136 169 raqFREFVFEQ-IRQ--RGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
493-679 |
3.90e-19 |
|
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: 87.34 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG---------TLAYVSQQAWIFHG-NVRENIL 562
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLYPKmKVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 -FGEKYDHQRYQHTVRVCGLQKDLsnlpygDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVGKH 640
Cdd:cd03269 93 yLAQLKGLKKEEARRRIDEWLERL------ELSEYANKRVEeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 89111135 641 VFEECIKKTLR-GKTVVLVTHQLQFLES-CDEVILLEDGEI 679
Cdd:cd03269 166 LLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
498-692 |
4.23e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.89 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 498 SISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENILFG- 564
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQENNLFpHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 ------EKYDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD---- 634
Cdd:COG3840 97 rpglklTAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 635 ---AHVGKHVFEEcikktlRGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELMEER 692
Cdd:COG3840 166 qemLDLVDELCRE------RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1131-1333 |
6.70e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.61 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1131 DNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS-LEDLRTKLTVIPQDP----- 1204
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1205 -------VLFvGTVRYNLDPFE--SHTDEmlwqVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNS 1275
Cdd:PRK13633 100 ativeedVAF-GPENLGIPPEEirERVDE----SLKKVGMYEYRRHAPHLL-----------SGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1276 KIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLNCDHVLVMENGKVI 1333
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1120-1341 |
7.36e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.25 E-value: 7.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDN-TPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLT 1198
Cdd:PRK13650 5 IEVKNLTFKYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1199 VIPQDP-VLFVGT-----VRYNLDPFESHTDEMLWQV---LERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVAR 1269
Cdd:PRK13650 85 MVFQNPdNQFVGAtveddVAFGLENKGIPHEEMKERVneaLELVGMQDFKEREPARL-----------SGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1270 ALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVL 1341
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
491-679 |
8.20e-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: 85.56 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 491 SLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVS---QQAWIF 553
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 554 HG-NVRENILfgekydhqryqhtvrvcglqkdLSNLpygdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLSA 632
Cdd:cd03215 91 LDlSVAENIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 89111135 633 VDahVG--KHVFEECIKKTLRGKTVVLVTHQLQ-FLESCDEVILLEDGEI 679
Cdd:cd03215 135 VD--VGakAEIYRLIRELADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1120-1333 |
9.02e-19 |
|
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: 86.65 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDN--TPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEdLRTKL 1197
Cdd:cd03266 2 ITADALTKRFRDVkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDPVLFVG-TVRYNLDPFES-HTdemlwqvLERTFMRDTIMKLPEKLQAEVTEN--GENFSVGERQLLCVARALLR 1273
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGlYG-------LKGDELTARLEELADRLGMEELLDrrVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1274 NSKIILLDEATASMdsktDTLVQNTIKDAFK-----GCTVLTIAHRLNTVLN-CDHVLVMENGKVI 1333
Cdd:cd03266 154 DPPVLLLDEPTTGL----DVMATRALREFIRqlralGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
493-689 |
1.06e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 87.48 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWI-FHGNVR 558
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHSSLaFPFTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFG-------EKYDHQRYQHTVRVCGLQkDLSNLPYgdlteigergLNLSGGQRQRISLARA-------VYSDRQLY 624
Cdd:COG4559 94 EVVALGraphgssAAQDRQIVREALALVGLA-HLAGRSY----------QTLSGGEQQRVQLARVlaqlwepVDGGPRWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 625 LLDDPLSAVD-AHVgKHVFEecIKKTL--RGKTVVLVTHQL----QFlesCDEVILLEDGEICEKGTHKELM 689
Cdd:COG4559 163 FLDEPTSALDlAHQ-HAVLR--LARQLarRGGGVVAVLHDLnlaaQY---ADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
495-690 |
1.07e-18 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 86.62 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENIL 562
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FG-------EKYDHQRYQHTVRVCGLQKDLSNLPygdlteigergLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:cd03299 94 YGlkkrkvdKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 636 HVGKHVFEEcIKKTLR--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 690
Cdd:cd03299 163 RTKEKLREE-LKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1120-1359 |
1.29e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.60 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID--EVDICILSLEDLRTKL 1197
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDP--VLFVGTVR-------YNLDPFESHTDEMLWQVLERTFMrdtimklpEKLQAEVTengENFSVGERQLLCVA 1268
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALKRTGI--------EHLKDKPT---HCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1269 RALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTV-LNCDHVLVMENGKVI-EFDKPEVLAEK 1344
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVIlQGNPKEVFAEK 233
|
250
....*....|....*
gi 89111135 1345 pdsafAMLLAAEVRL 1359
Cdd:PRK13636 234 -----EMLRKVNLRL 243
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
495-694 |
1.33e-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: 86.59 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT---------------LAYVSQQAWIF-HGNVR 558
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdltdskkdinklrrkVGMVFQQFNLFpHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGekydhqryqhTVRVCGLQKDlsnlpygDLTEIGER-----GL---------NLSGGQRQRISLARAVYSDRQLY 624
Cdd:COG1126 96 ENVTLA----------PIKVKKMSKA-------EAEERAMEllervGLadkadaypaQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 625 LLDDPLSAVDAhvgkhvfeECIK------KTL--RGKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELME----E 691
Cdd:COG1126 159 LFDEPTSALDP--------ELVGevldvmRDLakEGMTMVVVTHEMGFaREVADRVVFMDGGRIVEEGPPEEFFEnpqhE 230
|
...
gi 89111135 692 RGR 694
Cdd:COG1126 231 RTR 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1120-1345 |
1.72e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIFIDEVDICILSLEDLRTK 1196
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1197 LTVIPQDP-VLFVGT-----VRYNLDPFESHTDEML---WQVLERTFMRDTIMKLPeklqaevtengENFSVGERQLLCV 1267
Cdd:PRK13640 86 VGIVFQNPdNQFVGAtvgddVAFGLENRAVPRPEMIkivRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1268 ARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKPEVLAEKP 1345
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1136-1339 |
1.91e-18 |
|
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: 86.63 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIFIDEVDICILSLEDL------RTKltvipQDPV 1205
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDITGLPPHRIarlgiaRTF-----QNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 LFVG-TVRYNLD-PFESHTDEMLWQVLERTF--------MRDTIMKLPE--KLQAEVTENGENFSVGERQLLCVARALLR 1273
Cdd:COG0411 90 LFPElTVLENVLvAAHARLGRGLLAALLRLPrarreereARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1274 NSKIILLDEATASMDSK-TDTLVQ--NTIKDAFkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPE 1339
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEeTEELAEliRRLRDER-GITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1129-1343 |
2.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.03 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1129 YRDNTPL---VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIC--ILSLEDLRTKLTVIPQD 1203
Cdd:PRK13637 12 YMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1204 P--VLFVGTVR-------YNLDPFEshtDEMLWQVLERtfmrdtiMKLPeKLQAEVTENGENF--SVGERQLLCVARALL 1272
Cdd:PRK13637 92 PeyQLFEETIEkdiafgpINLGLSE---EEIENRVKRA-------MNIV-GLDYEDYKDKSPFelSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1273 RNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAE 1343
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPrEVFKE 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
459-688 |
2.40e-18 |
|
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: 85.25 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 459 QKRHLCKKqrseaYSERSPPAkgatgpeeqsdslksvLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVA 538
Cdd:cd03263 2 QIRNLTKT-----YKKGTKPA----------------VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 539 VNGTlaYVSQQAWIFHGNV----RENILFGE--KYDHQRYQHtvRVCGLqkdlSNLPYGDLTEIGERGLNL--------- 603
Cdd:cd03263 61 INGY--SIRTDRKAARQSLgycpQFDALFDEltVREHLRFYA--RLKGL----PKSEIKEEVELLLRVLGLtdkankrar 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 604 --SGGQRQRISLARAVYSDRQLYLLDDPLSAVDaHVGKHVFEECIKKTLRGKTVVLVTHQLQFLES-CDEVILLEDGEIC 680
Cdd:cd03263 133 tlSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
....*...
gi 89111135 681 EKGTHKEL 688
Cdd:cd03263 212 CIGSPQEL 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
495-691 |
2.47e-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: 85.75 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-----TLAY------VSQQAWIF-HGNVRENIL 562
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditnLPPHkrpvntVFQNYALFpHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FGekydhqryqhtVRVCGLQKDLSN------LPYGDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:cd03300 95 FG-----------LRLKKLPKAEIKervaeaLDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 636 HVGKHVFEEC--IKKTLrGKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:cd03300 164 KLRKDMQLELkrLQKEL-GITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
495-681 |
3.60e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.72 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT----------------LAYVSQQAW-IFHGNV 557
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrrIGVVFQDFRlLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENILFG---EKYDHQRYQHTVR-----VcGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:COG2884 97 YENVALPlrvTGKSRKEIRRRVRevldlV-GLSDKAKALPH-----------ELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 630 LSAVDAHVGK---HVFEEcIKKtlRGKTVVLVTHQLQFLESCDE-VILLEDGEICE 681
Cdd:COG2884 165 TGNLDPETSWeimELLEE-INR--RGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
499-689 |
4.00e-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: 87.86 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------------LAYVSQQAWIF-HGNVREN 560
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGEK-----YDHQRYQHTVRVCGLQKDLSNLPyGDLteigerglnlSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:TIGR02142 96 LRYGMKrarpsERRISFERVIELLGIGHLLGRLP-GRL----------SGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 636 HVGKHV--FEECIKKTLRgKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 689
Cdd:TIGR02142 165 PRKYEIlpYLERLHAEFG-IPILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1120-1334 |
4.16e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 87.44 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLV--LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT-- 1195
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 -KLTVIPQDpvlfvgtvrYNLdpFESHTdemlwqV-------LErtfmrdtIMKLP-EKLQAEVTE---------NGENF 1257
Cdd:COG1135 82 rKIGMIFQH---------FNL--LSSRT------VaenvalpLE-------IAGVPkAEIRKRVAEllelvglsdKADAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1258 ----SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENG 1330
Cdd:COG1135 138 psqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENG 217
|
....
gi 89111135 1331 KVIE 1334
Cdd:COG1135 218 RIVE 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
492-693 |
4.94e-18 |
|
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: 90.78 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 492 LKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVR 558
Cdd:TIGR00957 1298 LDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLniakiglhdlrfkITIIPQDPVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVg 638
Cdd:TIGR00957 1378 MNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET- 1456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 639 khvfEECIKKTLRGK----TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERG 693
Cdd:TIGR00957 1457 ----DNLIQSTIRTQfedcTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
511-691 |
5.79e-18 |
|
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: 86.78 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 511 ICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENILFGEKYDHQ-RYQHTVR 577
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdvtnvpphlrhINMVFQSYALFpHMTVEENVAFGLKMRKVpRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 578 VcglqkdLSNLPYGDLTEIGERG-LNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEEcIKKTLR--GKT 654
Cdd:TIGR01187 81 V------LEALRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE-LKTIQEqlGIT 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 89111135 655 VVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:TIGR01187 154 FVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1120-1332 |
5.94e-18 |
|
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: 84.12 E-value: 5.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS--LEDLRTKL 1197
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKknINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDpvlfvgtvrYNLDPfesHTDemlwqVLErtfmrdTIMKLPEKLQ----AEVTENGENF---------------- 1257
Cdd:cd03262 79 GMVFQQ---------FNLFP---HLT-----VLE------NITLAPIKVKgmskAEAEERALELlekvgladkadaypaq 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1258 -SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKV 1332
Cdd:cd03262 136 lSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1136-1334 |
6.07e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS-LEDLRTKLTVIPQDPVLFVG-TVRY 1213
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1214 NLdpF---ESHTDEML-W--------QVLERtfmrdtiMKLPEKLQAEVtengENFSVGERQLLCVARALLRNSKIILLD 1281
Cdd:COG1129 99 NI--FlgrEPRRGGLIdWramrrrarELLAR-------LGLDIDPDTPV----GDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1282 EATASMDSK-TDTL--VQNTIKDafKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:COG1129 166 EPTASLTEReVERLfrIIRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
490-699 |
6.70e-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: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 490 DSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGN 556
Cdd:cd03288 31 NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklplhtlrsrLSIILQDPILFSGS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAH 636
Cdd:cd03288 111 IRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 637 VgKHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM-EERGRYAKLI 699
Cdd:cd03288 191 T-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
495-683 |
7.50e-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: 83.96 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-----TLAYVSQQAWIFHGN--------VRENI 561
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEARRRLGFVSDStglydrltARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 L-FGEKYDHQRYQHTVRVCGLQKDLSNLPYGDlteigERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKH 640
Cdd:cd03266 100 EyFAGLYGLKGDELTARLEELADRLGMEELLD-----RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 89111135 641 VFEecIKKTLR--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 683
Cdd:cd03266 175 LRE--FIRQLRalGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1119-1346 |
7.94e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.46 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1119 EITFRDYQMRYRDNTP---LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdiCILS------ 1189
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGE---RVITagkknk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1190 -LEDLRTKLTVIPQDP--VLFVGTVRYNL-----------DPFESHTDEMLWQVlertfmrdtimKLPEKLqaeVTENGE 1255
Cdd:PRK13634 79 kLKPLRKKVGIVFQFPehQLFEETVEKDIcfgpmnfgvseEDAKQKAREMIELV-----------GLPEEL---LARSPF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1256 NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTdtlvQNTIKDAF------KGCTVLTIAHRLNTVLN-CDHVLVME 1328
Cdd:PRK13634 145 ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMH 220
|
250
....*....|....*...
gi 89111135 1329 NGKVIEFDKPEVLAEKPD 1346
Cdd:PRK13634 221 KGTVFLQGTPREIFADPD 238
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
493-691 |
8.06e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 84.75 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQawifhgN--- 556
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQE------Nhin 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 ----VRENILFGekydhqRYQHTvrvcglQKDLSN---------LPYGDLTEIGERGLN-LSGGQRQRISLARAVYSDRQ 622
Cdd:COG4604 88 srltVRELVAFG------RFPYS------KGRLTAedreiideaIAYLDLEDLADRYLDeLSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 623 LYLLDDPLSAVDAhvgKHVFEecIKKTLR------GKTVVLVTHQLQFlESC--DEVILLEDGEICEKGTHKELMEE 691
Cdd:COG4604 156 YVLLDEPLNNLDM---KHSVQ--MMKLLRrladelGKTVVIVLHDINF-ASCyaDHIVAMKDGRVVAQGTPEEIITP 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
493-692 |
9.37e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 9.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHG-NVR 558
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGE-----------KYDHQRYQHTVRVCGLqkdlsnlpygdlTEIGERGL-NLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:PRK11231 95 ELVAYGRspwlslwgrlsAEDNARVNQAMEQTRI------------NHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 627 DDPLSAVDAHvgkHVFEecIKKTLR-----GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 692
Cdd:PRK11231 163 DEPTTYLDIN---HQVE--LMRLMRelntqGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
217-411 |
1.20e-17 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 84.96 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 217 VGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPTALIGISVYVIFIPVQMFMAKLNSAFRRSAILVTD 296
Cdd:cd18559 94 SGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 297 KRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVSTIAIVLTLSCHILL--RRKLTA 374
Cdd:cd18559 174 PRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRhsLAGLVA 253
|
170 180 190
....*....|....*....|....*....|....*..
gi 89111135 375 PVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRRM 411
Cdd:cd18559 254 LKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1136-1334 |
1.20e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT---KLTVIPQDPVLFVG--- 1209
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQDSISAVNprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1210 TVRY----------NLDPFE--SHTDEMLWQVlertFMRDTIM-KLPEKLqaevtengenfSVGERQLLCVARALLRNSK 1276
Cdd:PRK10419 107 TVREiireplrhllSLDKAErlARASEMLRAV----DLDDSVLdKRPPQL-----------SGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1277 IILLDEATasmdSKTDTLVQNTIKDAFK------GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:PRK10419 172 LLILDEAV----SNLDLVLQAGVIRLLKklqqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1129-1327 |
1.33e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1129 YRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFV 1208
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1209 GTVRYNLdpfeshtdEMLWQV----LERTFMRDTIMK--LPEKLqaeVTENGENFSVGERQLLcvarALLRN----SKII 1278
Cdd:PRK10247 95 DTVYDNL--------IFPWQIrnqqPDPAIFLDDLERfaLPDTI---LTKNIAELSGGEKQRI----SLIRNlqfmPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1279 LLDEATASMDSKTDTLVQNTI----KDafKGCTVLTIAHRLNTVLNCDHVLVM 1327
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIhryvRE--QNIAVLWVTHDKDEINHADKVITL 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
494-679 |
1.71e-17 |
|
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: 83.25 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 494 SVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT---------LAYVSQQA--WIF-------HG 555
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlfaldedaRARLRARHvgFVFqsfqllpTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENI-----LFGEKYDHQRYQHTVRVCGLQKDLSNLPYGdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:COG4181 106 TALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 631 SAVDAHVGKHV----FEecIKKTlRGKTVVLVTHQLQFLESCDEVILLEDGEI 679
Cdd:COG4181 175 GNLDAATGEQIidllFE--LNRE-RGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
493-684 |
2.38e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------TLAYVSQQAWI-FHGNVR 558
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHSSLsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGeKYDHQRYQHTVR--------VCGLQkDLSNLPYgdlteigergLNLSGGQRQRISLARA------VYSDRQLY 624
Cdd:PRK13548 95 EVVAMG-RAPHGLSRAEDDalvaaalaQVDLA-HLAGRDY----------PQLSGGEQQRVQLARVlaqlwePDGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 625 LLDDPLSAVD-AHvGKHVFEecIKKTL---RGKTVVLVTHQL----QFlesCDEVILLEDGEICEKGT 684
Cdd:PRK13548 163 LLDEPTSALDlAH-QHHVLR--LARQLaheRGLAVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGT 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1136-1339 |
2.47e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL-FVGTVRY- 1213
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1214 -------NLDPFESHTDEMLwQVLERTFMRDTIMKLPEKlqaEVTEngenFSVGERQLLCVARALLRNSKIILLDEATAS 1286
Cdd:PRK09536 98 vemgrtpHRSRFDTWTETDR-AAVERAMERTGVAQFADR---PVTS----LSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1287 MD----SKTDTLVQNTIKDafkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPE 1339
Cdd:PRK09536 170 LDinhqVRTLELVRRLVDD---GKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPA 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
494-699 |
2.52e-17 |
|
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: 83.75 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 494 SVLHSISFVVRKGKILGICGNVGSGKSSLLAALLgQMQLQKGVVAVNG-------------TLAYVSQQAWIFHGNVREN 560
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGEKYDHQRYQHTVRVCGLQKDLSNLPyGDLT-EIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVGK 639
Cdd:cd03289 97 LDPYGKWSDEEIWKVAEEVGLKSVIEQFP-GQLDfVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-ITY 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 640 HVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLI 699
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
495-690 |
3.15e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.83 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLA---------------YVSQQAWIF-HGNVR 558
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkvderlirqeagMVFQQFYLFpHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGekydhqryqhTVRVCGLQK-DLSNLPYGDLTEIG--ERGLN----LSGGQRQRISLARAVYSDRQLYLLDDPLS 631
Cdd:PRK09493 96 ENVMFG----------PLRVRGASKeEAEKQARELLAKVGlaERAHHypseLSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 632 AVDAHVGKHVFEecIKKTL--RGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELME 690
Cdd:PRK09493 166 ALDPELRHEVLK--VMQDLaeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1120-1334 |
3.54e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.47 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLV--LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRT-- 1195
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 -KLTVIPQdpvlfvgtvRYNLdpFESHTdemlwqVLERTFMRDTIMKLP-EKLQAEVTENGE-------------NFSVG 1260
Cdd:PRK11153 82 rQIGMIFQ---------HFNL--LSSRT------VFDNVALPLELAGTPkAEIKARVTELLElvglsdkadrypaQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1261 ERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
493-691 |
3.64e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.00 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVREN 560
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrhVNTVFQSYALFpHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFG---EKYDHQryQHTVRVcglqkdLSNLPYGDLTEIGERG-LNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAH 636
Cdd:PRK09452 107 VAFGlrmQKTPAA--EITPRV------MEALRMVQLEEFAQRKpHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 637 VGKHVFEEcIKKTLR--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:PRK09452 179 LRKQMQNE-LKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1137-1357 |
5.57e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.45 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS---LEDLRTKLTVIPQDPVLFVG---T 1210
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1211 VRYN-LDPFESH--------TDEMLWqVLERTFMRdtimklPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLD 1281
Cdd:PRK10261 420 VGDSiMEPLRVHgllpgkaaAARVAW-LLERVGLL------PEHAWRYPHE----FSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1282 EATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLNCDH-VLVMENGKVIEFDKPEVLAEKPDSAFAMLLAAEV 1357
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHrVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
495-707 |
5.98e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.98 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENIL 562
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHYALFrHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FGEKY--DHQR-YQHTVRvcglQKDLSNLPYGDLTEIGER-GLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVG 638
Cdd:PRK10851 97 FGLTVlpRRERpNAAAIK----AKVTQLLEMVQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 639 KHvfeecIKKTLRGK------TVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL---------MEERGRYAKLIHNL 702
Cdd:PRK10851 173 KE-----LRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVwrepatrfvLEFMGEVNRLQGTI 247
|
....*
gi 89111135 703 RGLQF 707
Cdd:PRK10851 248 RGGQF 252
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1120-1314 |
6.39e-17 |
|
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: 79.51 E-value: 6.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVlDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdicilsledlRTKLTV 1199
Cdd:cd03223 1 IELENLSLATPDGRVLL-KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVGTVRynldpfeshtdEML---WQvlertfmrdtimklpeklqaevtengENFSVGERQLLCVARALLRNSK 1276
Cdd:cd03223 69 LPQRPYLPLGTLR-----------EQLiypWD--------------------------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 89111135 1277 IILLDEATASMDSKTDTLVQNTIKDAfkGCTVLTIAHR 1314
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHR 147
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
495-690 |
6.41e-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: 81.57 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQQAWIFHG-NVRE 559
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGE--KYDHQRYQHTV-RVCGLqkdlsnLPygDLTE-IGERGLNLSGGQRQRISLARAVYSDRQLYLLDDP---LSA 632
Cdd:COG0410 98 NLLLGAyaRRDRAEVRADLeRVYEL------FP--RLKErRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPslgLAP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 633 VdahVGKHVFeECIKKtLR--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELME 690
Cdd:COG0410 170 L---IVEEIF-EIIRR-LNreGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1136-1346 |
6.91e-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: 81.57 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL-RTKLTVIPQDPVLFVG-TVRY 1213
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1214 NLD------PFESHTDEMLWQVLERtFMRdtimkLPEKLQAEvtenGENFSVGERQLLCVARALLRNSKIILLDEATA-- 1285
Cdd:COG0410 98 NLLlgayarRDRAEVRADLERVYEL-FPR-----LKERRRQR----AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLgl 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1286 --SMdsktdtlVQN------TIKDAfkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 1346
Cdd:COG0410 168 apLI-------VEEifeiirRLNRE--GVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
493-731 |
1.78e-16 |
|
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: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALL------GQMQLQkGVVAVNGTL-------AYVSQQAWIFHGNVRE 559
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLrllsteGEIQID-GVSWNSVTLqtwrkafGVIPQKVFIFSGTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVGK 639
Cdd:TIGR01271 1311 NLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTL 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 640 HVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEERGRYAKLIHNLRGLQFKdPEHLYNAAMV 719
Cdd:TIGR01271 1390 QIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRLKLF-PLHRRNSSKR 1468
|
250
....*....|..
gi 89111135 720 EAFKESPAEREE 731
Cdd:TIGR01271 1469 KPQPKITALREE 1480
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
495-661 |
1.96e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG----TLAYVSQQAWIFHGN-------VRENILF 563
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdidDPDVAEACHYLGHRNamkpaltVAENLEF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 564 GEKYdhqRYQHTVRV------CGLQkDLSNLPYGdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHv 637
Cdd:PRK13539 97 WAAF---LGGEELDIaaaleaVGLA-PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA- 161
|
170 180
....*....|....*....|....*
gi 89111135 638 GKHVFEECIKKTL-RGKTVVLVTHQ 661
Cdd:PRK13539 162 AVALFAELIRAHLaQGGIVIAATHI 186
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
495-679 |
2.09e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.85 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGtlayvsqqawifhgnvrENILFGEKYDHQR--- 571
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------KEVSFASPRDARRagi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 572 ---YQhtvrvcglqkdlsnlpygdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEecIKK 648
Cdd:cd03216 78 amvYQ-----------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIR 126
|
170 180 190
....*....|....*....|....*....|....
gi 89111135 649 TLR--GKTVVLVTHQLQ-FLESCDEVILLEDGEI 679
Cdd:cd03216 127 RLRaqGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
503-683 |
4.39e-16 |
|
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: 78.69 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 503 VRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENILFG------ 564
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFaHLTVEQNVGLGlspglk 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 -EKYDHQRYQHTVRVCGLQKDLSNLPygdlteiGErglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD----AHVGK 639
Cdd:cd03298 101 lTAEDRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 89111135 640 HVFEECIKktlRGKTVVLVTHQLQFLESCDE-VILLEDGEICEKG 683
Cdd:cd03298 170 LVLDLHAE---TKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
462-691 |
5.01e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.03 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 462 HLCKKQRSEAYSERSPPAKGATGPE-------EQSDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQK 534
Cdd:PRK13536 16 LSPIERKHQGISEAKASIPGSMSTVaidlagvSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 535 GVVAVNGtlAYVSQQAWIfhgnVRENILFGEKYDHQRYQHTVR--------VCGLQKDLSNLPYGDLTEIGE-------R 599
Cdd:PRK13536 96 GKITVLG--VPVPARARL----ARARIGVVPQFDNLDLEFTVRenllvfgrYFGMSTREIEAVIPSLLEFARleskadaR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 600 GLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHvGKHVFEECIKKTL-RGKTVVLVTHQLQFLES-CDEVILLEDG 677
Cdd:PRK13536 170 VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAG 248
|
250
....*....|....
