|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-1226 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 882.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 46 RTGVRLRGAILTMAFKKILKLKNIKEKSL--GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLG 123
Cdd:PLN03130 367 RVGFRLRSTLVAAVFRKSLRLTHEGRKKFtsGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 124 SAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSIT 203
Cdd:PLN03130 447 SLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFN 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 204 VGVAPIVVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMIKNK 283
Cdd:PLN03130 527 SFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNP 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 284 PASPHI-KIEMKNATLAWDSShssiqnspkltpkmkkdkrasrgkkekvrqlqrtehqavlaeqkghllldsDERPspee 362
Cdd:PLN03130 607 PLEPGLpAISIKNGYFSWDSK---------------------------------------------------AERP---- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 363 eegkhihlghlrlqrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQM-TLLEGSIAISGTFAYVAQQAWILNATLR 441
Cdd:PLN03130 632 ---------------TLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpPRSDASVVIRGTVAYVPQVSWIFNATVR 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 521
Cdd:PLN03130 697 DNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 522 NHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLLlGDTPPVE--INSKK 599
Cdd:PLN03130 777 RQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NG---PLFQKLM-ENAGKMEeyVEENG 851
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 600 ETSGSQKKSQDKGPKTGSVKKEKAV---KPEEGQ--LVQLEEKGQGSVPWSVYGVYIQAAGGplaFLVIMALFMLNVGST 674
Cdd:PLN03130 852 EEEDDQTSSKPVANGNANNLKKDSSskkKSKEGKsvLIKQEERETGVVSWKVLERYKNALGG---AWVVMILFLCYVLTE 928
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 675 AF---STWWLSYWIKQGSGNTTvtrgnetsvsdsmkdnpRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDE 751
Cdd:PLN03130 929 VFrvsSSTWLSEWTDQGTPKTH-----------------GPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDA 991
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 752 LFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNV---ILVFFCVGMIAGVFPWflvAVGPLVILFSV 828
Cdd:PLN03130 992 MLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIfqlLSTFVLIGIVSTISLW---AIMPLLVLFYG 1068
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 829 LHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYnKGQEFLHRYQELLDDNQAPFFLFT-CAMRWLAVRLDLIS 907
Cdd:PLN03130 1069 AYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAY-KAYDRMAEINGRSMDNNIRFTLVNmSSNRWLAIRLETLG 1147
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 908 IALITTTGLMIVLMHGQI--PPAYA---GLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARIKNK 982
Cdd:PLN03130 1148 GLMIWLTASFAVMQNGRAenQAAFAstmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYID-LPSEAPLVIENN 1226
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 983 APSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI 1062
Cdd:PLN03130 1227 RPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF 1306
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1063 GLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIA 1142
Cdd:PLN03130 1307 GLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLA 1386
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1143 RALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSR 1222
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSA 1466
|
....
gi 1622900605 1223 FYAM 1226
Cdd:PLN03130 1467 FSKM 1470
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
47-1226 |
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: 870.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 47 TGVRLRGAILTMAFKKILKLKNIKEKS--LGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGS 124
Cdd:TIGR00957 385 SGMRIKTAVMGAVYRKALVITNSARKSstVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGV 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 125 AVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITV 204
Cdd:TIGR00957 465 AVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGT 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 205 GVAPIVVVIASVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEV--HMI 280
Cdd:TIGR00957 545 FTWVCTPFLVALITFAVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELepDSI 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 281 KNKPASP--HIKIEMKNATLAWDSshssiqnspkltpkmkkdkrasrgkkekvrqlqrtehqavlaeqkghllldsDERP 358
Cdd:TIGR00957 625 ERRTIKPgeGNSITVHNATFTWAR----------------------------------------------------DLPP 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 359 speeeegkhihlghlrlqrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA 438
Cdd:TIGR00957 653 -------------------TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQND 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:TIGR00957 714 SLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 519 HVGNHIFNSAI--RKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYAT---------------- 580
Cdd:TIGR00957 794 HVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEflrtyapdeqqghled 873
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 581 ---------------IFNNLLLGDTppVEINSKKETSGSQKKSQDKGPKTGSVKK-EKA-VKPEEGQLVQLEEKGQGSVP 643
Cdd:TIGR00957 874 swtalvsgegkeaklIENGMLVTDV--VGKQLQRQLSASSSDSGDQSRHHGSSAElQKAeAKEETWKLMEADKAQTGQVE 951
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 644 WSVYGVYIQAAGGPLAFLVIMaLFMLNVGSTAFSTWWLSYWIKQGSGNTTvtrGNETSVsdsmkdnpRMQYYASIYALS- 722
Cdd:TIGR00957 952 LSVYWDYMKAIGLFITFLSIF-LFVCNHVSALASNYWLSLWTDDPMVNGT---QNNTSL--------RLSVYGALGILQg 1019
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 723 MAVMLILKAIRGvvfvkGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF 802
Cdd:TIGR00957 1020 FAVFGYSMAVSI-----GGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVI 1094
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 803 FCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 882
Cdd:TIGR00957 1095 GALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKV 1174
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 883 DDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVE 962
Cdd:TIGR00957 1175 DENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVE 1254
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 963 RINHYIKTlSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALF 1042
Cdd:TIGR00957 1255 RLKEYSET-EKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF 1333
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1043 RLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLES 1122
Cdd:TIGR00957 1334 RINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDH 1413
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1123 EVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLA 1202
Cdd:TIGR00957 1414 ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLD 1493
|
1210 1220
....*....|....*....|....
gi 1622900605 1203 QGQVVEFDTPSVLLSNdSSRFYAM 1226
Cdd:TIGR00957 1494 KGEVAEFGAPSNLLQQ-RGIFYSM 1516
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
46-1226 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 813.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 46 RTGVRLRGAILTMAFKKILKLKNIKEKSL--GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLG 123
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARKNFasGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 124 SAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKA---GYFQ 200
Cdd:PLN03232 447 SLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAqllSAFN 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 201 SITVGVAPIVVviaSVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMI 280
Cdd:PLN03232 527 SFILNSIPVVV---TLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILA 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 281 KNKPASPHI-KIEMKNATLAWDSShssiqnspkltpkmkkdkrasrgkkekvrqlqrtehqavlaeqkghllldsDERPs 359
Cdd:PLN03232 604 QNPPLQPGApAISIKNGYFSWDSK---------------------------------------------------TSKP- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 360 peeeegkhihlghlrlqrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLE-GSIAISGTFAYVAQQAWILNA 438
Cdd:PLN03232 632 ------------------TLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNA 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:PLN03232 694 TVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 519 HVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNlNGdyaTIFNNLLlgdtppvEINSK 598
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK-SG---SLFKKLM-------ENAGK 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 599 KETSGSQKKSQD----KGPK-TGSVKKEKAVKPEEGQ-----LVQLEEKGQGSVPWSVYGVYIQAAGGPLAFLVIMALFM 668
Cdd:PLN03232 843 MDATQEVNTNDEnilkLGPTvTIDVSERNLGSTKQGKrgrsvLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYL 922
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 669 LNVGSTAFSTWWLSYWIKQgsgnttvtrgnetsvsdSMKDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRL 748
Cdd:PLN03232 923 TTEVLRVSSSTWLSIWTDQ-----------------STPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRL 985
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 749 HDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ---NVILVFFCVGMIAGVFPWflvAVGPLVIL 825
Cdd:PLN03232 986 HDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNqlwQLLSTFALIGTVSTISLW---AIMPLLIL 1062
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 826 FSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYnKGQEFLHRYQELLDDNQAPFFLFTCAM-RWLAVRLD 904
Cdd:PLN03232 1063 FYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAY-KAYDRMAKINGKSMDNNIRFTLANTSSnRWLTIRLE 1141
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 905 LISIALITTTGLMIVLMHGQIP-----PAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKtLSLEAPARI 979
Cdd:PLN03232 1142 TLGGVMIWLTATFAVLRNGNAEnqagfASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYID-LPSEATAII 1220
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 980 KNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI 1059
Cdd:PLN03232 1221 ENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV 1300
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1060 SDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLL 1139
Cdd:PLN03232 1301 AKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLL 1380
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1140 CIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1219
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
....*..
gi 1622900605 1220 SSRFYAM 1226
Cdd:PLN03232 1461 TSAFFRM 1467
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-1235 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 666.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 33 RSWSLALTWALNYRTGvrLRGAILTMAFKKILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYN 112
Cdd:PTZ00243 304 RFYYISIRCGLQYRSA--LNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 113 VIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRI 192
Cdd:PTZ00243 382 SRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRY 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 193 LEKAGYFQSIT--VGVAPIVVVIASVvtFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFkS 270
Cdd:PTZ00243 462 LRDVQLARVATsfVNNATPTLMIAVV--FTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRI-S 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 271 LFL------------MEE-VHMIKNKPASPHIKIEMKNAtlawdSSHSSIQNSPKLTPKMK----------------KDK 321
Cdd:PTZ00243 539 TFLecdnatcstvqdMEEyWREQREHSTACQLAAVLENV-----DVTAFVPVKLPRAPKVKtsllsralrmlcceqcRPT 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 322 RASRGKKEKVRQLQRTEHQAVLAEQKGHLLLDSDERPSPEEEEGKHIHLG-----HLRLQRTLHSIDLEIQEGKLVGICG 396
Cdd:PTZ00243 614 KRHPSPSVVVEDTDYGSPSSASRHIVEGGTGGGHEATPTSERSAKTPKMKtddffELEPKVLLRDVSVSVPRGKLTVVLG 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 397 SVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDL 476
Cdd:PTZ00243 694 ATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLE 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 477 TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIF 556
Cdd:PTZ00243 774 TEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVA 853
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 557 MKEGCITERGTHEELMNlNGDYATIFNNLLL------GDTPP----VEINSKKETSGSQKKSQDKGPKTGSVKkeKAVKP 626
Cdd:PTZ00243 854 LGDGRVEFSGSSADFMR-TSLYATLAAELKEnkdskeGDADAevaeVDAAPGGAVDHEPPVAKQEGNAEGGDG--AALDA 930
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 627 EEGQLVQLEEKGQGSVPWSVYGVYIQAAGGPLAFLVIMALFMLNVGSTAFSTWWLSYWikqgsgnTTvtrgNETSVSDSM 706
Cdd:PTZ00243 931 AAGRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMW-------ST----RSFKLSAAT 999
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 707 kdnprmqyYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVR 786
Cdd:PTZ00243 1000 --------YLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNT 1071
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 787 LPfqaeMFIQNVILVFF--CVGMIAGVF--PWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGL 862
Cdd:PTZ00243 1072 LP----MSYLYLLQCLFsiCSSILVTSAsqPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGS 1147
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 863 ATIHAYNKG----QEFLHRyqelLDDNQAPFFLFTCAMRWLAVRLDLIS------IALITTTGLMIVLMHGQIppAYAGL 932
Cdd:PTZ00243 1148 ATITAYGKAhlvmQEALRR----LDVVYSCSYLENVANRWLGVRVEFLSnivvtvIALIGVIGTMLRATSQEI--GLVSL 1221
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 933 AISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEA----------------------------PARIKNKAP 984
Cdd:PTZ00243 1222 SLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEDmpeldeevdalerrtgmaadvtgtvviePASPTSAAP 1301
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 985 SPdwPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGL 1064
Cdd:PTZ00243 1302 HP--VQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGL 1379
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1065 ADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARA 1144
Cdd:PTZ00243 1380 RELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1145 LLRHCKILIL-DEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRF 1223
Cdd:PTZ00243 1460 LLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
|
1290
....*....|..
gi 1622900605 1224 YAMFAAAENKVA 1235
Cdd:PTZ00243 1540 HSMVEALGRSEA 1551
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
656-968 |
0e+00 |
|
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: 537.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 656 GPLAFLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGNETSVSDSMKDNPRMQYYASIYALSMAVMLILKAIRGV 735
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 736 VFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWF 815
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 816 LVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCA 895
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 896 MRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 968
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
73-1231 |
1.36e-152 |
|
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: 496.74 E-value: 1.36e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 73 SLGELINICSNDGQRMFEAAAVGSLLAGGPVVAIL--GMIYNviILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVA 150
Cdd:TIGR01271 177 STGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILlmGLIWE--LLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 151 ATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAG---YFQSITVGVAPIVVVIASVVTFSVHMTLgf 227
Cdd:TIGR01271 255 KISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAylrYFYSSAFFFSGFFVVFLSVVPYALIKGI-- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 228 dlTAAQAFTvvTVFNSMTFALKVT---PFSVKSLSEASVAVDRFKSLFLMEEVHMIKNKPASPhiKIEMKNATLAWDSSH 304
Cdd:TIGR01271 333 --ILRRIFT--TISYCIVLRMTVTrqfPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTT--EVEMVNVTASWDEGI 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 305 SSIqnspkltpkmkkdkrasrgkKEKVRQlqrtehqavlaeqkghlllDSDERPSPEEEEGKHIHLGHLRLQRTLHSIDL 384
Cdd:TIGR01271 407 GEL--------------------FEKIKQ-------------------NNKARKQPNGDDGLFFSNFSLYVTPVLKNISF 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 385 EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCCL 464
Cdd:TIGR01271 448 KLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQL 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 465 RPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQ 544
Cdd:TIGR01271 528 EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSK 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 545 LQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF-------------NNLLLGDT--------------------- 590
Cdd:TIGR01271 608 LEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLlgleafdnfsaerRNSILTETlrrvsidgdstvfsgpetikq 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 591 ----PPVEINSKKETS------GSQKKSQ--DKGPKTGSVKKEKAVKPEEGQ----LVQLEEKGQGSVP----------- 643
Cdd:TIGR01271 688 sfkqPPPEFAEKRKQSiilnpiASARKFSfvQMGPQKAQATTIEDAVREPSErkfsLVPEDEQGEESLPrgnqyhhglqh 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 --------------------------------------------------------------------------------
Cdd:TIGR01271 768 qaqrrqsvlqlmthsnrgenrreqlqtsfrkkssitqqnelaseldiysrrlskdsvyeiseeineedlkecfaderenv 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 644 -----WSVYGVYIqAAGGPLAFLVIMAL--FMLNVGSTAFSTWWLS---YWIKQGSGNTTVTRgNETSVSDSMKDNPRMQ 713
Cdd:TIGR01271 848 fetttWNTYLRYI-TTNRNLVFVLIFCLviFLAEVAASLLGLWLITdnpSAPNYVDQQHANAS-SPDVQKPVIITPTSAY 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 714 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 793
Cdd:TIGR01271 926 YIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFD 1005
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 794 FIQNVILVFFCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQE 873
Cdd:TIGR01271 1006 FIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSY 1085
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 874 FLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHgQIPPAYAGLAISYAVQLTGLFQFTVRLASE 953
Cdd:TIGR01271 1086 FETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTN-QDGEGEVGIILTLAMNILSTLQWAVNSSID 1164
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 954 TEARFTSVERINHYI-------------KTLSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKP 1020
Cdd:TIGR01271 1165 VDGLMRSVSRVFKFIdlpqeeprpsgggGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEG 1244
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1021 KEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQI 1100
Cdd:TIGR01271 1245 GQRVGLLGRTGSGKSTLLSALLRLLSTEGE-IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEI 1323
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1101 WDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADC 1180
Cdd:TIGR01271 1324 WKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC 1403
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1181 TMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAMFAAAE 1231
Cdd:TIGR01271 1404 TVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAMSAAD 1453
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
992-1212 |
1.26e-136 |
|
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: 414.58 E-value: 1.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 992 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1071
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1151
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1152 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 1212
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
1-268 |
8.24e-128 |
|
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: 393.85 E-value: 8.24e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1 MVKHLLEYTQATESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTMAFKKILKLKNIKEKSLGELINI 80
Cdd:cd18592 20 LIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRSLGDKSVGELINI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 81 CSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMN 160
Cdd:cd18592 100 FSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 161 EVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLTAAQAFTVVTV 240
Cdd:cd18592 180 EILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLTAAQAFTVIAV 259
|
250 260
....*....|....*....|....*...
gi 1622900605 241 FNSMTFALKVTPFSVKSLSEASVAVDRF 268
Cdd:cd18592 260 FNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
714-1229 |
1.34e-116 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 375.27 E-value: 1.34e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 714 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 793
Cdd:COG1132 62 LLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 794 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLVILFSVLHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQ 872
Cdd:COG1132 142 LVRSVVTLIGALVVLFVIDWRLaLIVLLVLPLLLLVLRLFGR-RLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 873 EFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLI---SIALITTTGLMIVLmHGQIPPAYAGLAISYAVQLTGLFQFTVR 949
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLgnlGLALVLLVGGLLVL-SGSLTVGDLVAFILYLLRLFGPLRQLAN 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 950 LASETEARFTSVERINHYiktlsLEAPARIKNKA-PSPDWPQEGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVG 1028
Cdd:COG1132 300 VLNQLQRALASAERIFEL-----LDEPPEIPDPPgAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1029 RTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALE 1105
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAK 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1106 RTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTI 1185
Cdd:COG1132 452 AAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI 531
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1622900605 1186 AHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFAA 1229
Cdd:COG1132 532 AHRLSTIRNADRILVLDDGRIVEQGTHEELLARG-GLYARLYRL 574
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
378-560 |
6.46e-110 |
|
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: 342.91 E-value: 6.46e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 378 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNS 457
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 458 VLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLK-SK 536
Cdd:cd03250 100 VIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLnNK 179
|
170 180
....*....|....*....|....
gi 1622900605 537 TVLFVTHQLQYLVDCDEVIFMKEG 560
Cdd:cd03250 180 TRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
660-968 |
1.26e-103 |
|
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: 329.46 E-value: 1.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 660 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGnetsvsdsmkdnprmQYYASIYALSMAVMLILKAIRGVVFVK 739
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG---------------YYLGVYAALLVLASVLLVLLRWLLFVL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 740 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 819
Cdd:cd18580 66 AGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 820 GPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWL 899
Cdd:cd18580 146 PPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 900 AVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 968
Cdd:cd18580 226 GLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
713-1228 |
8.72e-99 |
|
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: 331.03 E-value: 8.72e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 713 QYYASIYALSMAVML------ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVR 786
Cdd:COG2274 190 QDLSTLWVLAIGLLLallfegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 787 LPFQAEMFIQNVILVFFCVGMIAGVFPWF----LVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSpflsHITSSIQGL 862
Cdd:COG2274 269 LTGSLLTALLDLLFVLIFLIVLFFYSPPLalvvLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQS----LLVETLRGI 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 863 ATIHAYNKGQEFLHRYQELLDDNQAPFFlftcAMRWLAVRLDLISIAL--ITTTGLMIV----LMHGQIPP-------AY 929
Cdd:COG2274 345 ETIKALGAESRFRRRWENLLAKYLNARF----KLRRLSNLLSTLSGLLqqLATVALLWLgaylVIDGQLTLgqliafnIL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 930 AGLAISYAVQLTGLFQftvRLAsetEARfTSVERINHYIKTLSLEAPARIKNKAPSPdwpqEGEVTFENAEMRYRENLPL 1009
Cdd:COG2274 421 SGRFLAPVAQLIGLLQ---RFQ---DAK-IALERLDDILDLPPEREEGRSKLSLPRL----KGDIELENVSFRYPGDSPP 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL 1089
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1090 ---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1166
Cdd:COG2274 570 tlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE 647
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1167 LLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFA 1228
Cdd:COG2274 648 AIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARK-GLYAELVQ 708
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
988-1212 |
3.44e-98 |
|
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: 311.27 E-value: 3.44e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 988 WPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL 1067
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1068 RSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALerthmkeciaqlplklesEVMENGDNFSVGERQLLCIARALLR 1147
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1148 HCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTP 1212
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
660-967 |
6.46e-87 |
|
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: 283.99 E-value: 6.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 660 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTvtrgnetsvsdsmKDNPRMQYYASIYALSMAVMLILKAIRGVVFVK 739
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGT-------------QDTEQRDYRLGVYGALGLGQAIFVFLGSLALAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 740 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 819
Cdd:cd18603 68 GCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 820 GPLVILFsvlHIVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAM 896
Cdd:cd18603 148 IPLAILY---FFIQRFYVatsRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSN 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 897 RWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 967
Cdd:cd18603 225 RWLAVRLEFLGNLIVLFAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
660-967 |
1.16e-85 |
|
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: 280.13 E-value: 1.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 660 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTvtrgnetsvsdsmkdnprmQYYASIYALSMAVMLILKAIRGVVFVK 739
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDFFGLSQ-------------------GFYIGIYAGLGVLQAIFLFLFGLLLAY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 740 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 819
Cdd:cd18606 62 LGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 820 GPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWL 899
Cdd:cd18606 142 PPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 900 AVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 967
Cdd:cd18606 222 AIRLDLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
660-968 |
2.96e-82 |
|
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: 271.26 E-value: 2.96e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 660 FLVIMALFMLNVGSTAFSTWWLSYWikqGSGNTTVTRGNETSVSdsmkdnprMQYYASIYALSMAVMLILKAIRGVVFVK 739
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIW---ASAYETSSALPPSEVS--------VLYYLGIYALISLLSVLLGTLRYLLFFF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 740 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 819
Cdd:cd18604 70 GSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 820 GPLVILFSVlhiVSRVLI---RELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAM 896
Cdd:cd18604 150 VVLAALYVY---IGRLYLrasRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 897 RWLAVRLDLISIALITTTGLMIVLMHGqIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 968
Cdd:cd18604 227 RWLSVRIDLLGALFSFATAALLVYGPG-IDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
660-968 |
2.97e-82 |
|
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: 271.33 E-value: 2.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 660 FLVIMALFMLNVGSTAFSTWWLSYWIkqgsgnttvtrgNETSVSDSMKDNPRMQYYASIYALSMAVMLILKAIRGVVFVK 739
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWV------------SHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 740 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVilvFFCVGMIAGV---FPWFL 816
Cdd:cd18605 69 GGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQL---FGLLGYLVVIcyqLPWLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 817 VAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAM 896
Cdd:cd18605 146 LLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAAS 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 897 RWLAVRLDLISIALITTTGLMIVLMH---GQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 968
Cdd:cd18605 226 QWLSIRLQLLGVLIVTFVALTAVVQHffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
656-967 |
6.94e-80 |
|
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: 265.34 E-value: 6.94e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 656 GPLAFLVIMALFMLNVGSTAFSTWWLSYWiKQGSGNTTVTRGNETSVSDSMKDNPRMQ--YYASIYALSMAVMLILKAIR 733
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYW-ANLEEKLNDTTDRVQGENSTNVDIEDLDrdFNLGIYAGLTAATFVFGFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 734 GVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFP 813
Cdd:cd18601 80 SLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 814 WFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFT 893
Cdd:cd18601 160 WVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 894 CAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 967
Cdd:cd18601 240 ATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
992-1223 |
1.73e-77 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 256.37 E-value: 1.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 992 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1071
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1151
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1152 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRF 1223
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
719-1219 |
6.12e-75 |
|
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: 259.69 E-value: 6.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 719 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV---R-LP-- 788
Cdd:COG4988 60 LLGLLLAVLLLRALlawlRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfaRyLPql 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 789 FQAeMFIQNVILVF-FCVGMIAGVFpwfLVAVGPLVILFSVL-HIVSRVLIRelKRLDNITQspfLS-HITSSIQGLATI 865
Cdd:COG4988 140 FLA-ALVPLLILVAvFPLDWLSGLI---LLVTAPLIPLFMILvGKGAAKASR--RQWRALAR---LSgHFLDRLRGLTTL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 866 HAYNKGQEFLHRYQELLDDnqapfflFTCA-MRWLavRLDLISIA---LITTTGLMIV-------LMHGQIPPAyAGLAI 934
Cdd:COG4988 211 KLFGRAKAEAERIAEASED-------FRKRtMKVL--RVAFLSSAvleFFASLSIALVavyigfrLLGGSLTLF-AALFV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 935 syaVQLTGLFQFTVR-LASETEARFTSV---ERInhyIKTLSLEAPARIKNKAPSPdWPQEGEVTFENAEMRYRENLPlV 1010
Cdd:COG4988 281 ---LLLAPEFFLPLRdLGSFYHARANGIaaaEKI---FALLDAPEPAAPAGTAPLP-AAGPPSIELEDVSFSYPGGRP-A 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLD 1090
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLR 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1091 PFN-QYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLI 1169
Cdd:COG4988 433 LGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1170 QETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1219
Cdd:COG4988 513 LQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
660-967 |
1.45e-74 |
|
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: 249.83 E-value: 1.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 660 FLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTrgneTSVSDSMKDNPRMQYYASIYALSMAVMLILKAIRGVVFVK 739
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASVV----FNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 740 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAV 819
Cdd:cd18602 77 AGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 820 GPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWL 899
Cdd:cd18602 157 IPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 900 AVRLDLISiALITTTGLMIVL---MHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHY 967
Cdd:cd18602 237 GIRLDYLG-AVIVFLAALSSLtaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
741-1228 |
5.42e-71 |
|
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: 248.53 E-value: 5.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 741 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD-----VRLPFqaemfIQNVILVFFCVGMIAGVFPWF 815
Cdd:COG4987 83 TLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDnlylrVLLPL-----LVALLVILAAVAFLAFFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 816 --LVAVGPLVILFSVLHIVSRV---LIRELKRLdnitQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQApff 890
Cdd:COG4987 158 alVLALGLLLAGLLLPLLAARLgrrAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAA--- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 891 lftcAMRWLAvRLDLISIALIT-TTGLMIVLM---------HGQIPPAYAG------LAISYAVQ-LTGLFQFTVRLASe 953
Cdd:COG4987 231 ----AQRRLA-RLSALAQALLQlAAGLAVVAVlwlaaplvaAGALSGPLLAllvlaaLALFEALApLPAAAQHLGRVRA- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 954 tearftSVERINHyiktLSLEAPARIKNKAPSPDwPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSG 1033
Cdd:COG4987 305 ------AARRLNE----LLDAPPAVTEPAEPAPA-PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1034 KSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMK 1110
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLG 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1111 ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLH 1190
Cdd:COG4987 452 DWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLA 531
|
490 500 510
....*....|....*....|....*....|....*...
gi 1622900605 1191 TVLGSDRIMVLAQGQVVEFDTPSVLLSNDsSRFYAMFA 1228
Cdd:COG4987 532 GLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
992-1216 |
9.48e-69 |
|
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: 230.58 E-value: 9.48e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 992 GEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1071
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSGTVRSNLDPFNQY-TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1150
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 1151 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLL 1216
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
715-1233 |
1.44e-62 |
|
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: 224.21 E-value: 1.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 715 YASIYALSMAVMLILKAIRGvvfvkgtlrassrlhdELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 794
Cdd:TIGR02203 72 FVSTYLLSWVSNKVVRDIRV----------------RMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 795 IQNVILVFFCVGMIAgVFPWFLVAVgpLVILFSVLHIVSRVLIRELKRLDNITQSPF--LSHITS-SIQGLATIHAYNkG 871
Cdd:TIGR02203 136 VRETLTVIGLFIVLL-YYSWQLTLI--VVVMLPVLSILMRRVSKRLRRISKEIQNSMgqVTTVAEeTLQGYRVVKLFG-G 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 872 QEF-LHRYQELlddnqapfflfTCAMRWLAVRLD------------LISIALITTtgLMIVLMHGQIPPAYAGLAISYAV 938
Cdd:TIGR02203 212 QAYeTRRFDAV-----------SNRNRRLAMKMTsagsisspitqlIASLALAVV--LFIALFQAQAGSLTAGDFTAFIT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 939 QLTGLFQFTVRLA---SETEARFTSVERINHYIKT-LSLEAPARIKNKApspdwpqEGEVTFENAEMRYRENLPLVLKKV 1014
Cdd:TIGR02203 279 AMIALIRPLKSLTnvnAPMQRGLAAAESLFTLLDSpPEKDTGTRAIERA-------RGDVEFRNVTFRYPGRDRPALDSI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1015 SFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DP 1091
Cdd:TIGR02203 352 SLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1092 fNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQE 1171
Cdd:TIGR02203 432 -EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQA 510
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1172 TIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAMFAAAENK 1233
Cdd:TIGR02203 511 ALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG--LYAQLHNMQFR 570
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
994-1227 |
1.56e-62 |
|
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: 212.86 E-value: 1.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1073
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 1148
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1149 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLsNDSSRFYAMF 1227
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMW 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
994-1205 |
2.02e-62 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 209.93 E-value: 2.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1073
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILI 1153
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1154 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQ 1205
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
75-583 |
5.68e-62 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 222.73 E-value: 5.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 75 GELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGP--TGFLGSAVFILFYPAMMFASRLTAYFRRKcVAAT 152
Cdd:COG1132 118 GDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWrlALIVLLVLPLLLLVLRLFGRRLRKLFRRV-QEAL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 153 DERVQKMNEVLTYIKFIKMYA----WVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIasVVTFSVHMTLGFD 228
Cdd:COG1132 197 AELNGRLQESLSGIRVVKAFGreerELERFREANEELRRANLRAARLSALFFPLMELLGNLGLAL--VLLVGGLLVLSGS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 229 LTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLflMEEVHMIKNKPASPHIK-----IEMKNATLAWDss 303
Cdd:COG1132 275 LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL--LDEPPEIPDPPGAVPLPpvrgeIEFENVSFSYP-- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 304 hssiqnspkltpkmkkdkrasrgkkekvrqlqrtehqavlaeqkghllldsDERPspeeeegkhihlghlrlqrTLHSID 383
Cdd:COG1132 351 ---------------------------------------------------GDRP-------------------VLKDIS 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 384 LEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNILFGK-E 449
Cdd:COG1132 361 LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdirdltleslrrqIGVVPQDTFLFSGTIRENIRYGRpD 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 450 YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsAI 529
Cdd:COG1132 441 ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQE-AL 519
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 530 RKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 583
Cdd:COG1132 520 ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
994-1226 |
3.48e-61 |
|
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: 209.01 E-value: 3.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1073
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSGTVRSNLdpfnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRH 1148
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1149 CKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSsrFYAM 1226
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGG--VYAK 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
378-560 |
5.64e-60 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 204.87 E-value: 5.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 378 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS-----------------GTFAYVAQQAWILNATL 440
Cdd:cd03290 16 TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesepsfeatrsrnrYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 441 RDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 520
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900605 521 GNHIFNSAIRKHLK--SKTVLFVTHQLQYLVDCDEVIFMKEG 560
Cdd:cd03290 176 SDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
719-1208 |
5.89e-60 |
|
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: 217.38 E-value: 5.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 719 YALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTG---RILNRFSKDMDEVdVRlpfqaeMFI 795
Cdd:COG5265 84 YGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGglsRDIERGTKGIEFL-LR------FLL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 796 QNVILVFFCVGMIAGVF-----PWF----LVAVGpLVILFSVLHIVSRV-LIRELKRLDNITQSpflsHITSSIQGLATI 865
Cdd:COG5265 157 FNILPTLLEIALVAGILlvkydWWFalitLVTVV-LYIAFTVVVTEWRTkFRREMNEADSEANT----RAVDSLLNYETV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 866 HAYNkGQEF-LHRYQELLDDnqapfflFTCAMRWLAVRLDLISI--ALITTTGLMIVL-------MHGQIPPAYAGLAIS 935
Cdd:COG5265 232 KYFG-NEAReARRYDEALAR-------YERAAVKSQTSLALLNFgqALIIALGLTAMMlmaaqgvVAGTMTVGDFVLVNA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 936 YAVQLT---GLFQFTVRlasETEARFTSVERInhyiKTLsLEAPARIKNKAPSPDWP-QEGEVTFENAEMRYRENLPlVL 1011
Cdd:COG5265 304 YLIQLYiplNFLGFVYR---EIRQALADMERM----FDL-LDQPPEVADAPDAPPLVvGGGEVRFENVSFGYDPERP-IL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1012 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLdp 1091
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI-- 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1092 fnQY-----TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1166
Cdd:COG5265 453 --AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622900605 1167 LLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1208
Cdd:COG5265 531 RAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
717-1229 |
4.48e-57 |
|
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: 208.40 E-value: 4.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 717 SIYALSMAVMLILKAIRGVVFVKGTL---RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 793
Cdd:TIGR02204 59 RYFAFLLVVALVLALGTAARFYLVTWlgeRVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSM 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 794 FIQNVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVLhivsrvLIRELKRLDNITQSPFL---SHITSSIQGLATIHA 867
Cdd:TIGR02204 139 ALRNALMCIGGLIMMFITSPkltSLVLLAVPLVLLPILL------FGRRVRKLSRESQDRIAdagSYAGETLGAIRTVQA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 868 YNKGQEFLHRYQELLDDNqapfflFTCAMRWLAVRLDLISIAL-ITTTGLMIVL-------MHGQIPPAYAGLAISYAVQ 939
Cdd:TIGR02204 213 FGHEDAERSRFGGAVEKA------YEAARQRIRTRALLTAIVIvLVFGAIVGVLwvgahdvIAGKMSAGTLGQFVFYAVM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 940 LTGLFQFTVRLASETEARFTSVERINHYIKTLS-LEAPARIKnkapSPDWPQEGEVTFENAEMRY--RENLPlVLKKVSF 1016
Cdd:TIGR02204 287 VAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdIKAPAHPK----TLPVPLRGEIEFEQVNFAYpaRPDQP-ALDGLNL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1017 TIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFN-QY 1095
Cdd:TIGR02204 362 TVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRpDA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1096 TEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE 1175
Cdd:TIGR02204 442 TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALET 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 1176 AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSndSSRFYAMFAA 1229
Cdd:TIGR02204 522 LMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA--KGGLYARLAR 573
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
376-576 |
1.76e-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: 206.15 E-value: 1.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRD 442
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWVPQNPYLFAGTIRE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 521
Cdd:COG4988 430 NLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 522 NHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 576
Cdd:COG4988 510 AEILQ-ALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
994-1219 |
1.27e-55 |
|
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: 193.14 E-value: 1.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1071
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSGTVRSNL-----DPfnqyTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALL 1146
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1147 RHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1219
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
72-584 |
4.55e-54 |
|
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: 202.37 E-value: 4.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 72 KSLGELINicsndgqRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGS---AVFILFYPAMMFASRLTAYFRRKC 148
Cdd:COG2274 250 RSVGDLAS-------RFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPplaLVVLLLIPLYVLLGLLFQPRLRRL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 149 VAATDERVQKMN----EVLTYIKFIKMYA--------WVKAFSQSVqKIREEERRILEKAGYFQSITVGVAPIVVVIASV 216
Cdd:COG2274 323 SREESEASAKRQsllvETLRGIETIKALGaesrfrrrWENLLAKYL-NARFKLRRLSNLLSTLSGLLQQLATVALLWLGA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 217 vtFSV---HMTLGfDLTAAQAFtVVTVFNSMT-FALKVTpfsvkSLSEASVAVDRFKSLFLME-EVHMIKNKPASPHIK- 290
Cdd:COG2274 402 --YLVidgQLTLG-QLIAFNIL-SGRFLAPVAqLIGLLQ-----RFQDAKIALERLDDILDLPpEREEGRSKLSLPRLKg 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 291 -IEMKNATLawdsshssiqnspkltpkmkkdkrasrgkkekvrqlqrtehqavlaeqkghllldsdeRPSPEEEEgkhih 369
Cdd:COG2274 473 dIELENVSF----------------------------------------------------------RYPGDSPP----- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 370 lghlrlqrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWIL 436
Cdd:COG2274 490 --------VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIdlrqidpaslrrqIGVVLQDVFLF 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 437 NATLRDNILFGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:COG2274 562 SGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 516 LDAHvGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 584
Cdd:COG2274 642 LDAE-TEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
31-267 |
8.96e-54 |
|
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: 190.00 E-value: 8.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 31 IVRSWSLALTWALNYRTGVRLRGAILTMAFkkilklknikEKSL------------GELINICSNDGQRMFEAAAVGSLL 98
Cdd:cd18579 50 LLQSLLLHQYFFLSFRLGMRVRSALSSLIY----------RKALrlsssarqetstGEIVNLMSVDVQRIEDFFLFLHYL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 99 AGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAF 178
Cdd:cd18579 120 WSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 179 SQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSL 258
Cdd:cd18579 200 LKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSL 279
|
....*....
gi 1622900605 259 SEASVAVDR 267
Cdd:cd18579 280 IEALVSLKR 288
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
717-1218 |
2.98e-53 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 199.95 E-value: 2.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 717 SIYALSM--AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 794
Cdd:TIGR00958 203 AIFFMCLlsIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 795 IQNVILVFFCVGMIAGVFPWF----LVAVGPLVILFSVLHIVSRVLIRELKrlDNITQSPFLSHitSSIQGLATIHAY-N 869
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 870 KGQEfLHRYQELLDDnqapfflftcaMRWLAVRLDLISIALITTTGLM------IVL-------MHGQIPpayAGLAIS- 935
Cdd:TIGR00958 359 EEGE-ASRFKEALEE-----------TLQLNKRKALAYAGYLWTTSVLgmliqvLVLyyggqlvLTGKVS---SGNLVSf 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 936 --YAVQLTGLFQFTVRLASETEARFTSVERINHYI-KTLSLEAPARIknkAPSPDwpqEGEVTFENAEMRY--RENLPlV 1010
Cdd:TIGR00958 424 llYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLdRKPNIPLTGTL---APLNL---EGLIEFQDVSFSYpnRPDVP-V 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLD 1090
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1091 -PFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLI 1169
Cdd:TIGR00958 577 yGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1622900605 1170 QETirEAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:TIGR00958 657 QES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
992-1207 |
3.50e-53 |
|
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: 185.49 E-value: 3.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 992 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKL 1071
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSGTVRSNLDPFNQYTEDQ-IWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1150
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1151 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVV 1207
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
992-1221 |
2.90e-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: 185.06 E-value: 2.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 992 GEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcIKIDGVRISDIGLADLRSKL 1071
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGD-IQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKI 1151
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1152 LILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSS 1221
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
379-588 |
9.30e-52 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 183.90 E-value: 9.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSV 458
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 459 LNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTV 538
Cdd:cd03291 133 VKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTR 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900605 539 LFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDyatiFNNLLLG 588
Cdd:cd03291 213 ILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPD----FSSKLMG 258
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
994-1220 |
1.20e-50 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 178.83 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1073
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1150
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1151 ILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 1220
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
379-579 |
1.17e-49 |
|
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: 186.13 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 445
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFDTTLRENLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 524
Cdd:COG4987 431 LARPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 525 FNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:COG4987 511 LA-DLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
720-1201 |
3.09e-47 |
|
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: 178.25 E-value: 3.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 720 ALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDvrlPFQAEMFI 795
Cdd:TIGR02857 47 LGALALVLLLRAllgwLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALD---GYFARYLP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 796 QNVILVFFCVGMIAGVFP--W----FLVAVGPLVILFSVL--HIVSRVLIRELKRLDNITqspflSHITSSIQGLATIHA 867
Cdd:TIGR02857 124 QLVLAVIVPLAILAAVFPqdWisglILLLTAPLIPIFMILigWAAQAAARKQWAALSRLS-----GHFLDRLRGLPTLKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 868 YNKGqeflHRYQELLDDNQAPF-----------FLFTCAMRWLAVrldlISIALITTT-GLMivLMHGQIPPAYAGLAIS 935
Cdd:TIGR02857 199 FGRA----KAQAAAIRRSSEEYrertmrvlriaFLSSAVLELFAT----LSVALVAVYiGFR--LLAGDLDLATGLFVLL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 936 YAVQltglFQFTVR-LASETEARFTSVERINHyIKTLsLEAPARIK-NKAPSPdWPQEGEVTFENAEMRYrENLPLVLKK 1013
Cdd:TIGR02857 269 LAPE----FYLPLRqLGAQYHARADGVAAAEA-LFAV-LDAAPRPLaGKAPVT-AAPASSLEFSGVSVAY-PGRRPALRP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---D 1090
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1091 PfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQ 1170
Cdd:TIGR02857 421 P--DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
490 500 510
....*....|....*....|....*....|.