gi 89111135 678 EICEKGTHKELMEE 691
Cdd:PRK13536 249 RKIAEGRPHALIDE 262
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
496-691 |
5.08e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------TLAYVSQQAWIFHGN---------VRE 559
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsKLQGIRKLVGIVFQNpetqfvgrtVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKydhqryqhtvRVCGLQKDLSNLPYGDLTEIG------ERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAV 633
Cdd:PRK13644 98 DLAFGPE----------NLCLPPIEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 634 DAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1130-1331 |
7.06e-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: 77.90 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1130 RDNTPLvLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIlSLEDLRTKLTVIPQDPVLFVG 1209
Cdd:COG4133 12 RGERLL-FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1210 -TVRYNLDpF------ESHTDEMLWQVLERtfmrdtiMKLPEKLQAEVtengENFSVGERQLLCVARALLRNSKIILLDE 1282
Cdd:COG4133 90 lTVRENLR-FwaalygLRADREAIDEALEA-------VGLAGLADLPV----RQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 89111135 1283 ATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLNCdHVLVMENGK 1331
Cdd:COG4133 158 PFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAA-RVLDLGDFK 206
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
486-688 |
9.75e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.89 E-value: 9.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 486 EEQSDSLKsVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAV----NG-------------------- 541
Cdd:PRK13631 33 EKQENELV-ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGdkknnhelitnpyskkiknf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 542 -----TLAYVSQ--QAWIFHGNVRENILFG------EKYD-HQRYQHTVRVCGLQKD-LSNLPYGdlteigerglnLSGG 606
Cdd:PRK13631 112 kelrrRVSMVFQfpEYQLFKDTIEKDIMFGpvalgvKKSEaKKLAKFYLNKMGLDDSyLERSPFG-----------LSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 607 QRQRISLARAVYSDRQLYLLDDPLSAVDAHvGKHVFEECIKKTLR-GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGT 684
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKAnNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
....
gi 89111135 685 HKEL 688
Cdd:PRK13631 260 PYEI 263
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1140-1359 |
1.02e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.15 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1140 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP---ASGTIFIDEVDICILS---LEDLRT-KLTVIPQDPVLfvgtvr 1212
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPekeLNKLRAeQISMIFQDPMT------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1213 yNLDPFeSHTDEMLWQVL-------------ERTFMRDTImKLPEKLQaEVTENGENFSVGERQLLCVARALLRNSKIIL 1279
Cdd:PRK09473 109 -SLNPY-MRVGEQLMEVLmlhkgmskaeafeESVRMLDAV-KMPEARK-RMKMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1280 LDEATASMD----SKTDTLVqNTIKDAFkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFAM-LL 1353
Cdd:PRK09473 185 ADEPTTALDvtvqAQIMTLL-NELKREF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQPSHPYSIgLL 262
|
....*.
gi 89111135 1354 AAEVRL 1359
Cdd:PRK09473 263 NAVPRL 268
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1136-1341 |
1.03e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL-FVGTV--- 1211
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVeev 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1212 ----RYNLDPFESHTDEMLWQVLERTfmrdtimklpeklqaEVTENGENF----SVGERQLLCVARALLRNS------KI 1277
Cdd:PRK13548 97 vamgRAPHGLSRAEDDALVAAALAQV---------------DLAHLAGRDypqlSGGEQQRVQLARVLAQLWepdgppRW 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1278 ILLDEATASMD----SKTDTLVQNTIKDAfkGCTVLTIAHRLN-TVLNCDHVLVMENGKVIEFDKP-EVL 1341
Cdd:PRK13548 162 LLLDEPTSALDlahqHHVLRLARQLAHER--GLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPaEVL 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
495-661 |
1.07e-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: 77.01 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT------LAYVSQQAWIFHGN-------VRENI 561
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrDEPHENILYLGHLPglkpelsALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFgekydhqrYQHTVRvcGLQKDLSNLpygdLTEIGERGLN------LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:TIGR01189 95 HF--------WAAIHG--GAQRTIEDA----LAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*..
gi 89111135 636 HvGKHVFEECIKKTL-RGKTVVLVTHQ 661
Cdd:TIGR01189 161 A-GVALLAGLLRAHLaRGGIVLLTTHQ 186
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
494-683 |
1.10e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 494 SVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWI-FHGNVRE 559
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrVASVPQDTSLsFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGekydhqRYQHTVRVCGLQKD-----LSNLPYGDLTEIGERGL-NLSGGQRQRISLARAVYSDRQLYLLDDPLSAV 633
Cdd:PRK09536 97 VVEMG------RTPHRSRFDTWTETdraavERAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 89111135 634 DAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 683
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
495-689 |
1.12e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.47 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG----------------------------TLAYV 546
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtrlTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 547 SQQAWIfHGNVRENILfgekydhqryQHTVRVCGLQKDLSN---LPYGDLTEIGERG-----LNLSGGQRQRISLARAVY 618
Cdd:PRK10619 100 HFNLWS-HMTVLENVM----------EAPIQVLGLSKQEAReraVKYLAKVGIDERAqgkypVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 619 SDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 689
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
494-675 |
1.15e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 494 SVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT----------LAYVSQQA---WIFHGNVREN 560
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGeKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGL-NLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGK 639
Cdd:PRK15056 101 VMMG-RYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIgELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 89111135 640 HVFEecIKKTLR--GKTVVLVTHQL-QFLESCDEVILLE 675
Cdd:PRK15056 180 RIIS--LLRELRdeGKTMLVSTHNLgSVTEFCDYTVMVK 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1136-1333 |
1.19e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 76.82 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIFIDEVDiciLSLEDLRTKLTVIPQDPVLFVG-TVR 1212
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1213 ynldpfeshtdEMLWQVLErtfMRdtimklpeklqaevtengeNFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 1292
Cdd:cd03213 101 -----------ETLMFAAK---LR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 89111135 1293 TLVQNTIKD-AFKGCTVLTIAHRLNTVL--NCDHVLVMENGKVI 1333
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1120-1346 |
1.36e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.72 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLV---LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICI----LSLED 1192
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTKLTVIPQDP--VLFVGTV-------RYNLDPFESHTDEMLWQVLERTFMRDTIM-KLPEKLqaevtengenfSVGER 1262
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVlkdvefgPKNFGFSEDEAKEKALKWLKKVGLSEDLIsKSPFEL-----------SGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1263 QLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK-GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEV 1340
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKE 231
|
....*.
gi 89111135 1341 LAEKPD 1346
Cdd:PRK13641 232 IFSDKE 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1136-1346 |
1.48e-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: 77.58 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSL-EDLRTKLTVIPQDPVLFVG-TVRY 1213
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1214 NLDpfeshtdemlwQVLErtfmrdtIMKLPEKLQAEVTE--------------NGENFSVGERQLLCVARALLRNSKIIL 1279
Cdd:cd03218 95 NIL-----------AVLE-------IRGLSKKEREEKLEelleefhithlrksKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1280 LDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 1346
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1136-1330 |
1.68e-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: 77.09 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID----EVDIC------ILsleDLRTK--------L 1197
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAqaspreIL---ALRRRtigyvsqfL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQ--------DPVLFVGTvrynlDPFESHTDEMLWqvLERtfmrdtiMKLPEKL--QAEVTengenFSVGERQLLCV 1267
Cdd:COG4778 103 RVIPRvsaldvvaEPLLERGV-----DREEARARAREL--LAR-------LNLPERLwdLPPAT-----FSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1268 ARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAfK--GCTVLTIAHRLNTVLN-CDHVLVMENG 1330
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KarGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
499-741 |
1.74e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.88 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-LAYVS----------QQAWIF-HGNVRENILFGEK 566
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPpyqrpinmmfQSYALFpHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 567 YDH-------QRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDahvgk 639
Cdd:PRK11607 118 QDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 640 hvfeecikKTLRGKTvvlvthQLQFLEscdevILLEDGEICEKGTH--KELMEERGRYAklIHNlRG--LQFKDPEHLYN 715
Cdd:PRK11607 182 --------KKLRDRM------QLEVVD-----ILERVGVTCVMVTHdqEEAMTMAGRIA--IMN-RGkfVQIGEPEEIYE 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 89111135 716 ----------AAMVEAFKESPAEREEDaGIIVLAPG 741
Cdd:PRK11607 240 hpttrysaefIGSVNVFEGVLKERQED-GLVIDSPG 274
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1120-1343 |
2.06e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIfidevDICILSLED----LRT 1195
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-----SLCGEPVPSrarhARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 KLTVIPQ----DPVLfvgTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTEngenFSVGERQLLCVARAL 1271
Cdd:PRK13537 81 RVGVVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1272 LRNSKIILLDEATASMDSKTDTLVQNTIKDAF-KGCTVLTIAH------RLntvlnCDHVLVMENGKVIEFDKPEVLAE 1343
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
493-674 |
2.31e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 76.68 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------LAYVSQQAWIFHGNVRE 559
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKYDHQRYQHTVrvcgLQKDLS--NLPygdlTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAH 636
Cdd:PRK10247 100 NLIFPWQIRNQQPDPAI----FLDDLErfALP----DTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 89111135 637 vGKHVFEECIKKTLRGK--TVVLVTHQLQFLESCDEVILL 674
Cdd:PRK10247 172 -NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1120-1334 |
2.33e-15 |
|
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: 76.74 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTP--LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICilsleDLRTKL 1197
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQDPVLFvgtvrynldPfeshtdemlWqvleRTfMRDTIMkLPEKLQ----AEVTENGENF---------------- 1257
Cdd:cd03293 76 GYVFQQDALL---------P---------W----LT-VLDNVA-LGLELQgvpkAEARERAEELlelvglsgfenayphq 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1258 -SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLN-TVLNCDHVLVMEN--GK 1331
Cdd:cd03293 132 lSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGR 211
|
...
gi 89111135 1332 VIE 1334
Cdd:cd03293 212 IVA 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
493-681 |
2.39e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 77.54 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVV----------------AVNGTLAYVSQQA------ 550
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyqldrkqrrAFRRDVQLVFQDSpsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 551 -----WIFHGNVRENILFGEKYDHQRYQHTVRVCGLQ-KDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLY 624
Cdd:TIGR02769 104 rmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPR-----------QLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 625 LLDDPLSAVDAHVGKHVFEECIKKTLRGKTV-VLVTHQLQFLES-CDEVILLEDGEICE 681
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1128-1335 |
2.46e-15 |
|
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: 76.46 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNtpLVLDSLNLNIQSGQTvGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIlSLEDLRTKLTVIPQDPVLF 1207
Cdd:cd03264 9 RYGKK--RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 VG-TVRYNLDPF-------ESHTDEMLWQVLERTFMRDtimKLPEKLQAevtengenFSVGERQLLCVARALLRNSKIIL 1279
Cdd:cd03264 85 PNfTVREFLDYIawlkgipSKEVKARVDEVLELVNLGD---RAKKKIGS--------LSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1280 LDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTV-LNCDHVLVMENGKVIEF 1335
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFE 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
495-684 |
3.52e-15 |
|
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: 76.32 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQQAWIFHG-NVRE 559
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKYDHQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGL------NLSGGQRQRISLARAVYSDRQLYLLDDP---L 630
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLadrpagELSYGQQRRLEIARALATDPKLLLLDEPaagL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 631 SAVDAHVGKHVFEEcIKKtlRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 684
Cdd:cd03219 175 NPEETEELAELIRE-LRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
493-694 |
3.71e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 76.71 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAAL------------LGQMQL--------QKGVV-AVNGTLAYVSQQAW 551
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIdtarslsqQKGLIrQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 552 IF-HGNVRENILFGekydhqryqhTVRVCGLQKDLS-NLPYGDLTEIGERG------LNLSGGQRQRISLARAVYSDRQL 623
Cdd:PRK11264 96 LFpHRTVLENIIEG----------PVIVKGEPKEEAtARARELLAKVGLAGketsypRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 624 YLLDDPLSAVDAHVGKHVFeecikKTLRG-----KTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELM----EERG 693
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVL-----NTIRQlaqekRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFadpqQPRT 240
|
.
gi 89111135 694 R 694
Cdd:PRK11264 241 R 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1137-1343 |
3.79e-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: 80.23 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI----DEVDICILSLeDLRTKLT----VIPQDPVLFV 1208
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1209 -GTVRYNLD-------PFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVtengenfSVGERQLLCVARALLRNSKIILL 1280
Cdd:TIGR03269 379 hRTVLDNLTeaiglelPDELARMKAVITLKMVGFDEEKAEEILDKYPDEL-------SEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1281 DEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAE 1343
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPeEIVEE 518
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
474-679 |
4.12e-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: 76.16 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 474 ERSPPAKGATGPEEQSDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQK---GVVAVNG--------- 541
Cdd:cd03234 1 QRVLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGqprkpdqfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 542 -TLAYVSQQ-AWIFHGNVRENILF------GEKYDHQRYQHTVRVCGLqKDLSNLPYGdlteiGERGLNLSGGQRQRISL 613
Cdd:cd03234 81 kCVAYVRQDdILLPGLTVRETLTYtailrlPRKSSDAIRKKRVEDVLL-RDLALTRIG-----GNLVKGISGGERRRVSI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 614 ARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQ-----LQFLescDEVILLEDGEI 679
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQprsdlFRLF---DRILLLSSGEI 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
495-674 |
4.36e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.82 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL--------AYVSQQ----AWIfhgNVRENIL 562
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQKdallPWL---NVLDNVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FGEKYD-------HQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:COG4525 99 FGLRLRgvpkaerRARAEELLALVGLADFARRRIW-----------QLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 89111135 636 HVGKHVFE---ECIKKTlrGKTVVLVTHQLQ---FLEScdEVILL 674
Cdd:COG4525 168 LTREQMQElllDVWQRT--GKGVFLITHSVEealFLAT--RLVVM 208
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
461-688 |
5.85e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.71 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 461 RHLCKKQRSEAYSERSPPAKGATGPEEQSDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAAL----LGQMQLQkGV 536
Cdd:TIGR00955 6 RNSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrsPKGVKGS-GS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 537 VAVNGTL----------AYVsQQAWIFHGN--VRENILFGEKYDHQRYQHTV----RVCGLQKDLSNLPYGDlTEIGERG 600
Cdd:TIGR00955 85 VLLNGMPidakemraisAYV-QQDDLFIPTltVREHLMFQAHLRMPRRVTKKekreRVDEVLQALGLRKCAN-TRIGVPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 601 L--NLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQ--LQFLESCDEVILLED 676
Cdd:TIGR00955 163 RvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAE 242
|
250
....*....|..
gi 89111135 677 GEICEKGTHKEL 688
Cdd:TIGR00955 243 GRVAYLGSPDQA 254
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1120-1353 |
6.36e-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: 80.37 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIfidevdicilsleDLRTKLTV 1199
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIIL 1279
Cdd:TIGR00957 704 VPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1280 LDEATASMDSKTDT-LVQNTI--KDAFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDK-PEVLAEkpDSAFAMLL 1353
Cdd:TIGR00957 784 FDDPLSAVDAHVGKhIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSyQELLQR--DGAFAEFL 859
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1136-1344 |
6.86e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSL-EDLRTKLTVIPQDPVLF------- 1207
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFrrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 ----VGTVRYNLDPfESHTD--EMLWQVLERTFMRDTImklpeklqaevtenGENFSVGERQLLCVARALLRNSKIILLD 1281
Cdd:PRK10895 98 nlmaVLQIRDDLSA-EQREDraNELMEEFHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1282 EATASMDSKTDTLVQNTI---KDAfkGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAEK 1344
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIehlRDS--GLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPtEILQDE 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1141-1349 |
1.08e-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: 75.76 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1141 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL----RTKLTVIPQDPVLFVG-TVRYN- 1214
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTVLENv 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1215 --------LDPFESHtdEMLWQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNSKIILLDEATAS 1286
Cdd:cd03294 124 afglevqgVPRAERE--ERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1287 MDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVLAEKPDSAF 1349
Cdd:cd03294 191 LDPLIRREMQDELLRlqAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
493-690 |
1.16e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAaLLGQMQ-LQKGVVAVNGT-------------LAYVSQQAWIFHG-NV 557
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQpPSEGEILLDAQpleswsskafarkVAYLPQQLPAAEGmTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENILFGeKY------------DHQRYQHTVRVCGLqKDLSNlpygDLTEigerglNLSGGQRQRISLARAVYSDRQLYL 625
Cdd:PRK10575 103 RELVAIG-RYpwhgalgrfgaaDREKVEEAISLVGL-KPLAH----RLVD------SLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 626 LDDPLSAVD-AHvgkHVFEECIKKTL---RGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 690
Cdd:PRK10575 171 LDEPTSALDiAH---QVDVLALVHRLsqeRGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
496-692 |
1.24e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLG----------QMQLQKGVVAVNGTLA-----YVSQQAWIFHG----- 555
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagsHIELLGRTVQREGRLArdirkSRANTGYIFQQfnlvn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 --NVRENILFGEKYDHQRYQHTVR-VCGLQKDLSnlpYGDLTEIG------ERGLNLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:PRK09984 100 rlSVLENVLIGALGSTPFWRTCFSwFTREQKQRA---LQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 627 DDPLSAVDAHVGKHVFEecikkTLR------GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEER 692
Cdd:PRK09984 177 DEPIASLDPESARIVMD-----TLRdinqndGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
500-679 |
1.47e-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: 74.13 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 500 SFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENILFGEK- 566
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtglapyqrpVSMLFQENNLFaHLTVRQNIGLGLHp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 567 ------YDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKH 640
Cdd:TIGR01277 98 glklnaEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 89111135 641 VFeeCIKKTL---RGKTVVLVTHQLQFL-ESCDEVILLEDGEI 679
Cdd:TIGR01277 167 ML--ALVKQLcseRQRTLLMVTHHLSDArAIASQIAVVSQGKI 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
493-661 |
1.65e-14 |
|
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: 73.68 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL------AYVSQQAWIFHGN-------VRE 559
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldfqrdSIARGLLYLGHAPgikttlsVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NIlfgekydhqRYQHtvRVCGLQKDLSNLPYGDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVG 638
Cdd:cd03231 93 NL---------RFWH--ADHSDEQVEEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|...
gi 89111135 639 KHVFEECIKKTLRGKTVVLVTHQ 661
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
493-678 |
1.73e-14 |
|
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: 72.10 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAV--NGTLAYVSQqawifhgnvrenilfgekydhq 570
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 571 ryqhtvrvcglqkdlsnlpygdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHvGKHVFEECIKKtL 650
Cdd:cd03221 71 --------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALEEALKE-Y 116
|
170 180
....*....|....*....|....*....
gi 89111135 651 RGkTVVLVTHQLQFLES-CDEVILLEDGE 678
Cdd:cd03221 117 PG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1136-1333 |
2.00e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSlEDLRTKL--TVIpQDPVLfvGTV-- 1211
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAKYigRVF-QDPMM--GTAps 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1212 ---------------RYNLDPfeSHTDEmlwqvlERTFMRDTI----MKLPEKLQAEVtengENFSVGERQLLCVARALL 1272
Cdd:COG1101 97 mtieenlalayrrgkRRGLRR--GLTKK------RRELFRELLatlgLGLENRLDTKV----GLLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1273 RNSKIILLDEATASMDSKTDTLV----QNTIKDafKGCTVLTIAHRLNTVLNC-DHVLVMENGKVI 1333
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVleltEKIVEE--NNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
495-684 |
2.02e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 76.27 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGqmqLQK---GVVAVNGT-LAYVSQQAW---------IF-HGN---- 556
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LERptsGSVLVDGVdLTALSERELraarrkigmIFqHFNllss 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 --VRENILFGekydhqryqhtVRVCGLQKDlsnlpygdltEIGER--------GL---------NLSGGQRQRISLARAV 617
Cdd:COG1135 97 rtVAENVALP-----------LEIAGVPKA----------EIRKRvaellelvGLsdkadaypsQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 618 YSDRQLYLLDDPLSAVDAHVGKHVFE---EcIKKTLrGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 684
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDllkD-INREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1136-1336 |
2.15e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIFIDEvdicilsledlRTKLTVIPQDPVLFVG-T 1210
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1211 VRYNLdpFESHTDemLWQVLER--------TFMRDTIMKLpEKLQAEVTENGE--------------------------N 1256
Cdd:COG0488 78 VLDTV--LDGDAE--LRALEAEleeleaklAEPDEDLERL-AELQEEFEALGGweaearaeeilsglgfpeedldrpvsE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1257 FSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDaFKGcTVLTIAH-R--LNTVlnCDHVLVMENGKVI 1333
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN-YPG-TVLVVSHdRyfLDRV--ATRILELDRGKLT 228
|
...
gi 89111135 1334 EFD 1336
Cdd:COG0488 229 LYP 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
493-690 |
2.17e-14 |
|
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: 74.12 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQQAWIFHG-NV 557
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENIL--FGEKYDHQRYQHTvRVCGLQKDLSnlpygdLTEIGER-GLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD 634
Cdd:cd03218 93 EENILavLEIRGLSKKEREE-KLEELLEEFH------ITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 635 AhvgKHVFE-ECIKKTLRGKTV-VLVT-HQL-QFLESCDEVILLEDGEICEKGTHKELME 690
Cdd:cd03218 166 P---IAVQDiQKIIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
493-690 |
3.23e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-TLAYVSQQAWIFHG------------NVRE 559
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGePVPSRARHARQRVGvvpqfdnldpdfTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NIL-FGEKYDHQRYQHTVRVCGLQkDLSNLPYGDLTEIGErglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHvG 638
Cdd:PRK13537 100 NLLvFGRYFGLSAAAARALVPPLL-EFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-A 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 639 KHVFEECIKKTL-RGKTVVLVTHqlqFLES----CDEVILLEDGEICEKGTHKELME 690
Cdd:PRK13537 174 RHLMWERLRSLLaRGKTILLTTH---FMEEaerlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1120-1341 |
4.33e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPL---VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS----LED 1192
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTKLTVIPQDP--VLFVGTV-----------RYNLDPFESHTDEMLwqvLERTFMRDTIMKLPEKLqaevtengenfSV 1259
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVereiifgpknfKMNLDEVKNYAHRLL---MDLGFSRDVMSQSPFQM-----------SG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1260 GERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFD 1336
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQT 228
|
....*
gi 89111135 1337 KPEVL 1341
Cdd:PRK13646 229 SPKEL 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1137-1330 |
4.76e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID-------------EVDICILSLEdlrtkLTVIPQD 1203
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINninynkldhklaaQLGIGIIYQE-----LSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1204 PV---LFVGtvrynldpfeSHTDEMLW--QVLERTFMRD--TIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSK 1276
Cdd:PRK09700 96 TVlenLYIG----------RHLTKKVCgvNIIDWREMRVraAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1277 IILLDEATASM-DSKTDTL--VQNTIKDAFKGctVLTIAHRLNTVLN-CDHVLVMENG 1330
Cdd:PRK09700 166 VIIMDEPTSSLtNKEVDYLflIMNQLRKEGTA--IVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
495-685 |
4.79e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.51 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAAL-------LGQMQL------------QKGVVAVNGTLAYVSQQ--AWIf 553
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIagnhfdfsktpsDKAIRELRRNVGMVFQQynLWP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 554 HGNVRENILfgekydhqryQHTVRVCGLQKD---------LSNLpygDLTEIGER-GLNLSGGQRQRISLARAVYSDRQL 623
Cdd:PRK11124 96 HLTVQQNLI----------EAPCRVLGLSKDqalaraeklLERL---RLKPYADRfPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 624 YLLDDPLSAVDAHVGKHVFEecIKKTLR--GKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTH 685
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVS--IIRELAetGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDA 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
496-679 |
4.81e-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: 72.83 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT---------LAYVSQQ--------AWIFHGNVR 558
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRKigvvfqdfRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILF-------GEKYDHQRYQHTVRVCGLQKDLSNLPYGdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLS 631
Cdd:cd03292 97 ENVAFalevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 89111135 632 AVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLESCDE-VILLEDGEI 679
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1120-1349 |
6.29e-14 |
|
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: 73.20 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGtifideVDICIL-------SLED 1192
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG------NDVRLFgerrggeDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTKL---------TVIPQDPVL------FVGTVrynlDPFESHTDEML---WQVLERTFMRDTIMKLPEKLqaevteng 1254
Cdd:COG1119 76 LRKRIglvspalqlRFPRDETVLdvvlsgFFDSI----GLYREPTDEQReraRELLELLGLAHLADRPFGTL-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1255 enfSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNC-DHVLVMENGK 1331
Cdd:COG1119 144 ---SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
250
....*....|....*....