gi 1622900605 1171 ETIREAFADCTMLTIAHRLHTVLGSDRIMVL 1201
Cdd:TIGR02857 499 EALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
751-1229 |
4.47e-47 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 179.00 E-value: 4.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 751 ELFRRILRSPMKFFDTTPTGRILNRFSKDMDEV-DVRLPFQAEMFIQNVILVFFCVgmIAGVFPWFLVAVgpLVILFSVL 829
Cdd:PRK13657 94 EYFERIIQLPLAWHSQRGSGRALHTLLRGTDALfGLWLEFMREHLATLVALVVLLP--LALFMNWRLSLV--LVVLGIVY 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 830 HIVSRVLIRELKRLDNITQ---SPFLSHITSSIQGLATIHAYNKGQ---EFLHRYQELLDDNQAPfflftcAMRWLAVRL 903
Cdd:PRK13657 170 TLITTLVMRKTKDGQAAVEehyHDLFAHVSDAIGNVSVVQSYNRIEaetQALRDIADNLLAAQMP------VLSWWALAS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 904 DL------ISIALITTTGLMIVLmHGQIPP----AYAGLAISYAVQLTGLFQFTVRLasetearFTSVERINHYIKTLsl 973
Cdd:PRK13657 244 VLnraastITMLAILVLGAALVQ-KGQLRVgevvAFVGFATLLIGRLDQVVAFINQV-------FMAAPKLEEFFEVE-- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 974 EAPARIKNKAPSPDWPQ-EGEVTFENAEMRYrENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI 1052
Cdd:PRK13657 314 DAVPDVRDPPGAIDLGRvKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1053 KIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL-----DPfnqyTEDQIWDALERTHMKECIAQLPLKLESEVMEN 1127
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGER 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1128 GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVV 1207
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
490 500
....*....|....*....|....*
gi 1622900605 1208 E---FDTpsvlLSNDSSRFYAMFAA 1229
Cdd:PRK13657 549 EsgsFDE----LVARGGRFAALLRA 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
752-1219 |
7.00e-47 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 178.29 E-value: 7.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 752 LFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD----------VRlpfQAEMFIQNVILVFFcvgmiagvFPWFLVavgp 821
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAssssgalitvVR---EGASIIGLFIMMFY--------YSWQLS---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 822 lVILFSVLHIVSrVLIREL-KRLDNIT---QSPfLSHITSS----IQGLATIHAYNkGQEF-LHRYQELLDDnqapfflf 892
Cdd:PRK11176 169 -LILIVIAPIVS-IAIRVVsKRFRNISknmQNT-MGQVTTSaeqmLKGHKEVLIFG-GQEVeTKRFDKVSNR-------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 893 tcaMRWLAVRL---DLIS---IALITTTGLMIVLMHGQIPPAYAGL-AISYAVQLTGLFQFTVRLASETE--ARFtsvER 963
Cdd:PRK11176 237 ---MRQQGMKMvsaSSISdpiIQLIASLALAFVLYAASFPSVMDTLtAGTITVVFSSMIALMRPLKSLTNvnAQF---QR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 964 INHYIKTL----SLEAPariKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGM 1039
Cdd:PRK11176 311 GMAACQTLfailDLEQE---KDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1040 ALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLD--PFNQYTEDQIWDALERTHMKECIAQLP 1117
Cdd:PRK11176 388 LLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMD 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1118 LKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDR 1197
Cdd:PRK11176 468 NGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADE 547
|
490 500
....*....|....*....|..
gi 1622900605 1198 IMVLAQGQVVEFDTPSVLLSND 1219
Cdd:PRK11176 548 ILVVEDGEIVERGTHAELLAQN 569
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
757-1227 |
1.13e-45 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 174.91 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 757 LRSPMKFFDTTPTGRILNRFSKDMdEVdVRlpfqaEMFIQNVILVFFCVGMIAGV------FPW--FLVAVG--PLVILF 826
Cdd:PRK10790 109 LRQPLSAFDTQPVGQLISRVTNDT-EV-IR-----DLYVTVVATVLRSAALIGAMlvamfsLDWrmALVAIMifPAVLVV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 827 SVLH------IVSRVlirelkrldnitqSPFLSHITS----SIQGLATIHAYNKGQEFLHRyqeLLDDNQAPFflftcAM 896
Cdd:PRK10790 182 MVIYqrystpIVRRV-------------RAYLADINDgfneVINGMSVIQQFRQQARFGER---MGEASRSHY-----MA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 897 RWLAVRLD------LISI--ALITTtGLMivLMHGQIPPAYAGLAISYA-VQLTG-----LFQFTVRLASETEArFTSVE 962
Cdd:PRK10790 241 RMQTLRLDgfllrpLLSLfsALILC-GLL--MLFGFSASGTIEVGVLYAfISYLGrlnepLIELTTQQSMLQQA-VVAGE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 963 RInhyiktlsLEAPARIKNKAPSPDWP-QEGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL 1041
Cdd:PRK10790 317 RV--------FELMDGPRQQYGNDDRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1042 FRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLE 1121
Cdd:PRK10790 388 MGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLY 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1122 SEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVL 1201
Cdd:PRK10790 468 TPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVL 547
|
490 500
....*....|....*....|....*.
gi 1622900605 1202 AQGQVVEFDTPSVLLSNdSSRFYAMF 1227
Cdd:PRK10790 548 HRGQAVEQGTHQQLLAA-QGRYWQMY 572
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
991-1206 |
2.39e-45 |
|
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: 163.41 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 991 EGEVTFENAEMRYReNLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR 1068
Cdd:cd03248 9 KGIVKFQNVTFAYP-TRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1069 SKLSIIPQEPVLFSGTVRSNLD-PFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLR 1147
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1148 HCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1206
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
374-560 |
7.14e-44 |
|
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: 156.77 E-value: 7.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 374 RLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATL 440
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAYVPQDPFLFSGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 441 RDNILfgkeydeerynsvlnscclrpdlailpssdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 520
Cdd:cd03228 93 RENIL-----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622900605 521 GNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEG 560
Cdd:cd03228 132 EALILE-ALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
741-1189 |
9.38e-44 |
|
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: 167.92 E-value: 9.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 741 TLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD---VR--LPfqaemfiqnvILVFFCVGMIA-GVFPW 814
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQdlyVRviVP----------AGVALVVGAAAvAAIAV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 815 FLVAVGP-----LVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQEL------LD 883
Cdd:TIGR02868 151 LSVPAALilaagLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEAdreltrAE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 884 DNQApfflftcamRWLAVRLDLISIALITTTGLMIVL-----MHGQIPPAYagLAISYAVQLT---GLFQFTVRLASETE 955
Cdd:TIGR02868 231 RRAA---------AATALGAALTLLAAGLAVLGALWAggpavADGRLAPVT--LAVLVLLPLAafeAFAALPAAAQQLTR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 956 ARfTSVERINHYIKTLSLEAPARIKNKAPSPdwPQEGEVTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKS 1035
Cdd:TIGR02868 300 VR-AAAERIVEVLDAAGPVAEGSAPAAGAVG--LGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1036 SLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKEC 1112
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADW 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1113 IAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL 1189
Cdd:TIGR02868 454 LRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1011-1229 |
1.14e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 168.87 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG-----GCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTV 1085
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSL------LNALLGflpyqGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 RSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 1162
Cdd:PRK11174 440 RDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1163 TETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE---FDTpsvlLSNDSSRFYAMFAA 1229
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE----LSQAGGLFATLLAH 583
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
743-1217 |
7.31e-42 |
|
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: 164.74 E-value: 7.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 743 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKdMDEVDVRLpfqAEMFIQNVILVFFC----VGMIAGVFPWFLVA 818
Cdd:TIGR03797 206 RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRIL---SGSTLTTLLSGIFAllnlGLMFYYSWKLALVA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 819 VGPLVILFSVLHIVSRVLIRELKRLDNItQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRW 898
Cdd:TIGR03797 282 VALALVAIAVTLVLGLLQVRKERRLLEL-SGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 899 LAVrldLISIALITTTGLMIVLMHGQIppAYAGLAISYAVQLTGLF-QFTVRLASETEARFTSVERINHYIKTLS-LEAP 976
Cdd:TIGR03797 361 LTV---FNAVLPVLTSAALFAAAISLL--GGAGLSLGSFLAFNTAFgSFSGAVTQLSNTLISILAVIPLWERAKPiLEAL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 977 ARIKNKAPSPDwPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLveLSG------G 1050
Cdd:TIGR03797 436 PEVDEAKTDPG-KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL----LRL--LLGfetpesG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1051 CIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDN 1130
Cdd:TIGR03797 509 SVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGT 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1131 FSVGERQLLCIARALLRHCKILILDEATAAMDTETdlliQETIREAFA--DCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1208
Cdd:TIGR03797 589 LSGGQRQRLLIARALVRKPRILLFDEATSALDNRT----QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQ 664
|
....*....
gi 1622900605 1209 FDTPSVLLS 1217
Cdd:TIGR03797 665 QGTYDELMA 673
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
366-583 |
9.78e-42 |
|
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: 153.15 E-value: 9.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 366 KHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQ 432
Cdd:cd03253 4 ENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 433 AWILNATLRDNILFGKE--YDEERYNSVLnSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILD 510
Cdd:cd03253 84 TVLFNDTIGYNIRYGRPdaTDEEVIEAAK-AAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 511 DPLSALDAHVGNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 583
Cdd:cd03253 163 EATSALDTHTEREIQA-ALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
378-576 |
5.66e-41 |
|
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: 150.84 E-value: 5.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 378 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 444
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdisrkslrsmIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 445 LFGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 523
Cdd:cd03254 98 RLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 524 IfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNG 576
Cdd:cd03254 178 I-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
379-579 |
9.49e-41 |
|
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: 150.46 E-value: 9.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 445
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHI 524
Cdd:cd03251 98 YGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT-ESERL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 525 FNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:cd03251 177 VQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
644-968 |
4.59e-40 |
|
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: 151.49 E-value: 4.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 644 WSVYGVYIQAAGGPLAFLV-IMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGNETSVSDSMKDNprmQYYASIYALS 722
Cdd:cd18600 3 WNTYLRYITSHKSLIFVLIlCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSS---YYVFYIYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 723 MAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF 802
Cdd:cd18600 80 ADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 803 FCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 882
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 883 DDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQiPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVE 962
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVS 318
|
....*.
gi 1622900605 963 RINHYI 968
Cdd:cd18600 319 RIFKFI 324
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1002-1206 |
1.96e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 145.73 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1002 RYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLF 1081
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1082 SGTVRSNLD-PFN----QYTEDQIWDALERthmkeciaqlpLKLESEVME-NGDNFSVGERQLLCIARALLRHCKILILD 1155
Cdd:COG4619 87 GGTVRDNLPfPFQlrerKFDRERALELLER-----------LGLPPDILDkPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1156 EATAAMDTETDLLIQETIREAFADC--TMLTIAH------RLhtvlgSDRIMVLAQGQV 1206
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
331-557 |
3.44e-39 |
|
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: 153.98 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 331 VRQLQRTEH---QAVLAEQKGHLLLDSDERPSPEEEEGKHIHLGHLRLQ----------RTLHSIDLEIQEGKLVGICGS 397
Cdd:TIGR02857 277 LRQLGAQYHaraDGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSgvsvaypgrrPALRPVSFTVPPGERVALVGP 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 398 VGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNILFGK-EYDEERYNSVLNSCC 463
Cdd:TIGR02857 357 SGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 464 LRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHLKSKTVLFVTH 543
Cdd:TIGR02857 437 LDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTH 515
|
250
....*....|....
gi 1622900605 544 QLQYLVDCDEVIFM 557
Cdd:TIGR02857 516 RLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
959-1226 |
3.75e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 154.98 E-value: 3.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 959 TSVERINHYIktlslEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLG 1038
Cdd:PRK11160 309 ASARRINEIT-----EQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1039 MALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMkECIAQ 1115
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGL-EKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1116 LPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGS 1195
Cdd:PRK11160 461 DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF 540
|
250 260 270
....*....|....*....|....*....|.
gi 1622900605 1196 DRIMVLAQGQVVEFDTPSVLLSNDsSRFYAM 1226
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLAQQ-GRYYQL 570
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
378-562 |
6.21e-39 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 144.65 E-value: 6.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 378 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 444
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 445 LFGKEY-DEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 523
Cdd:cd03245 99 TLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEER 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622900605 524 IFnSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 562
Cdd:cd03245 179 LK-ERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
754-1225 |
7.57e-39 |
|
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: 155.67 E-value: 7.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 754 RRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemfIQNVIL-VFFCVGMIAGVfPWFLVAVGPLVILFSVLHIV 832
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDA---------LASTILsLFLDMWILVIV-GLFLVRQNMLLFLLSLLSIP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 833 SRVLI-----RELKRLDN---ITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCA---MRWLAV 901
Cdd:TIGR01193 307 VYAVIiilfkRTFNKLNHdamQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKAdqgQQAIKA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 902 RLDLISIALITTTGLMIVLMH----GQIPpAYAGLaISYavqLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEAPA 977
Cdd:TIGR01193 387 VTKLILNVVILWTGAYLVMRGkltlGQLI-TFNAL-LSY---FLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINK 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 978 RIKNKAPSPDwpqeGEVTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGV 1057
Cdd:TIGR01193 462 KKRTELNNLN----GDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1058 RISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQ--YTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGE 1135
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1136 RQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREaFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 1215
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
490
....*....|
gi 1622900605 1216 LsnDSSRFYA 1225
Cdd:TIGR01193 696 L--DRNGFYA 703
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
31-267 |
2.33e-38 |
|
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: 145.29 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 31 IVRSWSLALTWALNYRTGVRLRGAILTMAFkkilklknikEKSL------------GELINICSNDGQRMFEAAAVGSLL 98
Cdd:cd18597 54 LLSSLLLNHFFYRSMLTGAQVRAALTKAIY----------RKSLrlsgksrhefpnGKITNLMSTDLSRIDFALGFFHFL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 99 AGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAF 178
Cdd:cd18597 124 WTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 179 SQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSL 258
Cdd:cd18597 204 LERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASMLSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSL 283
|
....*....
gi 1622900605 259 SEASVAVDR 267
Cdd:cd18597 284 ADALVALKR 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
382-584 |
2.38e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 152.69 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLlEGSIAISGT-------------FAYVAQQAWILNATLRDNILFGK 448
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIelreldpeswrkhLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 449 -EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNS 527
Cdd:PRK11174 448 pDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV-MQ 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 528 AIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 584
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
379-567 |
3.48e-37 |
|
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: 139.55 E-value: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 445
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIf 525
Cdd:cd03244 100 PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALI- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900605 526 NSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 567
Cdd:cd03244 179 QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
31-267 |
1.42e-36 |
|
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: 140.71 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 31 IVRSWSLALTWALNYRTGVRLRgAILTMA----------------------FKKILKLKNIKEKSLGELINICSNDGQRM 88
Cdd:cd18596 50 LLSSLLDQQYLWIGRRLSVRLR-AILTQLifekalrrrdksgssksseskkKDKEEDEDEKSSASVGKINNLMSVDANRI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 89 FEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKF 168
Cdd:cd18596 129 SEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRM 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 169 IKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVH-MTLGFDLTAAQAFTVVTVFNSMTFA 247
Cdd:cd18596 209 IKFFAWERKWEERILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTVVTFATYtLVMGQELTASVAFTSLALFNMLRGP 288
|
250 260
....*....|....*....|
gi 1622900605 248 LKVTPFSVKSLSEASVAVDR 267
Cdd:cd18596 289 LNVLPELITQLLQAKVSLDR 308
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
471-1201 |
1.83e-36 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 150.56 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 471 LPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIFNSAIR--KHLKSKTVLFVTHQLQYL 548
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 549 -------------------VDCDEVIFMKEGC----------------------------ITERGTHEELM-NLNGDYAT 580
Cdd:PTZ00265 644 ryantifvlsnrergstvdVDIIGEDPTKDNKennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMkNKNGIYYT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 581 IFNNLllgdtppvEINSKKETSGSQKKSQDKgpKTGSVK-KEKAVKPEEGQLVQLEEKGQGSVPWSVYGVYIQA----AG 655
Cdd:PTZ00265 724 MINNQ--------KVSSKKSSNNDNDKDSDM--KSSAYKdSERGYDPDEMNGNSKHENESASNKKSCKMSDENAsennAG 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 656 GPLAFL----------------------------VIMALFMLNVGS--TAFSTWWLSYwikqgsgnttvtrgnetsVSdS 705
Cdd:PTZ00265 794 GKLPFLrnlfkrkpkapnnlrivyreifsykkdvTIIALSILVAGGlyPVFALLYAKY------------------VS-T 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 706 MKDNPRMQYYA---SIYALSMAV-MLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDT---TPtGRILNRFSK 778
Cdd:PTZ00265 855 LFDFANLEANSnkySLYILVIAIaMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINR 933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 779 DMDEVDVRLPFQAEMFIQNVILvfFCVGMIAGVFPWFLVA---VGPLVILFSVLHIVSRVLIR---ELKRL--------- 843
Cdd:PTZ00265 934 DVHLLKTGLVNNIVIFTHFIVL--FLVSMVMSFYFCPIVAavlTGTYFIFMRVFAIRARLTANkdvEKKEInqpgtvfay 1011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 844 ---DNITQSP-------FLSHITSSIQGL---------ATIHAYNKGQEFLHRYQELL--DDNQAPFFLFTCAMrWLAVR 902
Cdd:PTZ00265 1012 nsdDEIFKDPsfliqeaFYNMNTVIIYGLedyfcnlieKAIDYSNKGQKRKTLVNSMLwgFSQSAQLFINSFAY-WFGSF 1090
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 903 LdlISIALITTTGLMIVLMHGQIPPAYAGLAISyavqltglfqftvrLASETEARFTSVERINHYIKTLSL-----EAPA 977
Cdd:PTZ00265 1091 L--IRRGTILVDDFMKSLFTFLFTGSYAGKLMS--------------LKGDSENAKLSFEKYYPLIIRKSNidvrdNGGI 1154
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 978 RIKNKAPSpdwpqEGEVTFENAEMRY--RENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL-------- 1047
Cdd:PTZ00265 1155 RIKNKNDI-----KGKIEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivf 1228
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1048 ----------------------------------------------SGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLF 1081
Cdd:PTZ00265 1229 knehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF 1308
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1082 SGTVRSNLDpFNQ--YTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 1159
Cdd:PTZ00265 1309 NMSIYENIK-FGKedATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1622900605 1160 AMDTETDLLIQETIREA--FADCTMLTIAHRLHTVLGSDRIMVL 1201
Cdd:PTZ00265 1388 SLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1010-1209 |
3.60e-36 |
|
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: 136.87 E-value: 3.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvR 1086
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDP-------M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLDPfnQYT-EDQIWDALE--RTHMKECIAQLPLKLESEVMENGDN--------FSVGERQLLCIARALLRHCKILILD 1155
Cdd:cd03257 93 SSLNP--RMTiGEQIAEPLRihGKLSKKEARKEAVLLLLVGVGLPEEvlnrypheLSGGQRQRVAIARALALNPKLLIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1156 EATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEF 1209
Cdd:cd03257 171 EPTSALDVSVqaqilDLLKK--LQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVEE 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
379-579 |
3.34e-35 |
|
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: 134.59 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 445
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FGKEY--DEERyNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNH 523
Cdd:cd03249 99 YGKPDatDEEV-EEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES-EK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 524 IFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1011-1159 |
4.36e-35 |
|
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: 130.85 E-value: 4.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSG-TVRSNL 1089
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1090 -------DPFNQYTEDQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATA 1159
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEK-------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
378-583 |
4.44e-35 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 142.55 E-value: 4.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 378 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNI 444
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladytlaslrrqVALVSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 445 LFGK--EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 522
Cdd:TIGR02203 427 AYGRteQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 523 HIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFN 583
Cdd:TIGR02203 507 LV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHN 566
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
379-578 |
9.01e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 141.39 E-value: 9.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------AISGTFAYVAQQAWILNATLRDNIL 445
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 524
Cdd:PRK10789 411 LGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 525 FNSaIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDY 578
Cdd:PRK10789 491 LHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
994-1208 |
1.18e-34 |
|
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: 130.90 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI 1073
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmenGDNFSVGERQLLCIARALLRHCKILI 1153
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1154 LDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1208
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
379-579 |
1.22e-34 |
|
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: 133.00 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 445
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FGKE-YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHI 524
Cdd:cd03252 98 LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD-YESEHA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 525 FNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:cd03252 177 IMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
997-1206 |
2.42e-34 |
|
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: 129.64 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1076
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1077 EPVLFSGTVRSNLdpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILILDE 1156
Cdd:cd03246 84 DDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1157 ATAAMDTETDLLIQETIREA-FADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1206
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
31-267 |
2.75e-34 |
|
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: 133.75 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 31 IVRSWSLALTWALNYRTGVRLRGAILTMAFkkilklknikEKSL------------GELINICSNDGQRMFEAAAVGSLL 98
Cdd:cd18595 49 IIQSLLLHQYFHRCFRLGMRIRTALTSAIY----------RKALrlsnsarkkstvGEIVNLMSVDAQRIQDLVPYLNML 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 99 AGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAF 178
Cdd:cd18595 119 WSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 179 SQSVQKIREEERRILEKAGYFQSITV---GVAPIVVviaSVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPF 253
Cdd:cd18595 199 EKKILKIREKELKLLKKAAYLNAVSSflwTCAPFLV---SLATFATYVLSDPDnvLDAEKAFVSLSLFNILRFPLSMLPM 275
|
250
....*....|....
gi 1622900605 254 SVKSLSEASVAVDR 267
Cdd:cd18595 276 VISNLVQASVSLKR 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
968-1208 |
4.38e-34 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 139.46 E-value: 4.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 968 IKTLSLEAPARIKNKAPSPDwpQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVEL 1047
Cdd:PRK10789 290 IRAMLAEAPVVKDGSEPVPE--GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1048 SGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL---DPfnQYTEDQIWDALERTHMKECIAQLPLKLESEV 1124
Cdd:PRK10789 368 SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1125 MENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQG 1204
Cdd:PRK10789 446 GERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHG 525
|
....
gi 1622900605 1205 QVVE 1208
Cdd:PRK10789 526 HIAQ 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
974-1218 |
3.98e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 135.42 E-value: 3.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 974 EAPARIKNKAPSPDWPQEGE--VTFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS 1048
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1049 GGCIKIDGVRISDIG---LADLRSKLSIIPQEPVlfsgtvrSNLDPFnqYT-EDQIWDALE------RTHMKECIAQLpL 1118
Cdd:COG1123 319 SGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPY-------SSLNPR--MTvGDIIAEPLRlhgllsRAERRERVAEL-L 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1119 K---LESEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHR 1188
Cdd:COG1123 389 ErvgLPPDLADrYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL----DVSVQAQILNLLRDlqrelgLTYLFISHD 464
|
250 260 270
....*....|....*....|....*....|.
gi 1622900605 1189 LHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:COG1123 465 LAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
968-1209 |
1.22e-32 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 134.88 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 968 IKTLSLEAPARIKNKA-PSPdwpqEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE 1046
Cdd:COG4618 308 LNELLAAVPAEPERMPlPRP----KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1047 LSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVME 1126
Cdd:COG4618 384 PTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1127 NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQ 1205
Cdd:COG4618 464 GGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGR 543
|
....
gi 1622900605 1206 VVEF 1209
Cdd:COG4618 544 VQAF 547
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
73-268 |
5.00e-32 |
|
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: 126.98 E-value: 5.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 73 SLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAAT 152
Cdd:cd18594 94 TTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 153 DERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLTAA 232
Cdd:cd18594 174 DERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLTGNTLTAR 253
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900605 233 QAFTVVTVFNS--MTFALKVtPFSVKSLSEASVAVDRF 268
Cdd:cd18594 254 KVFTVISLLNAlrMTITRFF-PESIQTLSESRVSLKRI 290
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
660-944 |
1.33e-31 |
|
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: 125.45 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 660 FLVIMALFMLNVGSTAFSTWWLSYWIKqgsgntTVTRGNETSVSDSMKdnprmqyYASIYALSMAVMLILKAIRGVVFVK 739
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD------VLLPDGDPETQALNV-------YSLALLLLGLAQFILSFLQSYLLNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 740 GTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVIlVFFCVGMIAGVFPWFL--- 816
Cdd:pfam00664 68 TGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLA-TIVGGIIVMFYYGWKLtlv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 817 -VAVGPLVILFSVlhIVSRVLiRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCA 895
Cdd:pfam00664 147 lLAVLPLYILVSA--VFAKIL-RKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 896 MRWLAVRLDLI---SIALITTTGlMIVLMHGQIPPAYAGLAISYAVQLTGLF 944
Cdd:pfam00664 224 NGLSFGITQFIgylSYALALWFG-AYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
994-1218 |
3.48e-31 |
|
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: 129.64 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGVRISDIGLADLRSK 1070
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1071 LSIIPQEPvlfsgtvRSNLDPFNqyTEDQIWDALE-----RTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIAR 1143
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVT--VGDQIAEALEnlglsRAEARARVLELleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1144 ALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
43-267 |
3.00e-30 |
|
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: 122.34 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 43 LNYRTGVRLRGAILTMAF----KKILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGP 118
Cdd:cd18591 79 IVIREGIRLKTALQAMIYekalRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 119 TGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGY 198
Cdd:cd18591 159 SALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAV 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 199 FQSITVGVAPIVVVIASVVTFSVHMTL-GFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 267
Cdd:cd18591 239 YWSLMTFLTQASPILVTLVTFGLYPYLeGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
376-579 |
6.75e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 126.48 E-value: 6.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRD 442
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGK-EYDEERYNSVLNscclRPDLAILPSSDL---TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:PRK11160 433 NLLLAApNASDEALIEVLQ----QVGLEKLLEDDKglnAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 519 HVGNHIFnSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:PRK11160 509 ETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
379-579 |
1.27e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 125.90 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 445
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdytlaslrnqVALVSQNVHLFNDTIANNIA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FGKE--YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNH 523
Cdd:PRK11176 439 YARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SER 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 524 IFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:PRK11176 518 AIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
343-545 |
1.89e-29 |
|
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: 124.78 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 343 LAEQKGHLLLDSDERPSPEEEEG-----KHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLE 417
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVGLGKptlelRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 418 GSIAISG-------------TFAYVAQQAWILNATLRDNILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERG 483
Cdd:TIGR02868 390 GEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 484 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKHLKSKTVLFVTHQL 545
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDLLAALSGRTVVLITHHL 530
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
995-1205 |
3.81e-29 |
|
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: 114.26 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 995 TFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSII 1074
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1075 PQepvlfsgtvrsnldpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILIL 1154
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1155 DEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTV-LGSDRIMVLAQGQ 1205
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
379-579 |
4.14e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 125.22 E-value: 4.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 445
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FG-KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI 524
Cdd:TIGR00958 577 YGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 525 FNSairKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:TIGR00958 657 QES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
379-558 |
4.33e-29 |
|
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: 116.09 E-value: 4.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA---WILNATLRDNIL-- 445
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRsidRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 ------FGKEYDEERYNSVLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVD---------EALERVGLSELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900605 519 HvGNHIFNSAIRK-HLKSKTVLFVTHQLQYLVD-CDEVIFMK 558
Cdd:cd03235 166 K-TQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
366-566 |
4.66e-29 |
|
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: 114.72 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 366 KHIHLGHL-RLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI------------AISGTFAYVAQQ 432
Cdd:cd03247 4 NNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItldgvpvsdlekALSSLISVLNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 433 AWILNATLRDNIlfgkeydeerynsvlnscclrpdlailpssdlteigerGANLSGGQRQRISLARALYSDRSIYILDDP 512
Cdd:cd03247 84 PYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 513 LSALDAHVGNHIFnSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERG 566
Cdd:cd03247 126 TVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
996-1205 |
6.14e-29 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 115.64 E-value: 6.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 996 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1075
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1076 QEP--VLFSGTVRSNL--DPFN-QYTEDQIW----DALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1146
Cdd:cd03225 82 QNPddQFFGPTVEEEVafGLENlGLPEEEIEerveEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1147 RHCKILILDEATAAMDTETDLLIQETIREaFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQ 1205
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
379-573 |
7.89e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.34 E-value: 7.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA---WILNATLRDNILFG 447
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAevdWDFPITVRDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 448 --------KEYDEERYNSVLNScclrpdLAILpssDLTE-----IGErganLSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:COG1121 102 rygrrglfRRPSRADREAVDEA------LERV---GLEDladrpIGE----LSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 515 ALDAHVGNHIFnsAIRKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITErGTHEELMN 573
Cdd:COG1121 169 GVDAATEEALY--ELLRELRRegKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
379-579 |
9.91e-29 |
|
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: 124.08 E-value: 9.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWI---LNATLRDNILFGKEYDEery 455
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLrrqMGVVLQENVLFSRSIRD--- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 456 nsvlNSCCLRPDLAI------------------LPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 517
Cdd:TIGR01846 550 ----NIALCNPGAPFehvihaaklagahdfiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 518 AHvGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:TIGR01846 626 YE-SEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYA 686
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
994-1205 |
1.71e-28 |
|
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: 114.10 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRY---RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsK 1070
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1071 LSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCK 1150
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1151 ILILDEATAAMDTET-DLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQ 1205
Cdd:cd03250 148 IYLLDDPLSAVDAHVgRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
376-579 |
1.84e-28 |
|
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: 122.12 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRD 442
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVdlrqldpaelrarMALVPQDPVLFAASVME 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGK--EYDEERYNSVLNScclRPDLAI--LPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:TIGR02204 433 NIRYGRpdATDEEVEAAARAA---HAHEFIsaLPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 519 HvGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:TIGR02204 510 E-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYA 569
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
368-579 |
2.56e-28 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 122.74 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 368 IHLGHLRLQRTLHS-IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQA 433
Cdd:TIGR03796 483 ITFGYSPLEPPLIEnFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGipreeiprevlanSVAMVDQDI 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 WILNATLRDNI-LFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDP 512
Cdd:TIGR03796 563 FLFEGTVRDNLtLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEA 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 513 LSALDAHVgNHIFNSAIRKhlKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:TIGR03796 643 TSALDPET-EKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYA 706
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
379-584 |
3.32e-28 |
|
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: 122.54 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 445
Cdd:TIGR01193 490 LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfINYLPQEPYIFSGSILENLL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FG--KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 523
Cdd:TIGR01193 570 LGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKK 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 524 IFNSAIRkhLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNN 584
Cdd:TIGR01193 650 IVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
379-579 |
4.45e-28 |
|
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: 121.08 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLI-----------SAIL--GQ----MTL--LEGSIAIsgtfayVAQQAWILNAT 439
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfydvtsGRILidGQdirdVTQasLRAAIGI------VPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 440 LRDNILFGK-EYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:COG5265 448 IAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 519 HVGNHIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:COG5265 528 RTERAI-QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYA 587
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
364-573 |
4.62e-28 |
|
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: 114.13 E-value: 4.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 364 EGKHIHLGH---LRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FA 427
Cdd:COG1124 3 EVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 428 YVAQQ-----------AWILNATLRdniLFGKEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISL 496
Cdd:COG1124 83 MVFQDpyaslhprhtvDRILAEPLR---IHGLPDREERIAELLEQVGLPPSFL----------DRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 497 ARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELM 572
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNllKDLREERGL-TYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLL 227
|
.
gi 1622900605 573 N 573
Cdd:COG1124 228 A 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
376-560 |
5.09e-28 |
|
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: 111.18 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfayvaQQAWILNATLRDNIlfgkeydeery 455
Cdd:cd00267 12 RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRI----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 456 nsvlnscclrpdlAILPSsdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGnHIFNSAIRKHLKS 535
Cdd:cd00267 76 -------------GYVPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAEE 129
|
170 180
....*....|....*....|....*..
gi 1622900605 536 -KTVLFVTHQLQYLVD-CDEVIFMKEG 560
Cdd:cd00267 130 gRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1010-1217 |
6.58e-28 |
|
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: 113.74 E-value: 6.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPvlfsgtvRSNL 1089
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP-------YASL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1090 DPF---------------NQYTEDQIWDALERTHMKECIA-QLPLKLesevmengdnfSVGERQLLCIARALLRHCKILI 1153
Cdd:COG1124 93 HPRhtvdrilaeplrihgLPDREERIAELLEQVGLPPSFLdRYPHQL-----------SGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1154 LDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1217
Cdd:COG1124 162 LDEPTSALDVSVqaeilNLL--KDLREER-GLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
73-267 |
4.36e-27 |
|
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: 112.70 E-value: 4.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 73 SLGELINICSNDGQRMFEAAAVGSLLAGGPV--VAILGMIYNVIilGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVA 150
Cdd:cd18593 95 TVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLqlIAVIYILWFEI--GWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 151 ATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLT 230
Cdd:cd18593 173 RTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILT 252
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622900605 231 AAQAFTVVTVFNS----MTFALkvtPFSVKSLSEASVAVDR 267
Cdd:cd18593 253 AERVFVTMALYNAvrltMTLFF---PFAIQFGSELSVSIRR 290
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
379-573 |
9.07e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.15 E-value: 9.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWI-LNATLRDNIL 445
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEPALyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 F-------GKEYDEERYNSVLNSCclrpdlailpssDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD 517
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELF------------GLTDaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 518 AhVGNHIFNSAIRKHLKS-KTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELMN 573
Cdd:COG1131 164 P-EARRELWELLRELAAEgKTVLLSTHYLeeaERL--CDRVAIIDKGRIVADGTPDELKA 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
994-1219 |
9.44e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 110.52 E-value: 9.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1073
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVL-FSGTVR--------SNLDPFNQYTED---QIWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCI 1141
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryPHLGLFGRPSAEdreAVEEALERTGLEH-LADRPV----------DELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1142 ARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
.
gi 1622900605 1219 D 1219
Cdd:COG1120 229 E 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
379-579 |
1.94e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.83 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 445
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtraslrrnIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FGKE--YDEErynsvlnsccLRPDLAILPSSDL---------TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:PRK13657 431 VGRPdaTDEE----------MRAAAERAQAHDFierkpdgydTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 515 ALDAHVGNHIfNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:PRK13657 501 ALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
364-582 |
2.70e-26 |
|
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: 115.37 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 364 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVA 430
Cdd:TIGR01192 336 EFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIdintvtreslrksIATVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 431 QQAWILNATLRDNILFGKE--YDEERYNSVLNSCCLRPDLAILPSSDlTEIGERGANLSGGQRQRISLARALYSDRSIYI 508
Cdd:TIGR01192 416 QDAGLFNRSIRENIRLGREgaTDEEVYEAAKAAAAHDFILKRSNGYD-TLVGERGNRLSGGERQRLAIARAILKNAPILV 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 509 LDDPLSALDAHVGNHIFNsAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIF 582
Cdd:TIGR01192 495 LDEATSALDVETEARVKN-AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
996-1219 |
3.59e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.31 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 996 FENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1075
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1076 QEPvlfsgtvrsnlDpfNQY----TEDQIWDALE-----RTHMKECIAQLPLKLEsevMEN-----GDNFSVGERQLLCI 1141
Cdd:PRK13632 90 QNP-----------D--NQFigatVEDDIAFGLEnkkvpPKKMKDIIDDLAKKVG---MEDyldkePQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1142 ARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSND 1219
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
379-573 |
4.03e-26 |
|
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: 108.59 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWI-LNATLRDNI 444
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVPQEPPApFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 445 LFG-----------KEYDEERYNSVLNSCclrpdlailpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDP 512
Cdd:COG1120 97 ALGryphlglfgrpSAEDREAVEEALERT------------GLEHLADRPVDeLSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 513 LSALDAHvgnHIFN--SAIRK--HLKSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 573
Cdd:COG1120 165 TSHLDLA---HQLEvlELLRRlaRERGRTVVMVLHDLnlaaRY---ADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
371-573 |
4.59e-26 |
|
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: 114.46 E-value: 4.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 371 GHLRLQR-----------TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------F 426
Cdd:COG4618 329 GRLSVENltvvppgskrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 427 AYVAQQAWILNATLRDNI-LFGKEYDEErynsVLNSCclrpDLA-----ILpssDL-----TEIGERGANLSGGQRQRIS 495
Cdd:COG4618 409 GYLPQDVELFDGTIAENIaRFGDADPEK----VVAAA----KLAgvhemIL---RLpdgydTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 496 LARALYSDRSIYILDDPLSALDAhVGNHIFNSAIRkHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDD-EGEAALAAAIR-ALKArgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
379-566 |
5.83e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.98 E-value: 5.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIaisgtfayvaqqawilnatlrdnILFGKEYDEerynsv 458
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-----------------------LLDGKDLAS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 459 LNSCCLRPDLAILPSS----DLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIR-KH 532
Cdd:cd03214 66 LSPKELARKIAYVPQAlellGLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRlAR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900605 533 LKSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERG 566
Cdd:cd03214 146 ERGKTVVMVLHDLnlaaRY---ADRVILLKDGRIVAQG 180
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
379-562 |
8.49e-26 |
|
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: 105.38 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 445
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGYLPQDDELFSGSIAENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 fgkeydeerynsvlnscclrpdlailpssdlteigerganlSGGQRQRISLARALYSDRSIYILDDPLSALDaHVGNHIF 525
Cdd:cd03246 98 -----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622900605 526 NSAIRkHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 562
Cdd:cd03246 136 NQAIA-ALKAAgaTRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
368-562 |
1.15e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 368 IHLGHLRLQRT----LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVA 430
Cdd:COG4619 1 LELEGLSFRVGgkpiLSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 431 QQAWILNATLRDNILF-----GKEYDEERYNSVLNSCCLRPDLAilpssdlteigERGA-NLSGGQRQRISLARALYSDR 504
Cdd:COG4619 81 QEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDIL-----------DKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 505 SIYILDDPLSALDAHvgN-HIFNSAIRKHLKSK--TVLFVTH---QLQYLvdCDEVIFMKEGCI 562
Cdd:COG4619 150 DVLLLDEPTSALDPE--NtRRVEELLREYLAEEgrAVLWVSHdpeQIERV--ADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
365-566 |
1.16e-25 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 106.82 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 365 GKHIHLGHLRlQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAY 428
Cdd:cd03257 8 SVSFPTGGGS-VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 429 VAQQA-----------WILNATLRdnILFGKEYDEERYNSVLNSCCLRPdlaiLPSSDLTEigeRGANLSGGQRQRISLA 497
Cdd:cd03257 87 VFQDPmsslnprmtigEQIAEPLR--IHGKLSKKEARKEAVLLLLVGVG----LPEEVLNR---YPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 498 RALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERG 566
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILD--LLKKLQEElglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
343-572 |
1.33e-25 |
|
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: 112.83 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 343 LAEQKGHLLLDS-DERPSPEEeegkhihlghlrlQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIA 421
Cdd:TIGR01842 310 LPEPEGHLSVENvTIVPPGGK-------------KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 422 ISG-------------TFAYVAQQAWILNATLRDNIL-FGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLS 487
Cdd:TIGR01842 377 LDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLS 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 488 GGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIrKHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCITER 565
Cdd:TIGR01842 457 GGQRQRIALARALYGDPKLVVLDEPNSNLDE-EGEQALANAI-KALKARgiTVVVITHRPSLLGCVDKILVLQDGRIARF 534
|
....*..