gi 89111135 1332 VIEF-DKPEVLAEKPDSAF 1349
Cdd:COG1119 221 VVAAgPKEEVLTSENLSEA 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1137-1346 |
6.69e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.59 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDP-VLFVGT----- 1210
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGAtvedd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1211 VRYNLDPFESHTDEMLWQVLERTF---MRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNSKIILLDEATASM 1287
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLavnMLDFKTREPARL-----------SGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1288 D--SKTDTL-VQNTIKDAFKgCTVLTIAHRLNTVLNCDHVLVMENGKVIEFDKP-EVLAEKPD 1346
Cdd:PRK13642 172 DptGRQEIMrVIHEIKEKYQ-LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPsELFATSED 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
546-699 |
6.83e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 546 VSQQAWIFHGNVRENILFGeKYDHQRyQHTVRVC---GLQKDLSNLPYGDLTEIGERGLNLSGGQRQRISLARAVYSDRQ 622
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFG-KEDATR-EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 623 LYLLDDPLSAVDAHVgkhvfEECIKKTL------RGKTVVLVTHQLQFLESCDEVILLEDGE-----ICEKGTHKELME- 690
Cdd:PTZ00265 1379 ILLLDEATSSLDSNS-----EKLIEKTIvdikdkADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSv 1453
|
....*....
gi 89111135 691 ERGRYAKLI 699
Cdd:PTZ00265 1454 QDGVYKKYV 1462
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
508-679 |
7.96e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.53 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 508 ILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL-----------------AYVSQQAWIF-HGNVRENILFG-EKYD 568
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrriGYVFQDARLFpHYKVRGNLRYGmAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 569 HQRYQHTVRVCGLQKDLSNLPygdlteigergLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHV--FEECI 646
Cdd:PRK11144 106 VAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELlpYLERL 174
|
170 180 190
....*....|....*....|....*....|....*
gi 89111135 647 KKTLrgKTVVL-VTHQLQ-FLESCDEVILLEDGEI 679
Cdd:PRK11144 175 AREI--NIPILyVSHSLDeILRLADRVVVLEQGKV 207
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
486-679 |
9.10e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.92 E-value: 9.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 486 EEQSDslksVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT---------LAYVSQQ--AWIFH 554
Cdd:PRK10535 18 EEQVE----VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldadaLAQLRREhfGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 555 gnvRENILfgekyDHQRYQHTVRV----CGLQKD---------LSNLPYGDltEIGERGLNLSGGQRQRISLARAVYSDR 621
Cdd:PRK10535 94 ---RYHLL-----SHLTAAQNVEVpavyAGLERKqrllraqelLQRLGLED--RVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 622 QLYLLDDPLSAVDAHVGKHVFeeCIKKTLR--GKTVVLVTHQLQFLESCDEVILLEDGEI 679
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVM--AILHQLRdrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1138-1334 |
1.25e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1138 DSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTK---LTVIPQDPV------LFV 1208
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLaslnprMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1209 GTVRynLDPFESHTDEMLWQ-VLERtfMRDTIMK---LPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLDEAT 1284
Cdd:PRK15079 118 GEII--AEPLRTYHPKLSRQeVKDR--VKAMMLKvglLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1285 ASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1136-1346 |
1.26e-13 |
|
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: 72.97 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIfidevdicilsleDLRTKLTVIPQDPVLFVGTVRYNL 1215
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1216 DPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDtlv 1295
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE--- 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1296 qntiKDAFKGC--------TVLTIAHRLNTVLNCDHVLVMENGKVIEFDK-PEVLAEKPD 1346
Cdd:cd03291 196 ----KEIFESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTfSELQSLRPD 251
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1119-1351 |
1.28e-13 |
|
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: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1119 EITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED------ 1192
Cdd:cd03296 2 SIEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 -----LRTKLTVIpqDPVLFVGTVRynldPFESHTDEMLwqvlertfMRDTIMKLPEKLQAEVTENG--ENFSVGERQLL 1265
Cdd:cd03296 80 fqhyaLFRHMTVF--DNVAFGLRVK----PRSERPPEAE--------IRAKVHELLKLVQLDWLADRypAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1266 CVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLA 1342
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVY 225
|
....*....
gi 89111135 1343 EKPDSAFAM 1351
Cdd:cd03296 226 DHPASPFVY 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1133-1346 |
1.53e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 76.10 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1133 TPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIfidevdicilsleDLRTKLTVIPQDPVLFVGTVR 1212
Cdd:TIGR01271 439 TP-VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1213 YNLdPFESHTDEMLWQ-VLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKT 1291
Cdd:TIGR01271 505 DNI-IFGLSYDEYRYTsVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1292 DtlvqntiKDAFKGC--------TVLTIAHRLNTVLNCDHVLVMENGKVIEFDK-PEVLAEKPD 1346
Cdd:TIGR01271 584 E-------KEIFESClcklmsnkTRILVTSKLEHLKKADKILLLHEGVCYFYGTfSELQAKRPD 640
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
499-688 |
1.65e-13 |
|
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: 71.25 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG------------TLAYVSQQAWIFHG-NVRENI-LFG 564
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLyIHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 EKYDHQRYQHTVRVCGLqkdlsnLPYGDLTEIGERGL-NLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFE 643
Cdd:cd03265 99 RLYGVPGAERRERIDEL------LDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 89111135 644 EcIKKTLR--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 688
Cdd:cd03265 173 Y-IEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1141-1345 |
1.66e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.30 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1141 NLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLR----TKLTVIPQDPVLF-----VGTV 1211
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMphmtvLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1212 RYNLD----PFESHTDEMLwQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNSKIILLDEATASM 1287
Cdd:PRK10070 128 AFGMElagiNAEERREKAL-DALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1288 DSKTDTLVQNTIK--DAFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVLAEKP 1345
Cdd:PRK10070 196 DPLIRTEMQDELVklQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
490-691 |
1.70e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 72.53 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 490 DSLKSVLHSISFVVRKGKILGICGNVGSGKSS---LLAALLGQMQLQKGVVAVNGTlAYVSQQAWifhgNVREN--ILFg 564
Cdd:PRK13640 17 DSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGI-TLTAKTVW----DIREKvgIVF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 EKYDHQRYQHTVR---VCGLQKdlSNLPYGDLTEIGERGL--------------NLSGGQRQRISLARAVYSDRQLYLLD 627
Cdd:PRK13640 91 QNPDNQFVGATVGddvAFGLEN--RAVPRPEMIKIVRDVLadvgmldyidsepaNLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 628 DPLSAVDAHvGKHVFEECIKKTLRGK--TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:PRK13640 169 ESTSMLDPA-GKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
493-677 |
1.80e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.04 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGV-----VAVNGTLA---YVSQQ----AWIfhgNVREN 560
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSitldgKPVEGPGAergVVFQNegllPWR---NVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGekydhQRYQHTVRVCGLQKDLSNLPYGDLTEIGERGL-NLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGK 639
Cdd:PRK11248 91 VAFG-----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 89111135 640 HVFEECIKKTLR-GKTVVLVTHQLQ---FLEScdEVILLEDG 677
Cdd:PRK11248 166 QMQTLLLKLWQEtGKQVLLITHDIEeavFMAT--ELVLLSPG 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
496-702 |
1.80e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.55 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-------------------TLAYVSQQAWIFHGN 556
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkkvSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFG-------EKYDHQRYQHTVRVCGLQKDLSNlpygdlteigERGLNLSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:PRK13641 103 VLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSEDLIS----------KSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 630 LSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERGRYAKliHNL 702
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKK--HYL 244
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
493-681 |
2.28e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.03 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-LAYVSQQAW---------IFHG-----NV 557
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEpLAKLNRAQRkafrrdiqmVFQDsisavNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENI--LFGEKYDH----------QRYQHTVRVCGLQ-KDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLY 624
Cdd:PRK10419 105 RKTVreIIREPLRHllsldkaerlARASEMLRAVDLDdSVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 625 LLDDPLSAVDAHVGKHVFEecIKKTLR---GKTVVLVTHQLQFLES-CDEVILLEDGEICE 681
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIR--LLKKLQqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1136-1334 |
2.48e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIFIDEVDICILS---LEDLRTKLTVIPQDPvlfvgtvR 1212
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1213 YNLDP---FESHTDEMLwQVLERTFmrdTIMKLPEKLQAEVTENG----------ENFSVGERQLLCVARALLRNSKIIL 1279
Cdd:PRK15134 373 SSLNPrlnVLQIIEEGL-RVHQPTL---SAAQREQQVIAVMEEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 1280 LDEATASMDsKTdtlVQNTIKDAFKG------CTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:PRK15134 449 LDEPTSSLD-KT---VQAQILALLKSlqqkhqLAYLFISHDLHVVRAlCHQVIVLRQGEVVE 506
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1136-1334 |
2.68e-13 |
|
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: 70.25 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMAL--FRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQDPVLFVGtvr 1212
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIPG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1213 ynldpfeshtdemlwqVLERTFMRDTimklpeklqaevtenGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 1292
Cdd:cd03217 92 ----------------VKNADFLRYV---------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 89111135 1293 TLVQNTIKD-AFKGCTVLTIAH--RLNTVLNCDHVLVMENGKVIE 1334
Cdd:cd03217 141 RLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
497-668 |
3.00e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 497 HSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL------AYVSQQAWIFHGN-------VRENILF 563
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPirrqrdEYHQDLLYLGHQPgikteltALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 564 ----GEKYDHQRYQHTVRVCGLQKdLSNLPYGdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHvGK 639
Cdd:PRK13538 98 yqrlHGPGDDEALWEALAQVGLAG-FEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-GV 165
|
170 180 190
....*....|....*....|....*....|
gi 89111135 640 HVFEECIKKTL-RGKTVVLVTHQLQFLESC 668
Cdd:PRK13538 166 ARLEALLAQHAeQGGMVILTTHQDLPVASD 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1115-1350 |
3.58e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 71.27 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1115 PSRGEITFRDYQMRY--RDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIFIDEVDIcil 1188
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDGKPV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1189 slEDLRTKLTVIPQDPVLF------------VGTVRYNLDPFESHTDEMLWQV-LERtFMRdtimKLPEKLqaevtenge 1255
Cdd:COG1116 76 --TGPGPDRGVVFQEPALLpwltvldnvalgLELRGVPKAERRERARELLELVgLAG-FED----AYPHQL--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1256 nfSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAH------RLntvlnCDHVLVM 1327
Cdd:COG1116 140 --SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVL 212
|
250 260 270
....*....|....*....|....*....|
gi 89111135 1328 EN--GKVIE-----FDKPEVLAEKPDSAFA 1350
Cdd:COG1116 213 SArpGRIVEeidvdLPRPRDRELRTSPEFA 242
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
871-1342 |
4.02e-13 |
|
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: 73.68 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 871 FVFTKTTLMASSSL-HDTVF-------DKILKSPMSFFDTTPTGRLMNRFSKDMD---ELDVRLPFhaenFLQQFFMVVF 939
Cdd:COG4615 62 LLSRLASQLLLTRLgQHAVArlrlrlsRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE----LLQSVALVLG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 940 ILVILA----AVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVsrspWFTHITSSMQGL----------------G 999
Cdd:COG4615 138 CLAYLAwlspPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDR----LFKHFRALLEGFkelklnrrrrraffdeD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1000 IIHAYGKKESCITYHLLYFNCALRWFALRMDVLMNILTFTVALLVTLSFSSISTSSkgLSLSYIIQ-LSGLLQVcVRTGT 1078
Cdd:COG4615 214 LQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFV--LVLLFLRGpLSQLVGA-LPTLS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1079 ETQAKFTSVELLREYISTCVPEcTHPLKVGTCPKDWpsrGEITFRDYQMRYR---DNTPLVLDSLNLNIQSGQTVGIVGR 1155
Cdd:COG4615 291 RANVALRKIEELELALAAAEPA-AADAAAPPAPADF---QTLELRGVTYRYPgedGDEGFTLGPIDLTIRRGELVFIVGG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1156 TGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVLFvgtvRYNLDPFESHTDEMLWQVLERtfm 1235
Cdd:COG4615 367 NGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLER--- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1236 rdtiMKLPEKLQAevtENGE----NFSVGERQLLCVARALLRNSKIILLDEATASMDSktdtlvqnTIKDAF-------- 1303
Cdd:COG4615 440 ----LELDHKVSV---EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDP--------EFRRVFytellpel 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 89111135 1304 --KGCTVLTIAH-----RLntvlnCDHVLVMENGKVIEFDKPEVLA 1342
Cdd:COG4615 505 kaRGKTVIAISHddryfDL-----ADRVLKMDYGKLVELTGPAALA 545
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1137-1358 |
4.72e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.42 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIFIDEVDICILSLEDLRTK--------LTVIPQDPV 1205
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKVLSGVYPHgtyEGEIIFEGEELQASNIRDTERAgiaiihqeLALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 L---FVGTV-----RYNLDPFESHTDEMLWQVlertfmrdtimklpeKLQAEVTENGENFSVGERQLLCVARALLRNSKI 1277
Cdd:PRK13549 100 LeniFLGNEitpggIMDYDAMYLRAQKLLAQL---------------KLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1278 ILLDEATASM-DSKTDTLVqNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEkpDSAFAMLLA 1354
Cdd:PRK13549 165 LILDEPTASLtESETAVLL-DIIRDlKAHGIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMTE--DDIITMMVG 241
|
....
gi 89111135 1355 AEVR 1358
Cdd:PRK13549 242 RELT 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
493-683 |
4.87e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQkGVVAVNGT----------LAYVSQQAWIFHG-----NV 557
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQplhnlnrrqlLPVRHRIQVVFQDpnsslNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENILfgekydhQRYQHTVRVcgLQKDLSNLPYGD--LTEIGERGLN----------LSGGQRQRISLARAVYSDRQLYL 625
Cdd:PRK15134 378 RLNVL-------QIIEEGLRV--HQPTLSAAQREQqvIAVMEEVGLDpetrhrypaeFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 626 LDDPLSAVDAHVGKHVFEecIKKTLRGK---TVVLVTHQLQFLES-CDEVILLEDGEICEKG 683
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILA--LLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1137-1343 |
5.72e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLgM-ALFRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQDPVLF-VGTVRY 1213
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLVpNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1214 NLdpfeshtdeML------WQVLERTFMRDTIMKLPEK------LQAEVtengENFSVGERQLLCVARALLRNSKIILLD 1281
Cdd:COG3845 100 NI---------VLgleptkGGRLDRKAARARIRELSERygldvdPDAKV----EDLSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1282 EATASM-DSKTDTLVQnTIKD-AFKGCTVLTIAHRLNTVL-NCDHVLVMENGKVI-EFDKPEV----LAE 1343
Cdd:COG3845 167 EPTAVLtPQEADELFE-ILRRlAAEGKSIIFITHKLREVMaIADRVTVLRRGKVVgTVDTAETseeeLAE 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
496-690 |
6.23e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.81 E-value: 6.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG------TLAYVSQQAWIFHGN---------VREN 560
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseeTVWDVRRQVGMVFQNpdnqfvgatVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFG------EKYDHQ-RYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAV 633
Cdd:PRK13635 103 VAFGlenigvPREEMVeRVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 634 DAHVGKHVFEecikkTLR------GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 690
Cdd:PRK13635 172 DPRGRREVLE-----TVRqlkeqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
473-692 |
6.30e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 473 SERSPPAKGATGPE--EQSD-SLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT------- 542
Cdd:COG1129 242 EDLFPKRAAAPGEVvlEVEGlSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsp 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 543 -------LAYVS----QQAWIFHGNVRENILFG--EKY------DHQRYQHTVRvcGLQKDLsNLPYGDL-TEIGerglN 602
Cdd:COG1129 322 rdairagIAYVPedrkGEGLVLDLSIRENITLAslDRLsrggllDRRRERALAE--EYIKRL-RIKTPSPeQPVG----N 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 603 LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDahVG-KhvFEecIKKTLR-----GKTVVLVTHQLQ-FLESCDEVILLE 675
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGID--VGaK--AE--IYRLIRelaaeGKAVIVISSELPeLLGLSDRILVMR 468
|
250
....*....|....*..
gi 89111135 676 DGEICEKGTHKELMEER 692
Cdd:COG1129 469 EGRIVGELDREEATEEA 485
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1133-1332 |
6.64e-13 |
|
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: 68.61 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1133 TPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQDPV---LFV 1208
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1209 G-TVRYNLdpfeshtdeMLWQVLertfmrdtimklpeklqaevtengenfSVGERQLLCVARALLRNSKIILLDEATASM 1287
Cdd:cd03215 92 DlSVAENI---------ALSSLL---------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 89111135 1288 DSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKV 1332
Cdd:cd03215 136 DVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
493-688 |
6.69e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAY-------------------VSQQAWIF 553
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiklrkevgmVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 554 -HGNVRENILF-------GEKYDHQR-YQHTVRVCGLQKDLSNlpygdltEIGERGLNLSGGQRQRISLARAVYSDRQLY 624
Cdd:PRK14246 103 pHLSIYDNIAYplkshgiKEKREIKKiVEECLRKVGLWKEVYD-------RLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 625 LLDDPLSAVDAhVGKHVFEECIKKTLRGKTVVLVTHQ-LQFLESCDEVILLEDGEICEKGTHKEL 688
Cdd:PRK14246 176 LMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1120-1336 |
8.06e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFRL----VEPASGTIFIDEvdicilsledlRT 1195
Cdd:COG0488 316 LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLlageLEPDSGTVKLGE-----------TV 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 KLTVIPQDpvlfvgtvRYNLDPfeshtDEMLWQVLERTFMRDTIMKL----------PEKLQAEVtengENFSVGERQLL 1265
Cdd:COG0488 379 KIGYFDQH--------QEELDP-----DKTVLDELRDGAPGGTEQEVrgylgrflfsGDDAFKPV----GVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1266 CVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDaFKGcTVLTIAH-R--LNTVlnCDHVLVMENGKVIEFD 1336
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
496-690 |
8.76e-13 |
|
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: 72.41 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGqMQLQKGVVAVNGT-LAYVSQQAW---------IF---HG------N 556
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdLDGLSRRALrplrrrmqvVFqdpFGslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRE------NILFGEKYDHQRYQHTVRVcglqkdlsnlpygdLTEIG--ERGLN-----LSGGQRQRISLARAVYSDRQL 623
Cdd:COG4172 381 VGQiiaeglRVHGPGLSAAERRARVAEA--------------LEEVGldPAARHrypheFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 624 YLLDDPLSAVDAHVGKHVFEecIKKTL---RGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELME 690
Cdd:COG4172 447 LVLDEPTSALDVSVQAQILD--LLRDLqreHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
488-681 |
9.29e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 9.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 488 QSDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-TLAYVSQQA----------WIFHG- 555
Cdd:PRK10584 18 QGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqPLHQMDEEAraklrakhvgFVFQSf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 ------NVRENI-----LFGEKyDHQRYQHTVRV---CGLQKDLSNLPygdlteigergLNLSGGQRQRISLARAVYSDR 621
Cdd:PRK10584 98 mliptlNALENVelpalLRGES-SRQSRNGAKALleqLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 622 QLYLLDDPLSAVDAHVGKHVFEECIKKTLR-GKTVVLVTHQLQFLESCDEVILLEDGEICE 681
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
500-689 |
9.46e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 500 SFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG---TLAYVSQQ--AWIF-------HGNVRENILFG--- 564
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRpvSMLFqennlfsHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 ----EKYDHQRYQHTVRVCGLQKDLSNLPygdlteiGErglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD----AH 636
Cdd:PRK10771 99 glklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 89111135 637 VGKHVFEECIKKTLrgkTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKELM 689
Cdd:PRK10771 168 MLTLVSQVCQERQL---TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
493-679 |
1.38e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVV--AVNGTLAYVSQQAWIFHGN--VRENIlfGEKYD 568
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklGETVKIGYFDQHQEELDPDktVLDEL--RDGAP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 569 HQRYQHTVRVCGlqkdlSNLPYGD--LTEIGerglNLSGGQRQRISLARAVYSDRQLYLLDDP-----LSAVDAhvgkhv 641
Cdd:COG0488 406 GGTEQEVRGYLG-----RFLFSGDdaFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPtnhldIETLEA------ 470
|
170 180 190
....*....|....*....|....*....|....*....
gi 89111135 642 FEECIkKTLRGkTVVLVTHQLQFLES-CDEVILLEDGEI 679
Cdd:COG0488 471 LEEAL-DDFPG-TVLLVSHDRYFLDRvATRILEFEDGGV 507
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1136-1334 |
1.75e-12 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 68.61 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSlEDLRTKL------------TVIP-- 1201
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDARARLrarhvgfvfqsfQLLPtl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1202 ------QDPVLFVGtvryNLDPFESHTDEmlwqvLERtfmrdtiMKLPEKLQAEVTEngenFSVGERQLLCVARALLRNS 1275
Cdd:COG4181 106 talenvMLPLELAG----RRDARARARAL-----LER-------VGLGHRLDHYPAQ----LSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1276 KIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIE 1334
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
493-679 |
1.82e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.94 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKG-VVAVNGTLAYVS-------QQA----WifhGNVREN 560
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGeLLAGTAPLAEARedtrlmfQDArllpW---KKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGEKYD-HQRYQHTVRVCGLQKDLSNLPYGdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVGK 639
Cdd:PRK11247 102 VGLGLKGQwRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDA-LTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 89111135 640 HVFEECIKKTLR--GKTVVLVTHQL-QFLESCDEVILLEDGEI 679
Cdd:PRK11247 170 IEMQDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1117-1334 |
1.88e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.79 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1117 RGEITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIFIDEVDICILSLE 1191
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1192 DLRTKLTVIPQDPVLFVgtvryNLDPFES---------------HTDEMLWQVLERTfmrdtimKLPEKLQAEVTENGEN 1256
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIP-----NLSIFENvalglklnrlvkskkELQERVRWALEKA-------QLWDEVKDRLDAPAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1257 FSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAH------RLNtvlncDHVLVMENG 1330
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKG 221
|
....
gi 89111135 1331 KVIE 1334
Cdd:PRK14247 222 QIVE 225
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
495-721 |
1.99e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 69.10 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL------AYVSQQA-WIFHG-----NVRENIl 562
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKleygdyKYRCKHIrMIFQDpntslNPRLNI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 fGEKYD--------------HQRYQHTVRVCGLQKDLSNLPYGDLteigerglnlSGGQRQRISLARAVYSDRQLYLLDD 628
Cdd:COG4167 107 -GQILEeplrlntdltaeerEERIFATLRLVGLLPEHANFYPHML----------SSGQKQRVALARALILQPKIIIADE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 629 PLSAVDAHVGKHV---FEEcIKKTLrGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELmeergryaklihnlrg 704
Cdd:COG4167 176 ALAALDMSVRSQIinlMLE-LQEKL-GISYIYVSQHLGIVKHIsDKVLVMHQGEVVEYGKTAEV---------------- 237
|
250
....*....|....*..
gi 89111135 705 lqFKDPEHLYNAAMVEA 721
Cdd:COG4167 238 --FANPQHEVTKRLIES 252
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
846-1006 |
2.02e-12 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 69.50 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 846 IGQHVYQWVYTASMVFMLVFGVTKGFVFTKTTLMASSS---LHD---TVFDKILKSPMSFFDTTPTGRLMNRFSKDMDEL 919
Cdd:cd07346 30 IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGqrvVFDlrrDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 920 DVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGLG 999
Cdd:cd07346 110 QNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIR 189
|
....*..
gi 89111135 1000 IIHAYGK 1006
Cdd:cd07346 190 VVKAFAA 196
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1140-1333 |
2.15e-12 |
|
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: 67.90 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1140 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICilSLEDLRTKLTVIPQDPVLFVG-TVRYNLD-- 1216
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGlg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1217 --P---FESHTDEMLWQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNSKIILLDEATASMDSKT 1291
Cdd:cd03298 95 lsPglkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 89111135 1292 DTLVQNTIKD--AFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVI 1333
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIA 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
496-710 |
2.38e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 69.28 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAV------NGT-----------LAYVSQ--QAWIFHGN 556
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKknkklkplrkkVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFG-------EKYDHQRYQHTVRVCGLQKD-LSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDD 628
Cdd:PRK13634 103 VEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEElLARSPF-----------ELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 629 PLSAVDAHvGKH----VFEECIKKtlRGKTVVLVTHQLQ-FLESCDEVILLEDGEICEKGTHKEL------MEERG---- 693
Cdd:PRK13634 172 PTAGLDPK-GRKemmeMFYKLHKE--KGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPREIfadpdeLEAIGldlp 248
|
250 260
....*....|....*....|
gi 89111135 694 ---RYAKLIHNLRGLQFKDP 710
Cdd:PRK13634 249 etvKFKRALEEKFGISFPKP 268
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
495-679 |
2.73e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-TLAYVSQQA------------WIFHG------ 555
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqPMSKLSSAAkaelrnqklgfiYQFHHllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 ---NVRENILFGEKYD---HQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:PRK11629 104 aleNVAMPLLIGKKKPaeiNSRALEMLAAVGLEHRANHRPS-----------ELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 89111135 630 LSAVDAHVGKHVFEECIKKTLRGKTVVL-VTHQLQFLESCDEVILLEDGEI 679
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLvVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1128-1341 |
2.73e-12 |
|
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: 67.78 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIcILSLEDLRTKLTVIPQDPvlf 1207
Cdd:cd03265 9 KYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIGIVFQDL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 vgtvryNLDPFESHTDEMLWQV----LERTFMRDTI------MKLPEKLQAEVtengENFSVGERQLLCVARALLRNSKI 1277
Cdd:cd03265 83 ------SVDDELTGWENLYIHArlygVPGAERRERIdelldfVGLLEAADRLV----KTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1278 ILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTV-LNCDHVLVMENGKVIEFDKPEVL 1341
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1120-1359 |
2.76e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.61 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDP--VLFVGTV-------RYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARA 1270
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1271 LLRNSKIILLDEATASMDSK-TDTLVqnTIKDAF--KGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKpd 1346
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRgQETLM--EILDRLhnQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE-- 228
|
250
....*....|...