gi 1622900605 566 GTHEELM 572
Cdd:TIGR01842 535 GERDEVL 541
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
377-577 |
2.89e-25 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 106.10 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtFAYVAQQAWILNA--------------TLRD 442
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG-EDVRKEPREARRQigvlpderglydrlTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NI-LFGKEYDEERYNsvlnsccLRPDLA-ILPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAh 519
Cdd:COG4555 94 NIrYFAELYGLFDEE-------LKKRIEeLIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 520 VGNHIFNSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNLNGD 577
Cdd:COG4555 166 MARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1014-1212 |
4.68e-25 |
|
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: 107.45 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGVRISDIGLADLR----SKLSIIPQEPVlfsgtvr 1086
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLDPFnqYT-EDQIWDALeRTH-------MKECIAQLpLKL-----ESEVMengDN----FSVGERQLLCIARALLRHC 1149
Cdd:COG0444 97 TSLNPV--MTvGDQIAEPL-RIHgglskaeARERAIEL-LERvglpdPERRL---DRypheLSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 1150 KILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTP 1212
Cdd:COG0444 170 KLLIADEPTTALDVTIqaqilNLLKD--LQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEegpveelFENP 242
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
340-590 |
4.69e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 111.73 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 340 QAVLAEQKGHLLLD-------SDERPSpeeeEGKHIHLGHLRL-----QRTLHSIDLEIQEGKLVGICGSVGSGKTSLIS 407
Cdd:PRK10790 310 QAVVAGERVFELMDgprqqygNDDRPL----QSGRIDIDNVSFayrddNLVLQNINLSVPSRGFVALVGHTGSGKSTLAS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 408 AILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSS 474
Cdd:PRK10790 386 LLMGYYPLTEGEIRLDGrplsslshsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 475 DLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNS--AIRKHlksKTVLFVTHQLQYLVDCD 552
Cdd:PRK10790 466 LYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAlaAVREH---TTLVVIAHRLSTIVEAD 542
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622900605 553 EVIFMKEGCITERGTHEELMNLNGDYATIFNNLLLGDT 590
Cdd:PRK10790 543 TILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
379-557 |
4.77e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.94 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA----WilnATLRDNILF 446
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVFQEPallpW---LTVLDNVAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 G-------KEYDEERYNSVLNSCCLRPDLAILPSsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDA- 518
Cdd:COG1116 104 GlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDAl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900605 519 ---HVGNHIFNsaIRKHLKsKTVLFVTHqlqylvDCDEVIFM 557
Cdd:COG1116 173 treRLQDELLR--LWQETG-KTVLFVTH------DVDEAVFL 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
994-1226 |
5.92e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.17 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsdiglADLRSKLSI 1073
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQE-------PVLFSGTVRSNLDP----FNQYTE---DQIWDALERTHMKE----CIAQLplklesevmengdnfSVGE 1135
Cdd:COG1121 80 VPQRaevdwdfPITVRDVVLMGRYGrrglFRRPSRadrEAVDEALERVGLEDladrPIGEL---------------SGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1136 RQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1213
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHGPPEE 224
|
250
....*....|...
gi 1622900605 1214 VLLSNDSSRFYAM 1226
Cdd:COG1121 225 VLTPENLSRAYGG 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1010-1215 |
6.54e-25 |
|
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: 104.57 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDGVRISDIGLAD--LRSKLSIIPQEPVLFS 1082
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegeVLLDGKDIYDLDVDVleLRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1083 GTVRSNLDpfnqYTeDQIWDALERTHMKECIAQLpLK---LESEVME--NGDNFSVGERQLLCIARALLRHCKILILDEA 1157
Cdd:cd03260 95 GSIYDNVA----YG-LRLHGIKLKEELDERVEEA-LRkaaLWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1158 TAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVL 1215
Cdd:cd03260 169 TSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
379-571 |
8.73e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 107.15 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtlLE----GSIAISGT--F----------AYVAQQAwilnA---- 438
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAG----LEtpdsGRIVLNGRdlFtnlpprerrvGFVFQHY----Alfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 -TLRDNILFG-------KEYDEERYNSVLnscclrpDLAilpssDLTEIGER-GANLSGGQRQRISLARALYSDRSIYIL 509
Cdd:COG1118 90 mTVAENIAFGlrvrppsKAEIRARVEELL-------ELV-----QLEGLADRyPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 510 DDPLSALDAHVgnhifnsaiRKHLKSK----------TVLFVTHQLQ--YLVdCDEVIFMKEGCITERGTHEEL 571
Cdd:COG1118 158 DEPFGALDAKV---------RKELRRWlrrlhdelggTTVFVTHDQEeaLEL-ADRVVVMNQGRIEQVGTPDEV 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
379-554 |
8.98e-25 |
|
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: 103.33 E-value: 8.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQ-AWILNATLRDNIL 445
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLGHAdGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 F-----GKEYDEERYNSVLnscclrpdlAILpssDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 519
Cdd:COG4133 98 FwaalyGLRADREAIDEAL---------EAV---GLAGLADLpVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622900605 520 vGNHIFNSAIRKHLKS-KTVLFVTHQLQYLVDCDEV 554
Cdd:COG4133 166 -GVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
379-562 |
1.30e-24 |
|
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: 101.71 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIsgtfayvaqqawilnatlrdnilFGKEYDEERyNSV 458
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-----------------------LGKDIKKEP-EEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 459 LNSCCLRPDLAILPSsDLTeiGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVGNHIFNSAIRKHLKS-KT 537
Cdd:cd03230 72 KRRIGYLPEEPSLYE-NLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELLRELKKEgKT 147
|
170 180
....*....|....*....|....*.
gi 1622900605 538 VLFVTHQLQYLVD-CDEVIFMKEGCI 562
Cdd:cd03230 148 ILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
378-560 |
1.65e-24 |
|
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: 102.93 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 378 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQawILNATL 440
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkvglvFQNPDDQ--FFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 441 RDNILFGKE---YDEERYNSVLNSCCLRPDLAILPSSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALD 517
Cdd:cd03225 94 EEEVAFGLEnlgLPEEEIEERVEEALELVGLEGLRDRSP-------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900605 518 AHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEG 560
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
997-1207 |
1.72e-24 |
|
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: 101.74 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1076
Cdd:cd03214 3 ENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1077 epvlfsgtvrsnldpfnqytedqiwdALERT---HMKEC-IAQLplklesevmengdnfSVGERQLLCIARALLRHCKIL 1152
Cdd:cd03214 81 --------------------------ALELLglaHLADRpFNEL---------------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1153 ILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRL-HTVLGSDRIMVLAQGQVV 1207
Cdd:cd03214 120 LLDEPTSHLDiahqIELLELLRRLARE--RGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
376-562 |
2.03e-24 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 102.60 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQaWIL--NATLRD 442
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD-YALfpHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFG----KEYDEERYNSVLNScclrpdLAILpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD 517
Cdd:cd03259 92 NIAFGlklrGVPKAEIRARVREL------LELV---GLEGLLNRYPHeLSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 518 AHVgnhifNSAIRKHLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCI 562
Cdd:cd03259 163 AKL-----REELREELKElqrelgITTIYVTHdQEEALALADRIAVMNEGRI 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
940-1202 |
3.97e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 110.50 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 940 LTGLFQFTVRLASETEarftsverinhYIKtlSLEAPA---RIKNKAPSPDWPQEGE-------VTFENAEMRY--RENL 1007
Cdd:PTZ00265 332 LISMFMLTIILPNITE-----------YMK--SLEATNslyEIINRKPLVENNDDGKklkdikkIQFKNVRFHYdtRKDV 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1008 PlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKI-DGVRISDIGLADLRSKLSIIPQEPVLFSGTVR 1086
Cdd:PTZ00265 399 E-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIK 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLDPF-----------NQYTED--------------------------QIWDALERTHMK------------------- 1110
Cdd:PTZ00265 478 NNIKYSlyslkdlealsNYYNEDgndsqenknkrnscrakcagdlndmsNTTDSNELIEMRknyqtikdsevvdvskkvl 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1111 --ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLT--IA 1186
Cdd:PTZ00265 558 ihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIA 637
|
330
....*....|....*.
gi 1622900605 1187 HRLHTVLGSDRIMVLA 1202
Cdd:PTZ00265 638 HRLSTIRYANTIFVLS 653
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
375-567 |
4.29e-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: 101.33 E-value: 4.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 375 LQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLR 441
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGKEYDEERYNSVLnscclrpdlailpssdltEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVg 521
Cdd:cd03369 100 SNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900605 522 NHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGT 567
Cdd:cd03369 161 DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
379-557 |
4.52e-24 |
|
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: 101.78 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQA----WilnATLRDNILF 446
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQDallpW---LTVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 GkeydeerynsvlnscclrPDLAILPSSDLTEIGER---------GAN-----LSGGQRQRISLARALYSDRSIYILDDP 512
Cdd:cd03293 97 G------------------LELQGVPKAEARERAEEllelvglsgFENayphqLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900605 513 LSALDAHVGNHIFN--SAIRKHLKsKTVLFVTHqlqylvDCDEVIFM 557
Cdd:cd03293 159 FSALDALTREQLQEelLDIWRETG-KTVLLVTH------DIDEAVFL 198
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
997-1213 |
5.28e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.17 E-value: 5.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1076
Cdd:PRK13635 9 EHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1077 EP-VLFSG-TVRSNLD--------PFNQYTEdQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1146
Cdd:PRK13635 89 NPdNQFVGaTVQDDVAfglenigvPREEMVE-RVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1147 RHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPS 1213
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
379-573 |
7.72e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 107.30 E-value: 7.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQ----QawiLNA 438
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslrelrrrVQMVFQdpysS---LNP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 --TLRDNILFG--------KEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISLARALYSDRSIYI 508
Cdd:COG1123 358 rmTVGDIIAEPlrlhgllsRAERRERVAELLERVGLPPDLA----------DRYPHELSGGQRQRVAIARALALEPKLLI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 509 LDDPLSALDAHVGNHIFN--SAIRKHLKsKTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 573
Cdd:COG1123 428 LDEPTSALDVSVQAQILNllRDLQRELG-LTYLFISHDLA-VVRyiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
376-573 |
8.08e-24 |
|
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: 101.42 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWILNA- 438
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSGALFDSl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNILF--------GKEYDEERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILD 510
Cdd:cd03261 93 TVFENVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 511 DPLSALDAhVGNHIFNSAIRKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:cd03261 162 EPTAGLDP-IASGVIDDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
379-514 |
9.11e-24 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 98.49 E-value: 9.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNA-TLRDNI 444
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 445 LFG-------KEYDEERYNSVLNScclrpdLAILPSSDlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:pfam00005 81 RLGlllkglsKREKDARAEEALEK------LGLGDLAD-RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
666-968 |
1.03e-23 |
|
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: 102.68 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 666 LFMLNVGSTAFSTWWLSYWikqgsgntTVTRGNETSvsdsmkdnPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRAS 745
Cdd:cd18559 7 LVLCNHVFSGPSNLWLLLW--------FDDPVNGPQ--------EHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 746 SRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF---IQNVILVFFcvgMIAGVFPWFLVAVgPL 822
Cdd:cd18559 71 RAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWmgpLQNVIGLYL---LILLAGPMAAVGI-PL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 823 VILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRyQELLDDNQAPFFLFTCAMRWLAVR 902
Cdd:cd18559 147 GLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQ-VDAKRDNELAYLPSIVYLRALAVR 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 903 LDLISIALITTTGLMIVLMHGQIpPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYI 968
Cdd:cd18559 226 LWCVGPCIVLFASFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1011-1208 |
1.55e-23 |
|
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: 106.31 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlFSG---- 1083
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 -TV-----------RSNLDPfnQYTEDQIWDALERTHmkeciaqlplkLESEVM-----EngdnFSVGERQLLCIARALL 1146
Cdd:COG4172 379 mTVgqiiaeglrvhGPGLSA--AERRARVAEALEEVG-----------LDPAARhryphE----FSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1147 RHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHRLHTV--LgSDRIMVLAQGQVVE 1208
Cdd:COG4172 442 LEPKLLVLDEPTSAL----DVSVQAQILDLLRDlqrehgLAYLFISHDLAVVraL-AHRVMVMKDGKVVE 506
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
956-1188 |
1.68e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.43 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 956 ARFTS-VERINHYIKtlSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGK 1034
Cdd:COG4178 326 AEWRAtVDRLAGFEE--ALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1035 SSLgmalFRLveLSG------GCIKI-DGVRISdigladlrsklsIIPQEPVLFSGTVRSNL---DPFNQYTEDQIWDAL 1104
Cdd:COG4178 403 STL----LRA--IAGlwpygsGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREAL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1105 ERTHMKECIAQLplkleSEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLT 1184
Cdd:COG4178 465 EAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVIS 539
|
....
gi 1622900605 1185 IAHR 1188
Cdd:COG4178 540 VGHR 543
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
994-1205 |
1.70e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 98.80 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG--LADLRSKL 1071
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSG-TVRSNLdpfnqytedqiwdalerthmkeciaQLPLklesevmengdnfSVGERQLLCIARALLRHCK 1150
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-------------------------ALGL-------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1151 ILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQ 1205
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
996-1204 |
2.27e-23 |
|
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: 99.53 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 996 FENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsdiglADLRSKLSIIP 1075
Cdd:cd03235 2 VEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1076 QE-------PVLFSGTVRSNLDP----FNQYTEDQ---IWDALERTHMKE----CIAQLplklesevmengdnfSVGERQ 1137
Cdd:cd03235 75 QRrsidrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSEladrQIGEL---------------SGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1138 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGS-DRIMVLAQG 1204
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLLNRT 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
997-1206 |
5.83e-23 |
|
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: 97.08 E-value: 5.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSIIPQ 1076
Cdd:cd03230 4 RNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1077 EPVLFSG-TVRSNLDpfnqytedqiwdalerthmkeciaqlplklesevmengdnFSVGERQLLCIARALLRHCKILILD 1155
Cdd:cd03230 81 EPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1156 EATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 1206
Cdd:cd03230 121 EPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
377-573 |
1.01e-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: 98.57 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFA-----------YVAQQ-AWILNATLRDNI 444
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqernvgFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 445 LFGKEYDEERYnsvlnscclRPDLA--------ILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:cd03296 96 AFGLRVKPRSE---------RPPEAeirakvheLLKLVQLDWLADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 516 LDAHVgnhifnsaiRKHLKS----------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:cd03296 167 LDAKV---------RKELRRwlrrlhdelhVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
994-1218 |
1.31e-22 |
|
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: 98.04 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGVRISDIGLADL 1067
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGlerpTSGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1068 ---RSKLSIIPQEPVLFSG-TVRSNLD-PFnqytedQIWdALERTHMKECIAQLpLK---LESEVMENGDNFSVGERQLL 1139
Cdd:cd03258 78 rkaRRRIGMIFQHFNLLSSrTVFENVAlPL------EIA-GVPKAEIEERVLEL-LElvgLEDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1140 CIARALLRHCKILILDEATAAMDTET-----DLLIQetIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1213
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETtqsilALLRD--INREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 1622900605 1214 VLLSN 1218
Cdd:cd03258 227 EVFAN 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1014-1208 |
2.26e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.81 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvRSNLD 1090
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-------YASLN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1091 PfnQYT-EDQIWDALE------RTHMKECIAQLPLK--LESEVM-----EngdnFSVGERQLLCIARALLRHCKILILDE 1156
Cdd:COG4608 110 P--RMTvGDIIAEPLRihglasKAERRERVAELLELvgLRPEHAdryphE----FSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1157 ATAAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRL----HTvlgSDRIMVLAQGQVVE 1208
Cdd:COG4608 184 PVSAL----DVSIQaqvlnllEDLQDEL-GLTYLFISHDLsvvrHI---SDRVAVMYLGKIVE 238
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
373-566 |
4.15e-22 |
|
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: 95.82 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 373 LRLQRTLHSIDLEIQ---EGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQ 432
Cdd:cd03297 4 VDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 433 AWIL-NATLRDNILFGkeydeerynsvLNSCCLRPDL----AILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSI 506
Cdd:cd03297 84 YALFpHLNVRENLAFG-----------LKRKRNREDRisvdELLDLLGLDHLLNRYpAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 507 YILDDPLSALDAHVGNHIFN--SAIRKHLKsKTVLFVTH---QLQYLvdCDEVIFMKEGCITERG 566
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPelKQIKKNLN-IPVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
366-560 |
6.07e-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: 95.63 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 366 KHIHLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAY 428
Cdd:cd03255 8 KTYGGGGEKVQ-ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 429 VAQQAWILNA-TLRDNILFG-------KEYDEERYNSVLNSCCLRPDLAILPSsdlteigergaNLSGGQRQRISLARAL 500
Cdd:cd03255 87 VFQSFNLLPDlTALENVELPlllagvpKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 501 YSDRSIYILDDPLSALDAHVGNHIFNsAIRK--HLKSKTVLFVTHQLQYLVDCDEVIFMKEG 560
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVME-LLRElnKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
379-572 |
7.71e-22 |
|
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: 95.48 E-value: 7.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG------TFAYVAQQAWIL---------NATLRDN 443
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRKVGLVfqnpddqlfAPTVEED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFG-------KEYDEERYNSVLNSCclrpdlailpssDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:COG1122 97 VAFGpenlglpREEIRERVEEALELV------------GLEHLADRPpHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 516 LDAHVGNHIFNsAIRK-HLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 572
Cdd:COG1122 165 LDPRGRRELLE-LLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
377-571 |
1.57e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 97.84 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQaWIL--NATLRDN 443
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQS-YALypHMTVYEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFG----KEYDEERYNSVLNScclrpdLAILpssDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:COG3839 96 IAFPlklrKVPKAEIDRRVREA------AELL---GLEDLLDRkPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 519 HVGNHifnsaIRKHLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:COG3839 167 KLRVE-----MRAEIKRlhrrlgTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1010-1222 |
2.35e-21 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 94.49 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLSIIPQEPVLFSG-TV 1085
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMGMLFQSGALFDSlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 RSNLD-PFNQYTEDQIWDALERThmKECIAQLPLKLESEVMEngDNFSVGERQLLCIARALLRHCKILILDEATAAMD-- 1162
Cdd:cd03261 95 FENVAfPLREHTRLSEEEIREIV--LEKLEAVGLRGAEDLYP--AELSGGMKKRVALARALALDPELLLYDEPTAGLDpi 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1163 --TETDLLIQeTIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1222
Cdd:cd03261 171 asGVIDDLIR-SLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
379-560 |
2.44e-21 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 92.64 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT---------------FAYVAQQaWIL--NATLR 441
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledelpplrrrIGMVFQD-FALfpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGkeydeerynsvlnscclrpdlailpssdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvg 521
Cdd:cd03229 95 ENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDP--- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900605 522 nhIFNSAIRKHLKS------KTVLFVTHQLQYLVD-CDEVIFMKEG 560
Cdd:cd03229 134 --ITRREVRALLKSlqaqlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1010-1208 |
4.04e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPQEPVLFSG-TVR 1086
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDA-QAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLdpF--NQYTEDQI--WDALERThMKECIAQL--PLKLESEVMEngdnFSVGERQLLCIARALLRHCKILILDEATAA 1160
Cdd:COG1129 98 ENI--FlgREPRRGGLidWRAMRRR-ARELLARLglDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1161 M-DTETDLLIqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:COG1129 171 LtEREVERLF-RIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1010-1207 |
5.17e-21 |
|
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: 90.95 E-value: 5.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsklsiipqEPVLFSGtvrsnl 1089
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFAS------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1090 dpfnqytedqIWDALErtHMKECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAM-DTETDLL 1168
Cdd:cd03216 69 ----------PRDARR--AGIAMVYQL---------------SVGERQMVEIARALARNARLLILDEPTAALtPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622900605 1169 IqETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:cd03216 122 F-KVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
994-1206 |
7.52e-21 |
|
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: 92.55 E-value: 7.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE-LSGGCIKIDGV---RISDIGLADL 1067
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTL-LNILGGLDrPTSGEVRVDGTdisKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1068 R-SKLSIIPQEPVLFSG-TVRSNLD-------PFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQL 1138
Cdd:cd03255 80 RrRHIGFVFQSFNLLPDlTALENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1139 LCIARALLRHCKILILDEATAAMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLGSDRIMVLAQGQV 1206
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
377-579 |
1.05e-20 |
|
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: 98.49 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDN 443
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGqdlagldvqavrrQLGVVLQNGRLMSGSIFEN 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD----AH 519
Cdd:TIGR03797 547 IAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDnrtqAI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 520 VgnhifnSAIRKHLKSkTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYA 579
Cdd:TIGR03797 627 V------SESLERLKV-TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFA 679
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1010-1218 |
1.22e-20 |
|
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: 91.73 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEPVLFSG-TVRS 1087
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1088 NL--------DPFNQYTEDQIWDALERthMKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEATA 1159
Cdd:cd03224 95 NLllgayarrRAKRKARLERVYELFPR--LKERRKQL-----------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1160 ----AMDTEtdllIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:cd03224 162 glapKIVEE----IFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
379-564 |
1.31e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.03 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISaILGqmTLL---EGSIAISGT-----------------FAYVAQQAWIL-N 437
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILG--GLDrptSGEVLIDGQdisslserelarlrrrhIGFVFQFFNLLpE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 438 ATLRDNILF-------GKEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSI 506
Cdd:COG1136 101 LTALENVALplllagvSRKERRERARELL---------------ERVGLGDRLdhrpSQLSGGQQQRVAIARALVNRPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 507 YILDDPLSALDAHVGNHIFNsAIRKHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITE 564
Cdd:COG1136 166 ILADEPTGNLDSKTGEEVLE-LLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
994-1208 |
1.75e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.65 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 1070
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1071 LSIIPQE-PVLFSGTVRSNL---------DPfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 1140
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENValplrvtgkSR--KEIRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1141 IARALLRHCKILILDEATAAMDTET-----DLLiqETIREafADCTMLtIA-HRLHTVLGSD-RIMVLAQGQVVE 1208
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETsweimELL--EEINR--RGTTVL-IAtHDLELVDRMPkRVLELEDGRLVR 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
379-562 |
1.86e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 91.38 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNIL 445
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FG-KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHI 524
Cdd:cd03248 110 YGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE-SEQQ 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900605 525 FNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCI 562
Cdd:cd03248 189 VQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
379-571 |
2.04e-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: 91.49 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWILNA-TLR 441
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrkarrrIGMIFQHFNLLSSrTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILF-------GKEYDEERYNSVLNscclrpdlailpssdLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 510
Cdd:cd03258 101 ENVALpleiagvPKAEIEERVLELLE---------------LVGLEDKAdaypAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 511 DPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 571
Cdd:cd03258 166 EATSALDPETTQSILAllRDINRELGL-TIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
377-573 |
2.77e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 96.13 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG---QMTLLEGSIAISGT-------------FAYVAQQAWI-LN-A 438
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRdllelsealrgrrIGMVFQDPMTqLNpV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNILFGKEYD----EERYNSVLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:COG1123 100 TVGDQIAEALENLglsrAEARARVL---------ELLEAVGLERRLDRYpHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 514 SALDAHVGNHIFnSAIRKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:COG1123 171 TALDVTTQAEIL-DLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
379-571 |
3.68e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.61 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILF 446
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 GKEYDEERYnsvlnscclRPDLAILPSS--------DLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALD 517
Cdd:PRK10851 98 GLTVLPRRE---------RPNAAAIKAKvtqllemvQLAHLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 518 AHVGNHIfNSAIRK-HLKSK-TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK10851 169 AQVRKEL-RRWLRQlHEELKfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
994-1231 |
4.79e-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: 90.82 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSI 1073
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSG-TVRSN--LDP-FNQYTEDQIwdaleRTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHC 1149
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKI-----RERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1150 KILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEFDTPS 1213
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFK-------------RLQQELGktivfvthdideafrlADRIAIMKNGEIVQVGTPD 221
|
250
....*....|....*...
gi 1622900605 1214 VLLSNDSSRFYAMFAAAE 1231
Cdd:cd03295 222 EILRSPANDFVAEFVGAD 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
368-577 |
4.82e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.58 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 368 IHLGHLRLQrtlhsIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQ-------QAWILN 437
Cdd:COG3840 9 YRYGDFPLR-----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAErpvsmlfQENNLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 438 A--TLRDNILFGkeydeerynsvlnsccLRPDL-----------AILPSSDLTEIGER-GANLSGGQRQRISLARALYSD 503
Cdd:COG3840 84 PhlTVAQNIGLG----------------LRPGLkltaeqraqveQALERVGLAGLLDRlPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 504 RSIYILDDPLSALDAhvgnhifnsAIRK---HLKSK-------TVLFVTHQLQylvD----CDEVIFMKEGCITERGTHE 569
Cdd:COG3840 148 RPILLLDEPFSALDP---------ALRQemlDLVDElcrerglTVLMVTHDPE---DaariADRVLLVADGRIAADGPTA 215
|
....*...
gi 1622900605 570 ELMNLNGD 577
Cdd:COG3840 216 ALLDGEPP 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
379-571 |
4.98e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 93.24 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQAwilnA-----TLRD 442
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQDY----AlfphlTVAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFG-------KEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDD 511
Cdd:COG3842 97 NVAFGlrmrgvpKAEIRARVAELL---------------ELVGLEGLAdrypHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 512 PLSALDAHVGNHIfNSAIRKHLKS--KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:COG3842 162 PLSALDAKLREEM-REELRRLQRElgITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
994-1188 |
5.53e-20 |
|
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: 88.36 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlRSKLSI 1073
Cdd:cd03223 1 IELENLSLATPDGRVLL-KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSGTVRsnldpfnqyteDQI---WDalerthmkeciaqlplklesevmengDNFSVGERQLLCIARALLRHCK 1150
Cdd:cd03223 69 LPQRPYLPLGTLR-----------EQLiypWD--------------------------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900605 1151 ILILDEATAAMDTETDLLIQETIREAFAdcTMLTIAHR 1188
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
376-571 |
5.60e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.96 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE---------GSIAISGTFAYVAQQAWILNatLRDNILF 446
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI----NLLEqpeagtirvGDITIDTARSLSQQKGLIRQ--LRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 -GKEYDEERYNSVLNSCCLRP--------DLAI-LPSSDLTEIGERGAN------LSGGQRQRISLARALYSDRSIYILD 510
Cdd:PRK11264 90 vFQNFNLFPHRTVLENIIEGPvivkgepkEEATaRARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 511 DPLSALDAHVGNHIFNSaIRKHLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 571
Cdd:PRK11264 170 EPTSALDPELVGEVLNT-IRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
40-268 |
6.18e-20 |
|
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: 91.46 E-value: 6.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 40 TWALNyRTGVRLRGAILTMAF--KKILKLKNIKEKSLGELINICSNDGQRMfeAAAVGSL--LAGGPV-VAI-LGMIY-- 111
Cdd:cd18598 59 NFQMN-KVSLKVRAALVTAVYrkALRVRSSSLSKFSTGEIVNLMSTDADRI--VNFCPSFhdLWSLPLqIIVaLYLLYqq 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 112 -NVIILGptgflGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEER 190
Cdd:cd18598 136 vGVAFLA-----GLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKEL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 191 RILEKAGYFQSITV---GVAPIVVviaSVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 267
Cdd:cd18598 211 KALKGRKYLDALCVyfwATTPVLI---SILTFATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKR 287
|
.
gi 1622900605 268 F 268
Cdd:cd18598 288 L 288
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
994-1175 |
1.12e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 88.69 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI 1073
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSG-TVRSNLDpF------NQYTEDQIWDALERTHMKECiAQLPLKlesevmengdNFSVGERQLLCIARALL 1146
Cdd:COG4133 80 LGHADGLKPElTVRENLR-FwaalygLRADREAIDEALEAVGLAGL-ADLPVR----------QLSAGQKRRVALARLLL 147
|
170 180
....*....|....*....|....*....
gi 1622900605 1147 RHCKILILDEATAAMDTETDLLIQETIRE 1175
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1010-1210 |
1.43e-19 |
|
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: 88.73 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADLRSKLSIIPQEPVLFSG-TVRSN 1088
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVFQDYALFPHlTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 LDpF--------NQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 1160
Cdd:cd03259 93 IA-FglklrgvpKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1161 MDTETDLLIQETIREAFA--DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1210
Cdd:cd03259 161 LDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
379-571 |
3.14e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 88.01 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAI-----LGQMTLLEGSIAISG---------------TFAYVAQQAWILNA 438
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNILFG--------KEYDEERYNSVLnscclrpDLAILPssdlTEIGER--GANLSGGQRQRISLARALYSDRSIYI 508
Cdd:cd03260 96 SIYDNVAYGlrlhgiklKEELDERVEEAL-------RKAALW----DEVKDRlhALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 509 LDDPLSALDAhVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 571
Cdd:cd03260 165 LDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
379-560 |
4.76e-19 |
|
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: 86.45 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTL--LEGSIAISGT----------FAYVAQQ-AWILNATLRDNIL 445
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRpldkrsfrkiIGYVPQDdILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FgkeydeerynsvlnSCCLRpdlailpssdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIF 525
Cdd:cd03213 105 F--------------AAKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900605 526 nSAIRKHLKS-KTVLFVTHQLQYLV--DCDEVIFMKEG 560
Cdd:cd03213 152 -SLLRRLADTgRTIICSIHQPSSEIfeLFDKLLLLSQG 188
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
994-1217 |
6.41e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.25 E-value: 6.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLP-LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 1072
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1073 IIPQepvlfsgtvrsnlDPFNQYT----EDQIWDALE-----RTHMKECIAQlplKLESEVMENGDN-----FSVGERQL 1138
Cdd:PRK13650 85 MVFQ-------------NPDNQFVgatvEDDVAFGLEnkgipHEEMKERVNE---ALELVGMQDFKEreparLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1139 LCIARALLRHCKILILDEATAAMDTETDL-LIQ--ETIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 1215
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLeLIKtiKGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
..
gi 1622900605 1216 LS 1217
Cdd:PRK13650 228 FS 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1011-1204 |
6.50e-19 |
|
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: 87.00 E-value: 6.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSK----LSIIPQEPVLFSGTVR 1086
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNL---DPFNQYTEDQIWDALErthMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1163
Cdd:cd03290 97 ENItfgSPFNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900605 1164 E-TDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQG 1204
Cdd:cd03290 174 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1010-1219 |
8.50e-19 |
|
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: 86.96 E-value: 8.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGL-ADLRSKLSI--IPQEPVLFSG-TV 1085
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLpPHRIARLGIgyVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 RSNLD--PFNQYTEDQIWDALERTH-----MKECIAQLplklesevmenGDNFSVGERQLLCIARALLRHCKILILDEAT 1158
Cdd:COG0410 96 EENLLlgAYARRDRAEVRADLERVYelfprLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1159 AAmdtetdL--LIQETIREAFAD-----CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 1219
Cdd:COG0410 165 LG------LapLIVEEIFEIIRRlnregVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1010-1206 |
1.02e-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: 86.04 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLRSKLSIIPQEPVLFSG-TVR 1086
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLdpfnqyTEDQIW--------------DALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKIL 1152
Cdd:cd03262 95 ENI------TLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1153 ILDEATAAMDTEtdlLIQE---TIREAFAD-CTMLTIAHRlhtvLG-----SDRIMVLAQGQV 1206
Cdd:cd03262 158 LFDEPTSALDPE---LVGEvldVMKDLAEEgMTMVVVTHE----MGfarevADRVIFMDDGRI 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1010-1213 |
1.09e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElSGGCIKIDGVRISDIG---LADLRSKLSIIPQEPvlfsgtvR 1086
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLDPfnQYTEDQIWDALERTHMKECIAQLPLKLESEVMEN-----------GDNFSVGERQLLCIARALLRHCKILILD 1155
Cdd:PRK15134 373 SSLNP--RLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEvgldpetrhryPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1156 EATAAMDTETD-----LL--IQETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE-------FDTPS 1213
Cdd:PRK15134 451 EPTSSLDKTVQaqilaLLksLQQKHQLAY-----LFISHDLHVVRAlCHQVIVLRQGEVVEqgdcervFAAPQ 518
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
994-1226 |
1.25e-18 |
|
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: 86.68 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSL-GMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 1072
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLlSLITGDLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1073 II---------PQEPVL------FSGTVrsnlDPFNQYTEDQI---WDALERTHMKECIAQLPLKLesevmengdnfSVG 1134
Cdd:COG1119 82 LVspalqlrfpRDETVLdvvlsgFFDSI----GLYREPTDEQReraRELLELLGLAHLADRPFGTL-----------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1135 ERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF-D 1210
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAgP 226
|
250
....*....|....*.
gi 1622900605 1211 TPSVLLSNDSSRFYAM 1226
Cdd:COG1119 227 KEEVLTSENLSEAFGL 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
366-571 |
1.28e-18 |
|
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: 86.47 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 366 KHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYV 429
Cdd:cd03256 4 ENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 430 AQQ-AWILNATLRDNILFGK-------------EYDEERYNSvlnscclrpdLAILPSSDLTE-IGERGANLSGGQRQRI 494
Cdd:cd03256 84 FQQfNLIERLSVLENVLSGRlgrrstwrslfglFPKEEKQRA----------LAALERVGLLDkAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 495 SLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAIRKHlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEE 570
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDpasSRQVMDLLKRINREE--GITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAE 231
|
.
gi 1622900605 571 L 571
Cdd:cd03256 232 L 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1010-1218 |
1.37e-18 |
|
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: 86.34 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISDIGlADLRSKLSIIP--QEPVLFSG 1083
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTL----FNLIsgflRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 -TVRSNL----------DPFNQYTEDQIWDALERTHmkECIAQLPLkleSEVM-ENGDNFSVGERQLLCIARALLRHCKI 1151
Cdd:cd03219 90 lTVLENVmvaaqartgsGLLLARARREEREARERAE--ELLERVGL---ADLAdRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1152 LILDEATAAM-DTETDLLIqETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:cd03219 165 LLLDEPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
997-1213 |
1.48e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.41 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD--IGLADLRSKL 1071
Cdd:PRK13637 6 ENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEP--VLFSGTVRSNLD--PFN-QYTEDQIWDALERThMKEciaqlpLKLESEVMENGDNF--SVGERQLLCIARA 1144
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAfgPINlGLSEEEIENRVKRA-MNI------VGLDYEDYKDKSPFelSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1145 LLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTI--AHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1213
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlvSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
367-572 |
1.76e-18 |
|
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: 88.62 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 367 HIHLGHLRLQrtlhsIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYV 429
Cdd:COG4148 8 RLRRGGFTLD-----VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrrIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 430 AQQAwILNATL--RDNILFGkeydeeRYNSVLNSCCLRPDLAIlpssDLTEIG---ERG-ANLSGGQRQRISLARALYSD 503
Cdd:COG4148 83 FQEA-RLFPHLsvRGNLLYG------RKRAPRAERRISFDEVV----ELLGIGhllDRRpATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 504 RSIYILDDPLSALDAHvgnhifnsaiRKH--------LKSKT---VLFVTHQL---QYLvdCDEVIFMKEGCITERGTHE 569
Cdd:COG4148 152 PRLLLMDEPLAALDLA----------RKAeilpylerLRDELdipILYVSHSLdevARL--ADHVVLLEQGRVVASGPLA 219
|
...
gi 1622900605 570 ELM 572
Cdd:COG4148 220 EVL 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
718-1208 |
2.51e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.58 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 718 IYALSMAVMLILKAIRGVVFVKGTLRASSRLHDEL----FRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV-------- 785
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLvaaiFHKSLRLTHEARKNFASGKVTNMITTDANALQQiaeqlhgl 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 786 -RLPFQaemFIQNVILVFFCVGmIAGVFpwflvavGPLVILfsVLHIVSRVLIRELKRL--DNITQSPFLSHITSSI-QG 861
Cdd:PLN03232 422 wSAPFR---IIVSMVLLYQQLG-VASLF-------GSLILF--LLIPLQTLIVRKMRKLtkEGLQWTDKRVGIINEIlAS 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 862 LATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLT 941
Cdd:PLN03232 489 MDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLR 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 942 GLFQFTVRLASETEARFTSVERINHYIktLSLEapaRIKNKAPsPDWPQEGEVTFENAEMRYRENLPL-VLKKVSFTIKP 1020
Cdd:PLN03232 569 SPLNMLPNLLSQVVNANVSLQRIEELL--LSEE---RILAQNP-PLQPGAPAISIKNGYFSWDSKTSKpTLSDINLEIPV 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1021 KEKIGIVGRTGSGKSSLGMALfrLVELSGgcikidgvriSDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQI 1100
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAM--LGELSH----------AETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERY 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1101 WDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTE-TDLLIQETIREAFAD 1179
Cdd:PLN03232 711 WRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKG 790
|
490 500
....*....|....*....|....*....
gi 1622900605 1180 CTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1208
Cdd:PLN03232 791 KTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1010-1218 |
2.52e-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: 86.25 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISdiGL-ADLRSKLSI-----IPQepv 1079
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTL----FNLItgfyRPTSGRILFDGRDIT--GLpPHRIARLGIartfqNPR--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1080 LFSG-TVRSN-----------------LDPFNQYTE-----DQIWDALERTHMKECIAQLPlklesevmengDNFSVGER 1136
Cdd:COG0411 90 LFPElTVLENvlvaaharlgrgllaalLRLPRARREerearERAEELLERVGLADRADEPA-----------GNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1137 QLLCIARALLRHCKILILDEATAAM-DTETDLLIqETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1212
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRlrDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTP 237
|
....*.
gi 1622900605 1213 SVLLSN 1218
Cdd:COG0411 238 AEVRAD 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
994-1207 |
2.86e-18 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 85.11 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRSKL 1071
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSG-TVRSNLDPFNQYTedqiwdALERTHMKECIAQLPLKLE-SEVME-NGDNFSVGERQLLCIARALLRH 1148
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGLY------GLKGDELTARLEELADRLGmEELLDrRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1149 CKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
355-544 |
3.01e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.87 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 355 DERPSPEEEEGKHIHLGHLRLQR-----TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtlL----EGSIAI--S 423
Cdd:COG4178 350 EAASRIETSEDGALALEDLTLRTpdgrpLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG----LwpygSGRIARpaG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 424 GTFAYVAQQAWILNATLRDNILF---GKEYDEERYNSVLNSCCLrPDLAilpsSDLTEIGERGANLSGGQRQRISLARAL 500
Cdd:COG4178 426 ARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGL-GHLA----ERLDEEADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900605 501 YSDRSIYILDDPLSALDAHVGNHIFnSAIRKHLKSKTVLFVTHQ 544
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALY-QLLREELPGTTVISVGHR 543
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
45-267 |
3.23e-18 |
|
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: 86.50 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 45 YRTGVRLRGAILTMAFKKILKLKNIKEKS--LGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFL 122
Cdd:cd18559 63 SIGGIFASRAVHLDLYHKALRSPISFFERtpSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 123 GSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSI 202
Cdd:cd18559 143 GIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRAL 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 203 TVGVAPIVVVIASVVTFSVHMTLGFD--LTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 267
Cdd:cd18559 223 AVRLWCVGPCIVLFASFFAYVSRHSLagLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
651-1156 |
3.37e-18 |
|
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: 89.86 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 651 IQAAGGPLAFLVIMALFmlnvgSTAFSTWWLSYwIkqgsgNTTVTRGNETSVSdsmkdnprmqyYASIYALSMAVMLILK 730
Cdd:COG4615 8 LRESRWLLLLALLLGLL-----SGLANAGLIAL-I-----NQALNATGAALAR-----------LLLLFAGLLVLLLLSR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 731 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMD---EVDVRLPFqaemFIQNVILVFFCVGM 807
Cdd:COG4615 66 LASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRtisQAFVRLPE----LLQSVALVLGCLAY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 808 IAgvfpW-----FLVAVGPLVILFSVLHIVSRVLIRELKRLDNiTQSPFLSHITSSIQGLA--TIHAyNKGQEFLHRY-- 878
Cdd:COG4615 142 LA----WlspplFLLTLVLLGLGVAGYRLLVRRARRHLRRARE-AEDRLFKHFRALLEGFKelKLNR-RRRRAFFDEDlq 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 879 ---QELLDDNQAPFFLFTCAMRWlavrldlISIALITTTGLmIVLMHGQIPPAYAGLAISYAvqLTGLF------QFTVR 949
Cdd:COG4615 216 ptaERYRDLRIRADTIFALANNW-------GNLLFFALIGL-ILFLLPALGWADPAVLSGFV--LVLLFlrgplsQLVGA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 950 LASETEARfTSVERINHYikTLSLEAPARIKNKAPSPDWPQE-GEVTFENAEMRYR---ENLPLVLKKVSFTIKPKEKIG 1025
Cdd:COG4615 286 LPTLSRAN-VALRKIEEL--ELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPgedGDEGFTLGPIDLTIRRGELVF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1026 IVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFsgtvRSNLDPFNQYTEDQIWDALE 1105
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLE 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 1106 RthmkeciaqlpLKLESEVMENGDNF-----SVGERQLLCIARALLRHCKILILDE 1156
Cdd:COG4615 439 R-----------LELDHKVSVEDGRFsttdlSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
375-581 |
5.08e-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: 85.35 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 375 LQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLR 441
Cdd:cd03288 33 LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIdisklplhtlrsrLSIILQDPILFSGSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 521
Cdd:cd03288 113 FNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 522 NhIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELM-NLNGDYATI 581
Cdd:cd03288 193 N-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
995-1229 |
5.21e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.42 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 995 TFENAEMRYrENLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlRsKLSII 1074
Cdd:COG3840 3 RLDDLTYRY-GDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1075 PQEPVLFSG-TVRSN----LDPFNQYTEDQ---IWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALL 1146
Cdd:COG3840 77 FQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1147 RHCKILILDEATAAMD----TETDLLIQETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSS 1221
Cdd:COG3840 146 RKRPILLLDEPFSALDpalrQEMLDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPP 223
|
....*...