gi 89111135 1347 safAMLLAAEVRL 1359
Cdd:PRK13647 229 ---DIVEQAGLRL 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
493-679 |
2.83e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG--TLAYVSQQAWIF-HGNVRENIL--FGEKY 567
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDdDLTVLDTVLdgDAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 568 DHQRYQHTVRVCGLQKDLSNLPYGDLTEIGER---------------GL------------NLSGGQRQRISLARAVYSD 620
Cdd:COG0488 91 ALEAELEELEAKLAEPDEDLERLAELQEEFEAlggweaearaeeilsGLgfpeedldrpvsELSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 621 RQLYLLDDP-----LSAVDAhvgkhvFEECIKKtlRGKTVVLVTHQLQFLES-CDEVILLEDGEI 679
Cdd:COG0488 171 PDLLLLDEPtnhldLESIEW------LEEFLKN--YPGTVLVVSHDRYFLDRvATRILELDRGKL 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
496-691 |
2.86e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.99 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQ-------------------QAWIFHGN 556
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikpvrkkvgvvfqfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFGEKYDHQRYQHTVRVCGLQKDLSNLPygdlTEIGERG-LNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD- 634
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLA----DEFWEKSpFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDp 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 635 -AHVGKHVFEECIKKTlrGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:PRK13643 178 kARIEMMQLFESIHQS--GQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
496-698 |
2.94e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.04 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-----------------TLAYVSQ--QAWIFHGN 556
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFGEKydhqRYQHTVrvcglqKDLSNLPYGDLTEIG-ERGL------NLSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:PRK13646 103 VEREIIFGPK----NFKMNL------DEVKNYAHRLLMDLGfSRDVmsqspfQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 630 LSAVDAHvGKHVFEECIKK--TLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERGRYAKL 698
Cdd:PRK13646 173 TAGLDPQ-SKRQVMRLLKSlqTDENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1136-1357 |
3.11e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.79 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSL-----GmalfrLVEPASGTIFIDEVDICI-LSLEDLRTKLtvIPQDPVLFVG 1209
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLlriiaG-----LETPDSGRIVLNGRDLFTnLPPRERRVGF--VFQHYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1210 -TVRYN-------LDPFEShtdemlwqvlERtfmRDTIMKLPEKLQAEVTEN-------GenfsvGERQLLCVARALLRN 1274
Cdd:COG1118 90 mTVAENiafglrvRPPSKA----------EI---RARVEELLELVQLEGLADrypsqlsG-----GQRQRVALARALAVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1275 SKIILLDEATASMDSK-TDTLVQNTIK--DAFKGcTVLTIAH------RLntvlnCDHVLVMENGKVIEFDKPEVLAEKP 1345
Cdd:COG1118 152 PEVLLLDEPFGALDAKvRKELRRWLRRlhDELGG-TTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDRP 225
|
250
....*....|..
gi 89111135 1346 DSAFAMLLAAEV 1357
Cdd:COG1118 226 ATPFVARFLGCV 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1128-1346 |
3.40e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 67.75 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFR----LVEPASGTIFIDEVDICILSLeDLRTKLTV--IP 1201
Cdd:COG1137 12 SYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDITHLPM-HKRARLGIgyLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1202 QDPVLFVG-TVRYNLdpfeshtdeMLwqVLERTFM-RDTIMKLPEKLQAE-----VTEN-GENFSVGERQLLCVARALLR 1273
Cdd:COG1137 85 QEASIFRKlTVEDNI---------LA--VLELRKLsKKEREERLEELLEEfgithLRKSkAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1274 NSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 1346
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHlKERGIGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1136-1342 |
4.77e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVdicilsledLRTKLT----------VIPQDPV 1205
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN---------PCARLTpakahqlgiyLVPQEPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 LFVG-TVRYNLdpfeshtdemLWQvLERTfmrdtiMKLPEKLQAEVTENGENFS---------VGERQLLCVARALLRNS 1275
Cdd:PRK15439 97 LFPNlSVKENI----------LFG-LPKR------QASMQKMKQLLAALGCQLDldssagsleVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1276 KIILLDEATASMD-SKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI------EFDKPEVLA 1342
Cdd:PRK15439 160 RILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIAlsgktaDLSTDDIIQ 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1120-1350 |
5.17e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 68.97 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIcilsledlrtkLTV 1199
Cdd:COG3842 6 LELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----------TGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPvlFVGTV--RYNLDPF---------------------ESHTDEMLwqvlERTFMRDTIMKLPEKLqaevtengen 1256
Cdd:COG3842 73 PPEKR--NVGMVfqDYALFPHltvaenvafglrmrgvpkaeiRARVAELL----ELVGLEGLADRYPHQL---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1257 fSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAH------RLntvlnCDHVLVME 1328
Cdd:COG3842 137 -SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHdqeealAL-----ADRIAVMN 210
|
250 260
....*....|....*....|..
gi 89111135 1329 NGKVIEFDKPEVLAEKPDSAFA 1350
Cdd:COG3842 211 DGRIEQVGTPEEIYERPATRFV 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
496-684 |
5.41e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.67 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT---------LAYVSQQ-AWIF-HGN------VR 558
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekeLRKARRQiGMIFqHFNllssrtVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFgekydhqryqhTVRVCGLQKDlsnlpygdltEIGER--------GL---------NLSGGQRQRISLARAVYSDR 621
Cdd:PRK11153 101 DNVAL-----------PLELAGTPKA----------EIKARvtellelvGLsdkadrypaQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 622 QLYLLDDPLSAVDAHVGKHVFE--ECIKKTLrGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGT 684
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILEllKDINREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
496-693 |
5.85e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.84 E-value: 5.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWI---------------FHGNVREN 560
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFG-------EKYDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAV 633
Cdd:PRK13647 101 VAFGpvnmgldKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 634 DAHVGKHVFEECIKKTLRGKTVVLVTHQLQF-LESCDEVILLEDGEICEKG-----THKELMEERG 693
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAG 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1121-1342 |
5.95e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.51 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1121 TFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVI 1200
Cdd:PRK15112 13 TFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1201 PQDPvlfvgtvRYNLDPfeshtDEMLWQVLERTFMRDTIMKLPEK-------------LQAEVTENGENFSVGERQLLCV 1267
Cdd:PRK15112 93 FQDP-------STSLNP-----RQRISQILDFPLRLNTDLEPEQRekqiietlrqvglLPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1268 ARALLRNSKIILLDEATASMDSKTDTLVQNTIKD--AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEF-DKPEVLA 1342
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLElqEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERgSTADVLA 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1120-1334 |
6.04e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.47 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDI-CILSLEDLRTKLT 1198
Cdd:PRK11264 4 IEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1199 VIPQDpvlfVGTVRYNLDPFESHTdeMLWQVLE-----RTFMRDTIMKLPEKLQAEVTENGEN------FSVGERQLLCV 1267
Cdd:PRK11264 82 QLRQH----VGFVFQNFNLFPHRT--VLENIIEgpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1268 ARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
496-683 |
6.20e-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: 66.45 E-value: 6.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKIL------------GICGNVGSGKSSLLAALLGQMQLQKGVVAVNG------------TLAYVSQQaw 551
Cdd:cd03264 3 LENLTKRYGKKRALdgvsltlgpgmyGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 552 iFhgNVRENILFGEKYDHQRYQHTV-------RVCGLQKDLsnlpygDLTEIGERGLN-LSGGQRQRISLARAVYSDRQL 623
Cdd:cd03264 81 -F--GVYPNFTVREFLDYIAWLKGIpskevkaRVDEVLELV------NLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 624 YLLDDPLSAVDAhVGKHVFEECIKKTLRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKG 683
Cdd:cd03264 152 LIVDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1128-1356 |
7.31e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 7.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL-----VEPASGTIFIDEVDICILSLEDLR----TKLT 1198
Cdd:PRK15134 16 RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1199 VIPQDPVLfvgtvryNLDPFesHTDE-MLWQVL------ERTFMRDTIMKLPEKL---QA--EVTENGENFSVGERQLLC 1266
Cdd:PRK15134 96 MIFQEPMV-------SLNPL--HTLEkQLYEVLslhrgmRREAARGEILNCLDRVgirQAakRLTDYPHQLSGGERQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1267 VARALLRNSKIILLDEATASMdsktDTLVQNTIKDAFK------GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPE 1339
Cdd:PRK15134 167 IAMALLTRPELLIADEPTTAL----DVSVQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAA 242
|
250
....*....|....*...
gi 89111135 1340 VLAEKPDSAFA-MLLAAE 1356
Cdd:PRK15134 243 TLFSAPTHPYTqKLLNSE 260
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1102-1334 |
8.40e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1102 THPLKVGTCPKDWPsrgEITFRDYQMRYRDNTpLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFID 1181
Cdd:PRK10522 308 KAEFPRPQAFPDWQ---TLELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1182 EVDICILSLEDLRTKLTVIPQDPVLFvgtvRYNLDPFESHTDEMLWQV-LERtfmrdtiMKLPEKLQaevTENGE----N 1256
Cdd:PRK10522 384 GKPVTAEQPEDYRKLFSAVFTDFHLF----DQLLGPEGKPANPALVEKwLER-------LKMAHKLE---LEDGRisnlK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1257 FSVGERQLLCVARALLRNSKIILLDEATASMDSK------TDTLVQntIKDafKGCTVLTIAHRLNTVLNCDHVLVMENG 1330
Cdd:PRK10522 450 LSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLPL--LQE--MGKTIFAISHDDHYFIHADRLLEMRNG 525
|
....
gi 89111135 1331 KVIE 1334
Cdd:PRK10522 526 QLSE 529
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
461-679 |
9.35e-12 |
|
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: 66.59 E-value: 9.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 461 RHLCKKQRSeaySERSPPAKGATG----PEEQSdslKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGV 536
Cdd:cd03267 4 SNLSKSYRV---YSKEPGLIGSLKslfkRKYRE---VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 537 VAVNGTLAYVSQQAWIfhgnVRENILFGekydhQRYQ--------HTVRvcgLQKDLSNLPYG----------DLTEIGE 598
Cdd:cd03267 78 VRVAGLVPWKRRKKFL----RRIGVVFG-----QKTQlwwdlpviDSFY---LLAAIYDLPPArfkkrldelsELLDLEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 599 ------RglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVGKHVFEECIKK--TLRGKTVVLVTHQLQFLES-CD 669
Cdd:cd03267 146 lldtpvR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV-VAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlAR 222
|
250
....*....|
gi 89111135 670 EVILLEDGEI 679
Cdd:cd03267 223 RVLVIDKGRL 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
489-698 |
9.86e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.94 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 489 SDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG------TLAYVSQQAWIFHGN------ 556
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKKIGIIFQNpdnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 ---VRENILFG---EKYDHQRYQ----HTVRVCGLQKDLSNLPygdlteigergLNLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:PRK13632 98 gatVEDDIAFGlenKKVPPKKMKdiidDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 627 DDPLSAVDAHvGKHVFEECIK--KTLRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELM--EERGRYAKL 698
Cdd:PRK13632 167 DESTSMLDPK-GKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILnnKEILEKAKI 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1135-1349 |
1.33e-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: 66.11 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1135 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIciLSLEDLRTKLTVIPQDPVLFVG-TVRY 1213
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1214 NL-----------DPFESHTDEMLWQVLertfMRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNSKIILLDE 1282
Cdd:cd03300 92 NIafglrlkklpkAEIKERVAEALDLVQ----LEGYANRKPSQL-----------SGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1283 ATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAF 1349
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1120-1344 |
1.64e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.55 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNtpLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIdeVDICILSLEDL-RTKLT 1198
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--LGVPVPARARLaRARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1199 VIPQ-DPVLFVGTVRYNLDPFESH-------TDEMLWQVLErtFMRdtimkLPEKLQAEVTEngenFSVGERQLLCVARA 1270
Cdd:PRK13536 118 VVPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLE--FAR-----LESKADARVSD----LSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1271 LLRNSKIILLDEATASMDSKTDTLVQNTIKDAF-KGCTVLTIAH------RLntvlnCDHVLVMENGKVIEFDKPEVLAE 1343
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHALID 261
|
.
gi 89111135 1344 K 1344
Cdd:PRK13536 262 E 262
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
493-691 |
1.71e-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: 64.86 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMqlqkGVVAVNGTLayvsqqawIFHGnvrENILFGEKYDHQR- 571
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHP----KYEVTEGEI--------LFKG---EDITDLPPEERARl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 572 -----YQHTVRVCGLQkdLSNLpygdLTEIGErglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEEcI 646
Cdd:cd03217 78 giflaFQYPPEIPGVK--NADF----LRYVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV-I 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 89111135 647 KKTLR-GKTVVLVTHQLQFLESC--DEVILLEDGEICEKGThKELMEE 691
Cdd:cd03217 148 NKLREeGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGD-KELALE 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
493-661 |
1.72e-11 |
|
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: 64.10 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVV--AVNGTLAYVSQQAWIFHGNVRENILFgekydhq 570
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmPEGEDLLFLPQRPYLPLGTLREQLIY------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 571 ryqhtvrvcglqkdlsnlPYGDlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECikkTL 650
Cdd:cd03223 87 ------------------PWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL---KE 136
|
170
....*....|.
gi 89111135 651 RGKTVVLVTHQ 661
Cdd:cd03223 137 LGITVISVGHR 147
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1137-1333 |
1.79e-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: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQ---SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEV---DICI-LSLEDLRTKLTVIPQDPVLFVG 1209
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1210 -TVRYNLdpfeshtdEMLWQVLERTFMRDTIMKLPEKLQAEVTENG--ENFSVGERQLLCVARALLRNSKIILLDEATAS 1286
Cdd:cd03297 90 lNVRENL--------AFGLKRKRNREDRISVDELLDLLGLDHLLNRypAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 89111135 1287 MDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTV-LNCDHVLVMENGKVI 1333
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1137-1359 |
1.83e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.91 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLE---DLRTKLTVIPQDPvlfVG---- 1209
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQNP---YGslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1210 --TVRYNL-DPFESHTDemlwqvLERTFMRDTIMKLPEK--LQAEVTENGEN-FSVGERQLLCVARALLRNSKIILLDEA 1283
Cdd:PRK11308 108 rkKVGQILeEPLLINTS------LSAAERREKALAMMAKvgLRPEHYDRYPHmFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1284 TASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFAM-LLAAEVRL 1359
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQaLLSATPRL 261
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1120-1347 |
2.01e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.50 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdiciLSLEDLRTKLTV 1199
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-----LKVNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDpvlfVGTV--RYNLDPFESHTDE-MLWQVLERTFMRDTIMKLPEKLQAEV--TENGENF----SVGERQLLCVARA 1270
Cdd:PRK09493 75 IRQE----AGMVfqQFYLFPHLTALENvMFGPLRVRGASKEEAEKQARELLAKVglAERAHHYpselSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1271 LLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLNCDHVLV-MENGKVIEFDKPEVLAEKPDS 1347
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEKVASRLIfIDKGRIAEDGDPQVLIKNPPS 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1137-1332 |
2.14e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.80 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE----PASGTIFIDEV---------DI--------CILSLEDLRT 1195
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRTvqregrlarDIrksrantgYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 KLTVIPQDPVLFVGTVrynldPFeshtdemlWQVLERTFMRdtiMKLPEKLQAeVTENG---------ENFSVGERQLLC 1266
Cdd:PRK09984 100 RLSVLENVLIGALGST-----PF--------WRTCFSWFTR---EQKQRALQA-LTRVGmvhfahqrvSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1267 VARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKV 1332
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
495-661 |
2.65e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAV--NGTLAYVSQQAWIFHGNVRENILF---GEKYDH 569
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSD 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 570 QRYQHTVRVCGLQkDLSnlpyGDLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEEcIKKT 649
Cdd:COG4178 458 AELREALEAVGLG-HLA----ERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREE 531
|
170
....*....|..
gi 89111135 650 LRGKTVVLVTHQ 661
Cdd:COG4178 532 LPGTTVISVGHR 543
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1128-1332 |
2.76e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVdicilSLEDLRTKLTVIPQDPVLF 1207
Cdd:PRK11247 21 RYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAEAREDTRLMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 vgtvrynldPFESHTDEM------LW-----QVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNSK 1276
Cdd:PRK11247 94 ---------PWKKVIDNVglglkgQWrdaalQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1277 IILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLN-TVLNCDHVLVMENGKV 1332
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1120-1346 |
3.24e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.91 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPLV---LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS----LED 1192
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTKLTVIPQDPvlfvgtvrynldpfEShtdemlwQVLERTFMRDTIM---------KLPEKLQAEVTE----------- 1252
Cdd:PRK13643 82 VRKKVGVVFQFP--------------ES-------QLFEETVLKDVAFgpqnfgipkEKAEKIAAEKLEmvgladefwek 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1253 NGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK-GCTVLTIAHRLNTVLN-CDHVLVMENG 1330
Cdd:PRK13643 141 SPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKG 220
|
250
....*....|....*.
gi 89111135 1331 KVIEFDKPEVLAEKPD 1346
Cdd:PRK13643 221 HIISCGTPSDVFQEVD 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1116-1348 |
3.33e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1116 SRGEITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIL------- 1188
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1189 ------SLEDLRTKLTVIPQdpvlfvgtvRYNLDPFESHTDEML---WQV--LERTFMRDTIMKLPEKLQAEVTENGE-- 1255
Cdd:PRK10619 80 kvadknQLRLLRTRLTMVFQ---------HFNLWSHMTVLENVMeapIQVlgLSKQEARERAVKYLAKVGIDERAQGKyp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1256 -NFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLNC-DHVLVMENGKV 1332
Cdd:PRK10619 151 vHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKI 230
|
250
....*....|....*.
gi 89111135 1333 IEFDKPEVLAEKPDSA 1348
Cdd:PRK10619 231 EEEGAPEQLFGNPQSP 246
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1131-1333 |
4.05e-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: 64.21 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1131 DNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA---SGTIFIDEV----------------DICILSLE 1191
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQprkpdqfqkcvayvrqDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1192 DLRTKLTVIPQ--DPVLFVGTVRYNLDPFESHTDemlwqvLERTFMRDTIMKlpeklqaevtengeNFSVGERQLLCVAR 1269
Cdd:cd03234 97 TVRETLTYTAIlrLPRKSSDAIRKKRVEDVLLRD------LALTRIGGNLVK--------------GISGGERRRVSIAV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1270 ALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAH--RLNTVLNCDHVLVMENGKVI 1333
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1137-1358 |
4.96e-11 |
|
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: 66.77 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIFIDEVDICILSLEDLRTK--------LTVIPQDPV 1205
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHgtwDGEIYWSGSPLKASNIRDTERAgiviihqeLTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 L---FVGTvRYNLDPFESHTDEMLWQVLErtFMRDtiMKLPEklqAEVTENGENFSVGERQLLCVARALLRNSKIILLDE 1282
Cdd:TIGR02633 96 AeniFLGN-EITLPGGRMAYNAMYLRAKN--LLRE--LQLDA---DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1283 ATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEkpDSAFAMLLAAEVR 1358
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSE--DDIITMMVGREIT 243
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
495-679 |
5.12e-11 |
|
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: 64.67 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICG-NvGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQQAWIFHG-NVR 558
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGpN-GAGKTTLFNLITGFYRPTSGRILFDGRditglpphriarlgIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGekydhqryQHTVRVCGLQKDLSNLP--YGDLTEIGER--------GL---------NLSGGQRQRISLARAVYS 619
Cdd:COG0411 98 ENVLVA--------AHARLGRGLLAALLRLPraRREEREARERaeellervGLadradepagNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 620 DRQLYLLDDPLSAVdAHVGKHVFEECIKK--TLRGKTVVLVTHQLQFLES-CDEVILLEDGEI 679
Cdd:COG0411 170 EPKLLLLDEPAAGL-NPEETEELAELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
496-709 |
5.18e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.25 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWIfhgNVRENI-LFGEKYDHQRYQH 574
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLM---KLRESVgMVFQDPDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 575 TVrvcglQKDLS------NLPYGDLTEIGERGLN--------------LSGGQRQRISLARAVYSDRQLYLLDDPLSAVD 634
Cdd:PRK13636 99 SV-----YQDVSfgavnlKLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 635 AhVGKHVFEECIKKTLR--GKTVVLVTHQLQFLE-SCDEVILLEDGEICEKGTHKELMEERG-------RYAKLIHNLRG 704
Cdd:PRK13636 174 P-MGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEmlrkvnlRLPRIGHLMEI 252
|
....*
gi 89111135 705 LQFKD 709
Cdd:PRK13636 253 LKEKD 257
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
493-663 |
5.40e-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: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVvAVNGTLAY---------------------VSQQAW 551
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGA-RVEGEILLdgediydpdvdvvelrrrvgmVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 552 IFHGNVRENILFGekydhqryqhtVRVCGLQKDlsnlpyGDLTEIGER------------------GLNLSGGQRQRISL 613
Cdd:COG1117 103 PFPKSIYDNVAYG-----------LRLHGIKSK------SELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 614 ARAVYSDRQLYLLDDPLSAVD----AHVgkhvfEECIKKtLRGK-TVVLVTHQLQ 663
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDpistAKI-----EELILE-LKKDyTIVIVTHNMQ 214
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1137-1333 |
7.72e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS----LED----LRTKLTVIPQDPV--- 1205
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSskeaLENgismVHQELNLVLQRSVmdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 LFVGtvRYNLDPFESHTDEMLwqvlertfmRDTImKLPEKLQAEV--TENGENFSVGERQLLCVARALLRNSKIILLDEA 1283
Cdd:PRK10982 94 MWLG--RYPTKGMFVDQDKMY---------RDTK-AIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1284 TASMDSK-TDTL--VQNTIKDafKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 1333
Cdd:PRK10982 162 TSSLTEKeVNHLftIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
495-689 |
9.43e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG--------------TLAYVSQQAWIF-HGNVRE 559
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVFsRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKY-DHQRYQHTV-RVCGLQKDLsnlpygdLTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHV 637
Cdd:PRK11614 100 NLAMGGFFaERDQFQERIkWVYELFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 638 GKHVFEECIKKTLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELM 689
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1136-1343 |
9.60e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.56 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVdicILSLEDLRT----KLTVIpqDPVLFVGTV 1211
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---VSALLELGAgfhpELTGR--ENIYLNGRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1212 rYNLDPFEshTDEMLWQVLErtFmrdtimklpeklqAEVtenGE-------NFSVGERQLLCVARALLRNSKIILLDEAT 1284
Cdd:COG1134 116 -LGLSRKE--IDEKFDEIVE--F-------------AEL---GDfidqpvkTYSSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1285 ASMDS----KTDTLVQNTIKdafKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLAE 1343
Cdd:COG1134 175 AVGDAafqkKCLARIRELRE---SGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPeEVIAA 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1128-1349 |
9.63e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.13 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLgmalFRLV----EPASGTIFID--EV--------DICIlsledl 1193
Cdd:PRK11432 15 RFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVagleKPTEGQIFIDgeDVthrsiqqrDICM------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1194 rtkltvIPQDPVLF----VG-TVRYNLDPFESHTDEMLWQVLERTFMRDtimklpekLQAEVTENGENFSVGERQLLCVA 1268
Cdd:PRK11432 83 ------VFQSYALFphmsLGeNVGYGLKMLGVPKEERKQRVKEALELVD--------LAGFEDRYVDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1269 RALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVLAEKP 1345
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELYRQP 228
|
....