gi 1622900605 1222 rfyAMFAA 1229
Cdd:COG3840 224 ---PALAA 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
381-573 |
7.41e-18 |
|
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: 84.27 E-value: 7.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 381 SIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQAWIL-NATLRDNI-L 445
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFpHMTVEENIaL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FGK--EYDEERYNSvlnscclRPD-LAILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvg 521
Cdd:cd03295 99 VPKllKWPKEKIRE-------RADeLLALVGLDPAEFADRyPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP--- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 522 nhIFNSAIR---KHLKS---KTVLFVTHQLQ-YLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:cd03295 169 --ITRDQLQeefKRLQQelgKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
378-566 |
7.91e-18 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 83.46 E-value: 7.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 378 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-----------TFAYVAQQ-AWILNATLRDNIL 445
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FG-------KEYDEERYNSVlnscclrpdlailpsSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:cd03301 95 FGlklrkvpKDEIDERVREV---------------AELLQIEHlldrKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 515 ALDAHVgnhifNSAIRKHLKS------KTVLFVTH-QLQYLVDCDEVIFMKEGCITERG 566
Cdd:cd03301 160 NLDAKL-----RVQMRAELKRlqqrlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
366-557 |
8.67e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.53 E-value: 8.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 366 KHIHL---GHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------FAYVAQQ-- 432
Cdd:COG4525 7 RHVSVrypGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadRGVVFQKda 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 433 --AWiLNAtlRDNILFGKeydeeRYNSVLNSCCLRPDLAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYIL 509
Cdd:COG4525 87 llPW-LNV--LDNVAFGL-----RLRGVPKAERRARAEELLALVGLADFARRRiWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 510 DDPLSALDA----HVGNHIFNSAIRKHlksKTVLFVTHqlqylvDCDEVIFM 557
Cdd:COG4525 159 DEPFGALDAltreQMQELLLDVWQRTG---KGVFLITH------SVEEALFL 201
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
379-555 |
1.01e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG--TFAYVAQQ---AWILNATLRDNI---LFGKEY 450
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRsevPDSLPLTVRDLVamgRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 451 DEERYN----SVLNSCCLRPDLAILPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 526
Cdd:NF040873 88 LWRRLTrddrAAVDDALERVGLADLAGRQLGE-------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160
|
170 180
....*....|....*....|....*....
gi 1622900605 527 SAIRKHLKSKTVLFVTHQLQYLVDCDEVI 555
Cdd:NF040873 161 LLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
381-596 |
1.57e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.54 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 381 SIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQ-------QAWIL--NATLRDNILFG- 447
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQrdicmvfQSYALfpHMSLGENVGYGl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 448 ---KEYDEERYNSVlnscclRPDLAILpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHvgnh 523
Cdd:PRK11432 104 kmlGVPKEERKQRV------KEALELV---DLAGFEDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDAN---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 524 ifnsaIRKHLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL---------MNLNGDyATIFN 583
Cdd:PRK11432 171 -----LRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELyrqpasrfmASFMGD-ANIFP 244
|
250
....*....|...
gi 1622900605 584 NLLLGDTppVEIN 596
Cdd:PRK11432 245 ATLSGDY--VDIY 255
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
379-573 |
1.76e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 83.85 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQ-AWILNATL 440
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaamsrkelrelrrkkISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 441 RDNILFG-------KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:cd03294 120 LENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 514 SALDahvgnhifnSAIRKHLKS----------KTVLFVTHqlqylvDCDEVI-------FMKEGCITERGTHEELMN 573
Cdd:cd03294 189 SALD---------PLIRREMQDellrlqaelqKTIVFITH------DLDEALrlgdriaIMKDGRLVQVGTPEEILT 250
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
364-563 |
2.00e-17 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 82.30 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 364 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------TFAYVAQQA 433
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 wilnatlrDNILFGkeydeeryNSVLNSCCLRPDLA---------ILPSSDLTEIGERG-ANLSGGQRQRISLARALYSD 503
Cdd:cd03226 81 --------DYQLFT--------DSVREELLLGLKELdagneqaetVLKDLDLYALKERHpLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 504 RSIYILDDPLSALDAH----VGNHIfnsairKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT 563
Cdd:cd03226 145 KDLLIFDEPTSGLDYKnmerVGELI------RELAAqgKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
382-572 |
2.28e-17 |
|
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: 85.16 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQAWIL-NATLRDN 443
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFGK-----EYDEERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:TIGR02142 96 LRYGMkrarpSERRISFERVIELLGIGHLLGRLP-----------GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 519 HVGNHI--FNSAIRKHLKSKtVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 572
Cdd:TIGR02142 165 PRKYEIlpYLERLHAEFGIP-ILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
989-1228 |
2.89e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.22 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 989 PQEGEVTFENAEMRYRENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLV----ELSGGCIKIDGVRISDI 1062
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggVTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIagleKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1063 GladlrSKLSIIPQEPVLFs-gTVRSN---------LDPfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfS 1132
Cdd:COG1116 79 G-----PDRGVVFQEPALLpwlTVLDNvalglelrgVPK--AERRERARELLELVGLAGFEDAYPHQL-----------S 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1133 VGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAH------RLhtvlgSDRIMVLAQ- 1203
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHdvdeavFL-----ADRVVVLSAr 215
|
250 260 270
....*....|....*....|....*....|.
gi 1622900605 1204 -GQV-----VEFDTPSVLLSNDSSRFYAMFA 1228
Cdd:COG1116 216 pGRIveeidVDLPRPRDRELRTSPEFAALRA 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1011-1208 |
3.56e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI---SDIGLADLRSKLSIIPQEPVlfsgtvrS 1087
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY-------A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1088 NLDPfNQYTEDQIWDALeRTH-----------MKECIAQLPLKLEsEVMENGDNFSVGERQLLCIARALLRHCKILILDE 1156
Cdd:PRK10261 413 SLDP-RQTVGDSIMEPL-RVHgllpgkaaaarVAWLLERVGLLPE-HAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1157 ATAAMDTET-----DLL--IQETIREAFadctmLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:PRK10261 490 AVSALDVSIrgqiiNLLldLQRDFGIAY-----LFISHDMAVVERiSHRVAVMYLGQIVE 544
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
379-573 |
4.83e-17 |
|
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: 82.00 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILF 446
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 G----KEYDEERYNSVLNsccLRPDLAIlpssdlTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVg 521
Cdd:cd03299 95 GlkkrKVDKKEIERKVLE---IAEMLGI------DHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 522 nhifNSAIRKHLK------SKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:cd03299 165 ----KEKLREELKkirkefGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
373-566 |
9.38e-17 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 80.23 E-value: 9.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 373 LRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQAwiLNATLRDNILFGKE 449
Cdd:cd03298 8 FSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRP--VSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 450 YDEERYnsvlnscclrpDLAILPSSDLTEIgERGA-------------------NLSGGQRQRISLARALYSDRSIYILD 510
Cdd:cd03298 86 TVEQNV-----------GLGLSPGLKLTAE-DRQAievalarvglaglekrlpgELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 511 DPLSALDAHVGNHIFNSAIRKHLKSK-TVLFVTHQLQYLVDCDE-VIFMKEGCITERG 566
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
379-573 |
1.07e-16 |
|
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: 80.79 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAwilnA---- 438
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditglsekelyelrrrIGMLFQGG----Alfds 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 -TLRDNILFG-KEYD-------EERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYIL 509
Cdd:COG1127 97 lTVFENVAFPlREHTdlseaeiRELVLEKLELVGLPGAADKMPSE-----------LSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 510 DDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:COG1127 166 DEPTAGLDPITSAVIDEliRELRDELGL-TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1011-1207 |
2.29e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLgM-ALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPQEPVLFSG-TVR 1086
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL-MkILYGLYQPDSGEILIDGkpVRIRSPRDA-IALGIGMVHQHFMLVPNlTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNL----DPFNQYTEDqiWDALeRTHMKECIAQLPLKL--ESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAA 1160
Cdd:COG3845 99 ENIvlglEPTKGGRLD--RKAA-RARIRELSERYGLDVdpDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1161 M-DTETDLLIqETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:COG3845 172 LtPQEADELF-EILRR-LAAegKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1010-1218 |
2.74e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.08 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGC-----IKIDGVRI--SDIGLADLRSKLSIIPQEPVLFS 1082
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1083 GTV---------------RSNLDpfnqytedqiwDALERThmkeciaqlpLK---LESEV----MENGDNFSVGERQLLC 1140
Cdd:COG1117 106 KSIydnvayglrlhgiksKSELD-----------EIVEES----------LRkaaLWDEVkdrlKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1141 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSV 1214
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFGPTEQ 239
|
....
gi 1622900605 1215 LLSN 1218
Cdd:COG1117 240 IFTN 243
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
994-1221 |
2.92e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 80.18 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLVLKKVSFTIkPKEK-IGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLS 1072
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNI-PKGQwTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1073 IIPQEPV-LFSGT-----VRSNLDPFNQYTEDqiwdalerthMKECIAQLpLKlESEVMENGDN----FSVGERQLLCIA 1142
Cdd:PRK13648 87 IVFQNPDnQFVGSivkydVAFGLENHAVPYDE----------MHRRVSEA-LK-QVDMLERADYepnaLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1143 RALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDS 1220
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
.
gi 1622900605 1221 S 1221
Cdd:PRK13648 235 E 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1010-1207 |
4.14e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSI--IPQEPVLFSG-TVR 1086
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLD---PFNQytedqiwDALERthMKECIAQLPLKLESEVmeNGDNFSVGERQLLCIARALLRHCKILILDEATAAMD- 1162
Cdd:PRK15439 105 ENILfglPKRQ-------ASMQK--MKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900605 1163 TETDLLIQEtIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:PRK15439 174 AETERLFSR-IRELLAqGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
376-564 |
4.17e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.73 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------------TFAYVAQQA------ 433
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrDIQMVFQDSisavnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 -----WILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISLARALYSDRSIYI 508
Cdd:PRK10419 105 rktvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVL----------DKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 509 LDDPLSALDAHVGNHIFnsAIRKHLKSKT---VLFVTHQLQyLVD--CDEVIFMKEGCITE 564
Cdd:PRK10419 175 LDEAVSNLDLVLQAGVI--RLLKKLQQQFgtaCLFITHDLR-LVErfCQRVMVMDNGQIVE 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
994-1208 |
4.85e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 78.67 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLP--LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrSKL 1071
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFS-GTVRSN--LDPfnqytEDQIWDALE-RTHMKECIAQLPLKlesevmENGDNF----SVGERQLLCIAR 1143
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvaLGL-----ELQGVPKAEaRERAEELLELVGLS------GFENAYphqlSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1144 ALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLH-TVLGSDRIMVLAQ--GQVVE 1208
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
379-573 |
5.90e-16 |
|
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: 79.51 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILgQMTLLEGSIAISG-------------TFAYVAQQAWILNATLRDNI- 444
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGVIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 445 LFGKEYDEERYNsVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvgnhI 524
Cdd:cd03289 99 PYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-----I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 525 FNSAIRKHLKSK----TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:cd03289 173 TYQVIRKTLKQAfadcTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1010-1207 |
6.30e-16 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 77.59 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIglaDLRSKLSIIPQEPVLFSG-TVR 1086
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKR---SFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLdpfnQYTedqiwdalerthmkeciAQLplklesevmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1166
Cdd:cd03213 101 ETL----MFA-----------------AKL------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900605 1167 LLIQETIRE-AFADCTMLTIAHRLHTVLGS--DRIMVLAQGQVV 1207
Cdd:cd03213 148 LQVMSLLRRlADTGRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
994-1226 |
6.56e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG-LADLRSKLS 1072
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1073 IIPQEP-VLFSG-TVRSNLdPFNqyTEDQIWDALE-RTHMKECIAQlpLKLESEVMENGDNFSVGERQLLCIARALLRHC 1149
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDL-AFG--PENLCLPPIEiRKRVDRALAE--IGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1150 KILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAM 1226
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1010-1238 |
9.37e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.90 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIkPKEKIGIV-GRTGSGKSSLGMALFRLVELSGGCIkidgvrisdigLADlRSkLSIIPQEPVLFSGTVRSN 1088
Cdd:PTZ00243 675 LLRDVSVSV-PRGKLTVVlGATGSGKSTLLQSLLSQFEISEGRV-----------WAE-RS-IAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 LDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET-DL 1167
Cdd:PTZ00243 741 ILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgER 820
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1168 LIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQvVEFdtpsvllSNDSSRF-----YAMFAA--AENKVAVKG 1238
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGR-VEF-------SGSSADFmrtslYATLAAelKENKDSKEG 890
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
376-573 |
1.04e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 77.66 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDN 443
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNyALFPHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFG-------KEYDEERYNSVLnscclrpDLAilpssDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:cd03300 93 IAFGlrlkklpKAEIKERVAEAL-------DLV-----QLEGYANRKpSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 516 LDAHvgnhifnsaIRKHLKSK----------TVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:cd03300 161 LDLK---------LRKDMQLElkrlqkelgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
366-573 |
1.05e-15 |
|
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: 77.47 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 366 KHIHLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQ 431
Cdd:cd03224 4 ENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 432 -QAWILNATLRDNILFG-----KEYDEERYNSVLNsccLRPDLAilpssdlTEIGERGANLSGGQRQRISLARALYSDRS 505
Cdd:cd03224 83 gRRIFPELTVEENLLLGayarrRAKRKARLERVYE---LFPRLK-------ERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 506 IYILDDPLSALDAHVGNHIFNsAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFE-AIRE-LRDEgvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
379-562 |
1.05e-15 |
|
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: 77.18 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWilnATLRDNI--LFgkeydeERYN 456
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI---NELRQKVgmVF------QQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 457 -----SVLNSCCLRPDLAI-LPSSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:cd03262 87 lfphlTVLENITLAPIKVKgMSKAEAEERALEllekvGladkadaypAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900605 517 DAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCI 562
Cdd:cd03262 167 DPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
376-564 |
2.34e-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: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------------TFAYVAQQA------ 433
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSpsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 -----WILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAilpssdlteiGERGANLSGGQRQRISLARALYSDRSIYI 508
Cdd:TIGR02769 104 rmtvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDA----------DKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 509 LDDPLSALDAHVGNHIFnsAIRKHLKSK---TVLFVTHQLQyLVD--CDEVIFMKEGCITE 564
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVIL--ELLRKLQQAfgtAYLFITHDLR-LVQsfCQRVAVMDKGQIVE 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
379-573 |
2.59e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.72 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWILNATLRD 442
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirklvgIVFQNPETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGKEydeerynsvlnSCCLRP-DLAILPSSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:PRK13644 98 DLAFGPE-----------NLCLPPiEIRKRVDRALAEIGlekyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 516 LDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
997-1232 |
3.49e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 76.22 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYREnlpLVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGVRIS----DI-GLADLRSKL 1071
Cdd:cd03299 4 ENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVL-------LETIAGFIKPDSGKILlngkDItNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSgtvrsnldpfNQYTEDQIWDALE-RTHMKEciaqlplKLESEVME-------------NGDNFSVGERQ 1137
Cdd:cd03299 74 SYVPQNYALFP----------HMTVYKNIAYGLKkRKVDKK-------EIERKVLEiaemlgidhllnrKPETLSGGEQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1138 LLCIARALLRHCKILILDEATAAMDTET-DLLIQE--TIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1213
Cdd:cd03299 137 RVAIARALVVNPKILLLDEPFSALDVRTkEKLREElkKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPE 215
|
250
....*....|....*....
gi 1622900605 1214 VLLSNDSSRFYAMFAAAEN 1232
Cdd:cd03299 216 EVFKKPKNEFVAEFLGFNN 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
376-572 |
4.20e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------AISGTFAYVAQQAWI-LNATLR 441
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVlvagddvealsarAASRRVASVPQDTSLsFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGKEYDEERYN-------SVLNSCCLRPDLAILPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:PRK09536 96 QVVEMGRTPHRSRFDtwtetdrAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 515 ALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 572
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
382-544 |
4.53e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQAWIL---NA-----TLRDNILFGKEy 450
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiDDPDVAEACHYLghrNAmkpalTVAENLEFWAA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 451 deerynsVLNSCCLRPD--LAILPSSDLTEIgeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHIFNSA 528
Cdd:PRK13539 100 -------FLGGEELDIAaaLEAVGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAEL 169
|
170
....*....|....*..
gi 1622900605 529 IRKHLKSK-TVLFVTHQ 544
Cdd:PRK13539 170 IRAHLAQGgIVIAATHI 186
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
382-544 |
5.03e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 75.09 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWILNA-TLRDNILFgk 448
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLPGLKPElSALENLHF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 449 eydeerYNSVLNSCCLRPDLAiLPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGNHIFNS 527
Cdd:TIGR01189 97 ------WAAIHGGAQRTIEDA-LAAVGLTGFEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAG 168
|
170
....*....|....*...
gi 1622900605 528 AIRKHL-KSKTVLFVTHQ 544
Cdd:TIGR01189 169 LLRAHLaRGGIVLLTTHQ 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
994-1218 |
5.28e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.76 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLV---ELSGGCIKIDGVRISDIGLADLRSK 1070
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1071 LSIIPQepvlfsgtvrsnlDPFNQY----TEDQIWDALE-----RTHMKECIAQLplkLESEVMEN-----GDNFSVGER 1136
Cdd:PRK13640 86 VGIVFQ-------------NPDNQFvgatVGDDVAFGLEnravpRPEMIKIVRDV---LADVGMLDyidsePANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1137 QLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1214
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
....
gi 1622900605 1215 LLSN 1218
Cdd:PRK13640 230 IFSK 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1010-1214 |
7.57e-15 |
|
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: 75.16 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRS-KLSIIPQ--------- 1076
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRArHVGFVFQsfqllptlt 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1077 --EPVLFSGTVRSNLDPFNQYTEdqiwdALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1154
Cdd:COG4181 107 alENVMLPLELAGRRDARARARA-----LLERVGLGHRLDHYPAQL-----------SGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1155 DEATAAMDTET-----DLLIQETiREAFAdcTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSV 1214
Cdd:COG4181 171 DEPTGNLDAATgeqiiDLLFELN-RERGT--TLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1010-1219 |
8.73e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVL-FSGTVRS- 1087
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1088 ---NLDPFNQ-YTEDQ--IWDALERThmkECIA-------QLplklesevmengdnfSVGERQLLCIARAL--LRHC--- 1149
Cdd:PRK13548 97 vamGRAPHGLsRAEDDalVAAALAQV---DLAHlagrdypQL---------------SGGEQQRVQLARVLaqLWEPdgp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1150 -KILILDEATAAMdtetDLLIQETIreafadctmLTIAHR------------LH----TVLGSDRIMVLAQGQVVEFDTP 1212
Cdd:PRK13548 159 pRWLLLDEPTSAL----DLAHQHHV---------LRLARQlaherglavivvLHdlnlAARYADRIVLLHQGRLVADGTP 225
|
....*..
gi 1622900605 1213 SVLLSND 1219
Cdd:PRK13548 226 AEVLTPE 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
379-571 |
9.19e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.04 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAISGT--------------------FayvaQQAW 434
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NLLErptsGSVLVDGVdltalserelraarrkigmiF----QHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 435 ILNA-TLRDNILF-------GKEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYS 502
Cdd:COG1135 93 LLSSrTVAENVALpleiagvPKAEIRKRVAELL---------------ELVGLSDKAdaypSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 503 DRSIYILDDPLSALDAHVGNHIFN--SAIRKHLKsKTVLFVTHQLqylvD-----CDEVIFMKEGCITERGTHEEL 571
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDllKDINRELG-LTIVLITHEM----DvvrriCDRVAVLENGRIVEQGPVLDV 228
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
707-964 |
9.76e-15 |
|
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: 76.44 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 707 KDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVR 786
Cdd:cd07346 33 GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 787 LPFQAEMFIQNVILVFFCVGMIAgVFPW--FLVAVGPLVILFSVLHIVSRvLIRELKRLDNITQSPFLSHITSSIQGLAT 864
Cdd:cd07346 113 VSSGLLQLLSDVLTLIGALVILF-YLNWklTLVALLLLPLYVLILRYFRR-RIRKASREVRESLAELSAFLQESLSGIRV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 865 IHAYNKGQEFLHRYQELLDDNqapFFLFTCAMRWLAvrLDLISIALITTTGLMIVL-------MHGQIPPAYAGLAISYA 937
Cdd:cd07346 191 VKAFAAEEREIERFREANRDL---RDANLRAARLSA--LFSPLIGLLTALGTALVLlyggylvLQGSLTIGELVAFLAYL 265
|
250 260
....*....|....*....|....*..
gi 1622900605 938 VQLTGLFQFTVRLASETEARFTSVERI 964
Cdd:cd07346 266 GMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
379-574 |
9.77e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.68 E-value: 9.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQAWILNA-----------TLRDNILF 446
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTvfqsyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 G----KEYDEERYNSVLNScclrpdlaiLPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 521
Cdd:PRK09452 110 GlrmqKTPAAEITPRVMEA---------LRMVQLEEFAQRKpHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 522 NHIFNSAirKHLKSK---TVLFVTH-QLQYLVDCDEVIFMKEGCITERGT----HEELMNL 574
Cdd:PRK09452 181 KQMQNEL--KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTpreiYEEPKNL 239
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
379-571 |
9.82e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.03 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAISGTfaYVAQQAWILNAtLRDNI--LFgkeyde 452
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCI----NLLEepdsGTITVDGE--DLTDSKKDINK-LRRKVgmVF------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 453 ERYN-----SVLNSCCLRPdlaI----LPSSDLTEIGER-----G---------ANLSGGQRQRISLARALYSDRSIYIL 509
Cdd:COG1126 84 QQFNlfphlTVLENVTLAP---IkvkkMSKAEAEERAMEllervGladkadaypAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 510 DDPLSALD----AHVGNHIfnsairKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 571
Cdd:COG1126 161 DEPTSALDpelvGEVLDVM------RDLAKEgmTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
960-1237 |
1.03e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 79.60 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 960 SVERINHYIKTLSLEaPARIKNKAPSPDwpQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGM 1039
Cdd:TIGR00957 606 SLKRLRIFLSHEELE-PDSIERRTIKPG--EGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1040 ALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLK 1119
Cdd:TIGR00957 683 ALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSG 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1120 LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETI---REAFADCTMLTIAHRLHTVLGSD 1196
Cdd:TIGR00957 750 DRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVD 829
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1622900605 1197 RIMVLAQGQVVEFDTPSVLLSNDSS--RFYAMFAAAENKVAVK 1237
Cdd:TIGR00957 830 VIIVMSGGKISEMGSYQELLQRDGAfaEFLRTYAPDEQQGHLE 872
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
997-1217 |
1.07e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRY-RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIP 1075
Cdd:PRK13642 8 ENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1076 QEP-VLFSGTVRSNLDPFNQytEDQiwdALERTHMKECI--AQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKIL 1152
Cdd:PRK13642 88 QNPdNQFVGATVEDDVAFGM--ENQ---GIPREEMIKRVdeALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1153 ILDEATAAMD----TETDLLIQEtIREAFaDCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLS 1217
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHE-IKEKY-QLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1010-1208 |
1.41e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 75.23 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSKLSIIPQE-PVLFSG-- 1083
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 TVRSNL-DPFNQYTEdqiwdaLERTHMKECIAQL--PLKLESEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEATA 1159
Cdd:TIGR02769 106 TVRQIIgEPLRHLTS------LDESEQKARIAELldMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1160 AMDTETDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:TIGR02769 180 NLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
379-573 |
1.46e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.41 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKtSLISAIL-GQMTLLEGSIAISG------TFAYVAQQAWI---------LNATLRD 442
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGK-STISKILtGLLKPQSGEIKIDGitiskeNLKEIRKKIGIifqnpdnqfIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGKEydeerynsvlNSCCLRPDLA--ILPSSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:PRK13632 104 DIAFGLE----------NKKVPPKKMKdiIDDLAKKVGMEDyldkEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 517 DAHVGNHI--FNSAIRKHlKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK13632 174 DPKGKREIkkIMVDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
376-566 |
1.60e-14 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 73.79 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF------------AYVAQQAWILNATLRDN 443
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSyqkniealrrigALIEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 I-LFGKEYD--EERYNSVLNSCCLRpdlailpssdlTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhV 520
Cdd:cd03268 93 LrLLARLLGirKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP-D 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900605 521 GNHIFNSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 566
Cdd:cd03268 161 GIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
707-947 |
1.61e-14 |
|
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: 75.50 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 707 KDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvr 786
Cdd:cd18544 35 GDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEAL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 787 lpfqAEMFIQNVILVFFCVGMIAGVF----------PWFLVAVGPLVILFSVLH-IVSRVLIRELKRLdnitqspfLSHI 855
Cdd:cd18544 112 ----NELFTSGLVTLIGDLLLLIGILiamfllnwrlALISLLVLPLLLLATYLFrKKSRKAYREVREK--------LSRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 856 TS----SIQGLATIHAYNKGQEFLHRYQELlddNQApffLFTCAMRwlAVRLDLI---SIALITTTGLMIVLMHGqippa 928
Cdd:cd18544 180 NAflqeSISGMSVIQLFNREKREFEEFDEI---NQE---YRKANLK--SIKLFALfrpLVELLSSLALALVLWYG----- 246
|
250
....*....|....*....
gi 1622900605 929 yAGLAISYAVQLTGLFQFT 947
Cdd:cd18544 247 -GGQVLSGAVTLGVLYAFI 264
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
379-560 |
1.77e-14 |
|
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: 72.46 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfayvaqqawilnatlrdnilfgkeydEERYNSv 458
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVSFAS- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 459 lnscclrPDLAIlpssdlteigERGAN----LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsAIRKhLK 534
Cdd:cd03216 69 -------PRDAR----------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK-VIRR-LR 129
|
170 180
....*....|....*....|....*....
gi 1622900605 535 S--KTVLFVTHQLQYLVD-CDEVIFMKEG 560
Cdd:cd03216 130 AqgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
394-571 |
1.95e-14 |
|
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: 75.99 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 394 ICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQ---------QAWIL--NATLRDNILFG----KEYDEERYNS 457
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdVTNVPPhlrhinmvfQSYALfpHMTVEENVAFGlkmrKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 458 VLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLK-S 535
Cdd:TIGR01187 81 VL---------EALRLVQLEEFADRKpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlG 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622900605 536 KTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:TIGR01187 152 ITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1010-1233 |
2.05e-14 |
|
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: 78.80 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLFSGTVRSNL 1089
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1090 DPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDlli 1169
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE--- 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 1170 qetiREAFADCTMLTIAHRlhtvlgsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENK 1233
Cdd:TIGR01271 585 ----KEIFESCLCKLMSNK-------TRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
372-560 |
2.08e-14 |
|
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: 72.85 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 372 HLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVA----QQA 433
Cdd:cd03215 9 GLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 WILNATLRDNILfgkeydeerynsvlnscclrpdLAILpssdlteigerganLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:cd03215 89 LVLDLSVAENIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900605 514 SALDahVG--NHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEG 560
Cdd:cd03215 133 RGVD--VGakAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
382-560 |
2.16e-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: 71.71 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--FAYVAQqawilnatlrdnilfgkeydeerynsvl 459
Cdd:cd03221 19 ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQ---------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 460 nscclrpdlailpssdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDahvgnhIFN-SAIRKHLKS--K 536
Cdd:cd03221 71 --------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD------LESiEALEEALKEypG 118
|
170 180
....*....|....*....|....*.
gi 1622900605 537 TVLFVTHQlQYLVD--CDEVIFMKEG 560
Cdd:cd03221 119 TVILVSHD-RYFLDqvATKIIELEDG 143
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1010-1205 |
2.27e-14 |
|
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: 74.01 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCI-------KIDGVRISDIGLADLRSK--------LSII 1074
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQASPREILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1075 PQ--------EPVLFSGTVRsnldpfnQYTEDQIWDALERTHMKECIAQLPLKlesevmengdNFSVGERQLLCIARALL 1146
Cdd:COG4778 106 PRvsaldvvaEPLLERGVDR-------EEARARARELLARLNLPERLWDLPPA----------TFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1147 RHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQ 1205
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
377-578 |
2.63e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT----------LLEGSIAISGTFA-----------YVAQQAWI 435
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGRLArdirksrantgYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 436 LNA-TLRDNILFGKEYDEERYNSvlnscCLR---PDLAILPSSDLTEIG------ERGANLSGGQRQRISLARALYSDRS 505
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPFWRT-----CFSwftREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 506 IYILDDPLSALDAHVGnHIFNSAIR--KHLKSKTVLFVTHQLQY-LVDCDEVIFMKEGCITERGTHEELMNLNGDY 578
Cdd:PRK09984 173 VILADEPIASLDPESA-RIVMDTLRdiNQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFDH 247
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
379-560 |
3.86e-14 |
|
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: 72.70 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---------TFAYVAQQAWI-LNATLRDNILF-- 446
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLyPKMKVIDQLVYla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 -----GKEYDEERYNSVLNscclRPDLAILPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAhVG 521
Cdd:cd03269 96 qlkglKKEEARRRIDEWLE----RLELSEYANKRVEE-------LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900605 522 NHIFNSAIRKHL-KSKTVLFVTHQLQyLVD--CDEVIFMKEG 560
Cdd:cd03269 164 VELLKDVIRELArAGKTVILSTHQME-LVEelCDRVLLLNKG 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1013-1207 |
3.91e-14 |
|
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: 72.71 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1013 KVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD----IGLADLRSKLSIIPQEPVLFSG-TVRS 1087
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1088 NL--------DPFNQYTEDQIWDALERTHMKEciaQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 1159
Cdd:cd03297 95 NLafglkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1160 AMDTETDLLIQETIREAFAD--CTMLTIAHRLHTV-LGSDRIMVLAQGQVV 1207
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1004-1227 |
3.94e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1004 RENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS----KLSIIPQEPV 1079
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1080 LFSG-TVRSNldpfNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 1158
Cdd:PRK10070 117 LMPHmTVLDN----TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1159 AAMDTETDLLIQETI--REAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMF 1227
Cdd:PRK10070 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
383-566 |
4.10e-14 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 72.59 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 383 DLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQAWIL-NATLRDNILFG--- 447
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQshtglapyqrpVSMLFQENNLFaHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 448 ----KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 523
Cdd:TIGR01277 98 glklNAEQQEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900605 524 IFnsAIRKHL---KSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 566
Cdd:TIGR01277 167 ML--ALVKQLcseRQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1010-1208 |
4.37e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.41 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGVRISDIGLADLRSKLSIIPQEP------ 1078
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1079 VLFS----GTVRSNLDPFNQYTEDQIWDALERthmkeciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILIL 1154
Cdd:PRK14247 98 SIFEnvalGLKLNRLVKSKKELQERVRWALEK-------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1155 DEATAAMDTETDLLIQETIREAFADCTMLTIAH------RLhtvlgSDRIMVLAQGQVVE 1208
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1008-1218 |
4.74e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1008 PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG-LADLRSKLSIIPQEP-------- 1078
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivati 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1079 ----VLFSGtvrSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1154
Cdd:PRK13633 103 veedVAFGP---ENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 1155 DEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
379-573 |
5.28e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.72 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------FAYVAQQ------------------AW 434
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdYKYRCKHirmifqdpntslnprlniGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 435 ILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLteigerganlSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:COG4167 109 ILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHML----------SSGQKQRVALARALILQPKIIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 515 ALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEELMN 573
Cdd:COG4167 179 ALDMSVRSQIIN--LMLELQEKlgiSYIYVSQHLG-IVKhiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1006-1232 |
6.60e-14 |
|
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: 73.74 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1006 NLPL----VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvrisdigladlrsKLSIIPQEPVLF 1081
Cdd:cd03291 44 NLCLvgapVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1082 SGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1161
Cdd:cd03291 111 PGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1162 DTETDlliqetiREAFADCTMLTIAHRlhtvlgsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 1232
Cdd:cd03291 191 DVFTE-------KEIFESCVCKLMANK-------TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
369-573 |
7.40e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 369 HLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAI--LGQMT---LLEGSIAISGTFA----------YVAQQA 433
Cdd:PRK09493 10 HFGPTQV---LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITsgdLIVDGLKVNDPKVderlirqeagMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 WIL-NATLRDNILFG--------KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDR 504
Cdd:PRK09493 87 YLFpHLTALENVMFGplrvrgasKEEAEKQARELLAKVGLAERAHHYPSE-----------LSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 505 SIYILDDPLSALDAHVGNHIFNsaIRKHLKSK--TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 573
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLK--VMQDLAEEgmTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1010-1208 |
8.43e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 74.34 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLVEL----SGGCIKIDGVRISDI---GLADLRSKLSIIPQEPVLFS 1082
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINLlerpTSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1083 G-TVRSNldpfnqytedqiwdalerthmkecIAqLPLKL--------ESEVME---------NGDNF----SVGERQLLC 1140
Cdd:COG1135 96 SrTVAEN------------------------VA-LPLEIagvpkaeiRKRVAEllelvglsdKADAYpsqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 1141 IARALLRHCKILILDEATAAMDTET-----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETtrsilDLL--KDINREL-GLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
379-571 |
8.79e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILG-QMTLLE--GSIAISGT----------FAYVAQQAWILNA-TLRDNI 444
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKgsGSVLLNGMpidakemraiSAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 445 LF----------GKEYDEERYNSVLNscclrpDLAILPSSDlTEIGERGA--NLSGGQRQRISLARALYSDRSIYILDDP 512
Cdd:TIGR00955 121 MFqahlrmprrvTKKEKRERVDEVLQ------ALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 513 LSALDAHVGNHIFnsAIRKHL--KSKTVLFVTHQLQYLVDC--DEVIFMKEGCITERGTHEEL 571
Cdd:TIGR00955 194 TSGLDSFMAYSVV--QVLKGLaqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
379-574 |
9.85e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 9.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFayvaqqAWIL--------NATLRDNILFG--- 447
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV------SALLelgagfhpELTGRENIYLNgrl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 448 -----KEYDeERYNSVLnscclrpdlailpssDLTEIGE------RgaNLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:COG1134 116 lglsrKEID-EKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 517 DAHvgnhiFN----SAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMNL 574
Cdd:COG1134 178 DAA-----FQkkclARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
379-573 |
9.92e-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: 72.42 E-value: 9.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEG-SIAISGT-------------FAYV--AQQAWIL-NATLR 441
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggedvwelrkrIGLVspALQLRFPrDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNIL---FG-----KEYDEERYNSVLnscclrpdlAILPSSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDP 512
Cdd:COG1119 99 DVVLsgfFDsiglyREPTDEQRERAR---------ELLELLGLAHLADRPfGTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 513 LSALDAHvGNHIFNSAIRK--HLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 573
Cdd:COG1119 170 TAGLDLG-ARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVLT 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
376-577 |
1.01e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.13 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtFAYVAQQAW----------------ILNAT 439
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-MVLSEETVWdvrrqvgmvfqnpdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 440 LRDNILFGKE-----YDE--ERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDP 512
Cdd:PRK13635 99 VQDDVAFGLEnigvpREEmvERVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 513 LSALDAhVGNHIFNSAIRkHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGD 577
Cdd:PRK13635 168 TSMLDP-RGRREVLETVR-QLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
379-555 |
1.28e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNATLRDNIL 445
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 F-----GKEYDEERynsvlnsccLRPDLAI--LPSSDLTEigeRGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:PRK10247 103 FpwqirNQQPDPAI---------FLDDLERfaLPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622900605 519 HvGNHIFNSAIRKHLKSK--TVLFVTHQLQYLVDCDEVI 555
Cdd:PRK10247 171 S-NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVI 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
994-1227 |
1.38e-13 |
|
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: 71.50 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrsklsi 1073
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVlfsGTVRSNLDPFNQYT-EDQIWDALERTHMKECI------AQLPL-KLESEVMENGDNFSVGERQLLCIARAL 1145
Cdd:cd03300 69 PHKRPV---NTVFQNYALFPHLTvFENIAFGLRLKKLPKAEikervaEALDLvQLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1146 LRHCKILILDEATAAMDTETDLLIQETIReafadctmltiahRLHTVLG----------------SDRIMVLAQGQVVEF 1209
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELK-------------RLQKELGitfvfvthdqeealtmSDRIAVMNKGKIQQI 212
|
250
....*....|....*...
gi 1622900605 1210 DTPSVLLSNDSSRFYAMF 1227
Cdd:cd03300 213 GTPEEIYEEPANRFVADF 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
376-557 |
1.44e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.04 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-----AISGTFA---YVAQQAWILN-ATLRDNILF 446
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkPVEGPGAergVVFQNEGLLPwRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 GKEY----DEERYNSVLnscclrpdlAILPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 521
Cdd:PRK11248 94 GLQLagveKMQRLEIAH---------QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622900605 522 NHIFNSAIRK-HLKSKTVLFVTHqlqylvDCDEVIFM 557
Cdd:PRK11248 165 EQMQTLLLKLwQETGKQVLLITH------DIEEAVFM 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1011-1210 |
1.75e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-----GGCIKIDGVRI--SDIGLADLRSKLSIIPQEPVLFSG 1083
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 TVRSNLD---PFNQYTEDQIWDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAA 1160
Cdd:PRK14239 101 SIYENVVyglRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1161 MDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1210
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
384-562 |
1.80e-13 |
|
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: 71.15 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 384 LEIQEGKLVGICGSVGSGKTSLISAILGQM---TLLEGSIAISG----------TFAYVAQQ-AWILNATLRDNILF--- 446
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETLTYtai 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 ---GKEYDEERYNSVLNSCCLRpDLAILPSSdlteiGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 523
Cdd:cd03234 108 lrlPRKSSDAIRKKRVEDVLLR-DLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900605 524 IFnsAIRKHL--KSKTVLFVTHQ-----LQYLvdcDEVIFMKEGCI 562
Cdd:cd03234 182 LV--STLSQLarRNRIVILTIHQprsdlFRLF---DRILLLSSGEI 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
372-574 |
1.85e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 372 HLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYV----AQQA 433
Cdd:COG1129 261 GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVpedrKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 WILNATLRDNILFGkeydeeRYNSVLNSCCLRP------------DLAILPSSDLTEIGergaNLSGGQRQRISLARALY 501
Cdd:COG1129 341 LVLDLSIRENITLA------SLDRLSRGGLLDRrreralaeeyikRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 502 SDRSIYILDDPLSALDahVGNH--IFNsAIRKhLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEEL 571
Cdd:COG1129 411 TDPKVLILDEPTRGID--VGAKaeIYR-LIRE-LAAegKAVIVISSELPELLGlSDRILVMREGRIVgeldrEEATEEAI 486
|
...
gi 1622900605 572 MNL 574
Cdd:COG1129 487 MAA 489
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
997-1222 |
1.95e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.03 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLaDLRSKLSII-- 1074
Cdd:cd03218 4 ENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIGyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1075 PQEPVLFSG-TVRSNLDPFNQYTEDQIWDALERThmKECIAQLplKLESEVMENGDNFSVGERQLLCIARALLRHCKILI 1153
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLSKKEREEKL--EELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1154 LDEATAAMDTETDLLIQETIREaFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1222
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKI-LKDRGIgvLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
379-566 |
2.05e-13 |
|
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: 70.86 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAY-----VAQQAWILNA--------TLRDNIL 445
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkepaeARRRLGFVSDstglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 -FGKEYDEERYNsvlnsccLRPDLAILpsSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhV 520
Cdd:cd03266 101 yFAGLYGLKGDE-------LTARLEEL--ADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV-M 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900605 521 GNHIFNSAIRkHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 566
Cdd:cd03266 171 ATRALREFIR-QLRAlgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
426-573 |
2.09e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.45 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 426 FAYVAQQAWILNATLRDNILFGKE-YDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDR 504
Cdd:PTZ00265 1298 FSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREP 1377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 505 SIYILDDPLSALDAHVGNHIFNSAIR-KHLKSKTVLFVTHQLQYLVDCDEVIFM----KEGCITE-RGTHEELMN 573
Cdd:PTZ00265 1378 KILLLDEATSSLDSNSEKLIEKTIVDiKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLS 1452
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1005-1206 |
2.71e-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: 69.38 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1005 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLAdLRSKLSIIPqepvl 1080
Cdd:cd03215 8 RGLsvKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDA-IRAGIAYVP----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1081 fsgtvrsnldpfnqytEDqiwdaleRTHMKeciaqlpLKLESEVMEN---GDNFSVGERQLLCIARALLRHCKILILDEA 1157
Cdd:cd03215 82 ----------------ED-------RKREG-------LVLDLSVAENialSSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1158 TAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQV 1206
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1010-1209 |
2.82e-13 |
|
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: 70.30 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIkPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSIIPQEPVLFSG-TVRSN 1088
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYPNfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 LDPFNqytedqiwdALERTHMKECIAQLPLKLESEVMENGDN-----FSVGERQLLCIARALLRHCKILILDEATAAMDT 1163
Cdd:cd03264 93 LDYIA---------WLKGIPSKEVKARVDEVLELVNLGDRAKkkigsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900605 1164 ETDLLIQETIREAFADCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEF 1209
Cdd:cd03264 164 EERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
367-573 |
3.66e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.91 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 367 HIHLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---------------------- 424
Cdd:COG4559 8 SVRLGGRTL---LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarrravlpqhs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 425 --TFAYVAQQ-------AWILNATLRDNILfgkeydeerynsvlnscclrpdLAILPSSDLTEIGERG-ANLSGGQRQRI 494
Cdd:COG4559 85 slAFPFTVEEvvalgraPHGSSAAQDRQIV----------------------REALALVGLAHLAGRSyQTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 495 SLARAL-------YSDRSIYILDDPLSALD-AHVgNHIFNSAirKHLKSK--TVLFVTHQL----QYlvdCDEVIFMKEG 560
Cdd:COG4559 143 QLARVLaqlwepvDGGPRWLFLDEPTSALDlAHQ-HAVLRLA--RQLARRggGVVAVLHDLnlaaQY---ADRILLLHQG 216
|
250
....*....|...
gi 1622900605 561 CITERGTHEELMN 573
Cdd:COG4559 217 RLVAQGTPEEVLT 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1014-1218 |
4.40e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.05 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLSIIPQEPvLFSGTVRSNL- 1089
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1090 ----DPFNQYTEDqiwdaLERTHMKECIAQLPLK---LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMD 1162
Cdd:PRK15079 119 eiiaEPLRTYHPK-----LSRQEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1163 TETDL----LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:PRK15079 194 VSIQAqvvnLLQQLQRE--MGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1011-1227 |
5.27e-13 |
|
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: 70.75 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRS----KLSIIPQEPVLFSG-TV 1085
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 RSNLdPF--------NQYTEDQIWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1157
Cdd:cd03294 120 LENV-AFglevqgvpRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1158 TAAMDTetdlLIQETIREAFADC------TMLTIAHRLHTV--LGsDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMF 1227
Cdd:cd03294 188 FSALDP----LIRREMQDELLRLqaelqkTIVFITHDLDEAlrLG-DRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
379-544 |
5.93e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 67.95 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAI---SGTFaYVAQQAWILNATLRDNIlfgkeydeery 455
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpegEDLL-FLPQRPYLPLGTLREQL----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 456 nsvlnscclrpdlaILPSSDlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnSAIRKHLks 535
Cdd:cd03223 85 --------------IYPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY-QLLKELG-- 138
|
....*....
gi 1622900605 536 KTVLFVTHQ 544
Cdd:cd03223 139 ITVISVGHR 147
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
368-544 |
7.40e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 368 IHLGHLRLQRTL-HSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------FAYVAQQAWI--LNA 438
Cdd:PRK13538 5 RNLACERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirrqrDEYHQDLLYLghQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 -----TLRDNILF----GKEYDEERYNSVLNSCCL--RPDLAIlpssdlteigergANLSGGQRQRISLARALYSDRSIY 507
Cdd:PRK13538 85 iktelTALENLRFyqrlHGPGDDEALWEALAQVGLagFEDVPV-------------RQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900605 508 ILDDPLSALDAHvGNHIFNSAIRKHLKSK-TVLFVTHQ 544
Cdd:PRK13538 152 ILDEPFTAIDKQ-GVARLEALLAQHAEQGgMVILTTHQ 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1010-1208 |
8.77e-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: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS----GGCIKIDGVRISDIGLADLR----SKLSIIPQEPVlf 1081
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPM-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1082 sgtvrSNLDPFnqYT-EDQIW-------------------DALERTHMKE---CIAQLPLKLesevmengdnfSVGERQL 1138
Cdd:COG4172 103 -----TSLNPL--HTiGKQIAevlrlhrglsgaaararalELLERVGIPDperRLDAYPHQL-----------SGGQRQR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1139 LCIARALLRHCKILILDEATAAMDTET-----DLL--IQETIREAfadctMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVqaqilDLLkdLQRELGMA-----LLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
370-570 |
1.01e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 370 LGHLRLQrtlhsIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------------FAYVAQQ 432
Cdd:PRK11144 10 LGDLCLT-----VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 433 AWIL-NATLRDNILFG-KEYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILD 510
Cdd:PRK11144 85 ARLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 511 DPLSALDAHvgnhifnsaiRKH-----LK--SKTV----LFVTHQLQYLVD-CDEVIFMKEGCITERGTHEE 570
Cdd:PRK11144 154 EPLASLDLP----------RKRellpyLErlAREInipiLYVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
382-571 |
1.02e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.21 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILFG-- 447
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergVGMVFQSyALYPHLSVAENMSFGlk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 448 -----KEYDEERYNSVLnscclrpdlAILPSSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA--HV 520
Cdd:PRK11000 102 lagakKEEINQRVNQVA---------EVLQLAHLLD--RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 521 GNHIFNSAIRKHLKSkTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK11000 171 QMRIEISRLHKRLGR-TMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
994-1218 |
1.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI----SDIGLAD 1066
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1067 LRSKLSIIPQ--EPVLFSGTVRSNLD--PFN-QYTEDQiwdalERTHMKECIAQLPLkleSEVMENGDNF--SVGERQLL 1139
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKNfGFSEDE-----AKEKALKWLKKVGL---SEDLISKSPFelSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1140 CIARALLRHCKILILDEATAAMDTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPS 1213
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPK 230
|
....*
gi 1622900605 1214 VLLSN 1218
Cdd:PRK13641 231 EIFSD 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1005-1210 |
1.35e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1005 ENL--PLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDI------GLA----DlRSK 1070
Cdd:COG1129 260 EGLsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPrdairaGIAyvpeD-RKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1071 LSIIPQEPVLFSGTVrSNLDPFNQYTedQIWDALERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLR 1147
Cdd:COG1129 339 EGLVLDLSIRENITL-ASLDRLSRGG--LLDRRRERALAEEYIKRLRIKtpsPEQPVG----NLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1148 HCKILILDEATAAMD----TEtdllIQETIREaFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 1210
Cdd:COG1129 412 DPKVLILDEPTRGIDvgakAE----IYRLIRE-LAAegKAVIVISSELPELLGlSDRILVMREGRIVgELD 477
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
994-1208 |
1.37e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.60 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVEL----SGGCIKIDGVRI---SDIGL 1064
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLlerpTSGRVLVDGQDLtalSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1065 ADLRSKLSIIPQEPVLFSG-TVRSNldpfnqytedqiwdalerthmkecIAqLPLKL--------ESEVMENGD------ 1129
Cdd:PRK11153 78 RKARRQIGMIFQHFNLLSSrTVFDN------------------------VA-LPLELagtpkaeiKARVTELLElvglsd 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1130 -------NFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLL--IQETIreafaDCTMLTIAHRLHTVLG- 1194
Cdd:PRK11153 133 kadrypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsilELLkdINREL-----GLTIVLITHEMDVVKRi 207
|
250
....*....|....
gi 1622900605 1195 SDRIMVLAQGQVVE 1208
Cdd:PRK11153 208 CDRVAVIDAGRLVE 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1010-1216 |
1.38e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI-SDIGLAdlRSKLSIIPQEPVL-FSGTVRS 1087
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVVPQFDNLdLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1088 NLDPFNQYTedqiwdaleRTHMKECIAQLPLKLESEVMENGDNFSV-----GERQLLCIARALLRHCKILILDEATAAMD 1162
Cdd:PRK13536 134 NLLVFGRYF---------GMSTREIEAVIPSLLEFARLESKADARVsdlsgGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1163 TETDLLIQETIREAFA--DCTMLTI-----AHRLhtvlgSDRIMVLAQGQVVEFDTPSVLL 1216
Cdd:PRK13536 205 PHARHLIWERLRSLLArgKTILLTThfmeeAERL-----CDRLCVLEAGRKIAEGRPHALI 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
379-543 |
1.42e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG--TFAYVAQQAWIL-NATLRDNIL--FGKEYD-E 452
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDdDLTVLDTVLdgDAELRAlE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 453 ERYNSVLNSCCLRPDLAILPSSDLTEIGERGA--------------------------NLSGGQRQRISLARALYSDRSI 506
Cdd:COG0488 94 AELEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPDL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900605 507 YILDDPLSALDAHvgnhifnsAIR---KHLKS--KTVLFVTH 543
Cdd:COG0488 174 LLLDEPTNHLDLE--------SIEwleEFLKNypGTVLVVSH 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
994-1221 |
1.66e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.58 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiGLADLRsklsI 1073
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDER----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEpvlfSGTVRSNLDPFNQYTedqiwdALE---------RTHMKECIAQLPLKLESEV--MENGDNF----SVGERQL 1138
Cdd:PRK09493 75 IRQE----AGMVFQQFYLFPHLT------ALEnvmfgplrvRGASKEEAEKQARELLAKVglAERAHHYpselSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1139 LCIARALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRL---HTVlGSdRIMVLAQGQVVEFDT 1211
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKvmQDLAEegMTMVIVTHEIgfaEKV-AS-RLIFIDKGRIAEDGD 219
|
250
....*....|
gi 1622900605 1212 PSVLLSNDSS 1221
Cdd:PRK09493 220 PQVLIKNPPS 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1011-1213 |
1.80e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.49 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG--VRISDIGLADLRSKLSIIPQEP--VLFSGTVR 1086
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLD--PFN-QYTEDQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEATAAMD- 1162
Cdd:PRK13636 102 QDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDp 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1163 ---TETDLLIQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVEFDTPS 1213
Cdd:PRK13636 175 mgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPK 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
379-566 |
1.92e-12 |
|
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: 67.94 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfayvaQQAWIL--------NATLRDNILFG--- 447
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLglgggfnpELTGRENIYLNgrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 448 ----KEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 519
Cdd:cd03220 112 lglsRKEIDEKIDEII---------------EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 520 vgnhiF----NSAIRKHLK-SKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 566
Cdd:cd03220 177 -----FqekcQRRLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
994-1207 |
1.95e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYrENLPLvlkKVSFTIKPKEKIGIVGRTGSGKSSLG--MALFRLVElsGGCIKIDGVRISDIGLAdlRSKL 1071
Cdd:PRK10771 2 LKLTDITWLY-HHLPM---RFDLTVERGERVAILGPSGAGKSTLLnlIAGFLTPA--SGSLTLNGQDHTTTPPS--RRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1072 SIIPQEPVLFSG-TVRSN----LDP---FNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIAR 1143
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNiglgLNPglkLNAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1144 ALLRHCKILILDEATAAMD----TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
382-560 |
2.16e-12 |
|
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: 67.92 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----TFAYVAQQA-----------WILnaTLRDNILF 446
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQSlgycpqfdalfDEL--TVREHLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 -----GKEYDEERYNSvlnscclrpdLAILPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 520
Cdd:cd03263 99 yarlkGLPKSEIKEEV----------ELLLRVLGLTDKANKRArTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622900605 521 GNHIFNsAIRKHLKSKTVLFVTHQLQ---YLvdCDEVIFMKEG 560
Cdd:cd03263 169 RRAIWD-LILEVRKGRSIILTTHSMDeaeAL--CDRIAIMSDG 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
379-573 |
2.50e-12 |
|
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: 67.95 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF--------------AYVAQQAWIL-NATLRDN 443
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarlgiGYLPQEASIFrKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 IL-------FGKEYDEERYNSVLNscclrpDLAILPSSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:cd03218 96 ILavleirgLSKKEREEKLEELLE------EFHITHLRK-----SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 517 DAHVGNHIfnSAIRKHLKSKT--VLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:cd03218 165 DPIAVQDI--QKIIKILKDRGigVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
379-571 |
2.52e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 68.98 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFayvaqqawiLNATLRDNIlfGkeY-DEERyns 457
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---------LDPEDRRRI--G--YlPEER--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 458 vlnscCLRPDLAI------------LPSSDLT----------EIGERGA----NLSGGQRQRISLARALYSDRSIYILDD 511
Cdd:COG4152 81 -----GLYPKMKVgeqlvylarlkgLSKAEAKrradewlerlGLGDRANkkveELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 512 PLSALDAhVGNHIFNSAIRKHLKS-KTVLFVTHQLQyLVD--CDEVIFMKEGCITERGTHEEL 571
Cdd:COG4152 156 PFSGLDP-VNVELLKDVIRELAAKgTTVIFSSHQME-LVEelCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
377-571 |
2.58e-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: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG------------TFAYVAQQAWILNA-TLRDN 443
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 I-LFGKEYD---EERYNSVLNscclrpdlaILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:cd03265 94 LyIHARLYGvpgAERRERIDE---------LLDFVGLLEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 519 HVGNHIFnSAIRKHLKSK--TVLFVTHqlqYLVD----CDEVIFMKEGCITERGTHEEL 571
Cdd:cd03265 165 QTRAHVW-EYIEKLKEEFgmTILLTTH---YMEEaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
486-573 |
2.77e-12 |
|
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: 70.87 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 486 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQ---YLvdCDEVIFMKE 559
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILD--LLRDLQREhglAYLFISHDLAvvrAL--AHRVMVMKD 501
|
90
....*....|....
gi 1622900605 560 GCITERGTHEELMN 573
Cdd:COG4172 502 GKVVEQGPTEQVFD 515
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
994-1165 |
2.83e-12 |
|
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: 67.43 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK 1070
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1071 LSIIPQEPVLFSG-TVRSNLDPFNQYTEDQIWDALERthMKECIAQLPLKLESEVMENGdnFSVGERQLLCIARALLRHC 1149
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKR--VPAALELVGLSHKHRALPAE--LSGGEQQRVAIARAIVNSP 155
|
170
....*....|....*.
gi 1622900605 1150 KILILDEATAAMDTET 1165
Cdd:cd03292 156 TILIADEPTGNLDPDT 171
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
968-1208 |
2.89e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 968 IKTLSLEAP-ARIKNKAPSPDWPQegeVTFENAEMRYRENlPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE 1046
Cdd:PRK10522 299 LNKLALAPYkAEFPRPQAFPDWQT---LELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1047 LSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTvrsnLDPFNQYTEDQIWDA-LERTHMKEciaqlplKLEsevM 1125
Cdd:PRK10522 375 PQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAH-------KLE---L 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1126 ENGD----NFSVGERQLLCIARALLRHCKILILDEATAAMDTE------TDLL--IQETIREAFAdctmltIAHRLHTVL 1193
Cdd:PRK10522 441 EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefyQVLLplLQEMGKTIFA------ISHDDHYFI 514
|
250
....*....|....*
gi 1622900605 1194 GSDRIMVLAQGQVVE 1208
Cdd:PRK10522 515 HADRLLEMRNGQLSE 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1010-1217 |
2.91e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL-----VELSGGCIKIDGVRISDIGLADLR----SKLSIIPQEPVL 1080
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1081 fsgtvrsNLDPFNQyTEDQIWDALE----------RTHMKEC-----IAQLPLKLEsevmENGDNFSVGERQLLCIARAL 1145
Cdd:PRK15134 104 -------SLNPLHT-LEKQLYEVLSlhrgmrreaaRGEILNCldrvgIRQAAKRLT----DYPHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1146 LRHCKILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1217
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1010-1218 |
2.99e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID------GVRISDIGLADLRSKLSIIPQEPVLFSG 1083
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 -TVRSNLD-PFNQYTedqIWDALE-RTHMKECIAQLPL--KLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEAT 1158
Cdd:PRK14246 105 lSIYDNIAyPLKSHG---IKEKREiKKIVEECLRKVGLwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1159 AAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1010-1218 |
3.47e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG-----GCIKIDGVRISD--IGLADLRSKLSIIPQEPVLFS 1082
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1083 GTVRSNLdpfnQYTEDQI-W------DALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILD 1155
Cdd:PRK14258 102 MSVYDNV----AYGVKIVgWrpkleiDDIVESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 1156 EATAAMDTETDLLIQETIREAF--ADCTMLTIAHRLHTVL-----------GSDRImvlaqGQVVEFDTPSVLLSN 1218
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSrlsdftaffkgNENRI-----GQLVEFGLTKKIFNS 246
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1010-1222 |
3.66e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVL-FSGTVR-- 1086
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRqv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 ---------SNLDPFNQYTEDQIWDALERTHMKECIAQlPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1157
Cdd:PRK09536 98 vemgrtphrSRFDTWTETDRAAVERAMERTGVAQFADR-PV----------TSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1158 TAAMDTETDLLIQETIRE-------AFADCTMLTIAHRLhtvlgSDRIMVLAQGQVVEFDTPSVLLSNDSSR 1222
Cdd:PRK09536 167 TASLDINHQVRTLELVRRlvddgktAVAAIHDLDLAARY-----CDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1014-1232 |
3.70e-12 |
|
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: 69.36 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISD----IGLADLRSKLSIIPQEPVLFSG-TVRSN 1088
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFPHlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 LdpfnQYTEDQIWDALERTHMKECIAQL---PLkLESEVmengDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1165
Cdd:COG4148 98 L----LYGRKRAPRAERRISFDEVVELLgigHL-LDRRP----ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1166 -----DLLiqETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 1232
Cdd:COG4148 169 kaeilPYL--ERLRDEL-DIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGS 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
379-573 |
4.33e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.69 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAY----------VAQQAWILNATLRDNILFgK 448
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLTMVF-Q 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 449 EYDEERYNSVLNSCCLRPDLAI-LPSSDLTE----------IGERG-----ANLSGGQRQRISLARALYSDRSIYILDDP 512
Cdd:PRK10619 100 HFNLWSHMTVLENVMEAPIQVLgLSKQEAREravkylakvgIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 513 LSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN 573
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
377-573 |
4.84e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.15 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------------TFAYVAQQawILN 437
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkkvglVFQYPEYQ--LFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 438 ATLRDNILFGK----EYDEERYNSVLNSCclrpDLAILPSSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:PRK13637 99 ETIEKDIAFGPinlgLSEEEIENRVKRAM----NIVGLDYEDYKD--KSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 514 SALDAHVGNHIFNSAIRKHLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFK 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1010-1222 |
4.89e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 4.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEPVLFSG-TVRS 1087
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1088 NLDPFNQYTEDQIWdaleRTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDL 1167
Cdd:PRK11614 100 NLAMGGFFAERDQF----QERIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1168 LIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR 1222
Cdd:PRK11614 175 QIFDTIEQLREQgMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAVR 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
376-573 |
5.26e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.42 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------FAYVAQQAWIL---NA-----TLR 441
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpSRELAKRLAILrqeNHinsrlTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFG---------KEYDEERYNSVLNSCclrpdlailpssDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDD 511
Cdd:COG4604 94 ELVAFGrfpyskgrlTAEDREIIDEAIAYL------------DLEDLADRYLDeLSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 512 PLSALDahvgnhIFNS-AIRKHLKS------KTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 573
Cdd:COG4604 162 PLNNLD------MKHSvQMMKLLRRladelgKTVVIVLHDInfasCY---ADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
379-581 |
5.99e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.81 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfAYVAQQAWILN----------------ATLRD 442
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWNLRrkigmvfqnpdnqfvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGKEYDEERYNSVLNscclRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 522
Cdd:PRK13642 102 DVAFGMENQGIPREEMIK----RVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 523 HIFNsaIRKHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATI 581
Cdd:PRK13642 178 EIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
376-562 |
6.57e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRT-LHSIDLEIQEGKLVGICGSVGSGKTSLISAILG-----QMTLLEGSIAIsgtfayvaqqawilnATLRDNILFgkE 449
Cdd:PRK11247 24 ERTvLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletpsAGELLAGTAPL---------------AEAREDTRL--M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 450 YDEER---YNSVLNSCCL------RPD-LAILPSSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:PRK11247 87 FQDARllpWKKVIDNVGLglkgqwRDAaLQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900605 519 HVG---NHIFNSAIRKHlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCI 562
Cdd:PRK11247 167 LTRiemQDLIESLWQQH--GFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1014-1206 |
7.30e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE-LSGGCIKIDG--VRIS------DIGLADL---RSKLSIIPQEPVLF 1081
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRnpqqaiAQGIAMVpedRKRDGIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1082 SGTVrSNLDPFNQYTedQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAM 1161
Cdd:PRK13549 361 NITL-AALDRFTGGS--RIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1162 DT----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQV 1206
Cdd:PRK13549 437 DVgakyEIYKLINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
379-543 |
7.35e-12 |
|
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: 66.28 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT---------FAYVAQQ--------AWILNATLR 441
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraIPYLRRKigvvfqdfRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGKEYDE-------ERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:cd03292 97 ENVAFALEVTGvppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|....*....
gi 1622900605 515 ALDAHVGNHIFNSAIRKHLKSKTVLFVTH 543
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1011-1205 |
7.89e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDGVRISDIGLADL-RSKLSIIPQEPVLF 1081
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTL-MKV-----LSGvyphgtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1082 SG-TVRSNLDPFNQYTEDQI--WDALERtHMKECIAQLPLKL--ESEVMENGdnfsVGERQLLCIARALLRHCKILILDE 1156
Cdd:PRK13549 95 KElSVLENIFLGNEITPGGImdYDAMYL-RAQKLLAQLKLDInpATPVGNLG----LGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1157 ATAAM-DTETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 1205
Cdd:PRK13549 170 PTASLtESETAVLL-DIIRDLKAhGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1010-1210 |
8.22e-12 |
|
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: 66.40 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS---DIGLAdLRSKLSIIpqEPVLFSGTVR 1086
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSsllGLGGG-FNPELTGR--ENIYLNGRLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLDPFNQYTEDQIWDALErthMKECIaQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATAAMDTETD 1166
Cdd:cd03220 113 GLSRKEIDEKIDEIIEFSE---LGDFI-DLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900605 1167 LLIQETIREAFADCTMLTIA-HRLHTVLG-SDRIMVLAQGQVVEFD 1210
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
985-1208 |
8.30e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 985 SPDWPQEGEVTFENAEMRYRENLPLV--LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG------ 1056
Cdd:PRK10261 4 SDELDARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1057 ----VRISDIGLADLR----SKLSIIPQEPVlfsgtvrSNLDPFNQYTEdQIWDALeRTHM----KECIAQLPLKL---- 1120
Cdd:PRK10261 84 srqvIELSEQSAAQMRhvrgADMAMIFQEPM-------TSLNPVFTVGE-QIAESI-RLHQgasrEEAMVEAKRMLdqvr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1121 --ESEVM--ENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTM--LTIAHRLHTVLG 1194
Cdd:PRK10261 155 ipEAQTIlsRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAE 234
|
250
....*....|....*
gi 1622900605 1195 -SDRIMVLAQGQVVE 1208
Cdd:PRK10261 235 iADRVLVMYQGEAVE 249
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
386-569 |
8.41e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 386 IQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfAYVAQQAWILNA---------------TLRDNIL-FGKE 449
Cdd:PRK13536 64 VASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARArigvvpqfdnldlefTVRENLLvFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 450 YdeeRYNSvlnscclRPDLAILPSsdLTEIGE-------RGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGN 522
Cdd:PRK13536 142 F---GMST-------REIEAVIPS--LLEFARleskadaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-AR 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900605 523 HIFNSAIRKHL-KSKTVLFVTHQLQYLVD-CDEVIFMKEGC-ITERGTHE 569
Cdd:PRK13536 209 HLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRkIAEGRPHA 258
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
379-573 |
8.96e-12 |
|
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: 66.16 E-value: 8.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWIL-NATLRDN 443
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFpSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFG------KEYDEERYNSVLNsccLRPDLAilpssdlteigER----GANLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:COG0410 99 LLLGayarrdRAEVRADLERVYE---LFPRLK-----------ERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 514 SALDAHVGNHIFNsAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:COG0410 165 LGLAPLIVEEIFE-IIRR-LNREgvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
997-1215 |
9.22e-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: 65.85 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDiglaDLRSKLSI 1073
Cdd:cd03265 4 ENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvVREPR----EVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSG-TVRSNLdpfnqYTEDQIWdALERTHMKECIAQLpLKLeSEVMENGD----NFSVGERQLLCIARALLRH 1148
Cdd:cd03265 78 VFQDLSVDDElTGWENL-----YIHARLY-GVPGAERRERIDEL-LDF-VGLLEAADrlvkTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1149 CKILILDEATAAMDTETDLLIQETIR---EAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVL 1215
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEklkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
379-573 |
9.59e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.42 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-------------------------------------A 421
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklviqktrfkkikkikE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 422 ISGTFAYVAQQA--WILNATLRDNILFG-------KEYDEERYNSVLNSCCLrpDLAILPSSDLteigergaNLSGGQRQ 492
Cdd:PRK13651 103 IRRRVGVVFQFAeyQLFEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQRSPF--------ELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 493 RISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG-THEE 570
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGdTYDI 252
|
...
gi 1622900605 571 LMN 573
Cdd:PRK13651 253 LSD 255
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1009-1218 |
9.86e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1009 LVLKKVSFTIkPKEKI-GIVGRTGSGKSSLGMALFRLVELSGGCiKIDGVRI--------SDIGLADLRSKLSIIPQEPV 1079
Cdd:PRK14243 24 LAVKNVWLDI-PKNQItAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgknlyaPDVDPVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1080 LFSGTVRSNLD---PFNQYTEDQiwDALERTHMKEciAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDE 1156
Cdd:PRK14243 102 PFPKSIYDNIAygaRINGYKGDM--DELVERSLRQ--AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1157 ATAAMDTETDLLIQETIREAFADCTMLTIAHRLH---------------TVLGSDRimvlaQGQVVEFDTPSVLLSN 1218
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQqaarvsdmtaffnveLTEGGGR-----YGYLVEFDRTEKIFNS 249
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
368-543 |
9.96e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 65.58 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 368 IHLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQmtlLEGSIAISGtfayvaqQAWI-------LNATL 440
Cdd:COG4136 9 ITLGGRPL---LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT---LSPAFSASG-------EVLLngrrltaLPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 441 R------------------DNILFG---KEYDEERYNSVLNScclrpdlaiLPSSDLTEIGERG-ANLSGGQRQRISLAR 498
Cdd:COG4136 76 RrigilfqddllfphlsvgENLAFAlppTIGRAQRRARVEQA---------LEEAGLAGFADRDpATLSGGQRARVALLR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900605 499 ALYSDRSIYILDDPLSALDAH----VGNHIFNSAIRKHLkskTVLFVTH 543
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAAlraqFREFVFEQIRQRGI---PALLVTH 192
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
379-550 |
1.17e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.84 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------------FAYVAQQAWIL-NATLR 441
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrrIGVVFQDFRLLpDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILF-----GKEYDE--ERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILD 510
Cdd:COG2884 98 ENVALplrvtGKSRKEirRRVREVL---------------DLVGLSDKAkalpHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622900605 511 DPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQyLVD 550
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE-LVD 201
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1010-1225 |
1.37e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVElsggciKIDGVRIS-DIGLA-----------DLRSKLSIIPQE 1077
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMND------KVSGYRYSgDVLLGgrsifnyrdvlEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1078 PVLFSGTVRSN---------LDPFNQY--------TEDQIWDALerthmKECIAQLPLKLesevmengdnfSVGERQLLC 1140
Cdd:PRK14271 110 PNPFPMSIMDNvlagvrahkLVPRKEFrgvaqarlTEVGLWDAV-----KDRLSDSPFRL-----------SGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1141 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTPSVLLSN- 1218
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSp 253
|
250
....*....|
gi 1622900605 1219 ---DSSRFYA 1225
Cdd:PRK14271 254 khaETARYVA 263
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
377-573 |
1.61e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.57 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqMTLLEGSIAISGTFAYVAQ---------------------QAWI 435
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNG-LIISETGQTIVGDYAIPANlkkikevkrlrkeiglvfqfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 436 LNATLRDNILFGK----EYDEERYNSVlnscclrPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDD 511
Cdd:PRK13645 104 FQETIEKDIAFGPvnlgENKQEAYKKV-------PELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 512 PLSALDAHVGNHIFNSAIR-KHLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1014-1217 |
1.88e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.29 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGG--CIKI--DGVRISDIGLaDLRSK----LSIIPQEPVLFsgTV 1085
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVgdEWVDMTKPGP-DGRGRakryIGILHQEYDLY--PH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 RSNLDPFNQYTEDQIWDALERthMKECIAQLPLKLESEVMEN-----GDNFSVGERQLLCIARALLRHCKILILDEATAA 1160
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELAR--MKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1161 MDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1217
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
376-545 |
2.06e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAiLGQMTLLEGSIAISGTFAYVAQQAWILNATL------------RDN 443
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYERRVNLnrlrrqvsmvhpKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFGKEYDEERYNSVLNSccLRPDLAI-------LPSSDL-----TEIGERGANLSGGQRQRISLARALYSDRSIYILDD 511
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVG--WRPKLEIddivesaLKDADLwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622900605 512 PLSALDA----HVGNHIFNSAIRKHLkskTVLFVTHQL 545
Cdd:PRK14258 177 PCFGLDPiasmKVESLIQSLRLRSEL---TMVIVSHNL 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1003-1173 |
2.24e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1003 YRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFS 1082
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1083 GTVRSNLD-PFnqytedQIW-DALERTHMKECIAQLPLKlESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAA 1160
Cdd:PRK10247 95 DTVYDNLIfPW------QIRnQQPDPAIFLDDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170
....*....|...
gi 1622900605 1161 MDTETDLLIQETI 1173
Cdd:PRK10247 168 LDESNKHNVNEII 180
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
379-571 |
2.46e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.79 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-----------FAYVAQQ-AWILNATLRDNILF 446
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelepadrdIAMVFQNyALYPHMSVRENMAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 G-------KEYDEERynsvlnscclrpdlaILPSSDLTEIGE----RGANLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:PRK11650 100 GlkirgmpKAEIEER---------------VAEAARILELEPlldrKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 516 LDAHVGNHIfNSAIRK-HLKSKTV-LFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK11650 165 LDAKLRVQM-RLEIQRlHRRLKTTsLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
376-572 |
2.82e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.42 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-------------FAYVAQQAWILNA-TLR 441
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGK-----------EYDEERYNSVLNScclrpdlailpsSDLTEIGERG-ANLSGGQRQRISLARALYSDRSIYIL 509
Cdd:PRK11231 95 ELVAYGRspwlslwgrlsAEDNARVNQAMEQ------------TRINHLADRRlTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 510 DDPLSALDAhvgNHIFN--SAIRK-HLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELM 572
Cdd:PRK11231 163 DEPTTYLDI---NHQVElmRLMRElNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1009-1194 |
2.99e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1009 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvriSDIGLADLRSKLSII----PQEPVLfsgT 1084
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLghrnAMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1085 VRSNLD---PFNQYTEDQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILILDEATAAM 1161
Cdd:PRK13539 90 VAENLEfwaAFLGGEELDIAAALEAVGLAP-LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|...
gi 1622900605 1162 DTETDLLIQETIREAFADCTMLTIAhrLHTVLG 1194
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAA--THIPLG 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
370-544 |
3.03e-11 |
|
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: 64.05 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 370 LGHLRLQRTLHS-IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWIL 436
Cdd:cd03231 6 LTCERDGRALFSgLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLGHAPGIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 437 NA-TLRDNILFgkeydeerynsvlnSCCLRPDLAI---LPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDD 511
Cdd:cd03231 86 TTlSVLENLRF--------------WHADHSDEQVeeaLARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....
gi 1622900605 512 PLSALDAHvGNHIFNSAIRKHL-KSKTVLFVTHQ 544
Cdd:cd03231 152 PTTALDKA-GVARFAEAMAGHCaRGGMVVLTTHQ 184
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1015-1207 |
3.06e-11 |
|
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: 64.44 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1015 SFTIKPKEKIGIVGRTGSGKSSLG--MALFrLVELSGGcIKIDGVrisDIGLADL-RSKLSIIPQEPVLFSG-TVRSNLD 1090
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLnlIAGF-ETPQSGR-VLINGV---DVTAAPPaDRPVSMLFQENNLFAHlTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1091 ----PFNQYTEDQ---IWDALERTHMKECIAQLPlklesevmengDNFSVGERQLLCIARALLRHCKILILDEATAAMD- 1162
Cdd:cd03298 93 lglsPGLKLTAEDrqaIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDp 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900605 1163 ---TETDLLIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:cd03298 162 alrAEMLDLVLDLHAE--TKMTVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
379-562 |
3.15e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISaILGQMtllegSIAISGTFAYVAQQAWILN----ATLRDN----------- 443
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCL-----DKPTSGTYRVAGQDVATLDadalAQLRREhfgfifqryhl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 --------------ILFGKEYDEERYNSVlnscclrpdlAILPSSDLTE-IGERGANLSGGQRQRISLARALYSDRSIYI 508
Cdd:PRK10535 98 lshltaaqnvevpaVYAGLERKQRLLRAQ----------ELLQRLGLEDrVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 509 LDDPLSALDAHVGNHIFnsAIRKHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCI 562
Cdd:PRK10535 168 ADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
379-573 |
3.20e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.59 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTS---LISAILGQMTLLEGSIAISGTfAYVAQQAW----------------ILNAT 439
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGI-TLTAKTVWdirekvgivfqnpdnqFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 440 LRDNILFGKEydeerynsvlNSCCLRPDLAILPSSDLTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:PRK13640 102 VGDDVAFGLE----------NRAVPRPEMIKIVRDVLADVGmldyidSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 514 SALDAHVGNHIFnSAIRKHLKSK--TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK13640 172 SMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
382-573 |
3.49e-11 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 64.77 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIA-----ISG-------------TFayvaQQAWIL-NATLRD 442
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGlppheiarlgigrTF----QIPRLFpELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGKEYDEERYNSVLNSCCLRPDL-----AILpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 514 SALD----AHVGNHIfnSAIRKHlkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:cd03219 172 AGLNpeetEELAELI--RELRER--GITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1017-1200 |
3.85e-11 |
|
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: 64.74 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1017 TIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGVrisDIGLAdlRSKLSIIPQE-PVLFSGTVRSNLdpfnqy 1095
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTF-------IKMLAGVLKPDEG---DIEIE--LDTVSYKPQYiKADYEGTVRDLL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1096 tEDQIWDALERTHMKECIAQlPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE 1175
Cdd:cd03237 83 -SSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*....
gi 1622900605 1176 aFA---DCTMLTIAHRLHTV-LGSDRIMV 1200
Cdd:cd03237 161 -FAennEKTAFVVEHDIIMIdYLADRLIV 188
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1010-1219 |
3.89e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGL-ADLRSKLSIIPQEPVLFSG-TVRS 1087
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1088 NLDPFNQYTEDqiwdaLERTHMKECIAQLPLKLESEVMEN--GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1165
Cdd:PRK10895 98 NLMAVLQIRDD-----LSAEQREDRANELMEEFHIEHLRDsmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1166 DLLIQETIrEAFADCTM--LTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 1219
Cdd:PRK10895 173 VIDIKRII-EHLRDSGLgvLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
379-564 |
4.29e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 64.38 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--FAyvaqqawiLN----ATLR-DNILFgkeyd 451
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlFA--------LDedarARLRaRHVGF----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 452 eerynsVLNSCCLRPDL-AI----LPssdLTEIGERGA----------------------NLSGGQRQRISLARALYSDR 504
Cdd:COG4181 95 ------VFQSFQLLPTLtALenvmLP---LELAGRRDArararallervglghrldhypaQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 505 SIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLF-VTHQLQYLVDCDEVIFMKEGCITE 564
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVlVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
376-573 |
4.99e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAIlGQMTLLEGSIAISGTFAY---------------------VAQQAW 434
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 435 ILNATLRDNILFGKEYDEERYNSVLNSCCLRpdlAILPSSDLTEIGER----GANLSGGQRQRISLARALYSDRSIYILD 510
Cdd:PRK14239 97 PFPMSIYENVVYGLRLKGIKDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 511 DPLSALDAHVGNHIFNSAIRkhLKSK-TVLFVTHQLQYLVD-CDEVIFMKEGCITERG-THEELMN 573
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLG--LKDDyTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNdTKQMFMN 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
996-1210 |
5.16e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 996 FENAEMRYreNLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSlgmaLFRLV----ELSGGCIKID-GVRIsdigladlrsk 1070
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKST----LLKILagelEPDSGEVSIPkGLRI----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1071 lSIIPQEPVLFSG-TVRSN-LDPFNQYteDQIWDALERTHMKECIAQLPLKLESEVME-----NG--------------- 1128
Cdd:COG0488 64 -GYLPQEPPLDDDlTVLDTvLDGDAEL--RALEAELEELEAKLAEPDEDLERLAELQEefealGGweaearaeeilsglg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1129 ----------DNFSVGERQLLCIARALLRHCKILILDEATAAMDTET-----DLLIQEtireafaDCTMLTIAH-R--LH 1190
Cdd:COG0488 141 fpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY-------PGTVLVVSHdRyfLD 213
|
250 260
....*....|....*....|
gi 1622900605 1191 TVlgSDRIMVLAQGQVVEFD 1210
Cdd:COG0488 214 RV--ATRILELDRGKLTLYP 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1011-1217 |
5.40e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdIGLADLRS-KLSIIPQEPV---------- 1079
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDPStslnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1080 -LFSGTVRSNLDPFNQYTEDQIWDALERTHM-KECIAQLPLKLESevmengdnfsvGERQLLCIARALLRHCKILILDEA 1157
Cdd:PRK15112 108 qILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAP-----------GQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1158 TAAMDTETD-------LLIQETIREAFADCTMlTIAHRLHTvlgSDRIMVLAQGQVVEF-DTPSVLLS 1217
Cdd:PRK15112 177 LASLDMSMRsqlinlmLELQEKQGISYIYVTQ-HLGMMKHI---SDQVLVMHQGEVVERgSTADVLAS 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1014-1208 |
6.24e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG---VRISDIGLADLRSKLSIIPQEPVlfsgtvrSNLD 1090
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKADPEAQKLLRQKIQIVFQNPY-------GSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1091 PfNQYTEDQIWDALE----------RTHMKECIAQLPLKLESEV----MengdnFSVGERQLLCIARALLRHCKILILDE 1156
Cdd:PRK11308 107 P-RKKVGQILEEPLLintslsaaerREKALAMMAKVGLRPEHYDryphM-----FSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1157 ATAAMDTEtdllIQETIREAFAD------CTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:PRK11308 181 PVSALDVS----VQAQVLNLMMDlqqelgLSYVFISHDLSVVEHiADEVMVMYLGRCVE 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
376-571 |
6.27e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 64.66 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAI------SGT---------------FAYVAQQaw 434
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKknkklkplrkkvgivFQFPEHQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 435 ILNATLRDNILFG-------KEYDEERYNSVLNSCCLRPDLaiLPSSDLteigergaNLSGGQRQRISLARALYSDRSIY 507
Cdd:PRK13634 98 LFEETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEEL--LARSPF--------ELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 508 ILDDPLSALDAHVGNHIFNSAIRKHL-KSKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
379-558 |
6.30e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT----------FAYVAQQA---WILNATLRDNIL 445
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 446 FG-----------KEYDEERYNSVLNscclRPDLAILPSSdltEIGErganLSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:PRK15056 103 MGryghmgwlrraKKRDRQIVTAALA----RVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622900605 515 ALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMK 558
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMVK 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
384-616 |
6.35e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.83 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 384 LEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCC 463
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 464 LRPDLAILPSSD--------LTEIG-ERGAN-----LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAI 529
Cdd:PRK10070 129 FGMELAGINAEErrekaldaLRQVGlENYAHsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 530 RKHLK-SKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEELMN--LNGDYATIFNNLLLGDTPPVEINSKKETSGSQ 605
Cdd:PRK10070 209 KLQAKhQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNnpANDYVRTFFRGVDISQVFSAKDIARRTPNGLI 288
|
250
....*....|.