gi 89111135 1346 DSAF 1349
Cdd:PRK11432 229 ASRF 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1132-1334 |
1.18e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.53 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1132 NTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEV------DICILSLEDLRTKLTVIPQDPV 1205
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 LFVGTVRYN--LDPFESHTDEMLWQVleRTFMRDTIMK--LPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLD 1281
Cdd:PRK14246 101 PFPHLSIYDniAYPLKSHGIKEKREI--KKIVEECLRKvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1282 EATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1118-1358 |
1.21e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 64.71 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1118 GEITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSL-----GmalfrLVEPASGTIFIDEVDIcilslED 1192
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaG-----LEDPTSGEILIGGRDV-----TD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTK---LTVIPQDPVLFVG-TVRYNLdpfeshtdemlwqvlerTF-MRdtIMKLP-EKLQAEVTENGE----------- 1255
Cdd:COG3839 70 LPPKdrnIAMVFQSYALYPHmTVYENI-----------------AFpLK--LRKVPkAEIDRRVREAAEllgledlldrk 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1256 --NFSVGERQLLCVARALLRNSKIILLDEATASMDSKtdtLVQNT---IKDAFK--GCTV----------LTIAhrlntv 1318
Cdd:COG3839 131 pkQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK---LRVEMraeIKRLHRrlGTTTiyvthdqveaMTLA------ 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 89111135 1319 lncDHVLVMENGKVIEFDKPEVLAEKPDSAF--------AM-LLAAEVR 1358
Cdd:COG3839 202 ---DRIAVMNDGRIQQVGTPEELYDRPANLFvagfigspPMnLLPGTVE 247
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
493-689 |
1.27e-10 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 63.18 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGK---ILGicGNvGSGKSSLLAALLGQM-QLQKGVVAVNGT-------------LAYVS---QQAWI 552
Cdd:COG1119 16 KTILDDISWTVKPGEhwaILG--PN-GAGKSTLLSLITGDLpPTYGNDVRLFGErrggedvwelrkrIGLVSpalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 553 FHGNVRENIL---FG-----EKY---DHQRYQHTVRVCGLQkDLSNLPYGDLteigerglnlSGGQRQRISLARAVYSDR 621
Cdd:COG1119 93 RDETVLDVVLsgfFDsiglyREPtdeQRERARELLELLGLA-HLADRPFGTL----------SQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 622 QLYLLDDPLSAVDAHvGKHVFEECIKK--TLRGKTVVLVTHQLQFLESC-DEVILLEDGEICEKGTHKELM 689
Cdd:COG1119 162 ELLILDEPTAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1124-1342 |
1.28e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.87 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1124 DYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI--DEVDICILSLEDLRTKLTVIP 1201
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgKPLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1202 QDP---VLFV---GTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAevtengenFSVGERQLLCVARALLRNS 1275
Cdd:PRK13638 84 QDPeqqIFYTdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQC--------LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1276 KIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP-EVLA 1342
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPgEVFA 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
493-688 |
1.29e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 63.26 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALlGQMQLQKGVVAVNGTLAY---------------------VSQQAW 551
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 552 IFHGNVRENILFGEK----YDHQRYQHTVrvcglQKDLSNLPYGDltEIGER----GLNLSGGQRQRISLARAVYSDRQL 623
Cdd:PRK14239 97 PFPMSIYENVVYGLRlkgiKDKQVLDEAV-----EKSLKGASIWD--EVKDRlhdsALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 624 YLLDDPLSAVDAhVGKHVFEECIKKTLRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 688
Cdd:PRK14239 170 ILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1136-1350 |
1.43e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICilSLEDLRTKLTVIPQDPVLFVG-TVRYN 1214
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1215 L-----------DPFESHTDEMLWQVlertFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNSKIILLDEA 1283
Cdd:PRK11607 112 IafglkqdklpkAEIASRVNEMLGLV----HMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1284 TASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFA 1350
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
493-690 |
1.45e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQQAWIFHG-NV 557
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFRKlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENIL----FGEKYDHQRYQhtvRVCGLQKDLSnlpygdLTEIGE-RGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSA 632
Cdd:COG1137 96 EDNILavleLRKLSKKEREE---RLEELLEEFG------ITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 633 VD--AhvgkhVFEecIKK---TLRGKTV-VLVT-HQLQ-FLESCDEVILLEDGEICEKGTHKELME 690
Cdd:COG1137 167 VDpiA-----VAD--IQKiirHLKERGIgVLITdHNVReTLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
500-689 |
1.47e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.05 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 500 SFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------------LAYVSQQ-AWIFHGNVRENI 561
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakisdaelrevrrkkIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFGEKY-------DHQRYQHTVRVCGLQkdlsNLPYGDLTEigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD 634
Cdd:PRK10070 128 AFGMELaginaeeRREKALDALRQVGLE----NYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 635 AHVGKHVFEECIK-KTLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELM 689
Cdd:PRK10070 197 PLIRTEMQDELVKlQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
496-663 |
1.47e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 63.26 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLL------------------AALLGQMQLQKGV--VAVNGTLAYVSQQAWIFHG 555
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlndlipgfrvegkVTFHGKNLYAPDVdpVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENILFGekydhqryqhtVRVCGLQKDLSNLPYGDLTE----------IGERGLNLSGGQRQRISLARAVYSDRQLYL 625
Cdd:PRK14243 106 SIYDNIAYG-----------ARINGYKGDMDELVERSLRQaalwdevkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 89111135 626 LDDPLSAVDAhVGKHVFEECIKKTLRGKTVVLVTHQLQ 663
Cdd:PRK14243 175 MDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
496-688 |
1.85e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.49 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLA------------ALLGQMQLQKGVVAVNGT--------LAYVSQQAWIFHG 555
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqTIVGDYAIPANLKKIKEVkrlrkeigLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 NVRENILFGEKYDHQRYQHTVRVCGLQKDLSNLPygdlTEIGERG-LNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD 634
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLP----EDYVKRSpFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 635 AHVGK---HVFEECIKKtlRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKEL 688
Cdd:PRK13645 183 PKGEEdfiNLFERLNKE--YKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
488-690 |
2.14e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.85 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 488 QSDSlKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLayVSQQAWifhGNVRENI-LFGEK 566
Cdd:PRK13648 18 QSDA-SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA--ITDDNF---EKLRKHIgIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 567 YDHQRYQHTVR---VCGLQKDLsnLPYGDLTEIGERGLN--------------LSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:PRK13648 92 PDNQFVGSIVKydvAFGLENHA--VPYDEMHRRVSEALKqvdmleradyepnaLSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 630 LSAVDAHvGKHVFEECIKKTLRGK--TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELME 690
Cdd:PRK13648 170 TSMLDPD-ARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
499-691 |
2.35e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYV--SQQAWIFHGN--VREN 560
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYIteSRRDNGFFPNfsIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGEKYDHQRYQHTV---------RVCGLQKDLSNLPYGDLTE-IGErglnLSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:PRK09700 362 MAISRSLKDGGYKGAMglfhevdeqRTAENQRELLALKCHSVNQnITE----LSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 631 SAVDAHVGKHVFEECIKKTLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRDDMSE 499
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1136-1336 |
2.38e-10 |
|
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: 62.16 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLE-DLRTKLTVIpqDPVLFVGTVrYN 1214
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGgGFNPELTGR--ENIYLNGRL-LG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1215 LDPfeshtDEMlwqvleRTFMRDTIM--KLPEKLQAEVtengENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 1292
Cdd:cd03220 114 LSR-----KEI------DEKIDEIIEfsELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 89111135 1293 TLVQNTIKDAFKGC-TVLTIAHRLNTVLN-CDHVLVMENGKVIEFD 1336
Cdd:cd03220 179 EKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1134-1359 |
2.51e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1134 PLVlDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA----SGTIFIDEVDIcilSLEDLRTKLT-VIPQDPvlfv 1208
Cdd:PRK10418 17 PLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPV---APCALRGRKIaTIMQNP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1209 gtvRYNLDPFE---SHTDEMLwQVLERTFMRDTimkLPEKLQAEVTENGE--------NFSVGERQLLCVARALLRNSKI 1277
Cdd:PRK10418 89 ---RSAFNPLHtmhTHARETC-LALGKPADDAT---LTAALEAVGLENAArvlklypfEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1278 ILLDEATASMDSktdtLVQNTIKD------AFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEFDKPEVLAEKPDSAFA 1350
Cdd:PRK10418 162 IIADEPTTDLDV----VAQARILDllesivQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
250
....*....|
gi 89111135 1351 -MLLAAEVRL 1359
Cdd:PRK10418 238 rSLVSAHLAL 247
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
495-661 |
2.67e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.77 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAV--NGTLAYVSQQAWIFHGNVRENILFGEKYDHQRy 572
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpaKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMK- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 573 QHTVRVCGLQKDLSNLpygDLTEIGERGLN----------LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVF 642
Cdd:TIGR00954 546 RRGLSDKDLEQILDNV---QLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
170
....*....|....*....
gi 89111135 643 EECIKKtlrGKTVVLVTHQ 661
Cdd:TIGR00954 623 RLCREF---GITLFSVSHR 638
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1136-1348 |
2.79e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDI---CILSLEDL---RTKLTVIPQDPVLFVG 1209
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRDVlefRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1210 TVRYN-LDPFESHTDEMLWQVLERTFMRDTIMKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMD 1288
Cdd:PRK14271 116 SIMDNvLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1289 SKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSA 1348
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
493-690 |
2.87e-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: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWI----FHGN---------VRE 559
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEKCGYVerpsKVGEpcpvcggtlEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKYDHQRYQHTVRVC-GLQKDLSnlPYGD----------LTEIGERGL------------------------NLS 604
Cdd:TIGR03269 93 EVDFWNLSDKLRRRIRKRIAiMLQRTFA--LYGDdtvldnvleaLEEIGYEGKeavgravdliemvqlshrithiarDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 605 GGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHV---FEECIKKtlRGKTVVLVTHQLQFLES-CDEVILLEDGEIC 680
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhnaLEEAVKA--SGISMVLTSHWPEVIEDlSDKAIWLENGEIK 248
|
250
....*....|
gi 89111135 681 EKGTHKELME 690
Cdd:TIGR03269 249 EEGTPDEVVA 258
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1137-1334 |
3.25e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQD----PVLfvgTV 1211
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQElhlvPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1212 RYNLdpfeshtdeMLWQ-------VLERTFMRDTIMKLpEKLQAEVTENG--ENFSVGERQLLCVARALLRNSKIILLDE 1282
Cdd:PRK11288 97 AENL---------YLGQlphkggiVNRRLLNYEAREQL-EHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1283 ATASMDSK-TDTL--VQNTIKDafKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:PRK11288 167 PTSSLSAReIEQLfrVIRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1136-1333 |
3.50e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.36 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL----RTKLTVIPQdpvlfvgtv 1211
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQ--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1212 RYNLDPFES--HTDEM--LWQVLERTFMRDTIMKLPEKLQAE--VTENGENFSVGERQLLCVARALLRNSKIILLDEATA 1285
Cdd:PRK10535 94 RYHLLSHLTaaQNVEVpaVYAGLERKQRLLRAQELLQRLGLEdrVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 89111135 1286 SMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLNCDHVLVMENGKVI 1333
Cdd:PRK10535 174 ALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
495-679 |
3.84e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICG-NvGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQQAWIF-HGNVR 558
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGeN-GAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQELNLVpNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGE------KYDHQR-YQHTVRVC---GLQKDLSnlpygdlTEIGErglnLSGGQRQRISLARAVYSDRQLYLLDD 628
Cdd:COG1129 98 ENIFLGReprrggLIDWRAmRRRARELLarlGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 89111135 629 PLSAVDAHVGKHVFEecIKKTLR--GKTVVLVTHQL-QFLESCDEVILLEDGEI 679
Cdd:COG1129 167 PTASLTEREVERLFR--IIRRLKaqGVAIIYISHRLdEVFEIADRVTVLRDGRL 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1136-1339 |
3.86e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.31 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTVIPQDPVL--------F 1207
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgditvqeL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 VGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLpeklqaeVTENGENFSVGERQLLCVARALLRNSKIILLDEATASM 1287
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHL-------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 1288 D--SKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPE 1339
Cdd:PRK10253 175 DisHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPK 229
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
846-975 |
4.62e-10 |
|
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: 62.45 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 846 IGQHVYQWVYTASmVFMLVFGVTKG-FVFTKTTLMASSS------LHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDE 918
Cdd:cd18542 30 IGGGLRELLWLLA-LLILGVALLRGvFRYLQGYLAEKASqkvaydLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDT 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 919 LDVRLPFHAENFLQQFFMVVFILVI-------LAAVFPAVLLVVASLAVGFFILLR-IFHRgVQE 975
Cdd:cd18542 109 IRRFLAFGLVELVRAVLLFIGALIImfsinwkLTLISLAIIPFIALFSYVFFKKVRpAFEE-IRE 172
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1128-1332 |
5.15e-10 |
|
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: 60.73 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIcilslEDLRTK---LTVIPQDp 1204
Cdd:cd03301 9 RFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKdrdIAMVFQN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1205 vlfvgtvrYNLDPFESHTDEMLWQVLERTFMRDTI----------MKLPEKLQAEVTEngenFSVGERQLLCVARALLRN 1274
Cdd:cd03301 81 --------YALYPHMTVYDNIAFGLKLRKVPKDEIdervrevaelLQIEHLLDRKPKQ----LSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1275 SKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKV 1332
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
493-689 |
5.27e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQ---LQKGVVAVNGTLA--------YVSQQAWIF-HGNVREN 560
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnFTGTILANNRKPTkqilkrtgFVTQDDILYpHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFgekydhqryqhtVRVCGLQKDLSNLPYGDLTE--IGERGLN--------------LSGGQRQRISLARAVYSDRQLY 624
Cdd:PLN03211 161 LVF------------CSLLRLPKSLTKQEKILVAEsvISELGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 625 LLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQ--LQFLESCDEVILLEDGEICEKGTHKELM 689
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1112-1341 |
5.68e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1112 KDWPSRGEITFRDYQMRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLE 1191
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1192 DLRTKLTVIPQdpvlfvgtvryNLDPFESHTDEML-------WQ-VLERTFMRDTimklpEKLQAEVTENG--------- 1254
Cdd:PRK10575 82 AFARKVAYLPQ-----------QLPAAEGMTVRELvaigrypWHgALGRFGAADR-----EKVEEAISLVGlkplahrlv 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1255 ENFSVGERQLLCVARALLRNSKIILLDEATASMD--SKTDT--LVQNTIKDafKGCTVLTIAHRLNTVLN-CDHVLVMEN 1329
Cdd:PRK10575 146 DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiaHQVDVlaLVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRG 223
|
250
....*....|..
gi 89111135 1330 GKVIEFDKPEVL 1341
Cdd:PRK10575 224 GEMIAQGTPAEL 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1135-1331 |
6.43e-10 |
|
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: 58.61 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1135 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdicilsledlRTKLTVIPQdpvlfvgtvryn 1214
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFEQ------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1215 ldpfeshtdemlwqvlertfmrdtimklpeklqaevtengenFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTL 1294
Cdd:cd03221 71 ------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 89111135 1295 VQNTIKDaFKGcTVLTIAH-R--LNTVlnCDHVLVMENGK 1331
Cdd:cd03221 109 LEEALKE-YPG-TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
127-679 |
6.45e-10 |
|
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: 63.28 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 127 IVANILCIIMAAIGPVILIHQILQQTERTSGK----VWVGIGLCIALFATefTKVFFWALAWAINyRTAIRLKVALSTLV 202
Cdd:COG4615 15 LLLALLLGLLSGLANAGLIALINQALNATGAAlarlLLLFAGLLVLLLLS--RLASQLLLTRLGQ-HAVARLRLRLSRRI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 203 FEnlVSFKTLTHISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAY-------AFFILgpTALIGISVYVIFIP 275
Cdd:COG4615 92 LA--APLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYlawlsppLFLLT--LVLLGLGVAGYRLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 276 VQMFMA--------------------------KLNS----AFRRSAILVTDKRVQTMNefltcIRLIKMYAWEKSFTNTI 325
Cdd:COG4615 168 VRRARRhlrrareaedrlfkhfrallegfkelKLNRrrrrAFFDEDLQPTAERYRDLR-----IRADTIFALANNWGNLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 326 QdirrrerkllekagFVqsgnsALAPIVSTIAIVLTLSchillrrkLTAPVAFSVIAMFnvMKFSIAILPFSIKAMAEAN 405
Cdd:COG4615 243 F--------------FA-----LIGLILFLLPALGWAD--------PAVLSGFVLVLLF--LRGPLSQLVGALPTLSRAN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 406 VSLRRMKKIliDKSPPSYITQPEDpdtvlllanatltwEHEASRKSTPKKLQ-NQKRHlckkqrseAYsersPPAKGAT- 483
Cdd:COG4615 294 VALRKIEEL--ELALAAAEPAAAD--------------AAAPPAPADFQTLElRGVTY--------RY----PGEDGDEg 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 484 ---GPeeqsdslksvlhsISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL-------AYVSQQAWIF 553
Cdd:COG4615 346 ftlGP-------------IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPvtadnreAYRQLFSAVF 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 554 ---HgnvreniLFGEKYDHQRYQHTVRVcglQKDLSNLPYGDLTEIgERG----LNLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:COG4615 413 sdfH-------LFDRLLGLDGEADPARA---RELLERLELDHKVSV-EDGrfstTDLSQGQRKRLALLVALLEDRPILVF 481
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 627 D------DPlsavdahVGKHVF-EECI---KKtlRGKTVVLVTHQLQFLESCDEVILLEDGEI 679
Cdd:COG4615 482 DewaadqDP-------EFRRVFyTELLpelKA--RGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1136-1356 |
7.05e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.16 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEP----ASGTIFIDEVDICILSLEDLRT----KLTVIPQDPVlf 1207
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 vgTvryNLDPFesHT-----DEMLW---------------QVLERTFMRDtimklPEK-LQAEVTEngenFSVGERQLLC 1266
Cdd:COG4172 103 --T---SLNPL--HTigkqiAEVLRlhrglsgaaararalELLERVGIPD-----PERrLDAYPHQ----LSGGQRQRVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1267 VARALLRNSKIILLDEATasmdskT--DTLVQNTIKDAFK------GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDK 1337
Cdd:COG4172 167 IAMALANEPDLLIADEPT------TalDVTVQAQILDLLKdlqrelGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
250 260
....*....|....*....|
gi 89111135 1338 PEVLAEKPDSAFA-MLLAAE 1356
Cdd:COG4172 241 TAELFAAPQHPYTrKLLAAE 260
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
496-677 |
8.85e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-TLAYVSQQAWIFHG--------------NVREN 560
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGekydhqRYQHTVRVCglqkDLSNLPYGDLTEIGERGLN---------LSGGQRQRISLARAVYSDRQLYLLDDPLS 631
Cdd:PRK11288 100 LYLG------QLPHKGGIV----NRRLLNYEAREQLEHLGVDidpdtplkyLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 89111135 632 AVDAHVGKHVFEecIKKTLR--GKTVVLVTHQL-QFLESCDEVILLEDG 677
Cdd:PRK11288 170 SLSAREIEQLFR--VIRELRaeGRVILYVSHRMeEIFALCDAITVFKDG 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
495-688 |
9.55e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.04 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-----------LAYVSQQAWIF-HGNVRENIL 562
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFpHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FGekydhqryqhtVRVCGLQKDLSN------LPYGDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:PRK11432 101 YG-----------LKMLGVPKEERKqrvkeaLELVDLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 636 HvgkhvfeecIKKTLRGK----------TVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 688
Cdd:PRK11432 170 N---------LRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1120-1338 |
9.56e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.30 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPL---VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILS----LED 1192
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTKLTVIPQDPvlfvgtvrynldpfEShtdemlwQVLERTFMRDTIM---------KLPEKLQAE------VTE----- 1252
Cdd:PRK13649 83 IRKKVGLVFQFP--------------ES-------QLFEETVLKDVAFgpqnfgvsqEEAEALAREklalvgISEslfek 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1253 NGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTdtlvQNTIKDAFK-----GCTVLTIAHRLNTVLN-CDHVLV 1326
Cdd:PRK13649 142 NPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG----RKELMTLFKklhqsGMTIVLVTHLMDDVANyADFVYV 217
|
250
....*....|..
gi 89111135 1327 MENGKVIEFDKP 1338
Cdd:PRK13649 218 LEKGKLVLSGKP 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
495-694 |
1.02e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.28 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWIfhG------------NVRENIL 562
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRI--GylpeerglypkmKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 -FGEkydhqryqhtvrvcglqkdLSNLPYGDLT----------EIGERGL----NLSGGQRQRISLARAVYSDRQLYLLD 627
Cdd:COG4152 94 yLAR-------------------LKGLSKAEAKrradewlerlGLGDRANkkveELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 628 DPLSAVDAhVGKHVFEECIK-KTLRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGR 694
Cdd:COG4152 155 EPFSGLDP-VNVELLKDVIReLAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1136-1341 |
1.03e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIL-SLEDLRTKLTVIPQDPVLFVG-TVRY 1213
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1214 NLDPFESHTDEMLWQV-LERTFmrdtimKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 1292
Cdd:PRK11614 100 NLAMGGFFAERDQFQErIKWVY------ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1293 TLVQNTIKDAF-KGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVL 1341
Cdd:PRK11614 174 QQIFDTIEQLReQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1120-1337 |
1.24e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYrdNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRL--VEP---ASGTIFIDEVDICILSLE--D 1192
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRTDtvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTKLTVIPQDPVLFVGT----VRYNLDPFESHTDEMLWQVLERTFMRDTIMklpEKLQAEVTENGENFSVGERQLLCVA 1268
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSiyenVVYGLRLKGIKDKQVLDEAVEKSLKGASIW---DEVKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1269 RALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDK 1337
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
493-684 |
1.31e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL--AYVSQQAWIfhgnvrENILFGEKYDHQ 570
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYL------DTTLPLTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 571 RYQHTVRVCGLQKDLSNLPYGDLTEIGERglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHvGKHVFEECIKKTL 650
Cdd:PRK09544 91 RLRPGTKKEDILPALKRVQAGHLIDAPMQ--KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN-GQVALYDLIDQLR 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 89111135 651 R--GKTVVLVTHQLQF-LESCDEVILLeDGEICEKGT 684
Cdd:PRK09544 168 RelDCAVLMVSHDLHLvMAKTDEVLCL-NHHICCSGT 203
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
497-683 |
1.46e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 497 HSISFVVRKGKILGICGNVGSGKSSLLAALLGQmqLQKGVVAVNGTLAY--VSQQAWIFHGNVRENILFGEK-------- 566
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGI--LPAGVRQTAGRVLLdgKPVAPCALRGRKIATIMQNPRsafnplht 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 567 -YDHQRyqHTVRVCGLQKDLSNLPYGdLTEIG----ERGLNL-----SGGQRQRISLARAVYSDRQLYLLDDPLSAVDAH 636
Cdd:PRK10418 98 mHTHAR--ETCLALGKPADDATLTAA-LEAVGlenaARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 89111135 637 VGKHVFE--ECIKKTlRGKTVVLVTHQLQFLESC-DEVILLEDGEICEKG 683
Cdd:PRK10418 175 AQARILDllESIVQK-RALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQG 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
496-689 |
1.53e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQ----QAWIFHGNV 557
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevvtrspqdglangIVYISEdrkrDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENI---------LFGEKYDHQRYQHTVrvcGLQKDLSNL--PYGDLTeIGerglNLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:PRK10762 348 KENMsltalryfsRAGGSLKHADEQQAV---SDFIRLFNIktPSMEQA-IG----LLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 627 DDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQL-QFLESCDEVILLEDGEIC-----EKGTHKELM 689
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMpEVLGMSDRILVMHEGRISgeftrEQATQEKLM 488
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1118-1338 |
1.67e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1118 GEITFRDYQMRYRDNTPL---VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIC-----ILS 1189
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1190 LEDLRTKLTVIPQDP--VLFVGTVRYNLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLqaeVTENGENFSVGERQLLCV 1267
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 1268 ARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP 1338
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
493-688 |
1.75e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.20 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT---------------LAYVSQQAWIFHGNV 557
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENILFG-------EKYDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:PRK13652 97 EQDIAFGpinlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 631 SAVDAHVGKHV--FEECIKKTLrGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKEL 688
Cdd:PRK13652 166 AGLDPQGVKELidFLNDLPETY-GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
498-691 |
1.81e-09 |
|
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: 61.74 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 498 SISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAV--------------------NGTLAYVSQQAWIF-HGN 556
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgrgraKRYIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENIL------FGEKYDHQRYQHTVRVCGLQKD-----LSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQLYL 625
Cdd:TIGR03269 382 VLDNLTeaigleLPDELARMKAVITLKMVGFDEEkaeeiLDKYPD-----------ELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 626 LDDPLSAVDAHVGKHVFEECIKKTLR-GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFvLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
493-662 |
1.94e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALlGQMQLQKGVVAVNGTLAYVSQQAWIFHGNV------------REN 560
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqvsmvhpKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGEKYDHQRYqhTVRVCGLQKDL-------SNLPYGDL-----TEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDD 628
Cdd:PRK14258 99 LFPMSVYDNVAY--GVKIVGWRPKLeiddiveSALKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190
....*....|....*....|....*....|....*
gi 89111135 629 PLSAVDAHVGKHVFEECIKKTLRGK-TVVLVTHQL 662
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNL 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
554-688 |
2.54e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 554 HGNVRENILFGEKYD-------HQRYQHTVRVCGLQKDLSNLPYGdlteigerglnLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:PRK11000 89 HLSVAENMSFGLKLAgakkeeiNQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLL 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 627 DDPLSAVDAHVGKHVFEECIK--KTLrGKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKEL 688
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRlhKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
489-688 |
2.71e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 489 SDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLaYVSQQAWifhgNVRENI-LFGEKY 567
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVW----DIRHKIgMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 568 DHQRYQHTVR---VCGLQKdlSNLPYGDLTEIGERGLN--------------LSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:PRK13650 91 DNQFVGATVEddvAFGLEN--KGIPHEEMKERVNEALElvgmqdfkereparLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 631 SAVDAHvGKHVFEECIKKTLR--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL 688
Cdd:PRK13650 169 SMLDPE-GRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1129-1338 |
2.93e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1129 YRDNTP---LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIC----------------ILS 1189
Cdd:PRK13631 31 FDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdkknnhelitnpyskkIKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1190 LEDLRTKLTVIPQDP--VLFVGTVR-------YNLDPFESHTDEMLWQVLERTFMRDTIMKlpeklqaevtENGENFSVG 1260
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEkdimfgpVALGVKKSEAKKLAKFYLNKMGLDDSYLE----------RSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1261 ERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK-GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKP 1338
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
857-1006 |
3.36e-09 |
|
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: 59.83 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 857 ASMVFMLVFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFM 936
Cdd:cd18563 51 GAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILM 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 937 VVFILVI---------LAAVFPAVLLVVASLAVGFFIlLRIFHRGVQELKKVENVsrspwfthITSSMQGLGIIHAYGK 1006
Cdd:cd18563 131 IIGIGVVlfslnwklaLLVLIPVPLVVWGSYFFWKKI-RRLFHRQWRRWSRLNSV--------LNDTLPGIRVVKAFGQ 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
496-678 |
3.61e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLG----------------QMQL-------QKGVVAVNGTLAYVSQQAwi 552
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifegeELQAsnirdteRAGIAIIHQELALVKELS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 553 fhgnVRENILFGEK--------YD--HQRYQHTVRvcGLQKDLS-NLPYGdlteigerglNLSGGQRQRISLARAVYSDR 621
Cdd:PRK13549 99 ----VLENIFLGNEitpggimdYDamYLRAQKLLA--QLKLDINpATPVG----------NLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 622 QLYLLDDPLSAVDAHVGKHVFEecIKKTLR--GKTVVLVTHQL-QFLESCDEVILLEDGE 678
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLD--IIRDLKahGIACIYISHKLnEVKAISDTICVIRDGR 220
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
853-1044 |
3.66e-09 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 59.71 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 853 WVYTASMVFMLVFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELdvrlpfhAE---- 928
Cdd:cd18544 45 LLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL-------NElfts 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 929 ---NFLQQFFMVVFILVI-------LAAVFPAVLLVVASLAVGFFILLRIFHRGVQELkkvenVSRSPwfTHITSSMQGL 998
Cdd:cd18544 118 glvTLIGDLLLLIGILIAmfllnwrLALISLLVLPLLLLATYLFRKKSRKAYREVREK-----LSRLN--AFLQESISGM 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 999 GIIHAYGKKESCITY-------HLLYFNCALRWFALRMDVLMNILTFTVALLV 1044
Cdd:cd18544 191 SVIQLFNREKREFEEfdeinqeYRKANLKSIKLFALFRPLVELLSSLALALVL 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1136-1344 |
3.84e-09 |
|
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: 60.97 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLV---EPASGTIfIDEVDICilsledlrTKLTVIpqDPVLFVGT-- 1210
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMdqyEPTSGRI-IYHVALC--------EKCGYV--ERPSKVGEpc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1211 --VRYNLDPFESHtdemLWQ---------------VLERTF-------MRDTIMK-LPE-------------------KL 1246
Cdd:TIGR03269 83 pvCGGTLEPEEVD----FWNlsdklrrrirkriaiMLQRTFalygddtVLDNVLEaLEEigyegkeavgravdliemvQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1247 QAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDH 1323
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDK 238
|
250 260
....*....|....*....|.
gi 89111135 1324 VLVMENGKVIEFDKPEVLAEK 1344
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAV 259
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
127-410 |
3.92e-09 |
|
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: 59.49 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 127 IVANILC-IIMAAIGPV------ILIHQILQQTERTSGKVWVGIGLCIALFATeftkVFFWALAWaINYRTAIRLKVALS 199
Cdd:cd07346 1 LLLALLLlLLATALGLAlplltkLLIDDVIPAGDLSLLLWIALLLLLLALLRA----LLSYLRRY-LAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 200 TLVFENL--VSFKTLTHISVGEVLNILSSDSYSLFEAALFCPLPATIPILMVFCAAYAFFILGPT-ALIGISVYVIFIPV 276
Cdd:cd07346 76 RDLFRHLqrLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKlTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 277 -QMFMAKLNSAFRRSAILVtDKRVQTMNEFLTCIRLIKMYAWEKSFTNTIQDIRRRERKLLEKAGFVQSGNSALAPIVST 355
Cdd:cd07346 156 lRYFRRRIRKASREVRESL-AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 356 I--AIVLTLSCHILLRRKLTAPVAFSVIAMFNVMKFSIAILPFSIKAMAEANVSLRR 410
Cdd:cd07346 235 LgtALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
496-678 |
4.18e-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: 60.61 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLG----------------QMQLQ-------KGVVAVNGTLAYVSQQAwi 552
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgsPLKASnirdterAGIVIIHQELTLVPELS-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 553 fhgnVRENILFGEKYDHQ-----------RYQHTVRVCGLQKDLSNLPYGDlteigerglnLSGGQRQRISLARAVYSDR 621
Cdd:TIGR02633 95 ----VAENIFLGNEITLPggrmaynamylRAKNLLRELQLDADNVTRPVGD----------YGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 622 QLYLLDDPLSAVDAHVGKHVFEecIKKTLRGKTV--VLVTHQLQFLES-CDEVILLEDGE 678
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
493-691 |
4.24e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.75 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQQAWIFHG-NV 557
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENIL--FGEKYDHQRYQHTVRVCGLQKDLSNLPYGDlteigERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:PRK10895 96 YDNLMavLQIRDDLSAEQREDRANELMEEFHIEHLRD-----SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 636 hvgKHVFEecIKKTL-----RGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:PRK10895 171 ---ISVID--IKRIIehlrdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1136-1346 |
4.49e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTifidevdicilsledlrtkltvIPQDPVLFVGTVrynl 1215
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV----------------------IKRNGKLRIGYV---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1216 dPFESHTDEMLWQVLERtFMR-------DTIMKLPEKLQAE--VTENGENFSVGERQLLCVARALLRNSKIILLDEATAS 1286
Cdd:PRK09544 73 -PQKLYLDTTLPLTVNR-FLRlrpgtkkEDILPALKRVQAGhlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1287 MDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVL-NCDHVLVMeNGKVIEFDKPEVLAEKPD 1346
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1143-1347 |
4.67e-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: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1143 NIQSGQTVGIVGRTGSGKSSLGMALFRLVEPasgtifiDEVDIcILSLEDLRTKLTVIPQDpvlFVGTVRYNLdpfESHT 1222
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKP-------DEGDI-EIELDTVSYKPQYIKAD---YEGTVRDLL---SSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1223 DEMLwqvlERTFMRDTIMKlPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDa 1302
Cdd:cd03237 87 KDFY----THPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1303 fkgctvlTIAHRLNTVLNCDHVLVMEN---GKVIEFD-KPEV--LAEKPDS 1347
Cdd:cd03237 161 -------FAENNEKTAFVVEHDIIMIDylaDRLIVFEgEPSVngVANPPQS 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1137-1333 |
6.26e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFI-------------DEVDICILSLEdlrtkLTVIPQD 1203
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpkssQEAGIGIIHQE-----LNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1204 PV---LFVGTvrynldPFESHTDEMLWQVlertfMRDTIMKLPEKLQAEVTEN---GEnFSVGERQLLCVARALLRNSKI 1277
Cdd:PRK10762 95 TIaenIFLGR------EFVNRFGRIDWKK-----MYAEADKLLARLNLRFSSDklvGE-LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1278 ILLDEAT-ASMDSKTDTL--VQNTIKDafKGCTVLTIAHRLNTVLN-CDHVLVMENGKVI 1333
Cdd:PRK10762 163 IIMDEPTdALTDTETESLfrVIRELKS--QGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
496-693 |
6.29e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.41 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGqMQLQKGVVAVNGTL-------------AYVSQQAwifhgnvreNIL 562
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawsaaelarhrAYLSQQQ---------TPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FGEKYDH--QRYQHT-VRVCGLQKDLSNLPYG-DLTEIGERGLN-LSGGQRQRISLA-------RAVYSDRQLYLLDDPL 630
Cdd:PRK03695 82 FAMPVFQylTLHQPDkTRTEAVASALNEVAEAlGLDDKLGRSVNqLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 631 SAVDahVGKHVFEECIKKTL--RGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEERG 693
Cdd:PRK03695 162 NSLD--VAQQAALDRLLSELcqQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
495-661 |
6.70e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT------LAYVSQQAWIFHGN-------VRENI 561
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVGHRSginpyltLRENC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 LFGEKYDHQRYQHT--VRVCGLQKdLSNLPYGdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGK 639
Cdd:PRK13540 96 LYDIHFSPGAVGITelCRLFSLEH-LIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 89111135 640 HVFEECIKKTLRGKTVVLVTHQ 661
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1140-1359 |
6.88e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1140 LNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDE----------VDICILSLEDLR----TKLTVIPQD-- 1203
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIFQEpm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1204 ----PVLFVG-----TVRynLDPFESHTDEMlwqvLERTFMRDTImKLPEKlQAEVTENGENFSVGERQLLCVARALLRN 1274
Cdd:PRK10261 115 tslnPVFTVGeqiaeSIR--LHQGASREEAM----VEAKRMLDQV-RIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1275 SKIILLDEATASMDSKTDTLVQNTIKDAFKGCT--VLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDSAFAM 1351
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
....*....
gi 89111135 1352 -LLAAEVRL 1359
Cdd:PRK10261 267 aLLAAVPQL 275
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1136-1333 |
7.60e-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: 57.73 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI-------------FIDEVDICILSLEDLRTKLTVIpq 1202
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkrrkkFLRRIGVVFGQKTQLWWDLPVI-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1203 DPVLFVGTVrYNLDPFEshtdemlwqvlertfMRDTIMKLPE--KLQAEVTENGENFSVGERQLLCVARALLRNSKIILL 1280
Cdd:cd03267 114 DSFYLLAAI-YDLPPAR---------------FKKRLDELSEllDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1281 DEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVI 1333
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
486-691 |
8.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.56 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 486 EEQSDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAW--------IFHGN- 556
Cdd:PRK13633 16 SNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmVFQNPd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 -------VRENILFG-------EKYDHQRYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQ 622
Cdd:PRK13633 96 nqivatiVEEDVAFGpenlgipPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 623 LYLLDDPLSAVDAHVGKHVFEEcIKKTLR--GKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNT-IKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
486-720 |
1.19e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.80 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 486 EEQSDSlkSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTlAYVSQQAWifhgNVRENI-LFG 564
Cdd:PRK13642 15 EKESDV--NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVW----NLRRKIgMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 EKYDHQRYQHTVR---VCGLQKdlSNLPYGDLTEIGERGL--------------NLSGGQRQRISLARAVYSDRQLYLLD 627
Cdd:PRK13642 88 QNPDNQFVGATVEddvAFGMEN--QGIPREEMIKRVDEALlavnmldfktrepaRLSGGQKQRVAVAGIIALRPEIIILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 628 DPLSAVDAhVGKHVFEECIKKtLRGK---TVVLVTHQLQFLESCDEVILLEDGEICEKGTHKEL------MEERGR---- 694
Cdd:PRK13642 166 ESTSMLDP-TGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELfatsedMVEIGLdvpf 243
|
250 260
....*....|....*....|....*..
gi 89111135 695 YAKLIHNLRGLQFKDPE-HLYNAAMVE 720
Cdd:PRK13642 244 SSNLMKDLRKNGFDLPEkYLSEDELVE 270
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
854-964 |
1.26e-08 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 58.18 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 854 VYTASMVFMLVFGvtkgFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDvrlpfhaeNFLQQ 933
Cdd:cd18547 54 LYLLSALFSYLQN----RLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNIS--------QALSQ 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 89111135 934 --------FFMVVFILVI-------LAAVfpAVLLVVASLAVGFFI 964
Cdd:cd18547 122 sltqlissILTIVGTLIMmlyisplLTLI--VLVTVPLSLLVTKFI 165
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1136-1340 |
1.35e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLED-LRTKLTVIPQD-------PVLf 1207
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPEDrkgeglvLDL- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 vgTVRYN-----LDPFESHTdeMLWQVLERTFMRDTIMKL---PEKLQAEVTengeNFSVGERQLLCVARALLRNSKIIL 1279
Cdd:COG1129 346 --SIRENitlasLDRLSRGG--LLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1280 LDEATASMD--SKTDtlVQNTIKD-AFKGCTVLTIAHRLNTVL-NCDHVLVMENGKVI-EFDKPEV 1340
Cdd:COG1129 418 LDEPTRGIDvgAKAE--IYRLIRElAAEGKAVIVISSELPELLgLSDRILVMREGRIVgELDREEA 481
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
493-695 |
1.55e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAAL-----------------LGQMQL--QKGVVAVNGTLAYVSQQAWIF 553
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvsgyrysgdvlLGGRSIfnYRDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 554 HGNVRENILFGekydhqryqhtVRVCGL--QKDLSNLPYGDLTEIG----------ERGLNLSGGQRQRISLARAVYSDR 621
Cdd:PRK14271 114 PMSIMDNVLAG-----------VRAHKLvpRKEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 622 QLYLLDDPLSAVDAHVGKHVfEECIKKTLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELME-----ERGRY 695
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSspkhaETARY 261
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1137-1332 |
1.56e-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: 59.64 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICIlSLEDLRTKLTVIPQDPVLFVGTVRYNLD 1216
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1217 PFESHTDEMLW---QVLERTFMRDTimklpeKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDT 1293
Cdd:TIGR01257 1025 LFYAQLKGRSWeeaQLEMEAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 89111135 1294 LVQNTIKDAFKGCTVLTIAHRLNTV-LNCDHVLVMENGKV 1332
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRL 1138
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
498-689 |
1.65e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 498 SISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVN------GTLAYVSQQA-WIFHG-----NVRENI---- 561
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRIrMIFQDpstslNPRQRIsqil 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 562 ---------LFGEKYDHQRYQhTVRVCGLQKDLSN-LPYGdlteigerglnLSGGQRQRISLARAVYSDRQLYLLDDPLS 631
Cdd:PRK15112 111 dfplrlntdLEPEQREKQIIE-TLRQVGLLPDHASyYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 89111135 632 AVDAHVGKHVFE---ECIKKtlRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELM 689
Cdd:PRK15112 179 SLDMSMRSQLINlmlELQEK--QGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1115-1314 |
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: 58.99 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1115 PSRGEITFRDYQMRYrDNTPLV-------LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdici 1187
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA----- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1188 lsledlRTKLTVIPQDPVLFVGTVR----YNLDPFE----SHTDEMLWQVLErtfmrdtIMKLPEKLQAE-----VTENG 1254
Cdd:TIGR00954 514 ------KGKLFYVPQRPYMTLGTLRdqiiYPDSSEDmkrrGLSDKDLEQILD-------NVQLTHILEREggwsaVQDWM 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1255 ENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAfkGCTVLTIAHR 1314
Cdd:TIGR00954 581 DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
494-688 |
2.28e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.01 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 494 SVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWIfhgNVREN--ILFgEKYDHQR 571
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLL---EVRKTvgIVF-QNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 572 YQHTVRV--------CGLQKD-LSNLPYGDLTEIGERGL------NLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAH 636
Cdd:PRK13639 92 FAPTVEEdvafgplnLGLSKEeVEKRVKEALKAVGMEGFenkpphHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 637 VGKHVFEECIKKTLRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKEL 688
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
496-677 |
2.89e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------LAY------VSQQ-AWIFHGNVREN 560
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhkLAAqlgigiIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFGE--------------KYDHQRYQHTVRVCGLQKDLSnlpygdlteigERGLNLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:PRK09700 101 LYIGRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 89111135 627 DDPLSAVDAHVGKHVFeeCIKKTLR--GKTVVLVTHQL-QFLESCDEVILLEDG 677
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF--LIMNQLRkeGTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
495-689 |
2.90e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.76 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQM---QLQKGV-----VAVNG----------------TLAYVSQQA 550
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGArvtgdVTLNGeplaaidaprlarlraVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 551 WIFhgNVRENILFGekydhqRYQHTVRVCGLQKDLSNLPYGDLTEIGERGL------NLSGGQRQRISLARAV------- 617
Cdd:PRK13547 96 FAF--SAREIVLLG------RYPHARRAGALTHRDGEIAWQALALAGATALvgrdvtTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 618 --YSDRQLYLLDDPLSAVD-AHvgKHVFEECIKKTLR--GKTVVLVTHQLQF-LESCDEVILLEDGEICEKGTHKELM 689
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDlAH--QHRLLDTVRRLARdwNLGVLAIVHDPNLaARHADRIAMLADGAIVAHGAPADVL 243
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1141-1288 |
3.22e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.74 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1141 NLNIQSGQTVGIVGRTGSGKSSLG--MALFrlVEPASGTIFIDEVDicilsledlrTKLTVIPQDPV--------LFVG- 1209
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLnlIAGF--LTPASGSLTLNGQD----------HTTTPPSRRPVsmlfqennLFSHl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1210 TVRYN----LDP---FESHTDEMLWQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARALLRNSKIILLDE 1282
Cdd:PRK10771 87 TVAQNiglgLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDE 155
|
....*.
gi 89111135 1283 ATASMD 1288
Cdd:PRK10771 156 PFSALD 161
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
495-690 |
3.31e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.16 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL-----------AYVSQQ-AWIFHGNVRENIL 562
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVvnelepadrdiAMVFQNyALYPHMSVRENMA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 563 FGEKY-----DH--QRYQHTVRVCGLQKDLSNLPygdlteigeRglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:PRK11650 99 YGLKIrgmpkAEieERVAEAARILELEPLLDRKP---------R--ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 636 HVGKHVFEEcIKKTLR--GKTVVLVTH-QLQFLESCDEVILLEDGEICEKGTHKELME 690
Cdd:PRK11650 168 KLRVQMRLE-IQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYE 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
493-691 |
3.73e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.59 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGtLAYVSQQAWIFHGNVRENILFgeKY-DHQR 571
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG-VDITDKKVKLSDIRKKVGLVF--QYpEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 572 YQHTVrvcglQKDL----SNLPYGDlTEIGER--------GLN-----------LSGGQRQRISLARAVYSDRQLYLLDD 628
Cdd:PRK13637 97 FEETI-----EKDIafgpINLGLSE-EEIENRvkramnivGLDyedykdkspfeLSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 629 PLSAVDAHVGKHVFEECikKTLRGK---TVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 691
Cdd:PRK13637 171 PTAGLDPKGRDEILNKI--KELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
841-978 |
4.07e-08 |
|
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: 56.41 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 841 AVLADIGQHVYQWvytASMVFMLVFGVTKGFVFTKTTLMA------SSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSK 914
Cdd:cd18557 25 TIIKGGDLDVLNE---LALILLAIYLLQSVFTFVRYYLFNiageriVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSS 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 915 DMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKK 978
Cdd:cd18557 102 DTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSK 165
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
602-690 |
4.16e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.00 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 602 NLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVGKHVFEECIKKTLRGKTVVLVTHQ-LQFLESCDEVILLEDGEIC 680
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
90
....*....|
gi 89111135 681 EKGTHKELME 690
Cdd:PRK14267 228 EVGPTRKVFE 237
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
495-691 |
4.46e-08 |
|
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: 56.60 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLG---QMQLQKGVVAVNGT-LAYVSQQAW----------IFHG----- 555
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEdLLKLSEKELrkirgreiqmIFQDpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 N--------VRENILFGEKYDH-QRYQHTVRV---CGL---QKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSD 620
Cdd:COG0444 100 NpvmtvgdqIAEPLRIHGGLSKaEARERAIELlerVGLpdpERRLDRYPH-----------ELSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 621 RQLYLLDDPLSAVDAHVGKHV---FEEcIKKTlRGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELMEE 691
Cdd:COG0444 169 PKLLIADEPTTALDVTIQAQIlnlLKD-LQRE-LGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
476-659 |
4.62e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 476 SPPAKGATGPEEQSDSlKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQ----AW 551
Cdd:PRK13543 8 APPLLAAHALAFSRNE-EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRsrfmAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 552 IFHgnvreniLFGEKYDHQRYQHTVRVCGLQ-KDLSNLPYGDLTEIGERGL------NLSGGQRQRISLARAVYSDRQLY 624
Cdd:PRK13543 87 LGH-------LPGLKADLSTLENLHFLCGLHgRRAKQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLW 159
|
170 180 190
....*....|....*....|....*....|....*
gi 89111135 625 LLDDPLSAVDAHvGKHVFEECIKKTLRGKTVVLVT 659
Cdd:PRK13543 160 LLDEPYANLDLE-GITLVNRMISAHLRGGGAALVT 193
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
495-677 |
4.88e-08 |
|
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: 55.13 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVN---------------------GTLAYVSQqawif 553
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIGYVSQ----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 554 hgnvrenilfgekydhqrYQHTV-RVCGLqkDLSNLPygdLTEIGE-------------RGLNL------------SGGQ 607
Cdd:COG4778 101 ------------------FLRVIpRVSAL--DVVAEP---LLERGVdreearararellARLNLperlwdlppatfSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 608 RQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLES-CDEVILLEDG 677
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
495-692 |
5.53e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.25 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSL---LAALL----GQMQ-----------------------LQ-------KGVV 537
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtGTIEwifkdeknkkktkekekvleklvIQktrfkkiKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 538 AVNGTLAYVSQQA--WIFHGNVRENILFG-------EKYDHQRYQHTVRVCGLQKD-LSNLPYgdlteigerglNLSGGQ 607
Cdd:PRK13651 102 EIRRRVGVVFQFAeyQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGLDESyLQRSPF-----------ELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 608 RQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKG-TH 685
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGdTY 250
|
....*..
gi 89111135 686 KELMEER 692
Cdd:PRK13651 251 DILSDNK 257
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1135-1299 |
5.60e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.88 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1135 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIcilSLEDLRTKLTVI-PQD---PVLfvgT 1210
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLgHRNamkPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1211 VRYNLDpfeshtdemLWqvleRTFMRDTIMKLPEKLQA----EVTE-NGENFSVGERQLLCVARALLRNSKIILLDEATA 1285
Cdd:PRK13539 90 VAENLE---------FW----AAFLGGEELDIAAALEAvglaPLAHlPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....
gi 89111135 1286 SMDSKTDTLVQNTI 1299
Cdd:PRK13539 157 ALDAAAVALFAELI 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
503-678 |
5.78e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 503 VRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQqaWI---FHGNVRENILF-GEKYDHQRYQHTVrV 578
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIkpdYDGTVEDLLRSiTDDLGSSYYKSEI-I 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 579 CGLQkdlsnlpygdLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVD-------AHVGKHVFEEcikktl 650
Cdd:PRK13409 439 KPLQ----------LERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE------ 502
|
170 180
....*....|....*....|....*...
gi 89111135 651 RGKTVVLVTHQLQFLESCDEVILLEDGE 678
Cdd:PRK13409 503 REATALVVDHDIYMIDYISDRLMVFEGE 530
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
505-665 |
5.98e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 505 KGKILGICGNVGSGKSSLLAALLGQMQLQ-KGVVAVNGTLAYVSQQAWIFHgnvrenilfgekydhqryqhtvrvcglqk 583
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 584 dlsnlpygdlTEIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEEC------IKKTLRGKTVVL 657
Cdd:smart00382 52 ----------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllLLKSEKNLTVIL 121
|
....*...
gi 89111135 658 VTHQLQFL 665
Cdd:smart00382 122 TTNDEKDL 129
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
496-672 |
7.37e-08 |
|
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: 53.87 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLgqmqlqkgvvAVNGTLAYVSqqawifhgnvrenilFGEKYDHQRyqhT 575
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----------YASGKARLIS---------------FLPKFSRNK---L 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 576 VRVCGLQKdLSNLPYGDLTeIGERGLNLSGGQRQRISLARAVYSD--RQLYLLDDPLSAVDaHVGKHVFEECIKKTL-RG 652
Cdd:cd03238 63 IFIDQLQF-LIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLH-QQDINQLLEVIKGLIdLG 139
|
170 180
....*....|....*....|
gi 89111135 653 KTVVLVTHQLQFLESCDEVI 672
Cdd:cd03238 140 NTVILIEHNLDVLSSADWII 159
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1120-1333 |
8.10e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRdNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIdevdICILSLEDLRTKLTV 1199
Cdd:PRK15056 7 IVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 -IPQD-------PVLFVGTV---RYN----LDPFESHTDEMLWQVLERTFMrdtimklpekLQAEVTENGEnFSVGERQL 1264
Cdd:PRK15056 82 yVPQSeevdwsfPVLVEDVVmmgRYGhmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1265 LCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAF-KGCTVLTIAHRLNTVLN-CDHVlVMENGKVI 1333
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEfCDYT-VMVKGTVL 220
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
796-1005 |
8.64e-08 |
|
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: 55.51 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 796 LFTVFLFLLMIGSAAFSNWWLGLWLDKGsrmtcGPQGNRTMcevgavladigqhvyqwVYTASMVFMLVFGVTKGFVFTK 875
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDI-----FVEKDLEA-----------------LLLVPLAIIGLFLLRGLASYLQ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 876 TTLMASSSLH------DTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVIL----- 944
Cdd:cd18552 60 TYLMAYVGQRvvrdlrNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLfyldw 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 945 ------AAVFPAVLLVVASLAvgffILLRIFHRGVQElkKVENVSrspwfTHITSSMQGLGIIHAYG 1005
Cdd:cd18552 140 kltliaLVVLPLAALPIRRIG----KRLRKISRRSQE--SMGDLT-----SVLQETLSGIRVVKAFG 195
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
485-721 |
9.14e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.48 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 485 PEEQSDSLKSVlHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-LAYVSQQAW---------IFH 554
Cdd:PRK15079 27 FWQPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWravrsdiqmIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 555 G-----NVRENI---------LFGEKYDHQRYQHTVRV----CGLQKDLSN-LPYgdlteigerglNLSGGQRQRISLAR 615
Cdd:PRK15079 106 DplaslNPRMTIgeiiaeplrTYHPKLSRQEVKDRVKAmmlkVGLLPNLINrYPH-----------EFSGGQCQRIGIAR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 616 AVYSDRQLYLLDDPLSAVDAHVGKHVFeECIKKTLR--GKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELmeer 692
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSIQAQVV-NLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV---- 249
|
250 260
....*....|....*....|....*....