gi 1622900605 606 KKSQDKGPKTG 616
Cdd:PRK10070 289 RKTPGFGPRSA 299
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
383-581 |
7.23e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.45 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 383 DLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQ-AWIL--------NATLRDNILFGkey 450
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPSRRpVSMLfqennlfsHLTVAQNIGLG--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 451 deerynsvlnsccLRPDL-----------AILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:PRK10771 96 -------------LNPGLklnaaqreklhAIARQMGIEDLLARlPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 519 HVGNHIFN----SAIRKHLkskTVLFVTHQLQylvDCDEV----IFMKEGCITERGTHEELMNLNGDYATI 581
Cdd:PRK10771 163 ALRQEMLTlvsqVCQERQL---TLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
376-566 |
7.66e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 62.98 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGkLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG------------TFAYVAQQAwilnaTLRDN 443
Cdd:cd03264 13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEF-----GVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 IlfgKEYDEERYNSVLNSC----CLRPDLAILPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALDa 518
Cdd:cd03264 87 F---TVREFLDYIAWLKGIpskeVKARVDEVLELVNLGDRAKKKIGsLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900605 519 hVGNHI-FNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERG 566
Cdd:cd03264 163 -PEERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1014-1206 |
9.71e-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: 65.62 E-value: 9.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELS-GGCIKIDGVRISDIGLAD-LRSKLSIIPQE-------PVLFSG- 1083
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQaIRAGIAMVPEDrkrhgivPILGVGk 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 -TVRSNLDPFNQYTedQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMD 1162
Cdd:TIGR02633 359 nITLSVLKSFCFKM--RIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900605 1163 T----ETDLLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQV 1206
Cdd:TIGR02633 436 VgakyEIYKLINQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
378-573 |
1.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.00 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 378 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSI-----AISG-TFAYVAQQAWIL---------NATLRD 442
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDdNFEKLRKHIGIVfqnpdnqfvGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGKE-----YDE--ERYNSVLNscclrpDLAILPSSDlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:PRK13648 104 DVAFGLEnhavpYDEmhRRVSEALK------QVDMLERAD-----YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 516 LDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK13648 173 LDPDARQNLLD--LVRKVKSEhniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1013-1211 |
1.09e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1013 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG---GCIKIDGVRISDI---GLADLRS-KLSIIPQEPVlfsgtv 1085
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLpekELNKLRAeQISMIFQDPM------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 rSNLDPFNQYTEdQIWDAL-------------ERTHMKECIaQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKIL 1152
Cdd:PRK09473 108 -TSLNPYMRVGE-QLMEVLmlhkgmskaeafeESVRMLDAV-KMPEARKRMKMYPHE-FSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 1153 ILDEATAAMDTETD----LLIQETIREaFaDCTMLTIAHRLHTVLGS-DRIMVLAQGQVVEFDT 1211
Cdd:PRK09473 184 IADEPTTALDVTVQaqimTLLNELKRE-F-NTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGN 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1010-1217 |
1.17e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.49 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSG-TVRSN 1088
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 L----DPFNQY-----TEDQ--IWDALERTHMKEcIAQLPLklesevmengDNFSVGERQLLCIARALLRHCKILILDEA 1157
Cdd:PRK11231 97 VaygrSPWLSLwgrlsAEDNarVNQAMEQTRINH-LADRRL----------TDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1158 TAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1217
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGkTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1010-1227 |
1.36e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKID-GVRISDIgladlRSKLSIIPQEPVLFSGTVRsn 1088
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYV-----PQKLYLDTTLPLTVNRFLR-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 LDPFNQytEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDL- 1167
Cdd:PRK09544 92 LRPGTK--KEDILPALKRVQAGHLIDAPMQKL-----------SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVa 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 1168 ---LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQgQVVEFDTPSVLLSNdsSRFYAMF 1227
Cdd:PRK09544 159 lydLIDQLRRE--LDCAVLMVSHDLHLVMAkTDEVLCLNH-HICCSGTPEVVSLH--PEFISMF 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1010-1208 |
1.39e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.16 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMAL--FRLVELSGGCIKIDGVRISDIgLADLRSKLSII--PQEPVLFSGtv 1085
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDL-PPEERARLGIFlaFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 rsnldpfnqytedqiwdalerthmkeciaqlpLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1165
Cdd:cd03217 92 --------------------------------VKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900605 1166 DLLIQETIRE-AFADCTMLTIAH--RLHTVLGSDRIMVLAQGQVVE 1208
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVK 185
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
997-1219 |
1.48e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.60 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYRENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQ 1076
Cdd:PRK13647 8 EDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1077 EP--VLFSGTVRSNL--DPFNQ-----YTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLR 1147
Cdd:PRK13647 87 DPddQVFSSTVWDDVafGPVNMgldkdEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1148 HCKILILDEATAAMDTETdlliQETIREAFADC-----TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND 1219
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRG----QETLMEILDRLhnqgkTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
377-573 |
1.50e-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: 65.21 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSI----AISGTFAYVAQQA----------------- 433
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvALCEKCGYVERPSkvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 ---WILNATLRDNI-------------LFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTE---IGER----GANLSGGQ 490
Cdd:TIGR03269 94 vdfWNLSDKLRRRIrkriaimlqrtfaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEmvqLSHRithiARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 491 RQRISLARALYSDRSIYILDDPLSALDAHVGNhIFNSAIRKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 567
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGEIKEEGT 252
|
....*.
gi 1622900605 568 HEELMN 573
Cdd:TIGR03269 253 PDEVVA 258
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
356-566 |
1.52e-10 |
|
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: 62.74 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 356 ERPSPEEEEGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----------- 424
Cdd:cd03267 14 SKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkrrkkfl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 425 -----TFAYVAQQAWILNAtlRDNILFGKE-YD--EERYNSVLNSCClrpdlailpssDLTEIGE------RgaNLSGGQ 490
Cdd:cd03267 94 rrigvVFGQKTQLWWDLPV--IDSFYLLAAiYDlpPARFKKRLDELS-----------ELLDLEElldtpvR--QLSLGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 491 RQRISLARALYSDRSIYILDDPLSALDAHVGNhifnsAIRKHLKS------KTVLFVTHqlqYLVD----CDEVIFMKEG 560
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQE-----NIRNFLKEynrergTTVLLTSH---YMKDiealARRVLVIDKG 230
|
....*.
gi 1622900605 561 CITERG 566
Cdd:cd03267 231 RLLYDG 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
961-1210 |
1.71e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 961 VERINHYIKtLSLEAPARIKNKApspdwpqegeVTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSlgma 1040
Cdd:COG0488 294 PPRRDKTVE-IRFPPPERLGKKV----------LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST---- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1041 LFRL----VELSGGCIKIdGVRIsdigladlrsKLSIIPQEpvlfsgtvRSNLDPfnqytEDQIWDALERTHmkeciaql 1116
Cdd:COG0488 357 LLKLlageLEPDSGTVKL-GETV----------KIGYFDQH--------QEELDP-----DKTVLDELRDGA-------- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1117 PLKLESEVME-------NGD-------NFSVGERQLLCIARALLRHCKILILDEATAAMDTETdlliqetiREAFADC-- 1180
Cdd:COG0488 405 PGGTEQEVRGylgrflfSGDdafkpvgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAld 476
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622900605 1181 ----TMLTIAH-R--LHTVlgSDRIMVLAQGQVVEFD 1210
Cdd:COG0488 477 dfpgTVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1011-1212 |
1.72e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 62.48 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGladlrsklsiiPQEPVLFSG------- 1083
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQNysllpwl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 TVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEvmENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1163
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAIVEEHIALVGLTEAAD--KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1164 ETDLLIQETIREAFAD--CTMLTIAHRL-HTVLGSDRIMVLAQ------GQVVEFDTP 1212
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEhrVTVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILEVPFP 205
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
716-881 |
1.75e-10 |
|
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: 63.58 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 716 ASIYALSMAVMLILkairGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfqAEMFI 795
Cdd:cd18547 52 LGLYLLSALFSYLQ----NRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNI-------SQALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 796 QNVILVFFCVGMIAGVF-------PWF-LVAVGPLVILFSVLHIV---SRVLIREL-KRLDNITqspflSHITSSIQGLA 863
Cdd:cd18547 121 QSLTQLISSILTIVGTLimmlyisPLLtLIVLVTVPLSLLVTKFIakrSQKYFRKQqKALGELN-----GYIEEMISGQK 195
|
170
....*....|....*...
gi 1622900605 864 TIHAYNKGQEFLHRYQEL 881
Cdd:cd18547 196 VVKAFNREEEAIEEFDEI 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
381-572 |
1.83e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 381 SIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS------GTFAYVAQQ------------------AWIL 436
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRirmifqdpstslnprqriSQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 437 NATLRDNILFGKEYDEERYNSVLNSCCLRPDLA-ILPSSdlteigerganLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:PRK15112 111 DFPLRLNTDLEPEQREKQIIETLRQVGLLPDHAsYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 516 LDAHVGNHIFNSAIRkhLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 572
Cdd:PRK15112 180 LDMSMRSQLINLMLE--LQEKqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1010-1208 |
1.88e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSKLSIIPQEP---VLFSG 1083
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisaVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 TVRSNLD-PFNQYT----EDQIWDALERTHMKECIAQLPLKLESEVmengdnfSVGERQLLCIARALLRHCKILILDEAT 1158
Cdd:PRK10419 107 TVREIIRePLRHLLsldkAERLARASEMLRAVDLDDSVLDKRPPQL-------SGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1159 AAMdtetDLLIQ-------ETIREAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:PRK10419 180 SNL----DLVLQagvirllKKLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
994-1207 |
2.08e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 61.91 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiglADLRSKLSI 1073
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSG-TVRSNLDPFNQ-------YTEDQIWDALERTHMKEciaqlplKLESEVMEngdnFSVGERQLLCIARAL 1145
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYLAQlkglkkeEARRRIDEWLERLELSE-------YANKRVEE----LSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 1146 LRHCKILILDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1014-1232 |
2.31e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.09 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIglADLRSKLSIIPQEPVLFSG-TVRSNLD-- 1090
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQNIAfg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1091 ------PFNQYTeDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTE 1164
Cdd:PRK11607 116 lkqdklPKAEIA-SRVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1165 ----TDLLIQETIREAFADCTMLTiaH---RLHTVLGsdRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAEN 1232
Cdd:PRK11607 184 lrdrMQLEVVDILERVGVTCVMVT--HdqeEAMTMAG--RIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVN 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
994-1219 |
2.39e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADL-RSKLS 1072
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRARHaRQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1073 IIPQ----EPVLfsgTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMEngdnFSVGERQLLCIARALLRH 1148
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1149 CKILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAH------RLhtvlgSDRIMVLAQGQVVEFDTPSVLLSND 1219
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1017-1200 |
2.58e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1017 TIKPKEKIGIVGRTGSGKSSLGMALfrlvelsGGCIKIDGvrisdiGLADLRSKLSIIPQE-PVLFSGTVRSNLDpfnqy 1095
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDE------GEVDPELKISYKPQYiKPDYDGTVEDLLR----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1096 tedQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 1174
Cdd:PRK13409 423 ---SITDDLGSSYYKSEIIK-PLQLE-RLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170 180 190
....*....|....*....|....*....|
gi 1622900605 1175 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 1200
Cdd:PRK13409 498 R-IAeerEATALVVDHDIYMIdYISDRLMV 526
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
378-571 |
3.02e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.44 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 378 TLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfAYVAQQAW----------------ILNATLR 441
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhkigmvfqnpdnqFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGKE-----YDE--ERYNSVLNscclrpdlaILPSSDLTEigERGANLSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:PRK13650 101 DDVAFGLEnkgipHEEmkERVNEALE---------LVGMQDFKE--REPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 515 ALDAHVGNHIFNS--AIRKHLKsKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK13650 170 MLDPEGRLELIKTikGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
379-573 |
3.18e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-----------------TFAYVAQ--QAWILNAT 439
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 440 LRDNILFG--------KEYDEERYNSVLNSCCLRPDLAILPssdlteigergANLSGGQRQRISLARALYSDRSIYILDD 511
Cdd:PRK13646 103 VEREIIFGpknfkmnlDEVKNYAHRLLMDLGFSRDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 512 PLSALDAHVGNHIFNSAIRKHLK-SKTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMnevaRY---ADEVIVMKEGSIVSQTSPKELFK 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
484-573 |
3.19e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 484 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKHLKSK---TVLFVTHQLQYLVD-CDEVIFMKE 559
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL--ALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQ 501
|
90
....*....|....
gi 1622900605 560 GCITERGTHEELMN 573
Cdd:PRK15134 502 GEVVEQGDCERVFA 515
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
706-828 |
3.55e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 62.56 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 706 MKDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDV 785
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSD 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622900605 786 RLPFQAEMFIQNVILVFFCVGMIAGVfPWFL-----VAVGPLVILFSV 828
Cdd:cd18572 109 PLSTNLNVFLRNLVQLVGGLAFMFSL-SWRLtllafITVPVIALITKV 155
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1010-1208 |
3.57e-10 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 61.39 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGlADLRSKLSI--IPQEPVLFSG-TVR 1086
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP-PHERARAGIayVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLdpfnqytedQI-WDALERTHMK--ECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1163
Cdd:TIGR03410 94 ENL---------LTgLAALPRRSRKipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900605 1164 ETDLLIQETIRE--AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:TIGR03410 165 SIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVA 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1017-1200 |
3.68e-10 |
|
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: 64.04 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1017 TIKPKEKIGIVGRTGSGKSSLgmalfrlVELSGGCIKIDGvrisdiGLADLRSKLSIIPQEPV-LFSGTVRSNLdpfnqy 1095
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTF-------AKILAGVLKPDE------GEVDEDLKISYKPQYISpDYDGTVEEFL------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1096 tEDQIWDALERTHMKECIAQlPLKLEsEVME-NGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR 1174
Cdd:COG1245 423 -RSANTDDFGSSYYKTEIIK-PLGLE-KLLDkNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|
gi 1622900605 1175 EaFA---DCTMLTIAHRLHTV-LGSDRIMV 1200
Cdd:COG1245 500 R-FAenrGKTAMVVDHDIYLIdYISDRLMV 528
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
993-1212 |
3.94e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.34 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 993 EVTFENAEMRYRENLP---LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIdGVRISDIG-----L 1064
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1065 ADLRSKLSIIPQ--EPVLFSGTVRSNL--DPFNQYTEDQiwDALERThmKECIAQlpLKLESEVMENGD-NFSVGERQLL 1139
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDIcfGPMNFGVSEE--DAKQKA--REMIEL--VGLPEELLARSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1140 CIARALLRHCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1212
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1010-1218 |
4.20e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.02 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI--SDIGLADLRSKLSIIPQEP--VLFSGTV 1085
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVFQNPddQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 RSNL--DPFN-----QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEAT 1158
Cdd:PRK13639 97 EEDVafGPLNlglskEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1159 AAMD----TETDLLIQETIREAfadctmLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:PRK13639 166 SGLDpmgaSQIMKLLYDLNKEG------ITIIISTHDVdlvpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
382-544 |
5.03e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISgtfayVAQQAWILNATLRDNILFGKEYDEERYnsVLNS 461
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDAVE--LLNA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 462 CCLrpdlailpsSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD---AHVGNHIFNSAIRKHlkSKTV 538
Cdd:COG2401 122 VGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARRA--GITL 190
|
....*.
gi 1622900605 539 LFVTHQ 544
Cdd:COG2401 191 VVATHH 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
379-567 |
5.07e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.98 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTfaYVAQQAWILNATLRDNILfGKEYDEER---- 454
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQKL-GFIYQFHHllpd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 455 YNSVLNSCC------LRPDLAILPSSD-LTEIG------ERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVG 521
Cdd:PRK11629 102 FTALENVAMplligkKKPAEINSRALEmLAAVGlehranHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900605 522 NHIFNSAIRKHLKSKTV-LFVTHQLQYLVDCDEVIFMKEGCITERGT 567
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAfLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
379-564 |
8.17e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--FAYVAQQAWIL--NATLRDNILFGKEYDEER 454
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETvkIGYFDQHQEELdpDKTVLDELRDGAPGGTEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 455 Y-NSVLNSCCLRPDLAilpssdLTEIGergaNLSGGQRQRISLARALYSDRSIYILDDPlsaldahvGNH-------IFN 526
Cdd:COG0488 411 EvRGYLGRFLFSGDDA------FKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP--------TNHldietleALE 472
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622900605 527 SAIRKHlkSKTVLFVTHQlQYLVD--CDEVIFMKEGCITE 564
Cdd:COG0488 473 EALDDF--PGTVLLVSHD-RYFLDrvATRILEFEDGGVRE 509
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1010-1213 |
8.55e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.90 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVE----LSGGCI--------------------------------K 1053
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDqyepTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1054 IDGVRISDIGLADLRSKLSIIPQEPVLFSG--TVRSN-LDPFNQ--YT-EDQIWDALERTHMkeciaqlpLKLESEVMEN 1127
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvLEALEEigYEgKEAVGRAVDLIEM--------VQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1128 GDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAF--ADCTMLTIAHRLHTVLG-SDRIMVLAQG 1204
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENG 245
|
....*....
gi 1622900605 1205 QVVEFDTPS 1213
Cdd:TIGR03269 246 EIKEEGTPD 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
994-1187 |
8.72e-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: 58.23 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcikidgvrisdigladlrskLSI 1073
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSGTVrsnldpfnqytedqiwdaleRTHMKECIAQLPlklesevmengdNFSVGERQLLCIARALLRHCKILI 1153
Cdd:cd03221 46 IAGELEPDEGIV--------------------TWGSTVKIGYFE------------QLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 1622900605 1154 LDEATAAMDTETDLLIQETIREaFaDCTMLTIAH 1187
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE-Y-PGTVILVSH 125
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
379-567 |
8.85e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.74 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmTLLE----GSIAISGT----------------FAYVAQQAWILNA 438
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI----NLLErptsGRVLVDGQdltalsekelrkarrqIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 -TLRDNILF-------GKEYDEERYNSVLnscclrpdlailpssDLTEIGERG----ANLSGGQRQRISLARALYSDRSI 506
Cdd:PRK11153 97 rTVFDNVALplelagtPKAEIKARVTELL---------------ELVGLSDKAdrypAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 507 YILDDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQLQyLVD--CDEVIFMKEGCITERGT 567
Cdd:PRK11153 162 LLCDEATSALDPATTRSILEllKDINRELGL-TIVLITHEMD-VVKriCDRVAVIDAGRLVEQGT 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1010-1207 |
9.75e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.87 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLADL-RSKL-SIIPQEPVL---FSGT 1084
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--KLPEYkRAKYiGRVFQDPMMgtaPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1085 VRSNLdpfnqytedqiwdAL-----------------ERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLR 1147
Cdd:COG1101 99 IEENL-------------ALayrrgkrrglrrgltkkRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 1148 HCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVL--GsDRIMVLAQGQVV 1207
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEEnnLTTLMVTHNMEQALdyG-NRLIMMHEGRII 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
382-571 |
1.00e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 61.61 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGqmtLLE------GSIAISGT-----------------FAYVAQQA----- 433
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILG---LLPppgitsGEILFDGEdllklsekelrkirgreIQMIFQDPmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 ------WILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAIL---PSsdlteigergaNLSGGQRQRISLARALYSDR 504
Cdd:COG0444 101 pvmtvgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------ELSGGMRQRVMIARALALEP 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 505 SIYILDDPLSALDAHVGNHIFN--SAIRKHLKSkTVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEEL 571
Cdd:COG0444 170 KLLIADEPTTALDVTIQAQILNllKDLQRELGL-AILFITHDLgvvAEI--ADRVAVMYAGRIVEEGPVEEL 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
367-573 |
1.06e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.56 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 367 HIHLGHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQA 433
Cdd:PRK13548 9 SVRLGGRTL---LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 434 WILNA-TLRDNILFG-------KEYDEERYNSVLNSCclrpDLAILPSSDLTEigerganLSGGQRQRISLARAL----- 500
Cdd:PRK13548 86 SLSFPfTVEEVVAMGraphglsRAEDDALVAAALAQV----DLAHLAGRDYPQ-------LSGGEQQRVQLARVLaqlwe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 501 -YSDRSIYILDDPLSALD-AH---VGNHIFNSAIRKHLkskTVLFVTHQL----QYlvdCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK13548 155 pDGPPRWLLLDEPTSALDlAHqhhVLRLARQLAHERGL---AVIVVLHDLnlaaRY---ADRIVLLHQGRLVADGTPAEV 228
|
..
gi 1622900605 572 MN 573
Cdd:PRK13548 229 LT 230
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
367-558 |
1.15e-09 |
|
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: 58.53 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 367 HIHLGHLRLQRTlhSIDLEIQEGKLVGICGSVGSGKTSLISAIlgqmtllegsiaisgtfayvaqqawILNATLRDNILF 446
Cdd:cd03227 1 KIVLGRFPSYFV--PNDVTFGEGSLTIITGPNGSGKSTILDAI-------------------------GLALGGAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 GKEYDEERYNSvlnsCCLRPDLAILPSSdlteigerganLSGGQRQRISLARAL----YSDRSIYILDDPLSALDAHVGN 522
Cdd:cd03227 54 RRSGVKAGCIV----AAVSAELIFTRLQ-----------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622900605 523 HIFNsAIRKHLKSK-TVLFVTHQLQYLVDCDEVIFMK 558
Cdd:cd03227 119 ALAE-AILEHLVKGaQVIVITHLPELAELADKLIHIK 154
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
379-569 |
1.22e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAilgqMTLLEgsIAISGTFAyVAQQAWILNAT--------LRDNI--LFgk 448
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNLLE--MPRSGTLN-IAGNHFDFSKTpsdkaireLRRNVgmVF-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 449 eydeERYN-----SVLNSCCLRP--------------DLAILPSSDLTEIGER-GANLSGGQRQRISLARALYSDRSIYI 508
Cdd:PRK11124 89 ----QQYNlwphlTVQQNLIEAPcrvlglskdqalarAEKLLERLRLKPYADRfPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 509 LDDPLSALDAHVGNHIFNsaIRKHLKSK--TVLFVTHQlqylVD-----CDEVIFMKEGCITERGTHE 569
Cdd:PRK11124 165 FDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHE----VEvarktASRVVYMENGHIVEQGDAS 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
382-566 |
1.25e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.97 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG----TFAYVAQQAWIL---------NATLRDNIL-FG 447
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVvpqfdnldpDFTVRENLLvFG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 448 keydeeRYNSVLNSCC--LRPDL---AILPSSDLTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHvGN 522
Cdd:PRK13537 106 ------RYFGLSAAAAraLVPPLlefAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-AR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 523 HIFNSAIRKHLKS-KTVLFVTHqlqylvdcdeviFMKEG-------CITERG 566
Cdd:PRK13537 175 HLMWERLRSLLARgKTILLTTH------------FMEEAerlcdrlCVIEEG 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
376-573 |
1.48e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWILNA-TL 440
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararrgIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 441 RDNIL--------FGKEYDEERYNSVL---NSCCLRPDLailpssdlteigerGANLSGGQRQRISLARALYSDRSIYIL 509
Cdd:PRK10895 96 YDNLMavlqirddLSAEQREDRANELMeefHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 510 DDPLSALDAHVGNHIfnSAIRKHLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK10895 162 DEPFAGVDPISVIDI--KRIIEHLRDSglGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
382-572 |
1.62e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.90 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQQAW-------------------------- 434
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSGRELrplrrrmqmvfqdpyaslnprmtvgd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 435 ILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAilpssdlteigERGAN-LSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:COG4608 117 IIAEPLRIHGLASKAERRERVAELLELVGLRPEHA-----------DRYPHeFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 514 SALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQL---QYLvdCDEVIFMKEGCITERGTHEELM 572
Cdd:COG4608 186 SALDVSIQAQVLN--LLEDLQDElglTYLFISHDLsvvRHI--SDRVAVMYLGKIVEIAPRDELY 246
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
72-248 |
1.83e-09 |
|
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: 59.96 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 72 KSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPT-GFLGSAVFILFYPAMMFASRLTAYFRRKCVA 150
Cdd:pfam00664 95 NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAVFAKILRKLSRKEQK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 151 ATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVT--FSVHMTLGFD 228
Cdd:pfam00664 175 AVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALAlwFGAYLVISGE 254
|
170 180
....*....|....*....|
gi 1622900605 229 LTAAQAFTVVTVFNSMTFAL 248
Cdd:pfam00664 255 LSVGDLVAFLSLFAQLFGPL 274
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
377-567 |
1.91e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG-----QMTLLEGSIAISGTfayvAQQAWILNATLRDNILFGKEYD 451
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSST----SKQKEIKPVRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 452 EERYNSVLNSCCLRP--------DLAILPSSDLTEIG------ERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:PRK13643 96 QLFEETVLKDVAFGPqnfgipkeKAEKIAAEKLEMVGladefwEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 517 DAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 567
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1011-1207 |
2.08e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQE-PVLFSGTVRSN 1088
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 LdPFNQYTEDQIW--DALERTHMKECIAQLPLK--LESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM-DT 1163
Cdd:PRK09700 101 L-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900605 1164 ETD---LLIQETIREAFAdctMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:PRK09700 180 EVDylfLIMNQLRKEGTA---IVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1011-1207 |
2.44e-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: 61.38 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVELSG---GCIKIDGVRISDIGLADLRSK-LSIIPQEPVLFSG-TV 1085
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 RSNLDPFNQYTE--DQIWDALERTHMKECIAQLPLKLESEVMENGDnFSVGERQLLCIARALLRHCKILILDEATAAM-D 1162
Cdd:TIGR02633 96 AENIFLGNEITLpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSSLtE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900605 1163 TETDLLIqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:TIGR02633 175 KETEILL-DIIRDLKAhGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
377-573 |
2.55e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.75 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILN---------------ATLR 441
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGKEYDEERYNSVLNscclRPDLAiLPSSDLTEIGERGA-NLSGGQRQRISLARALYSDRSIYILDDPLSALDAHV 520
Cdd:PRK13647 99 DDVAFGPVNMGLDKDEVER----RVEEA-LKAVRMWDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 521 GNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK13647 174 QETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
377-572 |
2.56e-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: 61.36 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtLLEGSiaiSGTFAYVAQQAWIL----------NATLRDNILF 446
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG---VLEPT---SGEVNVRVGDEWVDmtkpgpdgrgRAKRYIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 gKEYDEERYNSVLN------SCCLRPDLA------ILPSSDLTE-----IGERGAN-LSGGQRQRISLARALYSDRSIYI 508
Cdd:TIGR03269 372 -QEYDLYPHRTVLDnlteaiGLELPDELArmkaviTLKMVGFDEekaeeILDKYPDeLSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 509 LDDPLSALD----AHVGNHIFNSaiRKHLkSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELM 572
Cdd:TIGR03269 451 LDEPTGTMDpitkVDVTHSILKA--REEM-EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
82-571 |
2.75e-09 |
|
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: 61.35 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 82 SNDGQRMFEAAAVGSLLAGGPVVAILGMIYnVIILGPTGFLGSAVFI----LFYpaMMFASRLTAYFRRkcVAATDERVQ 157
Cdd:COG4615 112 TEDVRTISQAFVRLPELLQSVALVLGCLAY-LAWLSPPLFLLTLVLLglgvAGY--RLLVRRARRHLRR--AREAEDRLF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 158 K-MNEVLTYIKFIKM--------YAwvKAFSQSVQKIREEERRilekAGYFQSITVGVAPIV--VVIASVVTFSVHMtlg 226
Cdd:COG4615 187 KhFRALLEGFKELKLnrrrrrafFD--EDLQPTAERYRDLRIR----ADTIFALANNWGNLLffALIGLILFLLPAL--- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 227 FDLTAAQAFTVVTVF----NSMTFALKVTPfsvkSLSEASVAVDRFKSLFLMEEvhmiknkPASPHikiEMKNATLAWDS 302
Cdd:COG4615 258 GWADPAVLSGFVLVLlflrGPLSQLVGALP----TLSRANVALRKIEELELALA-------AAEPA---AADAAAPPAPA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 303 SHSSIQnspkltpkmkkdkrasrgkkekvrqLQRTEHQavlaeqkghllldsderpSPEEEEGKHIHLGhlrlqrtlhSI 382
Cdd:COG4615 324 DFQTLE-------------------------LRGVTYR------------------YPGEDGDEGFTLG---------PI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 383 DLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfAYVAQQAWilnATLRDNI--------LFGKEY---- 450
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG--QPVTADNR---EAYRQLFsavfsdfhLFDRLLgldg 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 451 --DEERynsvlnsccLRPDLAILPSSDLTEIgERGA----NLSGGQRQRISLARALYSDRSIYILD------DPlsalda 518
Cdd:COG4615 427 eaDPAR---------ARELLERLELDHKVSV-EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDewaadqDP------ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 519 hVGNHIFNSAIRKHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:COG4615 491 -EFRRVFYTELLPELKArgKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
708-921 |
2.85e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 60.16 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 708 DNPRMQYYASIYALSM----AVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTP--TGRILNRFSKDMD 781
Cdd:cd18578 43 DDDELRSEANFWALMFlvlaIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDAS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 782 EV----DVRLPfqaeMFIQNVILVFFCVGmIAGVFPWFL----VAVGPLVILFSVLHIvsRVLIR-ELKRLDNITQSpfl 852
Cdd:cd18578 123 DVrglvGDRLG----LILQAIVTLVAGLI-IAFVYGWKLalvgLATVPLLLLAGYLRM--RLLSGfEEKNKKAYEES--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 853 SHITS-SIQGLATIHAYNKGQEFLHRYQELLDDNQ-------------------APFFLFTCAMRWLAVrldLISIALIT 912
Cdd:cd18578 193 SKIASeAVSNIRTVASLTLEDYFLEKYEEALEEPLkkglrralisglgfglsqsLTFFAYALAFWYGGR---LVANGEYT 269
|
....*....
gi 1622900605 913 TTGLMIVLM 921
Cdd:cd18578 270 FEQFFIVFM 278
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1011-1219 |
2.89e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.26 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----------VELSGGCIKIDGVRISDIGLA-----------DLRS 1069
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLARDIRKSrantgyifqqfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1070 KLSIIpqEPVLFS--GTV---RSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARA 1144
Cdd:PRK09984 100 RLSVL--ENVLIGalGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTL-----------SGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1145 LLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVeFDTPSVLLSND 1219
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRyCERIVALRQGHVF-YDGSSQQFDNE 243
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1010-1212 |
3.01e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.94 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIS---DIGLA---DL--RsklsiipqEPVLF 1081
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSallELGAGfhpELtgR--------ENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1082 SGTVrsnldpfNQYTEDQIwdaleRTHMKECIA--------QLPLKlesevmengdNFSVGERQLLCIARALLRHCKILI 1153
Cdd:COG1134 112 NGRL-------LGLSRKEI-----DEKFDEIVEfaelgdfiDQPVK----------TYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1154 LDEATAAMDTE-----TDlLIQETIREAfadCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1212
Cdd:COG1134 170 VDEVLAVGDAAfqkkcLA-RIRELRESG---RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDP 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
381-544 |
3.06e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.30 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 381 SIDLEIQEGKLVGICGSVGSGKTSLISaILGQMTLLEG---SIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNS 457
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRG 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 458 VLNScclrpDL-AILPSSDLTEIGERGAN----------LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 526
Cdd:TIGR00954 549 LSDK-----DLeQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR 623
|
170
....*....|....*...
gi 1622900605 527 SAIRKHLkskTVLFVTHQ 544
Cdd:TIGR00954 624 LCREFGI---TLFSVSHR 638
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
997-1208 |
3.42e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 997 ENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG-----GCIKIDGVRI--SDIGLADLRS 1069
Cdd:PRK14267 8 VNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1070 KLSIIPQEPVLFSG-TVRSN----------LDPFNQYTEDQIWdALERthmkeciAQLPLKLESEVMENGDNFSVGERQL 1138
Cdd:PRK14267 86 EVGMVFQYPNPFPHlTIYDNvaigvklnglVKSKKELDERVEW-ALKK-------AALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1139 LCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHR-LHTVLGSDRIMVLAQGQVVE 1208
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIE 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
379-562 |
3.91e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.94 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVAQQA-WIL------------NATLRD 442
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRAkYIGrvfqdpmmgtapSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILF----GKEY---------DEERYnsvlnscclRPDLAILpssDL-------TEIGergaNLSGGQRQRISLARALYS 502
Cdd:COG1101 102 NLALayrrGKRRglrrgltkkRRELF---------RELLATL---GLglenrldTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 503 DRSIYILDDPLSALD---AHVGNHIFNSAIR-KHLkskTVLFVTHQLQYLVDC-DEVIFMKEGCI 562
Cdd:COG1101 166 KPKLLLLDEHTAALDpktAALVLELTEKIVEeNNL---TTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1010-1207 |
4.14e-09 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 58.50 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAdLRSKLSIIpqepvlfsgtvrsnl 1089
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-FLRRIGVV--------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1090 dpFNQYTEdQIWD--ALERTHMKECIAQLP-------LKLESEVMENGD-------NFSVGERQLLCIARALLRHCKILI 1153
Cdd:cd03267 100 --FGQKTQ-LWWDlpVIDSFYLLAAIYDLPparfkkrLDELSELLDLEElldtpvrQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1154 LDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1002-1190 |
7.62e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.52 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1002 RYREN--LPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGV---RISDIGLADLRS-KLSIIP 1075
Cdd:PRK11629 14 RYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNqKLGFIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1076 QepvlfsgtvrsnldpFNQYTEDqiWDALERTHMKECIAQLPLK--------------LESEVMENGDNFSVGERQLLCI 1141
Cdd:PRK11629 94 Q---------------FHHLLPD--FTALENVAMPLLIGKKKPAeinsralemlaavgLEHRANHRPSELSGGERQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1142 ARALLRHCKILILDEATAAMDTET-----DLLIQETIRE--AFADCTM-LTIAHRLH 1190
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNadsifQLLGELNRLQgtAFLVVTHdLQLAKRMS 213
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
707-923 |
7.83e-09 |
|
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: 58.25 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 707 KDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvr 786
Cdd:cd18545 34 GDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSL--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 787 lpfqAEMF---IQNVILVFFCVGMIAGVFPWF-----LVAVGPLVILFSVLhIVSRVLIRELKRLDNITQSPFLSHITSS 858
Cdd:cd18545 111 ----SDLLsngLINLIPDLLTLVGIVIIMFSLnvrlaLVTLAVLPLLVLVV-FLLRRRARKAWQRVRKKISNLNAYLHES 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 859 IQGLATIHAYNKGQEFLHRYQELLDDNQAPFflftcaMRwlAVRL-DLI--SIALITTTGLMIVLMHG 923
Cdd:cd18545 186 ISGIRVIQSFAREDENEEIFDELNRENRKAN------MR--AVRLnALFwpLVELISALGTALVYWYG 245
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
728-882 |
9.25e-09 |
|
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: 58.37 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 728 ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkDMDEVDVRLPFQAEMFIQNVILVFFCVGM 807
Cdd:cd18782 57 VLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLFSVIYIAV 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 808 IAgVFPWFL----VAVGPLVILFSVLhiVSRVLIRELKRLdNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 882
Cdd:cd18782 136 LF-SYSPLLtlvvLATVPLQLLLTFL--FGPILRRQIRRR-AEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRY 210
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
711-884 |
9.57e-09 |
|
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: 58.25 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 711 RMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdvrlpfQ 790
Cdd:cd18577 45 DVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLI------Q 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 791 ---AE---MFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLVILfsVLHIVSRVLIR-ELKRLDNITQSpfLSHITS 857
Cdd:cd18577 119 dgiGEklgLLIQSLSTFIagFIIAFIYS---WkltlVLLATLPLIAI--VGGIMGKLLSKyTKKEQEAYAKA--GSIAEE 191
|
170 180
....*....|....*....|....*..
gi 1622900605 858 SIQGLATIHAYNKGQEFLHRYQELLDD 884
Cdd:cd18577 192 ALSSIRTVKAFGGEEKEIKRYSKALEK 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
379-584 |
9.66e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.74 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAiLGQMTLL------EGSIAISGTFAY---------------VAQQAWILN 437
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRC-LNRMNDLipgarvEGEILLDGEDIYdpdvdvvelrrrvgmVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 438 ATLRDNILFGkeydeerynsvlnsccLRpDLAILPSSDLTEIGER------------------GANLSGGQRQRISLARA 499
Cdd:COG1117 106 KSIYDNVAYG----------------LR-LHGIKSKSELDEIVEEslrkaalwdevkdrlkksALGLSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 500 LYSDRSIYILDDPLSALD----AHVGNHIFNsairkhLKSK-TVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEElmn 573
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpistAKIEELILE------LKKDyTIVIVTHNMQQAARVsDYTAFFYLGELVEFGPTEQ--- 239
|
250
....*....|.
gi 1622900605 574 lngdyatIFNN 584
Cdd:COG1117 240 -------IFTN 243
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
994-1220 |
1.00e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.87 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS----DIGLAD 1066
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1067 LRSKLSIIPQ--EPVLFSGTVRSNL----DPFNQYTEDqiwdalerthMKECIAQLPLKL--ESEVMENGD-NFSVGERQ 1137
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIifgpKNFKMNLDE----------VKNYAHRLLMDLgfSRDVMSQSPfQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1138 LLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSV 1214
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE 232
|
....*.
gi 1622900605 1215 LLSNDS 1220
Cdd:PRK13646 233 LFKDKK 238
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1013-1217 |
1.08e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1013 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRlVELSGGCIKIDGVRISDIGLADL----RSKL-----SIIPQEPvlfsg 1083
Cdd:PRK15093 25 RVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDIDLLRLspreRRKLvghnvSMIFQEP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 tvRSNLDPfNQYTEDQIWDAL----------ERTHMK-----ECIAQLPLKLESEVMENGD-NFSVGERQLLCIARALLR 1147
Cdd:PRK15093 99 --QSCLDP-SERVGRQLMQNIpgwtykgrwwQRFGWRkrraiELLHRVGIKDHKDAMRSFPyELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1148 HCKILILDEATAAMDTETdlliQETIREAFA------DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1217
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTT----QAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
487-600 |
1.15e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.44 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 487 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN--SAIRKHLKSKTVlFVTHQLQyLVD--CDEVIFMKEGCI 562
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNlmMDLQQELGLSYV-FISHDLS-VVEhiADEVMVMYLGRC 233
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622900605 563 TERGTHEelmnlngdyaTIFNN-------LLLGDTPPVEINSKKE 600
Cdd:PRK11308 234 VEKGTKE----------QIFNNprhpytqALLSATPRLNPDDRRE 268
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
379-571 |
1.15e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.79 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAW----------------ILNATLRD 442
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmvfqnpdnqIVATIVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGKEydeerynsvlnscclrpDLAILPSsdltEIGERGAN-----------------LSGGQRQRISLARALYSDRS 505
Cdd:PRK13633 106 DVAFGPE-----------------NLGIPPE----EIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 506 IYILDDPLSALDAHVGNHIFNSAirKHLKSK---TVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTI--KELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
382-572 |
1.78e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQ----AWILNATLRDN 443
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYITESrrdnGFFPNFSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFGK---------------EYDEERYNSVLnscclRPDLAILPSSDLTEIGErganLSGGQRQRISLARALYSDRSIYI 508
Cdd:PRK09700 362 MAISRslkdggykgamglfhEVDEQRTAENQ-----RELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 509 LDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITE------RGTHEELM 572
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQiltnrdDMSEEEIM 503
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1012-1206 |
1.82e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1012 KKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIP---QEPVLF------ 1081
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1082 --SGTVRSNLDPFNQYT--EDQIwdaLERTHmkeciAQLPLKLeSEVMENGDNFSVGERQLLCIARALLRHCKILILDEA 1157
Cdd:PRK15439 360 wnVCALTHNRRGFWIKParENAV---LERYR-----RALNIKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1158 TAAMDTETDLLIQETIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQV 1206
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1000-1221 |
1.92e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.90 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1000 EMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDG-----VRISD--IGLAD------ 1066
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDgqLKVADknqlrl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1067 LRSKLSIIPQEPVLFSG-TVRSNLdpfnQYTEDQIWdALERTHMKECIAQLPLKL---ESEVMENGDNFSVGERQLLCIA 1142
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHmTVLENV----MEAPIQVL-GLSKQEARERAVKYLAKVgidERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1143 RALLRHCKILILDEATAAMDTEtdlLIQETIR--EAFAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1217
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPE---LVGEVLRimQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
....