gi 89111135 693 gryaklihnlrglqFKDPEHLYNAAMVEA 721
Cdd:PRK15079 250 --------------YHNPLHPYTKALMSA 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
499-692 |
1.02e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-TLAYVSQQAWIFHG-----------------NVREN 560
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkPIDIRSPRDAIRAGimlcpedrkaegiipvhSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 I---------LFG-------EKYDHQRYQHTVRVcglqkdlsNLPYGDlTEIGerglNLSGGQRQRISLARAVYSDRQLY 624
Cdd:PRK11288 352 InisarrhhlRAGclinnrwEAENADRFIRSLNI--------KTPSRE-QLIM----NLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 625 LLDDPLSAVDahVG-KHVFEECIKK-TLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 692
Cdd:PRK11288 419 LLDEPTRGID--VGaKHEIYNVIYElAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQATERQ 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
495-679 |
1.07e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQQAWIFHG-NVRE 559
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFG---EKYDHQRYQHTVRVCGLQKDLSnLPYGDLtEIGErglnlsggqRQRISLARAVYSDRQLYLLDDPLSAVDAH 636
Cdd:PRK15439 106 NILFGlpkRQASMQKMKQLLAALGCQLDLD-SSAGSL-EVAD---------RQIVEILRGLMRDSRILILDEPTASLTPA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 89111135 637 VGKHVFEEcIKKTL-RGKTVVLVTHQL-QFLESCDEVILLEDGEI 679
Cdd:PRK15439 175 ETERLFSR-IRELLaQGVGIVFISHKLpEIRQLADRISVMRDGTI 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1120-1346 |
1.31e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 54.46 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE-----PASGTIFIDEVDICILSLE--D 1192
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTKLTVIPQDPVLF----------VGTVRYNLDPFESHTDEMLWQVLERTfmrdtimKLPEKLQAEVTENGENFSVGER 1262
Cdd:PRK14267 83 VRREVGMVFQYPNPFphltiydnvaIGVKLNGLVKSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1263 QLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFKGCTVLTIAHR-LNTVLNCDHVLVMENGKVIEFDKPEVL 1341
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
....*
gi 89111135 1342 AEKPD 1346
Cdd:PRK14267 236 FENPE 240
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
493-706 |
1.37e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.61 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG--TLAYVSQQAWIFHGNVREN------ILFG 564
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehIQHYASKEVARRIGLLAQNattpgdITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 565 EKYDHQRYQHTVRVCGLQKD-----LSNLPYGDLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhvg 638
Cdd:PRK10253 100 ELVARGRYPHQPLFTRWRKEdeeavTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI--- 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 639 KHVFE--ECIKKTLR--GKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEergryAKLIHNLRGLQ 706
Cdd:PRK10253 177 SHQIDllELLSELNRekGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT-----AELIERIYGLR 244
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
493-679 |
1.51e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG--TLAYVSQQAWIFHgnvrenilfgeKYDHQ 570
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQHQLEFL-----------RADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 571 RYQHTVRVCGLQKDLSNLPY-------GD-LTEIGERglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVF 642
Cdd:PRK10636 394 PLQHLARLAPQELEQKLRDYlggfgfqGDkVTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 89111135 643 EECIKktLRGKTVVlVTHQLQFLES-CDEVILLEDGEI 679
Cdd:PRK10636 471 EALID--FEGALVV-VSHDRHLLRStTDDLYLVHDGKV 505
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
499-741 |
1.77e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVA----VNGT-LAYVSQQ----------AWIFHG-------- 555
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAekleFNGQdLQRISEKerrnlvgaevAMIFQDpmtslnpc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 -NVRENILFGEKYdHQ------RYQHTVRVCGL------QKDLSNLPYgdlteigerglNLSGGQRQRISLARAVYSDRQ 622
Cdd:PRK11022 106 yTVGFQIMEAIKV-HQggnkktRRQRAIDLLNQvgipdpASRLDVYPH-----------QLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 623 LYLLDDPLSAVDAHVGKHVFEECIkkTLRGK---TVVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELmeergryakl 698
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLL--ELQQKenmALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI---------- 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 89111135 699 ihnlrglqFKDPEHLYNAAMVEAFKESPAEREEDAGIIVLAPG 741
Cdd:PRK11022 242 --------FRAPRHPYTQALLRALPEFAQDKARLASLPGVVPG 276
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1137-1332 |
1.83e-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: 55.60 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPA-SGTIFIDEVDICILS-LEDLRTKLTVIPQD-------PVLF 1207
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 VGTvRYNLDPFESHTDEM-LWQVLERTFMRDTIMKLPEKLQAEVTENGeNFSVGERQLLCVARALLRNSKIILLDEATAS 1286
Cdd:TIGR02633 356 VGK-NITLSVLKSFCFKMrIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 89111135 1287 MDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKV 1332
Cdd:TIGR02633 434 VDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1135-1346 |
2.24e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 53.63 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1135 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFR---LVEP--ASGTIFIDEVDICILSLE--DLRTKLTVIPQDPVLF 1207
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 VGTVRYNL------DPFESHTDEMLWQVLERTFMRDTImklPEKLQaevtENGENFSVGERQLLCVARALLRNSKIILLD 1281
Cdd:PRK14243 104 PKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEV---KDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 1282 EATASMDSKTDTLVQNTIKDAFKGCTVLTIAHRL-------------NTVLNCDHVlvmENGKVIEFDKPEVLAEKPD 1346
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqqaarvsdmtaffNVELTEGGG---RYGYLVEFDRTEKIFNSPQ 251
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
839-966 |
2.53e-07 |
|
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: 54.09 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 839 VGAVLADIGQHVYqwvyTASMVFMLVFGVT-------KGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNR 911
Cdd:cd18572 23 IDAVVADGSREAF----YRAVLLLLLLSVLsglfsglRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSR 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 912 FSKDMDELDVRLPFHAENFLQQFFMVVFILVILAAVFPaVLLVVASLAVGFFILL 966
Cdd:cd18572 99 LTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSW-RLTLLAFITVPVIALI 152
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
496-697 |
2.56e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVSQQAWIfHGNVR--ENI-LFGekydhqry 572
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGL-NGQLTgiENIeLKG-------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 573 qhtvRVCGLQKDLSNLPYGDLTEIGERG-------LNLSGGQRQRISLARAVYSDRQLYLLDDPLSavdahVGKHVF-EE 644
Cdd:PRK13545 111 ----LMMGLTKEKIKEIIPEIIEFADIGkfiyqpvKTYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQTFtKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 645 CIKK----TLRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERGRYAK 697
Cdd:PRK13545 182 CLDKmnefKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
505-676 |
3.46e-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: 55.40 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 505 KGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG------------TLAYVSQQAWIFHG-NVRENILF-----GEK 566
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILFHHlTVAEHILFyaqlkGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 567 YDHQRYQHTVRV--CGLQKDLSnlpygdlteigERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEE 644
Cdd:TIGR01257 1035 WEEAQLEMEAMLedTGLHHKRN-----------EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|..
gi 89111135 645 CIKKTlRGKTVVLVTHQLqflescDEVILLED 676
Cdd:TIGR01257 1104 LLKYR-SGRTIIMSTHHM------DEADLLGD 1128
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
499-692 |
3.78e-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: 54.45 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQ-KGVVAVNG-TLAYVSQQAWIFHGNVreniLFGEkyDHQRyQHTV 576
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkPVDIRNPAQAIRAGIA----MVPE--DRKR-HGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 577 RVCGLQKD--LSNL-PYGDLTEIGE--------RGLN---------------LSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:TIGR02633 352 PILGVGKNitLSVLkSFCFKMRIDAaaelqiigSAIQrlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 631 SAVDAHVGKHVFEECIKKTLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 692
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1120-1349 |
3.98e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.80 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTplVLDSLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIFIDEVDICILSLEDlRT 1195
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIagfeTPDSGRIMLDGQDITHVPAEN-RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 KLTVIpQDPVLFVG-TVRYNL-----------DPFESHTDEMLWQV-LErtfmrDTIMKLPEKLqaevtengenfSVGER 1262
Cdd:PRK09452 88 VNTVF-QSYALFPHmTVFENVafglrmqktpaAEITPRVMEALRMVqLE-----EFAQRKPHQL-----------SGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1263 QLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPE 1339
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDQEEALTmSDRIVVMRDGRIEQDGTPR 230
|
250
....*....|
gi 89111135 1340 VLAEKPDSAF 1349
Cdd:PRK09452 231 EIYEEPKNLF 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1128-1344 |
4.55e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTPL-VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTK-LTVIPQDPv 1205
Cdd:COG3845 264 SVRDDRGVpALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDR- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1206 LFVG-----TVRYNLDpFESHTDEMLWQvleRTFM-RDTIMKLPEKLQAE---VTENGE----NFSVGERQLLCVARALL 1272
Cdd:COG3845 343 LGRGlvpdmSVAENLI-LGRYRRPPFSR---GGFLdRKAIRAFAEELIEEfdvRTPGPDtparSLSGGNQQKVILARELS 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1273 RNSKIIL-------LDEATASMdsktdtlVQNTIKDAF-KGCTVLTIAHRLNTVLN-CDHVLVMENGKVI-EFDKPEVLA 1342
Cdd:COG3845 419 RDPKLLIaaqptrgLDVGAIEF-------IHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATR 491
|
..
gi 89111135 1343 EK 1344
Cdd:COG3845 492 EE 493
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
495-676 |
4.96e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--------------LAYVSQ--QAwifHG--- 555
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrLG---RGlvp 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 --NVRENILFGEkYDHQRYQHT--------------------VRVCGLQkdlsnlpygdlTEIGerglNLSGGQRQRISL 613
Cdd:COG3845 350 dmSVAENLILGR-YRRPPFSRGgfldrkairafaeelieefdVRTPGPD-----------TPAR----SLSGGNQQKVIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 614 ARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLqflescDEVILLED 676
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDL------DEILALSD 470
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1127-1346 |
5.87e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.46 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1127 MRYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSlgmaLFRLV----EPASGTIFIDEVDICILS---LEDLRTKLTV 1199
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggqiAPDHGEILFDGENIPAMSrsrLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDPVLFVG-TVRYNLD-PFESHTDemlwqvLERTFMRDTIMKlpeKLQAEVTENGEN-----FSVGERQLLCVARALL 1272
Cdd:PRK11831 89 LFQSGALFTDmNVFDNVAyPLREHTQ------LPAPLLHSTVMM---KLEAVGLRGAAKlmpseLSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1273 RNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPD 1346
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
468-692 |
6.30e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 468 RSEAYS-ERSPPAKGATGPE--EQSDSLKS----VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVN 540
Cdd:COG1245 321 RDEPIEfEVHAPRREKEEETlvEYPDLTKSyggfSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 541 GTLAYVSQqaWI---FHGNVRENI--LFGEKYDHQRYQHTVrVCGLQkdlsnlpygdLTEIGERGL-NLSGGQRQRISLA 614
Cdd:COG1245 401 LKISYKPQ--YIspdYDGTVEEFLrsANTDDFGSSYYKTEI-IKPLG----------LEKLLDKNVkDLSGGELQRVAIA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 615 RAVYSDRQLYLLDDPLSAVD-------AHVGKHVFEEcikktlRGKTVVLVTHQLQFLESCDEVILLEDGEICEKGTHKE 687
Cdd:COG1245 468 ACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAEN------RGKTAMVVDHDIYLIDYISDRLMVFEGEPGVHGHASG 541
|
....*
gi 89111135 688 LMEER 692
Cdd:COG1245 542 PMDMR 546
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
495-693 |
6.87e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVV---------AVNGTLAYVSQQA--------WIFHGNV 557
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldySKRGLLALRQQVAtvfqdpeqQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENILFgekydhqryqhTVRVCGLQKDLSNLPYGD-LTEIGERGLN------LSGGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:PRK13638 96 DSDIAF-----------SLRNLGVPEAEITRRVDEaLTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 631 SAVDAhVGKHVFEECIKKTL-RGKTVVLVTHQLQFL-ESCDEVILLEDGEICEKG------THKELMEERG 693
Cdd:PRK13638 165 AGLDP-AGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
493-692 |
8.32e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQK-GVVAVNGTLAYVS--QQAwIFHG-------------- 555
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRnpQQA-IAQGiamvpedrkrdgiv 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 556 ---NVRENIL--------FGEKYDHQRYQHTVRvcglqKDLSNL----PYGDLtEIGerglNLSGGQRQRISLARAVYSD 620
Cdd:PRK13549 354 pvmGVGKNITlaaldrftGGSRIDDAAELKTIL-----ESIQRLkvktASPEL-AIA----RLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 621 RQLYLLDDPLSAVDahVGKHvFEecIKKTL-----RGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHKELMEER 692
Cdd:PRK13549 424 PKILILDEPTRGID--VGAK-YE--IYKLInqlvqQGVAIIVISSELpEVLGLSDRVLVMHEGKLKGDLINHNLTQEQ 496
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1135-1336 |
1.92e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1135 LVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdicilsledlRTKLTVIPQDPVLFVgtvryn 1214
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK-----------GIKLGYFAQHQLEFL------ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1215 ldpfesHTDEMLWQVLERTFMRDTIMKLPEKLQA------EVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMD 1288
Cdd:PRK10636 389 ------RADESPLQHLARLAPQELEQKLRDYLGGfgfqgdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1289 -----SKTDTLVQntikdaFKGCTVLTIAHRLNTVLNCDHVLVMENGKVIEFD 1336
Cdd:PRK10636 463 ldmrqALTEALID------FEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
496-678 |
2.05e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTLAYVS--QQAwIFHG--------------NVRE 559
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRspRDA-IALGigmvhqhfmlvpnlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKydhqryqhtvRVCGLQKDLSNLpYGDLTEIGER-GLN---------LSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:COG3845 100 NIVLGLE----------PTKGGRLDRKAA-RARIRELSERyGLDvdpdakvedLSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 630 lSAV--DAHVgKHVFEecikkTLR-----GKTVVLVTHQLQ-FLESCDEVILLEDGE 678
Cdd:COG3845 169 -TAVltPQEA-DELFE-----ILRrlaaeGKSIIFITHKLReVMAIADRVTVLRRGK 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1123-1346 |
2.16e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.76 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1123 RDYQMRYrdNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDL------RT- 1195
Cdd:PRK11300 9 SGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIarmgvvRTf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1196 -------KLTVIPQDPV---------LFVG---TVRYNLDPFESHTDEMLWqvLERTFMRDTIMKlpeklqaevtENGeN 1256
Cdd:PRK11300 87 qhvrlfrEMTVIENLLVaqhqqlktgLFSGllkTPAFRRAESEALDRAATW--LERVGLLEHANR----------QAG-N 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1257 FSVGERQLLCVARALLRNSKIILLDEATASMDSK-TDTLVQ--NTIKDAFkGCTVLTIAHRLNTVLN-CDHVLVMENGKV 1332
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKeTKELDEliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTP 232
|
250
....*....|....
gi 89111135 1333 IEFDKPEVLAEKPD 1346
Cdd:PRK11300 233 LANGTPEEIRNNPD 246
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1132-1318 |
2.22e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.81 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1132 NTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDIC-------ILSLEDLRTKLTVIPQDP 1204
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFnqniyerRVNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1205 VLF----VGTVRYNLDPFESHTDEMLWQVLERTfMRDTimKLPEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILL 1280
Cdd:PRK14258 98 NLFpmsvYDNVAYGVKIVGWRPKLEIDDIVESA-LKDA--DLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 89111135 1281 DEATASMDS----KTDTLVQNTIKDAfkGCTVLTIAHRLNTV 1318
Cdd:PRK14258 175 DEPCFGLDPiasmKVESLIQSLRLRS--ELTMVIVSHNLHQV 214
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1137-1334 |
2.38e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLgMALFRLVEPA---SGTIFID-------------EVDICILSLEdlrtkLTVI 1200
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKVLSGVYPHgsyEGEILFDgevcrfkdirdseALGIVIIHQE-----LALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1201 PQDPV---LFVG--TVRY---NLDPFESHTDEMLWQVlertfmrdtimKLPEKLQAEVTENGenfsVGERQLLCVARALL 1272
Cdd:NF040905 91 PYLSIaenIFLGneRAKRgviDWNETNRRARELLAKV-----------GLDESPDTLVTDIG----VGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1273 RNSKIILLDEATASM-DSKTDTLVqNTIKDaFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIE 1334
Cdd:NF040905 156 KDVKLLILDEPTAALnEEDSAALL-DLLLE-LKaqGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
604-721 |
2.91e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 604 SGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVF-------EECikktlrGKTVVLVTHQLQFLES-CDEVILLE 675
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLnlmmdlqQEL------GLSYVFISHDLSVVEHiADEVMVMY 229
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 89111135 676 DGEICEKGTHKELmeergryaklihnlrglqFKDPEHLYNAAMVEA 721
Cdd:PRK11308 230 LGRCVEKGTKEQI------------------FNNPRHPYTQALLSA 257
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
855-1008 |
2.96e-06 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 50.54 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 855 YTASMVFMLVFGVTKGFVFTKTTLMASSS---LHD---TVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAE 928
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGqriLYDlrqDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 929 NFLQQFFMVVFILVILAAVFP----AVLLVVASLAVGFFILLRIFHRGVQEL-KKVENVSrspwfTHITSSMQGLGIIHA 1003
Cdd:cd18545 120 NLIPDLLTLVGIVIIMFSLNVrlalVTLAVLPLLVLVVFLLRRRARKAWQRVrKKISNLN-----AYLHESISGIRVIQS 194
|
....*
gi 89111135 1004 YGKKE 1008
Cdd:cd18545 195 FARED 199
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
503-634 |
3.04e-06 |
|
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: 50.10 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 503 VRKGKILGICGNVGSGKSSLLAALLGQMQLQKG-VVAVNGTLAYVSQQAWI-FHGNVREnILFG---EKYDHQRYQhtvr 577
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdIEIELDTVSYKPQYIKAdYEGTVRD-LLSSitkDFYTHPYFK---- 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 578 vcglqKDLSNlPYGdLTEIGERGLN-LSGGQRQRISLARAVYSDRQLYLLDDPLSAVD 634
Cdd:cd03237 97 -----TEIAK-PLQ-IEQILDREVPeLSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
499-688 |
3.24e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTL-------AYVSQQA------WIFH------GNVRE 559
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvtaeqpeDYRKLFSavftdfHLFDqllgpeGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 NILFGEKYDHQRYQHTVRVCGLQkdLSNLpygdlteigerglNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVgK 639
Cdd:PRK10522 422 PALVEKWLERLKMAHKLELEDGR--ISNL-------------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-R 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 89111135 640 HVFEECIKKTLR--GKTVVLVTHQLQFLESCDEVILLEDGEICE-KGTHKEL 688
Cdd:PRK10522 486 REFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1120-1359 |
3.36e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.19 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1120 ITFRDYQMRYRDNTPlVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEVDICILSLEDLRTKLTV 1199
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1200 IPQDP--VLFVGTVRY-------NLDPFESHTDEMLWQVLERTFMRDTIMKLPEKLqaevtengenfSVGERQLLCVARA 1270
Cdd:PRK13652 83 VFQNPddQIFSPTVEQdiafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1271 LLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHRLNTVLN-CDHVLVMENGKVIEFDKPEVLAEKPDs 1347
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD- 230
|
250
....*....|..
gi 89111135 1348 afamlLAAEVRL 1359
Cdd:PRK13652 231 -----LLARVHL 237
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
496-683 |
3.66e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT------LAYVSQQ--------AWIF-HGNVRE- 559
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdLYALSEAerrrllrtEWGFvHQHPRDg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 560 ---------NIlfGEKYDHQRYQHtvrvcglqkdlsnlpYGDLTEIGERGLN---------------LSGGQRQRISLAR 615
Cdd:PRK11701 102 lrmqvsaggNI--GERLMAVGARH---------------YGDIRATAGDWLErveidaariddlpttFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 616 AVYSDRQLYLLDDPLSAVDAHVGKHVFEecikkTLRGKT------VVLVTHQL---QFLesCDEVILLEDGEICEKG 683
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLD-----LLRGLVrelglaVVIVTHDLavaRLL--AHRLLVMKQGRVVESG 234
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
496-678 |
3.96e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQ---------------------LQKGVVAVNGTLAYVSQQawifh 554
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQkdsgsilfqgkeidfksskeaLENGISMVHQELNLVLQR----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 555 gNVRENILFGeKY-------DHQR-YQHTVRVCGlQKDLSNLPYgdlteigERGLNLSGGQRQRISLARAVYSDRQLYLL 626
Cdd:PRK10982 89 -SVMDNMWLG-RYptkgmfvDQDKmYRDTKAIFD-ELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 89111135 627 DDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQL-QFLESCDEVILLEDGE 678
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRDGQ 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
603-688 |
5.56e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 603 LSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAhVGKHVFEECIKKTLRGKTVVLVTH-QLQFLESCDEVILLEDGEICE 681
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDP-ENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
....*..
gi 89111135 682 KGTHKEL 688
Cdd:PRK14247 226 WGPTREV 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1137-1351 |
5.65e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.16 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1137 LDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVePASGTIFIDEVDICILSLEDL-RTKLTVIPQDPVLFVGTVRYNL 1215
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1216 D---PFESHTDEM---LWQVLERTFMRDtimKLPEKLQAevtengenFSVGERQ-------LLCVARALLRNSKIILLDE 1282
Cdd:PRK03695 91 TlhqPDKTRTEAVasaLNEVAEALGLDD---KLGRSVNQ--------LSGGEWQrvrlaavVLQVWPDINPAGQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1283 ATASMD----SKTDTLVQntiKDAFKGCTVLTIAHRLNTVL-NCDHVLVMENGKVI------EFDKPEVLAEkpdsAFAM 1351
Cdd:PRK03695 160 PMNSLDvaqqAALDRLLS---ELCQQGIAVVMSSHDLNHTLrHADRVWLLKQGKLLasgrrdEVLTPENLAQ----VFGV 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
493-679 |
7.01e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 49.31 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGTlaYVSQQAwifhgnvrenilfgekyDHQRY 572
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVTKLP-----------------EYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 573 QHTVRV--------C-----------------------GLQKDLSNLpYGDLTEIGERGL---------NLSGGQRQRIS 612
Cdd:COG1101 80 KYIGRVfqdpmmgtApsmtieenlalayrrgkrrglrrGLTKKRREL-FRELLATLGLGLenrldtkvgLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 613 LARAVYSDRQLYLLDDPLSAVDAHVGKHVFE---ECIKKtlRGKTVVLVTHQLQF-LESCDEVILLEDGEI 679
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLElteKIVEE--NNLTTLMVTHNMEQaLDYGNRLIMMHEGRI 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
502-662 |
7.01e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 502 VVRKGKILGICGNVGSGKSSLLAALLGQM------------------------------QLQKGVVAVNGTLAYVSQQAW 551
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELipnlgdyeeepswdevlkrfrgtelqnyfkKLYNGEIKVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 552 IFHGNVREnILfgEKYDhQRyqhtvrvcGLQKDL-SNLpygDLTEIGERGL-NLSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:PRK13409 175 VFKGKVRE-LL--KKVD-ER--------GKLDEVvERL---GLENILDRDIsELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....*...
gi 89111135 630 LSAVDahvgkhVFE-----ECIKKTLRGKTVVLVTHQL 662
Cdd:PRK13409 240 TSYLD------IRQrlnvaRLIRELAEGKYVLVVEHDL 271
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
846-971 |
7.09e-06 |
|
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: 49.41 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 846 IGQHVYQWVYTASMVFMLVFGVTKGFVFTKTTLMASSS---LHDT---VFDKILKSPMSFFDTTPTGRLMNRFSKDMDEL 919
Cdd:cd18546 30 VRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGerlLYDLrlrVFAHLQRLSLDFHERETSGRIMTRMTSDIDAL 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 89111135 920 DVRLPFHAENFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHR 971
Cdd:cd18546 110 SELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR 161
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
499-691 |
7.52e-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: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-LAYVSQQAW---------IF---HG--NVR---EN 560
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELrplrrrmqmVFqdpYAslNPRmtvGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILfGEKYDhqryQHTVrvcglqkdlsnlpyGDLTEIGER--------GLN----------LSGGQRQRISLARAVYSDRQ 622
Cdd:COG4608 117 II-AEPLR----IHGL--------------ASKAERRERvaellelvGLRpehadrypheFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 623 LYLLDDPLSAVDAHVGKHV---FEEcIKKTLrGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEE 691
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVlnlLED-LQDEL-GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1144-1343 |
7.52e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1144 IQSGQTVGIVGRTGSGKSSLGMAL-FRL---VEpASGTIFIDEVDIcilSLEDLRTKLTVIPQDPvLFVG--TVRYNLDp 1217
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALaFRSpkgVK-GSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIPtlTVREHLM- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1218 FESHTD-----------EMLWQVLERTFMR---DTIMKLPEKLQAevtengenFSVGERQLLCVARALLRNSKIILLDEA 1283
Cdd:TIGR00955 122 FQAHLRmprrvtkkekrERVDEVLQALGLRkcaNTRIGVPGRVKG--------LSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111135 1284 TASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLNC--DHVLVMENGKVIEFDKPEVLAE 1343
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1146-1339 |
7.77e-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: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1146 SGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFidevdicILSLEDLRTKLTVipqdpvlfvgtvrynldpfeshtdem 1225
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-------YIDGEDILEEVLD-------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1226 lwqvlertfmrdtimklpEKLQAEVTENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ-------NT 1298
Cdd:smart00382 48 ------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLL 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 89111135 1299 IKDAFKGCTVLTIAHRLNTVLncDHVLVMENGKVIEFDKPE 1339
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLIL 148
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
603-672 |
8.86e-06 |
|
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: 47.35 E-value: 8.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 603 LSGGQRQRISLARAV----YSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVI 672
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
860-985 |
9.71e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 48.97 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 860 VFMLVFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVF 939
Cdd:cd18551 47 LLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVG 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 89111135 940 ILVILAAV-FPAVLLVVASLAVGFFILLRIfhrgvqeLKKVENVSRS 985
Cdd:cd18551 127 AVVLMFLLdWVLTLVTLAVVPLAFLIILPL-------GRRIRKASKR 166
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
864-978 |
1.02e-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: 350020 [Multi-domain] Cd Length: 289 Bit Score: 49.02 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 864 VFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPFHAENFLQQFFMVVFILVI 943
Cdd:cd18576 51 VFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVL 130
|
90 100 110
....*....|....*....|....*....|....*
gi 89111135 944 LAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKK 978
Cdd:cd18576 131 LFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSK 165
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
857-969 |
1.02e-05 |
|
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: 49.13 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 857 ASMVFMLVFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSkdmdELD-VRlpfhaeNFLQQ-- 933
Cdd:cd18782 50 VAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS----ELDtIR------GFLTGta 119
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 89111135 934 -------FFMVVFILVILAavFPAVLLVVASLAVGFFILLRIF 969
Cdd:cd18782 120 lttlldvLFSVIYIAVLFS--YSPLLTLVVLATVPLQLLLTFL 160
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
496-708 |
1.12e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.59 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 496 LHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT-------------------LAYVSQQAWIFHGN 556
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkvgLVFQFPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 VRENILFG-------EKYDHQRYQHTVRVCGLQKDLsnlpygdlteIGERGLNLSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:PRK13649 103 VLKDVAFGpqnfgvsQEEAEALAREKLALVGISESL----------FEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 630 LSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQL-QFLESCDEVILLEDGEICEKGTHK------ELMEERG----RYAKL 698
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGKPKdifqdvDFLEEKQlgvpKITKF 252
|
250
....*....|..