gi 1622900605 1218 NDSS 1221
Cdd:PRK10619 242 NPQS 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1010-1224 |
2.01e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.58 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFR----LVELSGGCIKIDGVRISDIGLaDLRSKLSI--IPQEPVLFSG 1083
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTT----FYmivgLVKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 -TVRSNLDPFNQYTEdqiwdaLERTHMKECIAQLplkLE----SEVMEN-GDNFSVGERQLLCIARALLRHCKILILDEA 1157
Cdd:COG1137 93 lTVEDNILAVLELRK------LSKKEREERLEEL---LEefgiTHLRKSkAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1158 TAAMD--TETDllIQETIREafadctmLT---IA-----HRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSR-FY 1224
Cdd:COG1137 164 FAGVDpiAVAD--IQKIIRH-------LKergIGvlitdHNVRETLGiCDRAYIISEGKVLAEGTPEEILNNPLVRkVY 233
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
720-884 |
2.12e-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: 57.19 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 720 ALSMAVMLILKAIrgVVFVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 793
Cdd:cd18557 39 ALILLAIYLLQSV--FTFVRYYLfniageRIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 794 FIQNVILVFFCVGMIA----GVFPWFLVAVGPLVILFSVLHIVSRVLIREL-KRLDNITQspflsHITSSIQGLATIHAY 868
Cdd:cd18557 117 LLRNILQVIGGLIILFilswKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVqDALAKAGQ-----VAEESLSNIRTVRSF 191
|
170
....*....|....*.
gi 1622900605 869 NKGQEFLHRYQELLDD 884
Cdd:cd18557 192 SAEEKEIRRYSEALDR 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
994-1210 |
2.73e-08 |
|
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: 55.72 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLSI 1073
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1074 IPQEPVLFSG-TVRSNLD---PFNQYTEDQIwdaLERTHMkecIAQLpLKLESEVMENGDNFSVGERQLLCIARALLRHC 1149
Cdd:cd03301 77 VFQNYALYPHmTVYDNIAfglKLRKVPKDEI---DERVRE---VAEL-LQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1150 KILILDEATAAMDTEtdlliqetIREAfadctMLTIAHRLHTVLG----------------SDRIMVLAQGQVVEFD 1210
Cdd:cd03301 150 KVFLMDEPLSNLDAK--------LRVQ-----MRAELKRLQQRLGtttiyvthdqveamtmADRIAVMNDGQIQQIG 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
379-571 |
2.93e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.21 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA-------------------- 438
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkevgmvfqqpnpfphl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNILFGKEY----DEERYNSVLNSCCLRPDLailpssdLTEIGER----GANLSGGQRQRISLARALYSDRSIYILD 510
Cdd:PRK14246 106 SIYDNIAYPLKShgikEKREIKKIVEECLRKVGL-------WKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 511 DPLSALDAhVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 571
Cdd:PRK14246 179 EPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
377-560 |
3.60e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSIAISGT--------------FAYVAQQ-AWILNAT 439
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 440 LRDNILFGKEYDEE----RYNSVLNSC-CLRPDLAILPSSDLTEIGERGanlsGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:TIGR02633 95 VAENIFLGNEITLPggrmAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900605 515 ALDAHVGNHIFNsaIRKHLKSKTV--LFVTHQLQYL-VDCDEVIFMKEG 560
Cdd:TIGR02633 171 SLTEKETEILLD--IIRDLKAHGVacVYISHKLNEVkAVCDTICVIRDG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
379-615 |
3.69e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.78 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAI----------SGTFAYVAQQAWILNA---------- 438
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFkelrrrvsmv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 -----------TLRDNILFG-------KEYDEERYNSVLNSCCLRPDLAilpssdlteigERGA-NLSGGQRQRISLARA 499
Cdd:PRK13631 122 fqfpeyqlfkdTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYL-----------ERSPfGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 500 LYSDRSIYILDDPLSALDAHvGNHIFNSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTheelmnlngD 577
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPK-GEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGT---------P 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622900605 578 YATIFNNLLLGDT----PPV--EINSKKETSGSQKKSQDKGPKT 615
Cdd:PRK13631 261 YEIFTDQHIINSTsiqvPRViqVINDLIKKDPKYKKLYQKQPRT 304
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
718-886 |
3.70e-08 |
|
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: 56.30 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 718 IYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmdevDVrlpfqaeM 793
Cdd:cd18570 43 IISIGLILLYLFQSllsyIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN------DA-------N 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 794 FIQNVI-----------LVFFCVGMIAGVFPW--FLVAVGPLVILFSVLHIVSRVLIRELKRLdNITQSPFLSHITSSIQ 860
Cdd:cd18570 110 KIREAIssttislfldlLMVIISGIILFFYNWklFLITLLIIPLYILIILLFNKPFKKKNREV-MESNAELNSYLIESLK 188
|
170 180
....*....|....*....|....*.
gi 1622900605 861 GLATIHAYNKGQEFLHRYQELLDDNQ 886
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLL 214
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
385-550 |
3.85e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.88 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 385 EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQAWILNATLRDNILFGKE---YDEERYNS-VL 459
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSITkdfYTHPYFKTeIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 460 NSCCLRPdlaiLPSSDLTEigerganLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHL--KSKT 537
Cdd:cd03237 101 KPLQIEQ----ILDREVPE-------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA-SKVIRRFAenNEKT 168
|
170
....*....|....*.
gi 1622900605 538 VLFVTHQL---QYLVD 550
Cdd:cd03237 169 AFVVEHDIimiDYLAD 184
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
376-557 |
4.03e-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: 54.25 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQmtllEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYdeery 455
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 456 nsvlnscclrpdlailpssdLTeIGERGANLSGGQRQRISLARALYSD--RSIYILDDPLSALDAHVGNHIFNSAIRKHL 533
Cdd:cd03238 79 --------------------LT-LGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHQQDINQLLEVIKGLID 137
|
170 180
....*....|....*....|....
gi 1622900605 534 KSKTVLFVTHQLQYLVDCDEVIFM 557
Cdd:cd03238 138 LGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1009-1207 |
4.20e-08 |
|
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: 55.35 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1009 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVE---LSGGCIKIDGVRISDiglADLRSKLSIIPQEPVLFSG-T 1084
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1085 VRSNLdpfnQYTedqiwdALERTHmkECIAQLPLKLESEVMENGD------------NFSVGERQLLCIARALLRHCKIL 1152
Cdd:cd03234 98 VRETL----TYT------AILRLP--RKSSDAIRKKRVEDVLLRDlaltriggnlvkGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1153 ILDEATAAMDTETDLLIQETIREafadctmltIAHRLHTVLGS------------DRIMVLAQGQVV 1207
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQ---------LARRNRIVILTihqprsdlfrlfDRILLLSSGEIV 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
377-571 |
4.39e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWIL-NATLR 441
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFG---KEYDEERYNSVLN--SCCLRPDLAilpssdlteigerGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:PRK15439 105 ENILFGlpkRQASMQKMKQLLAalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 517 DAHVGNHIFnSAIRKhLKSKTV--LFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 571
Cdd:PRK15439 172 TPAETERLF-SRIRE-LLAQGVgiVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
720-964 |
4.93e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 55.98 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 720 ALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVI 799
Cdd:cd18563 50 AGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 800 LVFFCVGMIAGVFPWFLVAV---GPLVILFSVLH--IVSRVLIRELKRLDNITqspflSHITSSIQGLATIHAYnkGQE- 873
Cdd:cd18563 130 MIIGIGVVLFSLNWKLALLVlipVPLVVWGSYFFwkKIRRLFHRQWRRWSRLN-----SVLNDTLPGIRVVKAF--GQEk 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 874 -----FLHRYQELLDDNqapfflftcamrwlaVRLDLIS------IALITTTGLMIV-------LMHGQIPP----AYag 931
Cdd:cd18563 203 reikrFDEANQELLDAN---------------IRAEKLWatffplLTFLTSLGTLIVwyfggrqVLSGTMTLgtlvAF-- 265
|
250 260 270
....*....|....*....|....*....|...
gi 1622900605 932 laISYAVQLTGLFQFTVRLASETEARFTSVERI 964
Cdd:cd18563 266 --LSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
377-541 |
4.99e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA---------------TLR 441
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFG-----KEYDEERYNSVLNsccLRPDLailpssdLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:PRK11614 99 ENLAMGgffaeRDQFQERIKWVYE---LFPRL-------HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180
....*....|....*....|....*
gi 1622900605 517 DAHVGNHIFNSAIRKHLKSKTVLFV 541
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
724-829 |
5.09e-08 |
|
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: 55.90 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 724 AVMLILKAIRGVV-FVKGTL------RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQ 796
Cdd:cd18542 43 LLILGVALLRGVFrYLQGYLaekasqKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVR 122
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622900605 797 NVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVL 829
Cdd:cd18542 123 AVLLFIGALIIMFSINWkltLISLAIIPFIALFSYV 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
356-550 |
5.82e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 356 ERPSPEEEEGKHIHLGHLRLQRTLHSIDL-----EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVA 430
Cdd:PRK13409 327 EERPPRDESERETLVEYPDLTKKLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 431 Q----------QAWILNATlrdnilfgKEYDEERYNSVLnsccLRP-DLAILPSSDLTEigerganLSGGQRQRISLARA 499
Cdd:PRK13409 407 QyikpdydgtvEDLLRSIT--------DDLGSSYYKSEI----IKPlQLERLLDKNVKD-------LSGGELQRVAIAAC 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 500 LYSDRSIYILDDPLSALDAH----VGnhifnSAIRKHL--KSKTVLFVTHQLqYLVD 550
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDVEqrlaVA-----KAIRRIAeeREATALVVDHDI-YMID 518
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1010-1218 |
5.84e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.14 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRI-SDIGLADLRSKLSIIPQEpvlfSGTVRSN 1088
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQLRQH----VGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 LDPFNQYTedqiwdALE---------RTHMKECIAQLPLKLESEVMENGDN------FSVGERQLLCIARALLRHCKILI 1153
Cdd:PRK11264 94 FNLFPHRT------VLEniiegpvivKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 1154 LDEATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSN 1218
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
994-1213 |
6.19e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.51 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPLV---LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG----LAD 1066
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1067 LRSKLSIIPQEP--VLFSGTVRSNL----DPFNQYTEDQIWDALERTHM----KECIAQLPLKLesevmengdnfSVGER 1136
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEMvglaDEFWEKSPFEL-----------SGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1137 QLLCIARALLRHCKILILDEATAAMDTETDLLIQ---ETIREAFAdcTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1212
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQSGQ--TVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
.
gi 1622900605 1213 S 1213
Cdd:PRK13643 229 S 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
377-573 |
6.30e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTL-HSIDLEIQEGKLVGICGSVGSGKTSLI------------SAILGQMTLLE-GSIAISGTFAYVAQQawiLNA---- 438
Cdd:PRK10575 24 RTLlHPLSLTFPAGKVTGLIGHNGSGKSTLLkmlgrhqppsegEILLDAQPLESwSSKAFARKVAYLPQQ---LPAaegm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNILFGK-----------EYDEERYNSVLNSCCLRPDLAILPSSdlteigerganLSGGQRQRISLARALYSDRSIY 507
Cdd:PRK10575 101 TVRELVAIGRypwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 508 ILDDPLSALD-AHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:PRK10575 170 LLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
379-571 |
7.11e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYV--AQQAWI------LN----ATLRDN 443
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvRFRSPrdAQAAGIaiihqeLNlvpnLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFGKEY------D----EERYNSVLNscclRPDLAILPSsdlTEIGErganLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:COG1129 100 IFLGREPrrggliDwramRRRARELLA----RLGLDIDPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 514 SALDAHVGNHIFNsAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 571
Cdd:COG1129 169 ASLTEREVERLFR-IIRR-LKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
714-923 |
7.97e-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: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 714 YYASIYALSMAVMLILKAIRgvvfvkgtlrassrlhDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 793
Cdd:cd18552 56 SYLQTYLMAYVGQRVVRDLR----------------NDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 794 FIQNVILVFFCVGMIAgVFPWFL----VAVGPLVILfsvlhiVSRVLIRELKRLDNITQSpFLSHITS----SIQGLATI 865
Cdd:cd18552 120 LVRDPLTVIGLLGVLF-YLDWKLtliaLVVLPLAAL------PIRRIGKRLRKISRRSQE-SMGDLTSvlqeTLSGIRVV 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 866 HAYNKGQEFLHRYQELLDDNqapfflFTCAMRWLAVRlDLIS--IALITTTGLMIVLMHG 923
Cdd:cd18552 192 KAFGAEDYEIKRFRKANERL------RRLSMKIARAR-ALSSplMELLGAIAIALVLWYG 244
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
719-923 |
8.54e-08 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 55.18 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 719 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMF 794
Cdd:cd18576 38 IALLLLGLFLLQAVfsffRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 795 IQNVILVFFCVGMIAGVFP---WFLVAVGPLVILFSVlhIVSRVlIREL--KRLDNITQSpfLSHITSSIQGLATIHAYN 869
Cdd:cd18576 118 LRQILTLIGGVVLLFFISWkltLLMLATVPVVVLVAV--LFGRR-IRKLskKVQDELAEA--NTIVEETLQGIRVVKAFT 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 870 KGQEFLHRYQELLDDnqapffLFTCAMRWLAVRLDLIS-IALITTTGLMIVLMHG 923
Cdd:cd18576 193 REDYEIERYRKALER------VVKLALKRARIRALFSSfIIFLLFGAIVAVLWYG 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1011-1211 |
9.32e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrLVELSG------GCIKIDG--VRISDIGLAdLRSKLSIIPQE----P 1078
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTL------LKILSGnyqpdaGSILIDGqeMRFASTTAA-LAAGVAIIYQElhlvP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1079 VLfsgTVRSNLdpfnqytedqiwdalerthmkeCIAQLPLK--------LESEVMEN----GDNF---------SVGERQ 1137
Cdd:PRK11288 93 EM---TVAENL----------------------YLGQLPHKggivnrrlLNYEAREQlehlGVDIdpdtplkylSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1138 LLCIARALLRHCKILILDEATAAMDT-ETDLLIQeTIREAFADCT-MLTIAHRLHTVLG-SDRIMVLAQGQVVE-FDT 1211
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRAEGRvILYVSHRMEEIFAlCDAITVFKDGRYVAtFDD 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
987-1219 |
9.32e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.79 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 987 DWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD 1066
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1067 LRSKLSIIPQE-PVLFSGTVRSnLDPFNQYTedqiWD-------ALERTHMKECIAQLPLK-LESEVMengDNFSVGERQ 1137
Cdd:PRK10575 83 FARKVAYLPQQlPAAEGMTVRE-LVAIGRYP----WHgalgrfgAADREKVEEAISLVGLKpLAHRLV---DSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1138 LLCIARALLRHCKILILDEATAAMD----TETDLLIQETIREafadcTMLTIAHRLHTVLGS----DRIMVLAQGQVVEF 1209
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQE-----RGLTVIAVLHDINMAarycDYLVALRGGEMIAQ 229
|
250
....*....|
gi 1622900605 1210 DTPSVLLSND 1219
Cdd:PRK10575 230 GTPAELMRGE 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1010-1212 |
9.34e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.24 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKpKEKI-GIVGRTGSGKSSLgmalfrlVELSGGCIKidgVRISDIGLADLRSKLSIIPQEPVLFSGT---- 1084
Cdd:PRK13631 41 ALNNISYTFE-KNKIyFIIGNSGSGKSTL-------VTHFNGLIK---SKYGTIQVGDIYIGDKKNNHELITNPYSkkik 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1085 ----VRSNLDPFNQYTEDQIW-DALERTHMKECIAQLPLKLES--------EVMENGDNF--------SVGERQLLCIAR 1143
Cdd:PRK13631 110 nfkeLRRRVSMVFQFPEYQLFkDTIEKDIMFGPVALGVKKSEAkklakfylNKMGLDDSYlerspfglSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1144 ALLRHCKILILDEATAAMDTETDLLIQETIREAFADC-TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1212
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1010-1213 |
1.07e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIG---LADLRSK-LSIIPQEPVLFSG-T 1084
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRREhFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1085 VRSNLD-PfnqytedQIWDALERTHMKECIAQL--PLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1161
Cdd:PRK10535 103 AAQNVEvP-------AVYAGLERKQRLLRAQELlqRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1162 DT---ETDLLIQETIREafADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEfDTPS 1213
Cdd:PRK10535 176 DShsgEEVMAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEIVR-NPPA 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
376-517 |
1.73e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.84 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQ---------QAWIL--NATLRDN 443
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPPyqrpinmmfQSYALfpHMTVEQN 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 444 ILFGKEYDEERYNSVLNSCClrpdlAILPSSDLTEIGERGAN-LSGGQRQRISLARALYSDRSIYILDDPLSALD 517
Cdd:PRK11607 112 IAFGLKQDKLPKAEIASRVN-----EMLGLVHMQEFAKRKPHqLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
379-573 |
1.95e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.49 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWIL-NATLRDN 443
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGYLPQEASIFrKLTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 IL-------FGKEYDEERYNSVLNscclrpDLailpssDLTEIGE-RGANLSGGQRQRISLARALYSDRSIYILD----- 510
Cdd:COG1137 99 ILavlelrkLSKKEREERLEELLE------EF------GITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDepfag 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 511 -DPLSALDahvgnhifnsaIRK---HLKSK--TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEELMN 573
Cdd:COG1137 167 vDPIAVAD-----------IQKiirHLKERgiGVLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
993-1227 |
2.05e-07 |
|
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: 53.50 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 993 EVTFENAEMRYrENLPlVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLS 1072
Cdd:cd03296 2 SIEVRNVSKRF-GDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1073 IIPQEPVLFSG-TVRSNL-----------DPFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLC 1140
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1141 IARALLRHCKILILDEATAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLS 1217
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
250
....*....|
gi 1622900605 1218 NDSSRFYAMF 1227
Cdd:cd03296 227 HPASPFVYSF 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
992-1233 |
2.61e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 992 GEVTFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSL------------GMALFRLVELSGGCIKIDG 1056
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMiqltngliisetGQTIVGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1057 VRisdiglaDLRSKLSIIPQEP--VLFSGTVRSNL--DPFNQYTEDQiwDALERTHMKECIAQLPlklESEVMENGDNFS 1132
Cdd:PRK13645 85 VK-------RLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENKQ--EAYKKVPELLKLVQLP---EDYVKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1133 VGERQLLCIARALLRHCKILILDEATAAMDT--ETDL--LIQETIREAFADCTMLTiaHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgEEDFinLFERLNKEYKKRIIMVT--HNMDQVLRiADEVIVMHEGKVI 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1622900605 1208 EFDTPSVLLSN---------DSSRFYAMFAAAENK 1233
Cdd:PRK13645 231 SIGSPFEIFSNqelltkieiDPPKLYQLMYKLKNK 265
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
366-564 |
2.66e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.86 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 366 KHIHLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGqmtLLEGSiaiSGTFAYVAQQAWILN----ATLR 441
Cdd:PRK10584 14 KSVGQGEHELS-ILTGVELVVKRGETIALIGESGSGKSTLLAILAG---LDDGS---SGEVSLVGQPLHQMDeearAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 -DNILFgkeydeerynsVLNSCCLRPDLAILPSSDLTEI----------------------GER----GANLSGGQRQRI 494
Cdd:PRK10584 87 aKHVGF-----------VFQSFMLIPTLNALENVELPALlrgessrqsrngakalleqlglGKRldhlPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 495 SLARALYSDRSIYILDDPLSALDAHVGNHIFN---SAIRKHlkSKTVLFVTHQLQYLVDCDEVIFMKEGCITE 564
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADllfSLNREH--GTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
939-1188 |
2.86e-07 |
|
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: 54.75 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 939 QLTGlfqFTVRLASetearFTSV-ERIN--HYIKTLSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYrENLPLV----- 1010
Cdd:TIGR00954 395 RLAG---FTARVDT-----LLQVlDDVKsgNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKF-ENIPLVtpngd 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 --LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLVelsGGCIKIDGVRISdiglADLRSKLSIIPQEPVLFSGTVRsn 1088
Cdd:TIGR00954 466 vlIESLSFEVPSGNNLLICGPNGCGKSSL----FRIL---GELWPVYGGRLT----KPAKGKLFYVPQRPYMTLGTLR-- 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 ldpfnqyteDQIW--DALERTHMK-------ECIAQLpLKLESEVMENG---------DNFSVGERQLLCIARALLRHCK 1150
Cdd:TIGR00954 533 ---------DQIIypDSSEDMKRRglsdkdlEQILDN-VQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQ 602
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622900605 1151 ILILDEATAAMDTETDLLIQETIREafADCTMLTIAHR 1188
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1011-1226 |
3.37e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmaLFRLVEL--SGGCIKIDGVRISDIGLADL---RSKLSiiPQEPVLFsgtv 1085
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTL---LARMAGLlpGSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 rsNLDPFnQY---------TEDQIWDALERthmkecIAQLpLKLESEVMENGDNFSVGERQ-------LLCIARALLRHC 1149
Cdd:PRK03695 83 --AMPVF-QYltlhqpdktRTEAVASALNE------VAEA-LGLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1150 KILILDEATAAMD----TETDLLIQETIREAFAdctMLTIAHRL-HTVLGSDRIMVLAQGQVVEFDTP-SVLLSNDSSRF 1223
Cdd:PRK03695 153 QLLLLDEPMNSLDvaqqAALDRLLSELCQQGIA---VVMSSHDLnHTLRHADRVWLLKQGKLLASGRRdEVLTPENLAQV 229
|
...
gi 1622900605 1224 YAM 1226
Cdd:PRK03695 230 FGV 232
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
379-555 |
3.66e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.00 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQ--MTLLEGSIAISGTFAYVAQQAWI----------LNATLRDN--- 443
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPalARRLHLKKEQPGNHDRIEGLEHIdkvividqspIGRTPRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ---------ILF-----GKEYDEE----RYNS-----VLNSCC------------LRPDLAILPSSDLTEI--GERGANL 486
Cdd:cd03271 91 ytgvfdeirELFcevckGKRYNREtlevRYKGksiadVLDMTVeealeffenipkIARKLQTLCDVGLGYIklGQPATTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 487 SGGQRQRISLARALySDRS----IYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVI 555
Cdd:cd03271 171 SGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
371-560 |
4.14e-07 |
|
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: 51.86 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 371 GHLRLqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT--LLEGSIAISG-----TFA----YVAQQ-AWILNA 438
Cdd:cd03232 18 GKRQL---LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGrpldkNFQrstgYVEQQdVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNILFgkeydeerynsvlnSCCLRpdlailpssdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDA 518
Cdd:cd03232 95 TVREALRF--------------SALLR-------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900605 519 HVGNHIFNsAIRKHLKS-KTVLFVTHQ-----LQYLvdcDEVIFMKEG 560
Cdd:cd03232 142 QAAYNIVR-FLKKLADSgQAILCTIHQpsasiFEKF---DRLLLLKRG 185
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
714-925 |
4.44e-07 |
|
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: 53.18 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 714 YYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEM 793
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 794 FIQNVILVFFCVGMIAGVFPWF-LVAVGPLVILFsvlhIVSRVLIRELKRLDNITQSPFlSHITSSIQ----GLATIHAY 868
Cdd:cd18541 121 LVDALFLGVLVLVMMFTISPKLtLIALLPLPLLA----LLVYRLGKKIHKRFRKVQEAF-SDLSDRVQesfsGIRVIKAF 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 869 NKGQEFLHRYQELLDDNQApfflftcamRWLA-VRLD---LISIALITTTGLMIVL-------MHGQI 925
Cdd:cd18541 196 VQEEAEIERFDKLNEEYVE---------KNLRlARVDalfFPLIGLLIGLSFLIVLwyggrlvIRGTI 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
486-571 |
5.19e-07 |
|
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: 53.92 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 486 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKHLKSKT---VLFVTHQLQyLVD--CDEVIFMKEG 560
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQIL--DLLKDLQRELgmaLLLITHDLG-VVRrfADRVAVMRQG 233
|
90
....*....|.
gi 1622900605 561 CITERGTHEEL 571
Cdd:COG4172 234 EIVEQGPTAEL 244
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
658-923 |
5.28e-07 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 52.87 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 658 LAFLVIMALFMLNVGSTafstwwLSYWIKQGSGNttvtrGNETSVSdsmkdnprmQYYASIYALSmAVMLILKAIRgVVF 737
Cdd:cd18575 2 LIALLIAAAATLALGQG------LRLLIDQGFAA-----GNTALLN---------RAFLLLLAVA-LVLALASALR-FYL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 738 VkGTL--RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAgVFPWF 815
Cdd:cd18575 60 V-SWLgeRVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLF-ITSPK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 816 LVAVGPLVILFSVLHIVsrVLIRELKRLDNITQSPFL---SHITSSIQGLATIHAYNKGQEFLHRYQELLDDNqapfflF 892
Cdd:cd18575 138 LTLLVLLVIPLVVLPII--LFGRRVRRLSRASQDRLAdlsAFAEETLSAIKTVQAFTREDAERQRFATAVEAA------F 209
|
250 260 270
....*....|....*....|....*....|..
gi 1622900605 893 TCAMRWLAVRLDLISIA-LITTTGLMIVLMHG 923
Cdd:cd18575 210 AAALRRIRARALLTALViFLVFGAIVFVLWLG 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1008-1208 |
5.28e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.39 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1008 PLVlKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRL----VELSGGCIKIDGVRISdigLADLRSKL-SIIPQEPvlfs 1082
Cdd:PRK10418 17 PLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVA---PCALRGRKiATIMQNP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1083 gtvRSNLDPFNQYtedqiwdaleRTHMKECI---------AQLPLKLESEVMENGD--------NFSVGERQLLCIARAL 1145
Cdd:PRK10418 89 ---RSAFNPLHTM----------HTHARETClalgkpaddATLTAALEAVGLENAArvlklypfEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1146 LRHCKILILDEATaamdTETDLLIQETIREAFADCT------MLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:PRK10418 156 LCEAPFIIADEPT----TDLDVVAQARILDLLESIVqkralgMLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1009-1218 |
5.29e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.30 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1009 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISdiGLadlrsklsiiPQEPVLFSGTVRS- 1087
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GL----------PGHQIARMGVVRTf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1088 -NLDPFNQYTedqiwdALE------RTHMKECIAQLPLKL------ESEVMENG-----------------DNFSVGERQ 1137
Cdd:PRK11300 87 qHVRLFREMT------VIEnllvaqHQQLKTGLFSGLLKTpafrraESEALDRAatwlervgllehanrqaGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1138 LLCIARALLRHCKILILDEATAAMD-TETDLLiQETI---REAFaDCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTP 1212
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNpKETKEL-DELIaelRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTP 238
|
....*.
gi 1622900605 1213 SVLLSN 1218
Cdd:PRK11300 239 EEIRNN 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1014-1207 |
5.40e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIP----QEPVLFSGTVRSN 1088
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 LD--------PFNQYTeDQIWdalERTHMKECIAQLPLK---LESEVMengdNFSVGERQLLCIARALLRHCKILILDEA 1157
Cdd:PRK11288 352 INisarrhhlRAGCLI-NNRW---EAENADRFIRSLNIKtpsREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1158 TAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQVV 1207
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
379-571 |
6.29e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.15 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAI-----LGQMTLLEGSIAISGTFAY--------VAQQAWIL--------N 437
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYspdvdpieVRREVGMVfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 438 ATLRDNILFG----------KEYDEerynsvlnscclRPDLAILPSSDLTEIGER----GANLSGGQRQRISLARALYSD 503
Cdd:PRK14267 100 LTIYDNVAIGvklnglvkskKELDE------------RVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 504 RSIYILDDPLSALDAhVGNHIFNSAIRKHLKSKTVLFVTHQ-LQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK14267 168 PKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
377-560 |
6.85e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQAWILNA-TLR 441
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGK------------EYDEERynSVLNSCCLRPDLAIlpssdltEIGERGANLSGGQRQRISLARALYSDRSIYIL 509
Cdd:PRK09700 99 ENLYIGRhltkkvcgvniiDWREMR--VRAAMMLLRVGLKV-------DLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 510 DDPLSALDAHVGNHIFnsAIRKHLKS--KTVLFVTHQLQYLVD-CDEVIFMKEG 560
Cdd:PRK09700 170 DEPTSSLTNKEVDYLF--LIMNQLRKegTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
376-555 |
6.92e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.04 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTF--AYVAQQAWiLNATLRDNIlfgkeydeE 453
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLY-LDTTLPLTV--------N 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 454 RYNSvlnsccLRPDLA---ILPSSDLTE----IGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALD--AHVGNHI 524
Cdd:PRK09544 88 RFLR------LRPGTKkedILPALKRVQaghlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvnGQVALYD 161
|
170 180 190
....*....|....*....|....*....|..
gi 1622900605 525 FNSAIRKHLKSkTVLFVTHQLQY-LVDCDEVI 555
Cdd:PRK09544 162 LIDQLRRELDC-AVLMVSHDLHLvMAKTDEVL 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
355-550 |
7.67e-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: 53.25 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 355 DERPSPEEEEGKHIhLGHLRLQRTLHSIDLEIQEGKL-----VGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYV 429
Cdd:COG1245 328 EVHAPRREKEEETL-VEYPDLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 430 AQqaWILN-------ATLRDNIlfGKEYDEERYNSVLnsccLRPdLAI--LPSSDLTEigerganLSGGQRQRISLARAL 500
Cdd:COG1245 407 PQ--YISPdydgtveEFLRSAN--TDDFGSSYYKTEI----IKP-LGLekLLDKNVKD-------LSGGELQRVAIAACL 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 501 YSDRSIYILDDPLSALDA----HVGnhifnSAIRKHLKS--KTVLFVTHQLqYLVD 550
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVeqrlAVA-----KAIRRFAENrgKTAMVVDHDI-YLID 520
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
701-884 |
7.81e-07 |
|
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: 52.13 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 701 SVSDSMKDNPRMQYYASIYALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRF 776
Cdd:cd18573 25 VASKESGDIEIFGLSLKTFALALLGVFVVGAAanfgRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 777 SKDMDEVdvrlpfqAEMFIQNV-------ILVFFCVGMIAGVFP---WFLVAVGPLVILFSVlhivsrVLIRELKRLDNI 846
Cdd:cd18573 105 SSDTSVV-------GKSLTQNLsdglrslVSGVGGIGMMLYISPkltLVMLLVVPPIAVGAV------FYGRYVRKLSKQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622900605 847 TQSPfLSHITSS----IQGLATIHAYNKGQEFLHRYQELLDD 884
Cdd:cd18573 172 VQDA-LADATKVaeerLSNIRTVRAFAAERKEVERYAKKVDE 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
377-571 |
8.68e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSID---LEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQQAWI----------------L 436
Cdd:PRK15079 32 KTLKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdLLGMKDDEWRavrsdiqmifqdplasL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 437 NA--TLRDNIL---------FGKEYDEERYNSVLNSCCLRPDLailpssdlteIGERGANLSGGQRQRISLARALYSDRS 505
Cdd:PRK15079 112 NPrmTIGEIIAeplrtyhpkLSRQEVKDRVKAMMLKVGLLPNL----------INRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 506 IYILDDPLSALDAHVGNHIFNsaIRKHLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGCITERGTHEEL 571
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVN--LLQQLQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
377-554 |
1.39e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSL---ISAILGQMTLlEGSIAISG---TFAYV--AQQAWIL----------NA 438
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTY-EGEIIFEGeelQASNIrdTERAGIAiihqelalvkEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNILFGKE--------YDE--ERYNSVLNscclRPDLAILPSsdlTEIGergaNLSGGQRQRISLARALYSDRSIYI 508
Cdd:PRK13549 98 SVLENIFLGNEitpggimdYDAmyLRAQKLLA----QLKLDINPA---TPVG----NLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900605 509 LDDPLSALDAHVGNHIFNsaIRKHLKSKTV--LFVTHQLqylvdcDEV 554
Cdd:PRK13549 167 LDEPTASLTESETAVLLD--IIRDLKAHGIacIYISHKL------NEV 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1010-1165 |
1.45e-06 |
|
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: 52.63 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcIKI-DGVRISDIGLADLRS--KLSIIPQEPVL-FSGTV 1085
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTL--------------LRImAGVDKDFNGEARPQPgiKVGYLPQEPQLdPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1086 RSN-----------LDPFNQ----YTE-DQIWDAL--ERTHMKECIAQLPL-KLESEV---ME-----NGD----NFSVG 1134
Cdd:TIGR03719 86 RENveegvaeikdaLDRFNEisakYAEpDADFDKLaaEQAELQEIIDAADAwDLDSQLeiaMDalrcpPWDadvtKLSGG 165
|
170 180 190
....*....|....*....|....*....|.
gi 1622900605 1135 ERQLLCIARALLRHCKILILDEATAAMDTET 1165
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
362-569 |
1.60e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.22 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 362 EEEGKHIhlghlrlqrtLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQM--TLLEGSIAISGTFayvaqqawILNAT 439
Cdd:cd03217 9 SVGGKEI----------LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGED--------ITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 440 L----RDNILFGKEYDEErYNSVLNSCCLRpdlailpssdltEIGErgaNLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:cd03217 71 PeeraRLGIFLAFQYPPE-IPGVKNADFLR------------YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 516 LDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYL--VDCDEVIFMKEGCITERGTHE 569
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
369-519 |
1.85e-06 |
|
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: 50.51 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 369 HLGHLRLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAIS---------------------GTFA 427
Cdd:COG4778 18 LQGGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggwvdlaqaspreilalrrRTIG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 428 YVAQqawILNATLRDNIL-----------FGKEYDEERYNSVLNSCCLRPDLAILPSsdlteigergANLSGGQRQRISL 496
Cdd:COG4778 97 YVSQ---FLRVIPRVSALdvvaepllergVDREEARARARELLARLNLPERLWDLPP----------ATFSGGEQQRVNI 163
|
170 180
....*....|....*....|...
gi 1622900605 497 ARALYSDRSIYILDDPLSALDAH 519
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAA 186
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
382-542 |
1.93e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAwilnatlrdnilfgkeydeeRYNSVLNS 461
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--------------------RFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 462 C-CLRPDLAIL-----------------PSSDLTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPLSALD 517
Cdd:PRK13543 90 LpGLKADLSTLenlhflcglhgrrakqmPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*
gi 1622900605 518 AHvGNHIFNSAIRKHLKSKTVLFVT 542
Cdd:PRK13543 170 LE-GITLVNRMISAHLRGGGAALVT 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1011-1208 |
2.04e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLgMALfrlveLSG--------GCIKIDG--VRISDIGLADlRSKLSIIPQE--- 1077
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL-MKV-----LSGvyphgsyeGEILFDGevCRFKDIRDSE-ALGIVIIHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1078 -PVLfsgTVRSNLDPFNQYTEDQI--WDALERtHMKECIAQLPLKlesevmENGD----NFSVGERQLLCIARALLRHCK 1150
Cdd:NF040905 90 iPYL---SIAENIFLGNERAKRGVidWNETNR-RARELLAKVGLD------ESPDtlvtDIGVGKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1151 ILILDEATAAMDtETD---LLiqETIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQVVE 1208
Cdd:NF040905 160 LLILDEPTAALN-EEDsaaLL--DLLLELKAqGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
717-884 |
2.10e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 50.97 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 717 SIYALSMAVMLILKA----IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSkdmDEVDVRlpfqaE 792
Cdd:cd18555 42 NVLGIGILILFLLYGlfsfLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRAN---SNVYIR-----Q 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 793 MFIQNVI--------LVFFCVGMIagVFPWFLVAVgplVILFSVLHIVSRVL----IRELKRLDNITQSPFLSHITSSIQ 860
Cdd:cd18555 114 ILSNQVIsliidlllLVIYLIYML--YYSPLLTLI---VLLLGLLIVLLLLLtrkkIKKLNQEEIVAQTKVQSYLTETLY 188
|
170 180
....*....|....*....|....
gi 1622900605 861 GLATIHAYNKGQEFLHRYQELLDD 884
Cdd:cd18555 189 GIETIKSLGSEKNIYKKWENLFKK 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1011-1205 |
2.44e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS--------DIGLADLRSKLSIIPQEPV--- 1079
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAGIGIIHQELNLIPQLTIaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1080 LFSGtvRSNLDPFNQYTEDQIW---DALerthmkecIAQLPLKLESEVMENgdNFSVGERQLLCIARALLRHCKILILDE 1156
Cdd:PRK10762 100 IFLG--REFVNRFGRIDWKKMYaeaDKL--------LARLNLRFSSDKLVG--ELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1157 ATAAM-DTETDLLIQeTIREAFA-DCTMLTIAHRLHTVLG-SDRIMVLAQGQ 1205
Cdd:PRK10762 168 PTDALtDTETESLFR-VIRELKSqGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
380-571 |
2.65e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 380 HSIDLEIQEGKLVGICGSVGSGKTSLISAILGQM----TLLEGSIAISGTFAYVAQQAWILNATLRDNilfgkeyDEERY 455
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGKPVAPCALRGRKIATIMQN-------PRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 456 NSVLN-------SCCLR---PDLAILPSSdLTEIG----ERGANL-----SGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:PRK10418 93 NPLHTmhthareTCLALgkpADDATLTAA-LEAVGlenaARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 517 DAHVGNHIFN---SAIRKHlkSKTVLFVTHQLQYLVDC-DEVIFMKEGCITERGTHEEL 571
Cdd:PRK10418 172 DVVAQARILDlleSIVQKR--ALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
379-563 |
2.70e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQ----QAWILNATL 440
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEdrlgRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 441 RDNILFGkEYDEERYNS--VLNSCCLRpDLA--------ILPSSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILD 510
Cdd:COG3845 354 AENLILG-RYRRPPFSRggFLDRKAIR-AFAeelieefdVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 511 DPLSALDahVGNhIfnSAIRKHL-----KSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 563
Cdd:COG3845 428 QPTRGLD--VGA-I--EFIHQRLlelrdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1010-1219 |
2.71e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.57 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEP--VLFSGTVRS 1087
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1088 NL--DPFN-----QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAA 1160
Cdd:PRK13652 99 DIafGPINlgldeETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 1161 MDTETdllIQETIR--EAFADCTMLTIAHRLHTV----LGSDRIMVLAQGQVVEFDTPSVLLSND 1219
Cdd:PRK13652 168 LDPQG---VKELIDflNDLPETYGMTVIFSTHQLdlvpEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1010-1175 |
2.80e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.01 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgMALFRLVEL-SGGCIKIDG------VRISDIGLADLRSKLSIIPQE----P 1078
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSL-LRVLNLLEMpRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1079 VLfsgTVRSNL--DPFN------QYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCK 1150
Cdd:PRK11124 96 HL---TVQQNLieAPCRvlglskDQALARAEKLLERLRLKPYADRFPLHL-----------SGGQQQRVAIARALMMEPQ 161
|
170 180
....*....|....*....|....*
gi 1622900605 1151 ILILDEATAAMDTETDLLIQETIRE 1175
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRE 186
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1010-1208 |
2.85e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI---GLADLRSK--------LSIIP--- 1075
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1076 -QEPVLFSGTVRSNLDpfnQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILIL 1154
Cdd:PRK10584 105 aLENVELPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900605 1155 DEATAAMDTET-----DLLIQETIREAfadCTMLTIAHRLHTVLGSDRIMVLAQGQVVE 1208
Cdd:PRK10584 171 DEPTGNLDRQTgdkiaDLLFSLNREHG---TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1014-1208 |
3.12e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADL---------RSKLSIIPQEP------ 1078
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdglrm 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1079 -VLFSGTVRSNLDPF--NQYTE--DQIWDALERTHMKEC-IAQLPlklesevmengDNFSVGERQLLCIARALLRHCKIL 1152
Cdd:PRK11701 105 qVSAGGNIGERLMAVgaRHYGDirATAGDWLERVEIDAArIDDLP-----------TTFSGGMQQRLQIARNLVTHPRLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 1153 ILDEATAAMDTET-----DLLiQETIREafADCTMLTIAHRLHTV-LGSDRIMVLAQGQVVE 1208
Cdd:PRK11701 174 FMDEPTGGLDVSVqarllDLL-RGLVRE--LGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1011-1206 |
4.32e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDI--------GLA---DLRSKLSIIPQEPV 1079
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaneainhGFAlvtEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1080 LFSGTVrSNLDPFNQYtedqiWDALERTHMKE----CIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILD 1155
Cdd:PRK10982 344 GFNSLI-SNIRNYKNK-----VGLLDNSRMKSdtqwVIDSMRVKTPGHRTQIG-SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1156 EATAAMDTETDLLIQETIRE-AFADCTMLTIAHRLHTVLG-SDRIMVLAQGQV 1206
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
374-560 |
4.33e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 374 RLQrTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT--LLEGSIAISG------TFAYVA---QQAWILN--ATL 440
Cdd:PLN03140 892 RLQ-LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkkqeTFARISgycEQNDIHSpqVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 441 RDNILFG------KEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGanLSGGQRQRISLARALYSDRSIYILDDPLS 514
Cdd:PLN03140 971 RESLIYSaflrlpKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900605 515 ALDAHVGNhIFNSAIRKHLKS-KTVLFVTHQ--LQYLVDCDEVIFMKEG 560
Cdd:PLN03140 1049 GLDARAAA-IVMRTVRNTVDTgRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
379-585 |
4.56e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVA-------QQAWILNATLRdNILFG--KE 449
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAissglngQLTGIENIELK-GLMMGltKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 450 YDEErynsvlnscclrpdlaILPSS-DLTEIG----ERGANLSGGQRQRISLARALYSDRSIYILDDPLSaldahVGNHI 524
Cdd:PRK13545 119 KIKE----------------IIPEIiEFADIGkfiyQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS-----VGDQT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622900605 525 FNSAIRKHL-----KSKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNL 585
Cdd:PRK13545 178 FTKKCLDKMnefkeQGKTIFFISHSLsQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQM 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
376-544 |
4.72e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT------------FAYVAQQAWI-LNATLRD 442
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlctyqkqLCFVGHRSGInPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILFGKEYDEEryNSVLNSCCLRPDLAILpssdlteIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 522
Cdd:PRK13540 94 NCLYDIHFSPG--AVGITELCRLFSLEHL-------IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|...