gi 89111135 699 IHNL--RGLQFK 708
Cdd:PRK13649 253 AQRLadRGISFS 264
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
853-980 |
1.29e-05 |
|
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: 48.67 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 853 WVYTASMVFMLVFGVTKGFVFTKTTLMASSS----LHDTVFDKILKSPMSFFDTTPTGRLMnrfsKDMDELD-VRlpfha 927
Cdd:cd18783 42 YVLTIGVVIALLFEGILGYLRRYLLLVATTRidarLALRTFDRLLSLPIDFFERTPAGVLT----KHMQQIErIR----- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 928 eNFL-QQFFMVVF----ILVILAAVFP-----AVLLVVASLAVGF--FILLRIFHRGVQELKKVE 980
Cdd:cd18783 113 -QFLtGQLFGTLLdatsLLVFLPVLFFysptlALVVLAFSALIALiiLAFLPPFRRRLQALYRAE 176
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1118-1332 |
1.53e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1118 GEITF--RDYQMRYRDNTPL-VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPAS-GTIFIDEVDICILSLED- 1192
Cdd:PRK13549 256 GEVILevRNLTAWDPVNPHIkRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNPQQa 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1193 LRTKLTVIPQD-------PVLFVG---TVRyNLDPFESHTdeMLWQVLERTFMRDTIMKLPEKlqaevTENGE----NFS 1258
Cdd:PRK13549 336 IAQGIAMVPEDrkrdgivPVMGVGkniTLA-ALDRFTGGS--RIDDAAELKTILESIQRLKVK-----TASPElaiaRLS 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 1259 VGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVLN-CDHVLVMENGKV 1332
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1119-1333 |
1.55e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.54 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1119 EITFRDYQMRYRDNTPL---VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTI----------------- 1178
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1179 -FIDEVDIC------ILSLEDLRTKLTVIPQ--DPVLF---------VGTVRYNLDPFEShtdemlwqvLERTFMRDTIM 1240
Cdd:PRK13651 82 kVLEKLVIQktrfkkIKKIKEIRRRVGVVFQfaEYQLFeqtiekdiiFGPVSMGVSKEEA---------KKRAAKYIELV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1241 KLPEK-LQaevtENGENFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKDAFK-GCTVLTIAHRLNTV 1318
Cdd:PRK13651 153 GLDESyLQ----RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNV 228
|
250
....*....|....*.
gi 89111135 1319 LN-CDHVLVMENGKVI 1333
Cdd:PRK13651 229 LEwTKRTIFFKDGKII 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
499-629 |
2.39e-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: 48.78 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNGT--LAYVSQQAWIFHGN--VRENILFGekYDHQR--- 571
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvkLAYVDQSRDALDPNktVWEEISGG--LDIIKlgk 418
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 572 YQHTVRV-CGL--------QKdlsnlpygdltEIGErglnLSGGQRQRISLARAVYSDRQLYLLDDP 629
Cdd:TIGR03719 419 REIPSRAyVGRfnfkgsdqQK-----------KVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1128-1314 |
3.44e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.49 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVE--PASGTIFIDEVDI--------CILSLEDLRTKL 1197
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFgreaslidAIGRKGDFKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1198 TVIPQ----DPVLFVgtvrynldpfeshtdemlwqvleRTFmrdtimklpeklqaevtengENFSVGERQLLCVARALLR 1273
Cdd:COG2401 117 ELLNAvglsDAVLWL-----------------------RRF--------------------KELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 89111135 1274 NSKIILLDEATASMDSKTDTLVQNTIKDAFK--GCTVLTIAHR 1314
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1144-1313 |
3.49e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1144 IQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDEvdicilsledlrtKLTVIPQ----DpvlFVGTVRYNLdpfE 1219
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL-------------KISYKPQyikpD---YDGTVEDLL---R 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1220 SHTDEmlwqvLERTFMRDTIMK---LPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQ 1296
Cdd:PRK13409 423 SITDD-----LGSSYYKSEIIKplqLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
170
....*....|....*....
gi 89111135 1297 NTIKDAF--KGCTVLTIAH 1313
Cdd:PRK13409 494 KAIRRIAeeREATALVVDH 512
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
852-1005 |
4.63e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 47.18 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 852 QWVYTASMVFmLVFGVTKGFVFTKTTLM---ASSSLHD---TVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDVRLPF 925
Cdd:cd18565 52 QLWLLGGLTV-AAFLLESLFQYLSGVLWrrfAQRVQHDlrtDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 926 HAENFLQQFFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQEL-----KKVENVSrspwfTHITSSMQGLGI 1000
Cdd:cd18565 131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRyravrEAVGDLN-----ARLENNLSGIAV 205
|
....*
gi 89111135 1001 IHAYG 1005
Cdd:cd18565 206 IKAFT 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1136-1337 |
5.02e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.57 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPAS--GTIFIDEVDICILSLEdlRTKLtvIPQDPVLFVG-TVR 1212
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK--RTGF--VTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1213 YNLdPFESHTDemlwqvLERTFMRDTIMKLPEKLQAEV----TEN---GENF----SVGERQLLCVARALLRNSKIILLD 1281
Cdd:PLN03211 159 ETL-VFCSLLR------LPKSLTKQEKILVAESVISELgltkCENtiiGNSFirgiSGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 1282 EATASMDSKTD-TLVQNTIKDAFKGCTVLTIAHRLNTVL--NCDHVLVMENGKVIEFDK 1337
Cdd:PLN03211 232 EPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEGRCLFFGK 290
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
855-915 |
5.09e-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: 5.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 855 YTASMVFMLVFGVTKGFVFTKTTLMASSS------LHDTVFDKILKSPMSFFDTTPTGRLMNRFSKD 915
Cdd:cd18573 41 KTFALALLGVFVVGAAANFGRVYLLRIAGerivarLRKRLFKSILRQDAAFFDKNKTGELVSRLSSD 107
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
841-956 |
5.30e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 46.70 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 841 AVLADIGQHVYQWVYTAsmVFMLVFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELD 920
Cdd:cd18577 41 EFLDDVNKYALYFVYLG--IGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQ 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 89111135 921 V----RLPFhaenFLQQFFMVV------FI------LVILaAVFPAVLLVVA 956
Cdd:cd18577 119 DgigeKLGL----LIQSLSTFIagfiiaFIyswkltLVLL-ATLPLIAIVGG 165
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
488-714 |
6.86e-05 |
|
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: 46.99 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 488 QSDSLKSVLHSISFVVRKGKILGICGNVGSGKS-SLLAAL-LgqmqLQKGVVAVNGTLAYVSQQ---------------- 549
Cdd:COG4172 18 QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrL----LPDPAAHPSGSILFDGQDllglserelrrirgnr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 550 -AWIF----------H--GN-VRENILFgekydHQRY---QHTVRVCGLqkdlsnlpygdLTEIG----ERGLN-----L 603
Cdd:COG4172 94 iAMIFqepmtslnplHtiGKqIAEVLRL-----HRGLsgaAARARALEL-----------LERVGipdpERRLDayphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 604 SGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEecIKKTL---RGKTVVLVTHQL----QFlesCDEVILLED 676
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD--LLKDLqreLGMALLLITHDLgvvrRF---ADRVAVMRQ 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 89111135 677 GEICEKGTHKELmeergryaklihnlrglqFKDPEHLY 714
Cdd:COG4172 233 GEIVEQGPTAEL------------------FAAPQHPY 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
487-661 |
7.17e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.72 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 487 EQSDSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNgtlayVSQQAWIFHGNVRENIL-FGE 565
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGrKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 566 KYDHQRYQHTvrvCGLqkdlsNLPYGDLTEIGErglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD---AHVGKHVF 642
Cdd:COG2401 112 FKDAVELLNA---VGL-----SDAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNL 179
|
170
....*....|....*....
gi 89111135 643 EECIKKtlRGKTVVLVTHQ 661
Cdd:COG2401 180 QKLARR--AGITLVVATHH 196
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
596-678 |
9.62e-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: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 596 IGERGLNLSGGQRQRISLARAVY---SDRQLYLLDDPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVI 672
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
|
....*...
gi 89111135 673 LL--EDGE 678
Cdd:cd03271 243 DLgpEGGD 250
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1143-1321 |
9.65e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1143 NIQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIFIDevdicilsledlrTKLTVIPQDpvlfvgTVRYNLDPfesht 1222
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------------TKLEVAYFD------QHRAELDP----- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1223 demlwqvlERTFMRDtimkLPEKLQaEVTENG---------ENF--------------SVGERQLLCVARALLRNSKIIL 1279
Cdd:PRK11147 397 --------EKTVMDN----LAEGKQ-EVMVNGrprhvlgylQDFlfhpkramtpvkalSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 89111135 1280 LDEATASMDSKTDTLVQNTIkDAFKGcTVLTIAH-RL---NTVLNC 1321
Cdd:PRK11147 464 LDEPTNDLDVETLELLEELL-DSYQG-TVLLVSHdRQfvdNTVTEC 507
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
593-690 |
1.37e-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: 46.54 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 593 LTEIGER-------GLN----------LSGGQRQRISLARAVYSDRQ--LYLLDDPlsavdaHVGKHVFE-ECIKKTLR- 651
Cdd:TIGR00630 462 LKEIRERlgflidvGLDylslsraagtLSGGEAQRIRLATQIGSGLTgvLYVLDEP------SIGLHQRDnRRLINTLKr 535
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 89111135 652 ----GKTVVLVTHQLQFLESCDEVILL------EDGEICEKGTHKELME 690
Cdd:TIGR00630 536 lrdlGNTLIVVEHDEDTIRAADYVIDIgpgageHGGEVVASGTPEEILA 584
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
864-978 |
1.43e-04 |
|
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: 45.32 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 864 VFGVTKGFVFTKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELD----VRLPFHAENFLQQFFMVVF 939
Cdd:cd18780 57 IATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQnavtVNLSMLLRYLVQIIGGLVF 136
|
90 100 110
....*....|....*....|....*....|....*....
gi 89111135 940 ILVILAAVFPAVLLVVASLAVGFfillRIFHRGVQELKK 978
Cdd:cd18780 137 MFTTSWKLTLVMLSVVPPLSIGA----VIYGKYVRKLSK 171
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
490-742 |
1.52e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.49 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 490 DSLKSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGqmqlqkgVVAVNGTlayVSQQAwIFHG----NVRENILfge 565
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG-------LLAANGR---IGGSA-TFNGreilNLPEKEL--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 566 kyDHQRYQHTVRVcgLQKDLSNL-PY---GD-LTEI--GERGLN------------------------------LSGGQR 608
Cdd:PRK09473 92 --NKLRAEQISMI--FQDPMTSLnPYmrvGEqLMEVlmLHKGMSkaeafeesvrmldavkmpearkrmkmypheFSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 609 QRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFE--ECIKKTLrGKTVVLVTHQLQFLE-SCDEVILLEDGEICEKGTH 685
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTllNELKREF-NTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGNA 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 686 KELmeergryaklihnlrglqFKDPEHLYNAAMVEAFKESPAEREEDAGIivlaPGN 742
Cdd:PRK09473 247 RDV------------------FYQPSHPYSIGLLNAVPRLDAEGESLLTI----PGN 281
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
499-693 |
1.64e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSS-------LLAA------LLGQ------MQLQKGVvavngtlAYVSQqAWIFHG--NV 557
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPAsegeawLFGQpvdagdIATRRRV-------GYMSQ-AFSLYGelTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENI-----LFG--EKYDHQRYQHTVRVCGLQKDLSNLPygdlteigeRGLNLsgGQRQRISLARAVYSDRQLYLLDDPL 630
Cdd:NF033858 357 RQNLelharLFHlpAAEIAARVAEMLERFDLADVADALP---------DSLPL--GIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111135 631 SAVDAhVGKHVFEECIKKTLR--GKTVVLVTHqlqFL---ESCDEVILLEDGEICEKGTHKELMEERG 693
Cdd:NF033858 426 SGVDP-VARDMFWRLLIELSRedGVTIFISTH---FMneaERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
503-692 |
2.28e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 503 VRKGKILGICGNVGSGKSSLLAALLGQMQLQKG-------VVAVNGTLAyvSQQAW--IFHG--------NVRENILFGE 565
Cdd:PRK10762 27 VYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkEVTFNGPKS--SQEAGigIIHQelnlipqlTIAENIFLGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 566 KY-------DHQR-YQHTVRvcgLQKDLsNLPYGDLTEIGErglnLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHV 637
Cdd:PRK10762 105 EFvnrfgriDWKKmYAEADK---LLARL-NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 638 GKHVFEecIKKTLR--GKTVVLVTHQLQ-FLESCDEVILLEDGE-ICEKGThKELMEER 692
Cdd:PRK10762 177 TESLFR--VIRELKsqGRGIVYISHRLKeIFEICDDVTVFRDGQfIAEREV-ADLTEDS 232
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
888-975 |
2.76e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 44.45 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 888 VFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDvRLPFHA-ENFLQ---QFFMVVFIL----VILAAV--FPAVLLVVas 957
Cdd:cd18778 79 LYDKLQRLSLRYFDDRQTGDLMSRVINDVANVE-RLIADGiPQGITnvlTLVGVAIILfsinPKLALLtlIPIPFLAL-- 155
|
90
....*....|....*...
gi 89111135 958 LAVGFFILLRIFHRGVQE 975
Cdd:cd18778 156 GAWLYSKKVRPRYRKVRE 173
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
493-679 |
3.25e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.71 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 493 KSVLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG---------TLAYVSQQ-AWIFHGN------ 556
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrEVPFLRRQiGMIFQDHhllmdr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 557 -VREN-----ILFGEKYD--HQRYQHTVRVCGLQKDLSNLPygdlteigergLNLSGGQRQRISLARAVYSDRQLYLLDD 628
Cdd:PRK10908 95 tVYDNvaiplIIAGASGDdiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 629 PLSAVDAHVGKHV---FEECIKKtlrGKTVVLVTHQLQFLESCD-EVILLEDGEI 679
Cdd:PRK10908 164 PTGNLDDALSEGIlrlFEEFNRV---GVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1128-1335 |
3.29e-04 |
|
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: 43.41 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1128 RYRDNTPLVLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALFRLVEPAsgtifidevdiciLSLEdlrtkltvipqdpvlf 1207
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGN-------------VSVE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1208 vGTVRYN---LDPF-ESHTDEMLWQVLERTFM-----RDTiMKLPEKLQAEvtENGENFSVGERQLLCVARALLRNSKII 1278
Cdd:cd03233 65 -GDIHYNgipYKEFaEKYPGEIIYVSEEDVHFptltvRET-LDFALRCKGN--EFVRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111135 1279 LLDEATASMDSKTDTLVQNTIK---DAFKGCTVLTIAHRLNTVLNC-DHVLVMENGKVIEF 1335
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRtmaDVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQIYY 201
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
558-693 |
3.32e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RENI-LFGEKYDHQRYQHTVRVCGLQKDLSnlpygdLTEI-GERGLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVDA 635
Cdd:NF000106 104 RENLyMIGR*LDLSRKDARARADELLERFS------LTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 89111135 636 HVGKHVFEECIKKTLRGKTVVLVTHQLQFLES-CDEVILLEDGEICEKGTHKELMEERG 693
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
499-721 |
4.31e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 499 ISFVVRKGKILGICGNVGSGKSSLLAALL------------GQMQLQK---GVVAVNGTLAYVSQQ------AWIFHGNV 557
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMrlleqagglvqcDKMLLRRrsrQVIELSEQSAAQMRHvrgadmAMIFQEPM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 558 RE-NILF--GEKYD-----HQ------------RYQHTVRVCGLQKDLSNLPYgdlteigerglNLSGGQRQRISLARAV 617
Cdd:PRK10261 115 TSlNPVFtvGEQIAesirlHQgasreeamveakRMLDQVRIPEAQTILSRYPH-----------QLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 618 YSDRQLYLLDDPLSAVDAHVGKHVFEecIKKTLRGKT---VVLVTHQLQFL-ESCDEVILLEDGEICEKGTHKELmeerg 693
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMsmgVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQI----- 256
|
250 260
....*....|....*....|....*...
gi 89111135 694 ryaklihnlrglqFKDPEHLYNAAMVEA 721
Cdd:PRK10261 257 -------------FHAPQHPYTRALLAA 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
604-678 |
4.79e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 4.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111135 604 SGGQRQRISLARAVYSDRQLYLLDDPLSAVDAHVGKHVFEECIKKTlrgKTVVLVTHQLQFLESCDEVILLEDGE 678
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNTVVTDILHLHGQ 417
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
502-678 |
5.72e-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: 42.17 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 502 VVRKGKILGICGNVGSGKSSLLAALLGQMQLQKGVVAVNG-TLAYVSQQawifhgnvrenilfgekydhqryqhtvrvcg 580
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 581 lqkdlsnlpygdlteigergLNLSGGQRQRISLARAVYSDRQLYLLDDPLSAVD-------AHVGKHVFEEcikktlRGK 653
Cdd:cd03222 70 --------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrlnaARAIRRLSEE------GKK 123
|
170 180
....*....|....*....|....*
gi 89111135 654 TVVLVTHQLQFLESCDEVILLEDGE 678
Cdd:cd03222 124 TALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
596-688 |
6.01e-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: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 596 IGERGLNLSGGQRQRISLARAVY---SDRQLYLLDDPLSavdahvGKHvFEEcIKKTL--------RGKTVVLVTHQLQF 664
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTT------GLH-FDD-IKKLLevlqrlvdKGNTVVVIEHNLDV 894
|
90 100 110
....*....|....*....|....*....|
gi 89111135 665 LESCDEVILL------EDGEICEKGTHKEL 688
Cdd:TIGR00630 895 IKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
889-1008 |
6.23e-04 |
|
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: 43.55 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 889 FDKILKSPMSFFDTTPTGRLMNRFSKDMDEldVR--LPFHAENFLQQFFMVVFILVI---------LAAVFPAVLLVVAS 957
Cdd:cd18541 80 FAHLLTLSPSFYQKNRTGDLMARATNDLNA--VRmaLGPGILYLVDALFLGVLVLVMmftispkltLIALLPLPLLALLV 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 89111135 958 LAVGFFILLRifHRGVQElkKVENVSrspwfTHITSSMQGLGIIHAYGKKE 1008
Cdd:cd18541 158 YRLGKKIHKR--FRKVQE--AFSDLS-----DRVQESFSGIRVIKAFVQEE 199
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
559-674 |
6.94e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 559 ENILFGEKYDHQRYQhtvRVCGLQkdLSNLPYGdlteigeRGL-NLSGGQRQRISLARAVYSDRQ---LYLLDDPLSAVD 634
Cdd:PRK00635 777 EKFFLDEPSIHEKIH---ALCSLG--LDYLPLG-------RPLsSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLH 844
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 89111135 635 AHVGKHVFEECIKKTLRGKTVVLVTHQLQFLESCDEVILL 674
Cdd:PRK00635 845 THDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
853-964 |
8.28e-04 |
|
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: 42.86 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 853 WVYTASMVFM-LVFGVTKGFVF---TKTTLMASSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDELDvRLPFHAE 928
Cdd:cd18579 39 YLLALALFLVsLLQSLLLHQYFflsFRLGMRVRSALSSLIYRKALRLSSSARQETSTGEIVNLMSVDVQRIE-DFFLFLH 117
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 89111135 929 NFLQQFFMVVFILVIL-----AAVFPAVLLVVASLAVGFFI 964
Cdd:cd18579 118 YLWSAPLQIIVALYLLyrllgWAALAGLGVLLLLIPLQAFL 158
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
853-1008 |
8.70e-04 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 42.82 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 853 WVYTASMVFMLVFGVtkGFVFTKTTLMA------SSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSkdmDELDVRlpfh 926
Cdd:cd18570 42 NIISIGLILLYLFQS--LLSYIRSYLLLklsqklDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN---DANKIR---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 927 aeNFLQQ--------FFMVVFILVILAAVFPAVLLVVASLAVGFFILLRIFHRGVQELKKVENVSRSPWFTHITSSMQGL 998
Cdd:cd18570 113 --EAISSttislfldLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGI 190
|
170
....*....|
gi 89111135 999 GIIHAYGKKE 1008
Cdd:cd18570 191 ETIKSLNAEE 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1144-1300 |
1.16e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 43.23 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1144 IQSGQTVGIVGRTGSGKSSLGMALFRLVEPASGTIfidevdicilsleDLRTKLTVIPQ----DpvlFVGTVRYNL---- 1215
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyispD---YDGTVEEFLrsan 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1216 -DPFESHtdemLWQ--VLERtfmrdtiMKLPEKLQAEVTEngenFSVGERQLLCVARALLRNSKIILLDEATASMDSKTD 1292
Cdd:COG1245 427 tDDFGSS----YYKteIIKP-------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
....*...
gi 89111135 1293 TLVQNTIK 1300
Cdd:COG1245 492 LAVAKAIR 499
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
495-677 |
3.77e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 495 VLHSISFVVRKGKILGICGNVGSGKSSLLAALLGQMQ--LQKGVVAVNG------TLAYVS---QQAWIfHG---NVREN 560
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkqeTFARISgycEQNDI-HSpqvTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 561 ILFG---------EKYDHQRY----QHTVRVCGLQKDLSNLPygdlteiGERGLnlSGGQRQRISLARAVYSDRQLYLLD 627
Cdd:PLN03140 974 LIYSaflrlpkevSKEEKMMFvdevMELVELDNLKDAIVGLP-------GVTGL--STEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 89111135 628 DPLSAVDAHVGKHVFEECIKKTLRGKTVVLVTHQ--LQFLESCDEVILLEDG 677
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
832-959 |
4.81e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 40.57 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 832 GNRTMCEVGAVLADIGQHVYQWVYTASMVFMLVFGVTKGFVFTKTTLMAS------SSLHDTVFDKILKSPMSFFDTTPT 905
Cdd:cd18564 31 GDKPLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALvgqrvvLDLRRDLFAHLQRLSLSFHDRRRT 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89111135 906 GRLMNRFSKDMDEL-----DVRLPFHAeNFLQQFFMVVFILVI---LA----AVFPAVLLVVASLA 959
Cdd:cd18564 111 GDLLSRLTGDVGAIqdllvSGVLPLLT-NLLTLVGMLGVMFWLdwqLAlialAVAPLLLLAARRFS 175
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
861-918 |
8.80e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 39.84 E-value: 8.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111135 861 FMLVFGVTKGFVFTKTTLMA------SSSLHDTVFDKILKSPMSFFDTTPTGRLMNRFSKDMDE 918
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSvvgervAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQE 111
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1136-1185 |
9.18e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 9.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 89111135 1136 VLDSLNLNIQSGQTVGIVGRTGSGKSSLGMALF-----RLVepaSGTIFID--EVDI 1185
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrsygRNI---SGTVFKDgkEVDV 328
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1258-1336 |
9.46e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 38.76 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 1258 SVGERQLLCVARALLRNSKIILLDEATASMDSKTDTLVQNTIKD-AFKGCTVLTIAHRLNTVL--NCDHVLVME-NGKVI 1333
Cdd:cd03232 110 SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSASIfeKFDRLLLLKrGGKTV 189
|
...
gi 89111135 1334 EFD 1336
Cdd:cd03232 190 YFG 192
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
888-971 |
9.72e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 39.77 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111135 888 VFDKILKSPMSFFDTTPTGRLMNRFSKDMDEldVR-----LPFhaenFLQQFFMVVFILVILAAVFPAVLLVVASLAVGF 962
Cdd:cd18543 78 LFAHLQRLDGAFHDRWQSGQLLSRATSDLSL--VQrflafGPF----LLGNLLTLVVGLVVMLVLSPPLALVALASLPPL 151
|
....*....
gi 89111135 963 FILLRIFHR 971
Cdd:cd18543 152 VLVARRFRR 160
|
|
| |