gi 1622900605 523 HIFnSAIRKH-LKSKTVLFVTHQ 544
Cdd:PRK13540 165 TII-TKIQEHrAKGGAVLLTSHQ 186
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1026-1210 |
5.10e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1026 IVGRTGSGKSSLGMALFRLVELSGGCIKIDGvRIsdigLADLRSKLSIIP---------QEPVLFSG-TVRSNL----DP 1091
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNG-RV----LFDAEKGICLPPekrrigyvfQDARLFPHyKVRGNLrygmAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1092 FNQYTEDQIWDALERTHMkecIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDT--ETDLL- 1168
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPL---LDRYPGSL-----------SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprKRELLp 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622900605 1169 -IQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFD 1210
Cdd:PRK11144 170 yLERLARE--INIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
386-560 |
5.77e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 386 IQEGKLVGICGSVGSGKTSLISAILGQMT------------------------------LLEGSIAISGTFAYVAQQAWI 435
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIpnlgdyeeepswdevlkrfrgtelqnyfkkLYNGEIKVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 436 LNATLRDnILfgKEYDE----ERYNSVLNscclrpdlailpssdLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILD 510
Cdd:PRK13409 176 FKGKVRE-LL--KKVDErgklDEVVERLG---------------LENILDRDiSELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 511 DPLSALDahVGNHIfNSA--IRKHLKSKTVLFVTHQ---LQYLVDCDEVIFMKEG 560
Cdd:PRK13409 238 EPTSYLD--IRQRL-NVArlIRELAEGKYVLVVEHDlavLDYLADNVHIAYGEPG 289
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
724-964 |
6.03e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 49.40 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 724 AVMLILKAIRGVVFV-------KGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVdVRLPFQAEMFIQ 796
Cdd:cd18543 43 LLLLALGVAEAVLSFlrrylagRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 797 NVILVFFCVGMIAGVFPWF-LVAVGPLVILFsvlhIVSRVLIRELKRLDNITQS---PFLSHITSSIQGLATIHAYNKGQ 872
Cdd:cd18543 122 NLLTLVVGLVVMLVLSPPLaLVALASLPPLV----LVARRFRRRYFPASRRAQDqagDLATVVEESVTGIRVVKAFGRER 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 873 EFLHRYQELLDDnqapffLFTCAMRwlAVRLDLISIALITT---TGLMIVL-------MHGQIPpayAG--LA-ISYAVQ 939
Cdd:cd18543 198 RELDRFEAAARR------LRATRLR--AARLRARFWPLLEAlpeLGLAAVLalggwlvANGSLT---LGtlVAfSAYLTM 266
|
250 260
....*....|....*....|....*
gi 1622900605 940 LTGLFQFTVRLASETEARFTSVERI 964
Cdd:cd18543 267 LVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
376-555 |
6.27e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRTLHSIDLEIQEGKLVGICGSVGSGKTSL----------------ISA----ILGQM-----TLLEG-SIAIS------ 423
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAyarqFLGQMdkpdvDSIEGlSPAIAidqktt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 424 -----GTFAYVAQqawiLNATLRdnILFGKEYDEERYNSvlnscclrpdlailpssdLTEIG------ERGAN-LSGGQR 491
Cdd:cd03270 88 srnprSTVGTVTE----IYDYLR--LLFARVGIRERLGF------------------LVDVGlgyltlSRSAPtLSGGEA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 492 QRISLARALYSDRS--IYILDDPLSALDAHvGNHIFNSAIrKHLKSK--TVLFVTHQLQYLVDCDEVI 555
Cdd:cd03270 144 QRIRLATQIGSGLTgvLYVLDEPSIGLHPR-DNDRLIETL-KRLRDLgnTVLVVEHDEDTIRAADHVI 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1013-1224 |
6.65e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1013 KVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIsDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPF 1092
Cdd:TIGR01257 948 RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILF 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1093 NQYTEDQIWD--ALERTHMKECIAqlplkLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQ 1170
Cdd:TIGR01257 1027 YAQLKGRSWEeaQLEMEAMLEDTG-----LHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 1171 ETIREAFADCTMLTIAHRLHT--VLGsDRIMVLAQGQVVEFDTPSVLLSNDSSRFY 1224
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEadLLG-DRIAIISQGRLYCSGTPLFLKNCFGTGFY 1156
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
377-577 |
7.96e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNA---------------TLR 441
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgvaiiyqelhlvpemTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGK------EYDEERYNSVLNSCCLRPDLAILPSSDLteigergANLSGGQRQRISLARALYSDRSIYILDDPLSA 515
Cdd:PRK11288 98 ENLYLGQlphkggIVNRRLLNYEAREQLEHLGVDIDPDTPL-------KYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622900605 516 LDAHVGNHIFnSAIRKhLKS--KTVLFVTHQLQYLVD-CDEVIFMKEGCITErgTHEELMNLNGD 577
Cdd:PRK11288 171 LSAREIEQLF-RVIRE-LRAegRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDMAQVDRD 231
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
689-884 |
8.16e-06 |
|
Six-transmembrane helical domain 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: 350002 [Multi-domain] Cd Length: 312 Bit Score: 49.20 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 689 SGNTTVTRGNETSVSDSM----KDNPRMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFF 764
Cdd:cd18558 31 NGGMTNITGNSSGLNSSAgpfeKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 765 DTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF--FCVGMIAGvfpW----FLVAVGPLVILFSVL--HIVSRVL 836
Cdd:cd18558 111 DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGtgFIIGFIRG---WkltlVILAISPVLGLSAVVwaKILSGFT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622900605 837 IRELKRLDNITQSPflshiTSSIQGLATIHAYNKGQEFLHRYQELLDD 884
Cdd:cd18558 188 DKEKKAYAKAGAVA-----EEVLEAFRTVIAFGGQQKEETRYAQNLEI 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
373-571 |
8.25e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.76 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 373 LRLQ----RTLHSIDLEIQEGKLVGICGSVGSGKTSLISaILGQMTLLEGSIAISGTFAYVAQQAW-------------- 434
Cdd:PRK14247 9 LKVSfgqvEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEARVSGEVYLDGQDIFkmdvielrrrvqmv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 435 ------ILNATLRDNILFG---------KEYDEERYNSVLNSCCLRPDLAilpssdlTEIGERGANLSGGQRQRISLARA 499
Cdd:PRK14247 88 fqipnpIPNLSIFENVALGlklnrlvksKKELQERVRWALEKAQLWDEVK-------DRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 500 LYSDRSIYILDDPLSALDAHvgnhifNSAIRKHL-----KSKTVLFVTH-QLQYLVDCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPE------NTAKIESLflelkKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
481-556 |
8.29e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.01 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 481 ERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAhvgnhIFNSAIR---KHLKSK-TVLFVTHQLQ---------- 546
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP-----ISTLRIEelmHELKEQyTIIIVTHNMQqaarvsdmta 221
|
90 100
....*....|....*....|....*.
gi 1622900605 547 --------------YLVDCD--EVIF 556
Cdd:PRK14243 222 ffnveltegggrygYLVEFDrtEKIF 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
486-571 |
8.77e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 486 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN-SAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCIT 563
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAV 248
|
....*...
gi 1622900605 564 ERGTHEEL 571
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
379-574 |
1.03e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQ--------MTLLEG--------SIAISGTFAYVA----QQAWILNA 438
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygrnisgTVFKDGkevdvstvSDAIDAGLAYVTedrkGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 439 TLRDNI----LFG----------KEYDE-ERYnsvlnscclRPDLAILPSSDLTEIGergaNLSGGQRQRISLARALYSD 503
Cdd:NF040905 356 DIKRNItlanLGKvsrrgvidenEEIKVaEEY---------RKKMNIKTPSVFQKVG----NLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 504 RSIYILDDPLSALDahVGN--HIFnSAIRKHLKS-KTVLFVTHQLQYLVD-CDEVIFMKEGCIT-----ERGTHEELMNL 574
Cdd:NF040905 423 PDVLILDEPTRGID--VGAkyEIY-TIINELAAEgKGVIVISSELPELLGmCDRIYVMNEGRITgelprEEASQERIMRL 499
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
990-1207 |
1.14e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 48.73 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 990 QEGEVTFENAEMRYReNLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDiglADLRS 1069
Cdd:PRK15056 3 QQAGIVVNDVTVTWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1070 KLSIIPQE-------PVLFSGTVRSN-------LDPFNQYTEDQIWDALERTHMkeciaqlplkLESEVMENGDnFSVGE 1135
Cdd:PRK15056 79 LVAYVPQSeevdwsfPVLVEDVVMMGryghmgwLRRAKKRDRQIVTAALARVDM----------VEFRHRQIGE-LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1136 RQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFAD-CTMLTIAHRLHTVLGSDRIMVLAQGQVV 1207
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
487-571 |
1.29e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.95 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 487 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHI----------FNSAIrkhlksktvLFVTHQLQYLVD-CDEVI 555
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQImtllnelkreFNTAI---------IMITHDLGVVAGiCDKVL 233
|
90
....*....|....*.
gi 1622900605 556 FMKEGCITERGTHEEL 571
Cdd:PRK09473 234 VMYAGRTMEYGNARDV 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
367-517 |
1.37e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 367 HIHLGHLRLQ--RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISgtFAYVA-----QQAWILNAT 439
Cdd:PRK10938 5 QISQGTFRLSdtKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ--FSHITrlsfeQLQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 440 LRDN---ILFGKEYDEERYNSVL-------NSCCLRpdLA-ILPSSDLteIGERGANLSGGQRQRISLARALYSDRSIYI 508
Cdd:PRK10938 83 WQRNntdMLSPGEDDTGRTTAEIiqdevkdPARCEQ--LAqQFGITAL--LDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
....*....
gi 1622900605 509 LDDPLSALD 517
Cdd:PRK10938 159 LDEPFDGLD 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1009-1214 |
1.47e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1009 LVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLR-SKLSIIPQEP-----VLfS 1082
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRlgrglVP-D 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1083 GTVRSNLDpFNQYTEDQI-------WDALeRTHMKECIAQLPLK---LESEVmengDNFSVGERQLLCIARALLRHCKIL 1152
Cdd:COG3845 351 MSVAENLI-LGRYRRPPFsrggfldRKAI-RAFAEELIEEFDVRtpgPDTPA----RSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622900605 1153 I-------LDEATAAMdtetdllIQETIREAfAD--CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFDTPSV 1214
Cdd:COG3845 425 IaaqptrgLDVGAIEF-------IHQRLLEL-RDagAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEA 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
377-560 |
1.49e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT--------------FAYVAQQA-WILNATLR 441
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 442 DNILFGkeydeeRYNS----VLNSCCLRPDLAILPSSDL-TEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:PRK10982 92 DNMWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIdIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622900605 517 DAHVGNHIFnSAIRKhLKSK--TVLFVTHQLQYLVD-CDEVIFMKEG 560
Cdd:PRK10982 166 TEKEVNHLF-TIIRK-LKERgcGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
382-545 |
1.54e-05 |
|
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: 49.63 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-----TFAYVAQ------QAWIL--NATLRDNILF-- 446
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietNLDAVRQslgmcpQHNILfhHLTVAEHILFya 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 447 ---GKEYDEERYNSVlnscclrpdlAILPSSDLT-EIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGN 522
Cdd:TIGR01257 1029 qlkGRSWEEAQLEME----------AMLEDTGLHhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180
....*....|....*....|...
gi 1622900605 523 HIFNsAIRKHLKSKTVLFVTHQL 545
Cdd:TIGR01257 1099 SIWD-LLLKYRSGRTIIMSTHHM 1120
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
385-550 |
1.69e-05 |
|
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: 46.80 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 385 EIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQAwilnatlrdnilfgkeydeerynsvlnscc 463
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQYI------------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 464 lrpdlailpssdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHLK--SKTVLFV 541
Cdd:cd03222 71 ---------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEegKKTALVV 128
|
170
....*....|..
gi 1622900605 542 THQL---QYLVD 550
Cdd:cd03222 129 EHDLavlDYLSD 140
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
486-573 |
1.83e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.78 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 486 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIfNSAIRKHLKSKTVLFVTHQL-QYLVDCDEVIFMKEGCITE 564
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVE 242
|
....*....
gi 1622900605 565 RGTHEELMN 573
Cdd:PRK14271 243 EGPTEQLFS 251
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
367-519 |
1.88e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 367 HIHLGHlRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMT--------LLEGSIAISGT--FAYVAQQAWIL 436
Cdd:PRK13547 6 HLHVAR-RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEplAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 437 NATL------------RDNILFGKeYDEERYNSVLN-------SCCL-RPDLAILPSSDLTeigergaNLSGGQRQRISL 496
Cdd:PRK13547 85 RAVLpqaaqpafafsaREIVLLGR-YPHARRAGALThrdgeiaWQALaLAGATALVGRDVT-------TLSGGELARVQF 156
|
170 180 190
....*....|....*....|....*....|...
gi 1622900605 497 ARAL---------YSDRSIYILDDPLSALD-AH 519
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDlAH 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
486-573 |
1.92e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 486 LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFnsAIRKHLKSK---TVLFVTHQLQYLVD-CDEVIFMKEGC 561
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIL--QLLRELQQElnmGLLFITHNLSIVRKlADRVAVMQNGR 234
|
90
....*....|..
gi 1622900605 562 ITERGTHEELMN 573
Cdd:PRK15134 235 CVEQNRAATLFS 246
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
364-571 |
2.99e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.15 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 364 EGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT-FAYVAQQawILNatLRD 442
Cdd:PRK13636 7 KVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRKG--LMK--LRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NI-LFGKEYDEERYN-SVLNSCCLRPDLAILPSSDLTEIGERGAN--------------LSGGQRQRISLARALYSDRSI 506
Cdd:PRK13636 83 SVgMVFQDPDNQLFSaSVYQDVSFGAVNLKLPEDEVRKRVDNALKrtgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 507 YILDDPLSALDAhVGnhifNSAIRKHLKSK------TVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK13636 163 LVLDEPTAGLDP-MG----VSEIMKLLVEMqkelglTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
379-571 |
3.23e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG-TFAYVAQQawILNATLRDNILFGKEYDEERYNS 457
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGePIKYDKKS--LLEVRKTVGIVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 458 VLNSCCLRPDLAILPSSD--------LTEIGERG------ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNH 523
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEvekrvkeaLKAVGMEGfenkppHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900605 524 IFNSAIRKHLKSKTVLFVTHQLQYL-VDCDEVIFMKEGCITERGTHEEL 571
Cdd:PRK13639 176 IMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
974-1206 |
3.43e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 46.98 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 974 EAPARIKNKAPspdwpqegeVTFENAEMRYRENLplVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGcik 1053
Cdd:PRK11247 2 MNTARLNQGTP---------LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1054 idGVRISDIGLADLRSKLSIIPQEPVLF-------------SGTVRsnldpfnqyteDQIWDALERTHMKECIAQLPLKL 1120
Cdd:PRK11247 68 --ELLAGTAPLAEAREDTRLMFQDARLLpwkkvidnvglglKGQWR-----------DAALQALAAVGLADRANEWPAAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1121 esevmengdnfSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETI-----REAFadcTMLTIAHRL-HTVLG 1194
Cdd:PRK11247 135 -----------SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIeslwqQHGF---TVLLVTHDVsEAVAM 200
|
250
....*....|..
gi 1622900605 1195 SDRIMVLAQGQV 1206
Cdd:PRK11247 201 ADRVLLIEEGKI 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
377-567 |
3.55e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.05 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 377 RTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGT---------------------FAYVAQQawI 435
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkvglvFQFPESQ--L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 436 LNATLRDNILFG-------KEYDEERynsvlnsccLRPDLAILPSSDltEIGERGA-NLSGGQRQRISLARALYSDRSIY 507
Cdd:PRK13649 99 FEETVLKDVAFGpqnfgvsQEEAEAL---------AREKLALVGISE--SLFEKNPfELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 508 ILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVD-CDEVIFMKEGCITERGT 567
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1014-1210 |
3.69e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1014 VSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD-LRSKLSIIPQEP----VLFSGTVRSN 1088
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 -----LDPFNqYTEDQIWDALERTHMKECIAQLPLKLESEVMENGdNFSVGERQLLCIARALLRHCKILILDEATAAMDT 1163
Cdd:PRK10762 351 msltaLRYFS-RAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1164 ETDLLIQETIREAFAD-CTMLTIAHRLHTVLG-SDRIMVLAQGQVV-EFD 1210
Cdd:PRK10762 429 GAKKEIYQLINQFKAEgLSIILVSSEMPEVLGmSDRILVMHEGRISgEFT 478
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1010-1165 |
3.93e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLG--MAlfrlvelsgGCIK-IDG-VRISDiGLadlrsKLSIIPQEPVL-FSGT 1084
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLriMA---------GVDKeFEGeARPAP-GI-----KVGYLPQEPQLdPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1085 VRSN-----------LDPFNQ----YTE-DQIWDAL--ERTHMKECIAQLPL-KLESEV---ME-----NGD----NFSV 1133
Cdd:PRK11819 87 VRENveegvaevkaaLDRFNEiyaaYAEpDADFDALaaEQGELQEIIDAADAwDLDSQLeiaMDalrcpPWDakvtKLSG 166
|
170 180 190
....*....|....*....|....*....|..
gi 1622900605 1134 GERQLLCIARALLRHCKILILDEATAAMDTET 1165
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
732-843 |
3.97e-05 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 46.92 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 732 IRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVF-FCVGMIag 810
Cdd:cd18784 55 IRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIgVIVFMF-- 132
|
90 100 110
....*....|....*....|....*....|...
gi 1622900605 811 VFPWFLVAVgpLVILFSVLHIVSRVLIRELKRL 843
Cdd:cd18784 133 KLSWQLSLV--TLIGLPLIAIVSKVYGDYYKKL 163
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1015-1164 |
4.61e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.95 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1015 SFTIKPKEKIGIVGRTGSGKSSlgmaLFRLveLSG------GCIKIDGVRISDIGlADLRSKLsiipqepvLFSG----- 1083
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTS----LLRI--LAGlarpdaGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 ----TVRSNLDpFNQ-----YTEDQIWDALERTHMKEcIAQLPLKlesevmengdNFSVGERQLLCIARALLRHCKILIL 1154
Cdd:PRK13538 86 ktelTALENLR-FYQrlhgpGDDEALWEALAQVGLAG-FEDVPVR----------QLSAGQQRRVALARLWLTRAPLWIL 153
|
170
....*....|
gi 1622900605 1155 DEATAAMDTE 1164
Cdd:PRK13538 154 DEPFTAIDKQ 163
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1129-1227 |
4.65e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.02 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1129 DNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIRE---AFaDCTMLTIAHRLHTVLG-SDRIMVLAQG 1204
Cdd:PRK11432 135 DQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRElqqQF-NITSLYVTHDQSEAFAvSDTVIVMNKG 213
|
90 100
....*....|....*....|...
gi 1622900605 1205 QVVEFDTPSVLLSNDSSRFYAMF 1227
Cdd:PRK11432 214 KIMQIGSPQELYRQPASRFMASF 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
379-554 |
4.88e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.33 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFA--YVAQQAWI--------L--NATLRDN 443
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvRIRspRDAIALGIgmvhqhfmLvpNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFGKEydeerynsvlNSCCLRPDLAILpSSDLTEIGER-G---------ANLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:COG3845 101 IVLGLE----------PTKGGRLDRKAA-RARIRELSERyGldvdpdakvEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622900605 514 SALDAHVGNHIFnsAIRKHLKS--KTVLFVTHQLqylvdcDEV 554
Cdd:COG3845 170 AVLTPQEADELF--EILRRLAAegKSIIFITHKL------REV 204
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
382-564 |
5.25e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.27 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGtfAYVAQQAW-----ILNATLRDNILF-------GKE 449
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG--KPVTAEQPedyrkLFSAVFTDFHLFdqllgpeGKP 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 450 YDEERYNSVLNSCCLRpdlailpsSDLTEIGERGAN--LSGGQRQRISLARALYSDRSIYILDDPLSALDAHVgNHIFNS 527
Cdd:PRK10522 420 ANPALVEKWLERLKMA--------HKLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQ 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622900605 528 AIRKHLKS--KTVLFVTHQLQYLVDCDEVIFMKEGCITE 564
Cdd:PRK10522 491 VLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
376-560 |
6.17e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 376 QRT-LHSIDLEIQEGKLVGICGSVGSGKTSLISAILG--QMTLLEGSIAISG---------TFAYVAQQAWIL-NATLRD 442
Cdd:PLN03211 80 ERTiLNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNrkptkqilkRTGFVTQDDILYpHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 443 NILF------GKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGanLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:PLN03211 160 TLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900605 517 DAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLV--DCDEVIFMKEG 560
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyqMFDSVLVLSEG 283
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1010-1162 |
8.88e-05 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 44.79 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLgmalFRLveLSGGCIKIDG-VRISDIGLADLRSKLsiipQEPVLFSG----- 1083
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTL----LRI--LAGLSPPLAGrVLLNGGPLDFQRDSI----ARGLLYLGhapgi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1084 ----TVRSNLDPFNQY-TEDQIWDALERTHMK----ECIAQLplklesevmengdnfSVGERQLLCIARALLRHCKILIL 1154
Cdd:cd03231 85 kttlSVLENLRFWHADhSDEQVEEALARVGLNgfedRPVAQL---------------SAGQQRRVALARLLLSGRPLWIL 149
|
....*...
gi 1622900605 1155 DEATAAMD 1162
Cdd:cd03231 150 DEPTTALD 157
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
379-560 |
1.05e-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: 44.56 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 379 LHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQmtlLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEydEERYNSV 458
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSE--EDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 459 LN-------SCCLRPDLAIlpssdlteigeRGanLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSaIR- 530
Cdd:cd03233 98 LTvretldfALRCKGNEFV-----------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC-IRt 163
|
170 180 190
....*....|....*....|....*....|...
gi 1622900605 531 --KHLKSKTVLFVTHQLQYLVDC-DEVIFMKEG 560
Cdd:cd03233 164 maDVLKTTTFVSLYQASDEIYDLfDKVLVLYEG 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1010-1165 |
1.13e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDgVRISDIGladlrSKLSIIPQEPVlfsgtvrsnL 1089
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFG-----REASLIDAIGR---------K 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 1090 DPFNQYTEdqiwdALERTHMKEciAQLPLKLESEvmengdnFSVGERQLLCIARALLRHCKILILDEATAAMDTET 1165
Cdd:COG2401 110 GDFKDAVE-----LLNAVGLSD--AVLWLRRFKE-------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
720-921 |
1.42e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents 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: 350010 [Multi-domain] Cd Length: 294 Bit Score: 45.27 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 720 ALSMAVML--ILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFsKDMDEVDVRLPFQAEMFIQN 797
Cdd:cd18566 47 GVVIAILLesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 798 VILVFFCVGMIAgVFPWFLVAVgPLVIL--FSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFL 875
Cdd:cd18566 126 LPFVLIFLGLIW-YLGGKLVLV-PLVLLglFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQML 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900605 876 HRYQELLDDnqapfflftCAMRWLAVRlDLISIALITTTGLMIVLM 921
Cdd:cd18566 204 RRYERLQAN---------AAYAGFKVA-KINAVAQTLGQLFSQVSM 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1010-1226 |
1.56e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.98 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNL 1089
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1090 DPFNQYTEDQI---W-----DALERTHMKECIAQLPLklesevmENGDNFSVGERQLLCIARALLRHCKILILDEATAAM 1161
Cdd:PRK10253 102 VARGRYPHQPLftrWrkedeEAVTKAMQATGITHLAD-------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 1162 DT--ETDL--LIQETIREafADCTMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSND-SSRFYAM 1226
Cdd:PRK10253 175 DIshQIDLleLLSELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAElIERIYGL 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1010-1234 |
1.81e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.07 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADlrSKLSIIPQEPVLFSG-TVRSN 1088
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1089 LD-----------PFNQYTEDQIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEA 1157
Cdd:PRK10851 95 IAfgltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1158 TAAMDTETDLLIQETIREAFADC--TMLTIAHRLHTVLG-SDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENKV 1234
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVNRL 243
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1011-1210 |
2.10e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.08 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLgmalfrlvelsggcIKIdgvrISDIgladlrsklsIIPQepvlfSGTVRSN-L 1089
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTT--------------IKM----LTGI----------LVPT-----SGEVRVLgY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1090 DPFNQYTE--DQI-----------WD--ALERTHMKECIAQLP-------LKLESEVMENGD-------NFSVGERQLLC 1140
Cdd:COG4586 85 VPFKRRKEfaRRIgvvfgqrsqlwWDlpAIDSFRLLKAIYRIPdaeykkrLDELVELLDLGElldtpvrQLSLGQRMRCE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 1141 IARALLRHCKILILDEATAAMdtetDLLIQETIREAFAD------CTMLTIAHRLHTV--LgSDRIMVLAQGQVVeFD 1210
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGL----DVVSKEAIREFLKEynrergTTILLTSHDMDDIeaL-CDRVIVIDHGRII-YD 236
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1020-1212 |
2.21e-04 |
|
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: 42.75 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1020 PKEKIGIVGRTGSGKSSLGMALFR-LVELSGGCIKIDGVRISDIGLADLRSKLsiipqepvlfsgtvrsnldpfnqyted 1098
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1099 qiwdalerthmkeciaqlplkleseVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIR---- 1174
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622900605 1175 ---EAFADCTMLTIAHRLHTVLgsDRIMVLAQGQVVEFDTP 1212
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
733-884 |
2.73e-04 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); 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: 350034 [Multi-domain] Cd Length: 289 Bit Score: 44.25 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 733 RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILvffCVGMIAgvf 812
Cdd:cd18590 56 RGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK---TLGMLG--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 813 pwFLVAVGPLVILFSVLHIVSRVLI--------RELKR--LDNITQSPFLshITSSIQGLATIHAYNKGQEFLHRYQELL 882
Cdd:cd18590 130 --FMLSLSWQLTLLTLIEMPLTAIAqkvyntyhQKLSQavQDSIAKAGEL--AREAVSSIRTVRSFKAEEEEACRYSEAL 205
|
..
gi 1622900605 883 DD 884
Cdd:cd18590 206 ER 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1011-1207 |
3.01e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.71 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1011 LKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLAD---LRSKLSIIPQEP-VLFSGTVR 1086
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLD-PF---NQYTED---QIWDALERTHMKECIAQLPLKLesevmengdnfSVGERQLLCIARALLRHCKILILDEATA 1159
Cdd:PRK10908 98 DNVAiPLiiaGASGDDirrRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622900605 1160 AMDTEtdllIQETIREAFAD-----CTMLTIAHRLHTVLGSD-RIMVLAQGQVV 1207
Cdd:PRK10908 167 NLDDA----LSEGILRLFEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
382-570 |
3.06e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 382 IDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISG---TFAYVA---------------QQAWILNATLRDN 443
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpiDIRSPRdairagimlcpedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 444 ILFGKeydeeRYNSVLNSCCLRP------------DLAILPSSDLTEIGergaNLSGGQRQRISLARALYSDRSIYILDD 511
Cdd:PRK11288 352 INISA-----RRHHLRAGCLINNrweaenadrfirSLNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622900605 512 PLSALDahVG------NHIFNSAIRKhlksKTVLFVTHQL-QYLVDCDEVIFMKEGCITERGTHEE 570
Cdd:PRK11288 423 PTRGID--VGakheiyNVIYELAAQG----VAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
392-571 |
3.29e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 392 VGICGSVGSGKTSLISAILGQMTLLEGSIAISG-------------TFAYVAQQA--WILNATLRDNILFG-------KE 449
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQNPddQIFSPTVEQDIAFGpinlgldEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 450 YDEERYNSVLNSCCLRPDLAILPSsdlteigergaNLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIF---N 526
Cdd:PRK13652 113 TVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIdflN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622900605 527 SAIRKHlkSKTVLFVTHQLQYLVDCDEVIF-MKEGCITERGTHEEL 571
Cdd:PRK13652 182 DLPETY--GMTVIFSTHQLDLVPEMADYIYvMDKGRIVAYGTVEEI 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
387-550 |
5.12e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 387 QEGKLVGICGSVGSGKTSLISAILGQMT------------------------------LLEGSIAISGTFAYVAQQAWIL 436
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkrfrgtelqdyfkkLANGEIKVAHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 437 NATLRDnILfgKEYDEErynSVLNSccLRPDLAILPSSDlTEIGErganLSGGQRQRISLARALYSDRSIYILDDPLSAL 516
Cdd:COG1245 177 KGTVRE-LL--EKVDER---GKLDE--LAEKLGLENILD-RDISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622900605 517 DahVGNHIfNSA--IRKHLKS-KTVLFVTHQ---LQYLVD 550
Cdd:COG1245 244 D--IYQRL-NVArlIRELAEEgKYVLVVEHDlaiLDYLAD 280
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
720-880 |
5.35e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 43.65 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 720 ALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpFQAEMFI 795
Cdd:cd18564 57 AAALVGIALLRGLasyaGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQD---LLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 796 QNVILVFFCVGMIAGVFpWF-----LVAVGPL-VILFSVLHIVSRvlIRELKRldniTQSPFLSHITS----SIQGLATI 865
Cdd:cd18564 134 PLLTNLLTLVGMLGVMF-WLdwqlaLIALAVApLLLLAARRFSRR--IKEASR----EQRRREGALASvaqeSLSAIRVV 206
|
170
....*....|....*
gi 1622900605 866 HAYNKGQEFLHRYQE 880
Cdd:cd18564 207 QAFGREEHEERRFAR 221
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
481-578 |
5.64e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 481 ERGAN-LSGGQRQRISLARALYSDRS--IYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFM 557
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDI 562
|
90 100 110
....*....|....*....|....*....|.
gi 1622900605 558 KE------GCITERGTHEELMN----LNGDY 578
Cdd:TIGR00630 563 GPgagehgGEVVASGTPEEILAnpdsLTGQY 593
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
994-1162 |
5.72e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.19 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 994 VTFENAEMRYRENLPL---VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRIS------DIgl 1064
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkDI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1065 ADLRSKLSIIPQ--EPVLFSGTVRSNL----DPFNQYTEDQIWDALERTHM----KECIAQLPLKLesevmengdnfSVG 1134
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALvgisESLFEKNPFEL-----------SGG 149
|
170 180
....*....|....*....|....*...
gi 1622900605 1135 ERQLLCIARALLRHCKILILDEATAAMD 1162
Cdd:PRK13649 150 QMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
743-783 |
5.79e-04 |
|
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: 43.30 E-value: 5.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1622900605 743 RASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEV 783
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEF 112
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1010-1209 |
6.65e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.10 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1010 VLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSG--GCIKIDGVRISDiglaDLRSKLSIIPQEPVLFSG-TVR 1086
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1087 SNLDPFNQYTEDQIWDALERTHMKE-CIAQLPL-KLESEVMENG--DNFSVGERQLLCIARALLRHCKILILDEATAAMD 1162
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAEsVISELGLtKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 1163 TETDL-LIQetireafadcTMLTIAHRLHTVLGS------------DRIMVLAQGQVVEF 1209
Cdd:PLN03211 239 ATAAYrLVL----------TLGSLAQKGKTIVTSmhqpssrvyqmfDSVLVLSEGRCLFF 288
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
487-526 |
7.66e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 7.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622900605 487 SGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFN 526
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
368-514 |
1.09e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 368 IHLGHLRL----QRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAIL-------GQMTLLEGSIAISGTFAYVAQQ-AWI 435
Cdd:NF033858 2 ARLEGVSHrygkTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarkiqqGRVEVLGGDMADARHRRAVCPRiAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 436 -------LNATL--RDNI-----LFGKEYDEERYnsvlnscclRPDlAILPSSDLTEIGERGA-NLSGGQRQRISLARAL 500
Cdd:NF033858 82 pqglgknLYPTLsvFENLdffgrLFGQDAAERRR---------RID-ELLRATGLAPFADRPAgKLSGGMKQKLGLCCAL 151
|
170 180
....*....|....*....|
gi 1622900605 501 YSDRSIYILD------DPLS 514
Cdd:NF033858 152 IHDPDLLILDepttgvDPLS 171
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
479-571 |
1.23e-03 |
|
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: 43.08 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 479 IGERGANLSGGQRQRISLARALY---SDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVI 555
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYII 902
|
90 100
....*....|....*....|..
gi 1622900605 556 FM------KEGCITERGTHEEL 571
Cdd:TIGR00630 903 DLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
748-946 |
1.26e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 42.14 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 748 LHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNViLVFFCVGMIAGVFPWFLVAVG----PLV 823
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNV-LTLVGVAIILFSINPKLALLTlipiPFL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 824 ILFSVLH-IVSRVLIRELKRldnitqspFLSHITS----SIQGLATIHAYNKGQEFLHRYQELLDDnqapffLFTCAMRw 898
Cdd:cd18778 154 ALGAWLYsKKVRPRYRKVRE--------ALGELNAllqdNLSGIREIQAFGREEEEAKRFEALSRR------YRKAQLR- 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622900605 899 lAVRLDLI---SIALITTTGLMIVLMHGqippayAGLAISYAVQLTGLFQF 946
Cdd:cd18778 219 -AMKLWAIfhpLMEFLTSLGTVLVLGFG------GRLVLAGELTIGDLVAF 262
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
71-267 |
1.44e-03 |
|
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: 42.15 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 71 EKSLGELINICSNDgqrmfeAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLG---SAVFILFYPAMMFASRltaYFRRK 147
Cdd:cd07346 92 RNRTGDLMSRLTSD------VDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNwklTLVALLLLPLYVLILR---YFRRR 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 148 CVAATDERVQKM-------NEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFS 220
Cdd:cd07346 163 IRKASREVRESLaelsaflQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622900605 221 V--HMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDR 267
Cdd:cd07346 243 YggYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
720-887 |
1.56e-03 |
|
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: 42.09 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 720 ALSMAVMLILKAIRGVVFVKGTLRASSR-LHD---ELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVrlpfqaemFI 795
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERlLYDlrlRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSE--------LL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 796 QN-----VILVFFCVGMIAGVF----PWFLVAVGPLVILFsvlhIVSRVLIRELKRL-----DNITQSpfLSHITSSIQG 861
Cdd:cd18546 114 QTglvqlVVSLLTLVGIAVVLLvldpRLALVALAALPPLA----LATRWFRRRSSRAyrrarERIAAV--NADLQETLAG 187
|
170 180
....*....|....*....|....*.
gi 1622900605 862 LATIHAYNKGQEFLHRYQELLDDNQA 887
Cdd:cd18546 188 IRVVQAFRRERRNAERFAELSDDYRD 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
484-550 |
1.60e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.61 E-value: 1.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 484 ANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH-VgnhifnSAIRKHLK--SKTVLFVTHQlQYLVD 550
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsV------AWLERHLQeyPGTVVAVTHD-RYFLD 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
475-550 |
1.87e-03 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 41.58 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 475 DLTEIGERG-ANLSGGQRQRISLARALYSDRSIYILDDPLSALDahVGNHIfNSA--IRKHLK-SKTVLFVTHQ---LQY 547
Cdd:cd03236 128 ELRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQRL-NAArlIRELAEdDNYVLVVEHDlavLDY 204
|
...
gi 1622900605 548 LVD 550
Cdd:cd03236 205 LSD 207
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
731-779 |
1.87e-03 |
|
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: 41.85 E-value: 1.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622900605 731 AIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKD 779
Cdd:cd18780 60 FLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSD 108
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
369-571 |
2.16e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 369 HLGHLRlqrTLHSIDLEIQEGKLVGICGSVGSG--KTSLISAILGQ---------MTLLEGSIAISGTFAY--VAQQAWI 435
Cdd:NF000106 22 HFGEVK---AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPdagrrpwrf*TWCANRRALRRTIG*hrPVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 436 LNATLRDNI-LFGKEYDEERYNSVLnscclRPDlAILPSSDLTEI-GERGANLSGGQRQRISLARALYSDRSIYILDDPL 513
Cdd:NF000106 99 ESFSGRENLyMIGR*LDLSRKDARA-----RAD-ELLERFSLTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900605 514 SALDAHVGNHIFNSAIRKHLKSKTVLFVThqlQYLVDCD----EVIFMKEGCITERGTHEEL 571
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLLTT---QYMEEAEqlahELTVIDRGRVIADGKVDEL 231
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
486-575 |
3.82e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 486 LSGGQRQRISLARALYS---DRSIYILDDPLSAL---DAHVGNHIFNSAIRkhlKSKTVLFVTHQLQYLVDCDEVIFM-- 557
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTH---QGHTVVIIEHNMHVVKVADYVLELgp 886
|
90 100
....*....|....*....|..
gi 1622900605 558 ----KEGCITERGTHEELMNLN 575
Cdd:PRK00635 887 eggnLGGYLLASCSPEELIHLH 908
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
727-882 |
5.90e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. 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. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 40.24 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 727 LILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDmDEVDVRLPFQAEMFIQNVILVFFCVG 806
Cdd:cd18568 56 ILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLG 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 807 MIAgVFPWFL--VAVGpLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELL 882
Cdd:cd18568 135 LMF-YYNLQLtlIVLA-FIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKF 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
452-519 |
6.16e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 6.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622900605 452 EERYNSVLNSCCLRPDLAIlpssdlteigERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAH 519
Cdd:PLN03073 321 EARAASILAGLSFTPEMQV----------KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH 378
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
719-873 |
7.05e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 40.09 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 719 YALSMAVMLILKAI----RGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVD---VR-LP-- 788
Cdd:cd18584 39 LLLLLLAALLLRALlawaQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDgyfARyLPql 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900605 789 FQAeMFIQNVILVF-FCVGMIAGVfpwFLVAVGPLVILFSVL-----HIVSRVLIRELKRLDNitqspflsHITSSIQGL 862
Cdd:cd18584 119 VLA-AIVPLLILVAvFPLDWVSAL---ILLVTAPLIPLFMILigkaaQAASRRQWAALSRLSG--------HFLDRLRGL 186
|
170
....*....|.
gi 1622900605 863 ATIHAYNKGQE 873
Cdd:cd18584 187 PTLKLFGRARA 197
|
|
| |
